>d1scta_ 1.1.1.1.1 Hemoglobin I {Ark clam (Scapharca inaequivalvis)}
xvdaavakvcgseaikanlrrswgvlsadieatglmlmsnlftlrpdtktyftrlgdvqk
gkansklrghaitltyalnnfvdslddpsrlkcvvekfavnhinrkisgdafgaivepmk
etlkarmgnyysddvagawaalvgvvqaal
>d1sctb_ 1.1.1.1.1 Hemoglobin I {Ark clam (Scapharca inaequivalvis)}
kvaelanavvsnadqkdllrmswgvlsvdmegtglmlmanlfktspsakgkfarlgdvsa
gkdnsklrghsitlmyalqnfvdalddverlkcvvekfavnhinrqisadefgeivgplr
qtlkarmgnyfdedtvaawaslvavvqasl
>d3sdha_ 1.1.1.1.1 Hemoglobin I {Ark clam (Scapharca inaequivalvis)}
svydaaaqltadvkkdlrdswkvigsdkkgngvalmttlfadnqetigyfkrlgnvsqgm
andklrghsitlmyalqnfidqldnpddlvcvvekfavnhitrkisaaefgkingpikkv
lasknfgdkyanawaklvavvqaal
>d1b0b__ 1.1.1.1.2 Hemoglobin I {Clam (Lucina pectinata)}
lsaaqkdnvksswakasaawgtagpeffmalfdahddvfakfsglfsgaakgtvkntpem
aaqaqsfkglvsnwvdnldnagalegqcktfaanhkargisagqleaafkvlagfmksyg
gdegawtavagalmgmirpdm
>d2hbg__ 1.1.1.1.3 Glycera globin {Marine bloodworm (Glycera dibranchiata)}
glsaaqrqviaatwkdiagadngagvgkkclikflsahpqmaavfgfsgasdpgvaalga
kvlaqigvavshlgdegkmvaqmkavgvrhkgygnkhikaqyfeplgasllsamehrigg
kmnaaakdawaaayadisgalisglqs
>d1a6m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1mba__ 1.1.1.1.5 Myoglobin {Sea hare (Aplysia limacina)}
xslsaaeadlagkswapvfanknangldflvalfekfpdsanffadfkgksvadikaspk
lrdvssriftrlnefvnnaanagkmsamlsqfakehvgfgvgsaqfenvrsmfpgfvasv
aappagadaawtklfgliidalkaaga
>d1myt__ 1.1.1.1.12 Myoglobin {Yellowfin tuna (Thunnus albacares)}
adfdavlkcwgpveadyttmgglvltrlfkehpetqklfpkfagiaqadiagnaaisahg
atvlkklgellkakgshaailkplanshatkhkipinnfklisevlvkvmhekagldagg
qtalrnvmgiiiadleanykelgfsg
>d1eco__ 1.1.1.1.13 Erythrocruorin {Midge (Chironomous thummi thummi), fraction III}
lsadqistvqasfdkvkgdpvgilyavfkadpsimakftqfagkdlesikgtapfethan
rivgffskiigelpnieadvntfvashkprgvthdqlnnfragfvsymkahtdfagaeaa
wgatldtffgmifskm
>d2gdm__ 1.1.1.1.14 Leghemoglobin {Yellow lupin (Lupinus luteus)}
galtesqaalvkssweefnanipkhthrffilvleiapaakdlfsflkgtsevpqnnpel
qahagkvfklvyeaaiqlevtgvvvtdatlknlgsvhvskgvadahfpvvkeailktike
vvgakwseelnsawtiaydelaivikkemddaa
>d1fsla_ 1.1.1.1.15 Leghemoglobin {Soybean (Glycine max), isoform A}
vaftekqdalvsssfeafkanipqysvvfytsilekapaakdlfsflangvdptnpkltg
haeklfalvrdsagqlkasgtvvadaalgsvhaqkavtdpqfvvvkeallktikaavgdk
wsdelsrawevaydelaaaikka
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1hbra_ 1.1.1.1.21 Hemoglobin D {Chicken (Gallus gallus)}
mltaedkkliqqawekaashqeefgaealtrmfttypqtktyfphfdlspgsdqvrghgk
kvlgalgnavknvdnlsqamaelsnlhaynlrvdpvnfkllsqciqvvlavhmgkdytpe
vhaafdkflsavsavlaekyr
>d1outa_ 1.1.1.1.23 Hemoglobin D {Trout (Oncorhyncus mykiss)}
sltakdksvvkafwgkisgkadvvgaealgrmltaypqtktyfshwadlspgsgpvkkhg
giimgaigkavglmddlvggmsalsdlhafklrvdpgnfkilshnilvtlaihfpsdftp
evhiavdkflaavsaaladkyr
>d1cg5a_ 1.1.1.1.25 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vlssqnkkaieelgnlikanaeawgadalarlfelhpqtktyfskfsgfeacneqvkkhg
krvmnaladathhldnlhlhledlarkhgenllvdphnfhlfadcivvtlavnlqaftpv
thcavdkflelvayelsscyr
>d1t1na_ 1.1.1.1.26 Hemoglobin D {Fish (Trematomus newnesi)}
slsdkdkaavralwskigkssdaigndalsrmivvypqtkiyfshwpdvtpgspnikahg
kkvmggialavskiddlktglmelseqhayklrvdpsnfkilnhcilvvistmfpkeftp
eahvsldkflsgvalalaeryr
>d1spga_ 1.1.1.1.27 Hemoglobin D {Teleost fish (Leiostomus xanthurus)}
slsatdkarvkalwdkiegksaelgaealgrmlvsfpqtkiyfsewgqdlgpqtpqvrnh
gavimaavgkavksidnlvgglsqlselhafklrvdpanfkilahniilvismyfpgdft
pevhlsvdkflaclalalsekyr
>d1babb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1outb_ 1.1.1.1.38 Hemoglobin D {Trout (Oncorhyncus mykiss)}
vewtdaekstisavwgkvnideigplalarvlivypwtqryfgsfgnvstpaaimgnpkv
aahgkvvcgaldkavknmgnilatykslsethanklfvdpdnfrvladvltiviaakfga
sftpeiqatwqkfmkvvvaamgsryf
>d1cg5b_ 1.1.1.1.40 Hemoglobin D {Cartilaginous fish akaei (Dasyatis akajei)}
vklsedqehyikgvwkdvdhkqitakalervfvvypwttrlfsklqglfsandigvqqha
dkvqralgeaiddlkkveinfqnlsgkhqeigvdtqnfkllgqtfmvelalhykktfrpk
ehaaaykffrlvaealssnyh
>d1t1nb_ 1.1.1.1.41 Hemoglobin D {Fish (Trematomus newnesi)}
vewtdkersiisdifshmdyddigpkalsrclvvypwtqryfsgfgnlynaegimsnanv
aahgikvlhgldrgmknmdniadaytdlstlhseklhvdpdnfkllsdcitivlaakmgh
aftaetqgafqkflaavvsalgkqyh
>d1spgb_ 1.1.1.1.42 Hemoglobin D {Teleost fish (Leiostomus xanthurus)}
vdwtdaeraaikalwgkidvgeigpqalsrllivypwtqrhfkgfgnistnaailgnakv
aehgktvmggldravqnmdniknvykqlsikhsekihvdpdnfrllgeiitmcvgakfgp
saftpeiheawqkflavvvsalgrqyh
>d2lhb__ 1.1.1.1.43 Lamprey globin {Sea lamprey (Petromyzon marinus)}
pivdtgsvaplsaaektkirsawapvystyetsgvdilvkfftstpaaqeffpkfkgltt
adelkksadvrwhaeriinavddavasmddtekmsmklrnlsgkhaksfqvdpeyfkvla
aviadtvaagdagfeklmsmicillrsay
>d1ash__ 1.1.1.1.44 Ascaris hemoglobin, domain 1 {Pig roundworm (Ascaris suum)}
anktrelcmkslehakvdtsnearqdgidlykhmfenypplrkyfksreeytaedvqndp
ffakqgqkillachvlcatyddretfnaytrelldrhardhvhmppevwtdfwklfeeyl
gkkttldeptkqawheigrefakeink
>d1itha_ 1.1.1.1.45 Hemoglobin {Innkeeper worm (Urechis caupo)}
gltaaqikaiqdhwflnikgclqaaadsiffkyltaypgdlaffhkfssvplyglrsnpa
ykaqtltvinyldkvvdalggnagalmkakvpshdamgitpkhfgqllklvggvfqeefs
adpttvaawgdaagvlvaamk
>d1hlb__ 1.1.1.1.46 Hemoglobin {Sea cucumber (Caudina (Molpadia) arenicola)}
xggtlaiqaqgdltlaqkkivrktwhqlmrnktsfvtdvfirifaydpsaqnkfpqmagm
sasqlrssrqmqahairvssimseyveeldsdilpellatlarthdlnkvgadhynlfak
vlmealqaelgsdfnektrdawakafsvvqavllvkhg
>d1vhba_ 1.1.1.1.47 Bacterial dimeric hemoglobin {Vitreoscilla stercoraria}
ldqqtiniikatvpvlkehgvtitttfyknlfakhpevrplfdmgrqesleqpkalamtv
laaaqnienlpailpavkkiavkhcqagvaaahypivgqellgaikevlgdaatddilda
wgkaygviadvfiqveadlyaqav
>d1cqxa1 1.1.1.1.48 (1-150) Flavohemoglobin, N-terminal domain {Alcaligenes eutrophus}
mltqktkdivkatapvlaehgydiikcfyqrmfeahpelknvfnmahqeqgqqqqalara
vyayaeniedpnslmavlkniankhaslgvkpeqypivgehllaaikevlgnaatddiis
awaqaygnladvlmgmeselyersaeqpgg
>d1phna_ 1.1.1.2.1 Phycocyanin {Red alga (Cyanidium caldarium)}
mktpiteaiaaadnqgrflsntelqavngryqraaasleaarsltsnaerlingaaqavy
skfpytsqmpgpqyassavgkakcardigyylrmvtyclvvggtgpmdeyliagleeinr
tfdlspswyvealnyikanhglsgqaaneantyidyainals
>d1phnb_ 1.1.1.2.1 Phycocyanin {Red alga (Cyanidium caldarium)}
mldafakvvaqadargeflsntqldalskmvsegnkrldvvnritsnasaivtnaaralf
seqpqliqpggxaytnrrmaaclrdmeiilryvsyaiiagdssilddrclnglretyqal
gvpgasvavgiekmkdsaiaiandpsgittgdcsalmaevgtyfdraatavq
>d1alla_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
sivtksivnadaearylspgeldriksfvtsgerrvriaetmtgareriikqagdqlfgk
rpdvvspggnaygadmtatclrdldyylrlitygivagdvtpieeigvvgvremykslgt
pieaiaegvramksvatsllsgadaaeagsyfdyligams
>d1allb_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
mqdaitsvinssdvqgkyldasaiqklkayfatgelrvraattisanaanivkeavaksl
lysdvtrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpigatvqaiqamkevtaglvgggagkemgiyfdyicsgls
>d1b8da_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mksvitttisaadaagrfpsssdlesiqgniqraaarleaaqklsgnheavvkeagdacf
akysylknageagdspekinkcyrdidhymrlinyslvvggtgpvdewgiagsrevyral
nlpgsayiaaftftrdrlcvprdmssqagveftsaldyvinslc
>d1qgwc_ 1.1.1.2.7 Phycoerythrin {Rhodomonas cs 24}
dafsrvvtnadskaayvggadlqalkkfisegnkrldsvnsivsnascivsdavsgmice
npslispsgxcytnrrmaaclrdgeiilryvsyallsgdasvledrclnglketysslgv
pansnaravsimkacavafvnntasqkklstpqgdcsglasevggyfdkvtaais
>d1grj_1 1.2.1.1.1 (2-79) GreA transcript cleavage protein, N-terminal domain {Escherichia coli}
qaipmtlrgaeklreeldflksvrrpeiiaaiaearehgdlkenaeyhaareqqgfcegr
ikdieaklsnaqvidvtk
>d1hdj__ 1.2.2.1.1 HSP40 {Human (Homo sapiens)}
mgkdyyqtlglargasdeeikrayrrqalryhpdknkepgaeekfkeiaeaydvlsdprk
reifdrygeeglkgsgc
>d1bq0__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeqgg
>d1bqz__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeqgg
>d1xbl__ 1.2.2.1.2 DnaJ chaperone, N-terminal (J) domain {Escherichia coli}
akqdyyeilgvsktaeereirkaykrlamkyhpdrnqgdkeaeakfkeikeayevltdsq
kraaydqyghaafeq
>d1cxzb_ 1.2.3.1.1 Effector domain of the protein kinase pkn/prk1 {Human (Homo sapiens)}
wslleqlglagadlaapgvqqqlelererlrreirkelklkegaenlrrattdlgrslgp
velllrgssrrldllhqqlqelhahv
>d1seta1 1.2.4.1.1 (1-110) Seryl-tRNA synthetase (SerRS), N-terminal domain {Thermus thermophilus, strain hb27}
mvdlkrlrqepevfhrairekgvaldleallaldrevqelkkrlqevqternqvakrvpk
appeekealiargkalgeeakrleealrekearlealllqvplppwpgap
>d1a36a1 1.2.5.1.1 (641-712) Eukaryotic DNA topoisomerase I, dispensable insert domain {Human (Homo sapiens)}
eksmmnlqtkidakkeqladarrdlksakadakvmkdaktkkvveskkkavqrleeqlmk
levqatdreenk
>d1aqt_1 1.2.6.1.1 (87-136) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkk
>d1bsha1 1.2.6.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1bsna1 1.2.6.1.1 (87-138) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkkam
>d1idsa1 1.2.7.1.1 (2-85) Fe superoxide dismutase (FeSOD) {Mycobacterium tuberculosis}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsb1 1.2.7.1.1 (2-85) Fe superoxide dismutase (FeSOD) {Mycobacterium tuberculosis}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsc1 1.2.7.1.1 (2-85) Fe superoxide dismutase (FeSOD) {Mycobacterium tuberculosis}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d1idsd1 1.2.7.1.1 (2-85) Fe superoxide dismutase (FeSOD) {Mycobacterium tuberculosis}
aeytlpdldwdygalephisgqinelhhskhhatyvkgandavakleearakedhsaill
neknlafnlaghvnhtiwwknlsp
>d3sdpa1 1.2.7.1.2 (5-83) Fe superoxide dismutase (FeSOD) {Pseudomonas ovalis}
pplpyahdalqphisketleyhhdkhhntyvvnlnnlvpgtpefegktleeivksssggi
fnnaaqvwnhtfywnclsp
>d3sdpb1 1.2.7.1.2 (5-83) Fe superoxide dismutase (FeSOD) {Pseudomonas ovalis}
pplpyahdalqphisketleyhhdkhhntyvvnlnnlvpgtpefegktleeivksssggi
fnnaaqvwnhtfywnclsp
>d1isaa1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isab1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isba1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isbb1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1isca1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1iscb1 1.2.7.1.3 (1-82) Fe superoxide dismutase (FeSOD) {Escherichia coli}
sfelpalpyakdalaphisaetieyhygkhhqtyvtnlnnlikgtafegksleeiirsse
ggvfnnaaqvwnhtfywnclap
>d1coja1 1.2.7.1.4 (2-90) Fe superoxide dismutase (FeSOD) {Aquifex pyrophilus}
vhklepkdhlkpqnlegisneqiephfeahykgyvakyneiqekladqnfadrskanqny
seyrelkveetfnymgvvlhelyfgmltp
>d1sssa1 1.2.7.1.5 (4-92) Fe superoxide dismutase (FeSOD) {Sulfolobus solfataricus}
iqfkkyelpplpykidalepyiskdiidvhynghhkgyvngansllerlekvvkgdlqtg
qydiqgiirgltfninghklhalywenma
>d1sssb1 1.2.7.1.5 (4-92) Fe superoxide dismutase (FeSOD) {Sulfolobus solfataricus}
iqfkkyelpplpykidalepyiskdiidvhynghhkgyvngansllerlekvvkgdlqtg
qydiqgiirgltfninghklhalywenma
>d1b06a1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1b06b1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1b06c1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1b06d1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1b06e1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1b06f1 1.2.7.1.6 (3-92) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
viqlkryefpqlpykvdalepyiskdiidvhynghhkgyvnganslldrleklikgdlpq
gqydlqgilrgltfninghklhaiywnnma
>d1abma1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abmb1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5a1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5b1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6a1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6b1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1msda1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1msdb1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1qnma1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1qnmb1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1vara1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqtal
qpalkfnggghinhsifwtnlsp
>d1varb1 1.2.7.1.7 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqtal
qpalkfnggghinhsifwtnlsp
>d1mmma1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1mmmb1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1vewa1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1vewb1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1vewc1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1vewd1 1.2.7.1.8 (1-90) Mn superoxide dismutase (MnSOD) {Escherichia coli}
sytlpslpyaydalephfdkqtmeihhtkhhqtyvnnanaaleslpefanlpveelitkl
dqlpadkktvlrnnagghanhslfwkglkk
>d1mnga1 1.2.7.1.9 (1-92) Mn superoxide dismutase (MnSOD) {Thermus thermophilus}
pypfklpdlgypyealephidaktmeihhqkhhgayvtnlnaalekypylhgvevevllr
hlaalpqdiqtavrnnggghlnhslfwrlltp
>d1ar4a1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4b1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5a1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5b1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avma1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avmb1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bs3a1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bs3b1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bsma1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bsmb1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bt8a1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1bt8b1 1.2.7.1.10 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1b7ca_ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Bacillus pasteurii}
vdaeavvqqkcischggdltgasapaidkaganyseeeildiilngqggmpggiakgaea
eavaawlaekk
>d1a2s__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1ced__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1ctj__ 1.3.1.1.2 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1c53__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscvgchgadgskqamgvghavkgqkadelfkklkgyadgsyggekkavmtnl
vkrysdeemkamadymskl
>d1dvh__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscigchgadgskaamgsakpvkgqgaeelykkmkgyadgsyggerkammtna
vkkysdeelkaladymskl
>d2dvh__ 1.3.1.1.3 Cytochrome c6 (synonym: cytochrome c553) {Desulfovibrio vulgaris, different strains}
adgaalykscigchgadgskaamgsakpvkgqgaeelykkmkgyadgsyggerkammtna
vkkasdeelkaladymskl
>d1cyi__ 1.3.1.1.4 Cytochrome c6 (synonym: cytochrome c553) {Chlamydomonas reinhardtii}
adlalgaqvfngncaachmggrnsvmpektldkaaleqyldggfkvesiiyqvengkgam
pawadrlseeeiqavaeyvfkqatdaawk
>d1cyj__ 1.3.1.1.4 Cytochrome c6 (synonym: cytochrome c553) {Chlamydomonas reinhardtii}
adlalgaqvfngncaachmggrnsvmpektldkaaleqyldggfkvesiiyqvengkgam
pawadrlseeeiqavaeyvfkqatdaawky
>d1c6s__ 1.3.1.1.5 Cytochrome c6 (synonym: cytochrome c553) {Blue-green alga cyanobacterium (Synechococcus elongatus)}
adlangakvfsgncaachmgggnvvmanktlkkealeqfgmysedaiiyqvqhgknampa
fagrltdeqiqdvaayvldqaakgwag
>d1c52__ 1.3.1.1.6 Cytochrome c552 {Thermus thermophilus}
qadgakiyaqcagchqqngqgipgafpplaghvaeilakeggreylilvllyglqgqiev
kgmkyngvmssfaqlkdeeiaavlnhiatawgdakkvkgfkpftaeevkklrakkltpqq
vlaerkklglk
>d1cnoa_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnob_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnoc_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnod_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnoe_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnof_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1cnog_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaaa
>d1cnoh_ 1.3.1.1.7 Cytochrome c552 {Pseudomonas nautica}
agdieagkakaavcaachgqngisqvpiypnlagqkeqylvaalkaykagqrqggqapvm
qgqatalsdadianlaayyasnpaaa
>d1ql3a_ 1.3.1.1.8 Cytochrome c552 {Paracoccus denitrificans}
adpaagekvfgkckachkldgndgvgphlngvvgrtvagvdgfnysdpmkahggdwtpea
lqefltnpkavvkgtkmafaglpkiedranliaylegqq
>d1ycc__ 1.3.1.1.9 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
tefkagsakkgatlfktrclqchtvekggphkvgpnlhgifgrhsgqaegysytdanikk
nvlwdennmseyltnpkkyipgtkmafgglkkekdrndlitylkkace
>d1ytc__ 1.3.1.1.9 Mitochondrial cytochrome c {Baker's yeast (Saccharomyces cerevisiae)}
akestgfkpgsakkgatlfktrcqqchtieeggpnkvgpnlhgifgrhsgqvkgysytda
iinknvkwdedsmseyltnpkkyipgtkmafaglkkekdrndlitymtkaak
>d1wejf_ 1.3.1.1.10 Mitochondrial cytochrome c {Horse (Equus caballus)}
gdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitwk
eetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1ccr__ 1.3.1.1.11 Mitochondrial cytochrome c {Rice embryos (Oryza sativa)}
xasfseappgnpkagekifktkcaqchtvdkgaghkqgpnlnglfgrqsgttpgysysta
dknmaviweentlydyllnpkkyipgtkmvfpglkkpqeradlisylkeats
>d5cytr_ 1.3.1.1.12 Mitochondrial cytochrome c {Albacore tuna (Thunnus alalunga)}
xgdvakgkktfvqkcaqchtvenggkhkvgpnlwglfgrktgqaegysytdankskgivw
nndtlmeylenpkkyipgtkmifagikkkgerqdlvaylksats
>d3c2c__ 1.3.1.1.14 Cytochrome c2 {Rhodospirillum rubrum}
egdaaagekvskkclachtfdqggankvgpnlfgvfentaahkdnyaysesytemkakgl
twteanlaayvknpkafvleksgdpkakskmtfkltkddeienviaylktlk
>d1c2ra_ 1.3.1.1.15 Cytochrome c2 {Rhodobacter capsulatus}
gdaakgekefnkcktchsiiapdgteivkgaktgpnlygvvgrtagtypefkykdsival
gasgfawteediatyvkdpgaflkeklddkkaktgmafklakggedvaaylasvvk
>d1cxc__ 1.3.1.1.16 Cytochrome c2 {Rhodobacter spaeroides}
qegdpeagakafnqcqtchvivddsgttiagrnaktgpnlygvvgrtagtqadfkgygeg
mkeagakglawdeehfvqyvqdptkflkeytgdakakgkmtfklkkeadahniwaylqqv
avrp
>d1co6a_ 1.3.1.1.17 Cytochrome c2 {Rhodopseudomonas viridis}
qdaasgeqvfkqclvchsigpgaknkvgpvlnglfgrhsgtiegfaysdanknsgitwte
evfreyirdpkakipgtkmifagvkdeqkvsdliayikqfnadgskk
>d1hroa_ 1.3.1.1.18 Cytochrome c2 {Rhodopila globiformis}
sappgdpvegkhlfhticitchtdikgankvgpslygvvgrhsgiepgynyseaniksgi
vwtpdvlfkyiehpqkivpgtkmgypgqpdpqkradiiayletlk
>d1cot__ 1.3.1.1.19 Cytochrome c2 {Paracoccus denitrificans}
dgdaakgekefnkckachmiqapdgtdiikggktgpnlygvvgrkiaseegfkygegile
vaeknpdltwteadlieyvtdpkpwlvkmtddkgaktkmtfkmgknqadvvaflaqnspd
a
>d1cc5__ 1.3.1.1.20 Cytochrome c5 {Azotobacter vinelandii}
gggarsgddvvakycnachgtgllnapkvgdsaawktradakggldgllaqslsglnamp
pkgtcadcsddelkaaigkmsgl
>d1cch__ 1.3.1.1.21 Cytochrome c551 {Pseudomonas stutzeri}
qdgealfkskpcaachsvdtkmvgpalkevaaknagvegaadtlalhikngsqgvwgpip
mppnpvteeeakilaewvlslk
>d1cor__ 1.3.1.1.21 Cytochrome c551 {Pseudomonas stutzeri}
xdgealfkskpcaachsidaklvgpafkevaakyagqdgaadllaghikngsqgvwgpip
mppnpvteeeakilaewilsqk
>d2pac__ 1.3.1.1.22 Cytochrome c551 {Pseudomonas aeruginosa}
edpevlfknkgcvachaidtkmvgpaykdvaakfagqagaeaelaqrikngsqgvwgpip
mppnavsddeaqtlakwvlsqk
>d351c__ 1.3.1.1.22 Cytochrome c551 {Pseudomonas aeruginosa}
edpevlfknkgcvachaidtkmvgpaykdvaakfagqagaeaelaqrikngsqgvwgpip
mppnavsddeaqtlakwvlsqk
>d451c__ 1.3.1.1.22 Cytochrome c551 {Pseudomonas aeruginosa}
edpevlfknkgcvachaidtkmvgpaykdvaakfagqagaeaelaqrikngsqgvwgpip
mppnavsddeaqtlakwvlsqk
>d2mtac_ 1.3.1.1.23 Cytochrome c551 {Paracoccus denitrificans}
apqffniidgsplnfddameegrdteavkhfletgenvynedpeilpeaeelyagmcsgc
hghyaegkigpglndaywtypgnetdvglfstlyggatgqmgpmwgsltldemlrtmawv
rhlytgdpkdaswltdeqkagftpfqp
>d1gks__ 1.3.1.1.24 Cytochrome c551 {Ectothiorhodospira halophila}
dgesiyingtaptcsschdrgvagapelnapedwadrpssvdelvestlagkgampaydg
radredlvkaieymlstl
>d1ayg__ 1.3.1.1.25 Cytochrome c552 {Hydrogenobacter thermophilus}
neqlakqkgcmachdlkakkvgpayadvakkyagrkdavdylagkikkggsgvwgsvpmp
pqnvtdaeakqlaqwilsik
>d1a56__ 1.3.1.1.26 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1a8c__ 1.3.1.1.26 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1diic_ 1.3.1.1.28 p-Cresol methylhydroxylase, cytochrome c subunit {Pseudomonas putida}
sqwgsgknlydkvcghchkpevgvgpvlegrglpeayikdivrngframpafpasyvdde
sltqvaeylsslp
>d1diid_ 1.3.1.1.28 p-Cresol methylhydroxylase, cytochrome c subunit {Pseudomonas putida}
sqwgsgknlydkvcghchkpevgvgpvlegrglpeayikdivrngframpafpasyvdde
sltqvaeylsslp
>d1diqc_ 1.3.1.1.28 p-Cresol methylhydroxylase, cytochrome c subunit {Pseudomonas putida}
sqwgsgknlydkvcghchkpevgvgpvlegrglpeayikdivrngframpafpasyvdde
sltqvaeylsslpa
>d1diqd_ 1.3.1.1.28 p-Cresol methylhydroxylase, cytochrome c subunit {Pseudomonas putida}
sqwgsgknlydkvcghchkpevgvgpvlegrglpeayikdivrngframpafpasyvdde
sltqvaeylsslpa
>d1nira1 1.3.1.2.2 (6-117) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Pseudomonas aeruginosa}
aaeqyqgaasavdpahvvrtngapdmsesefneakqiyfqrcagchgvlrkgatgkpltp
ditqqrgqqylealitygtplgmpnwgssgelskeqitlmakyiqhtppqpp
>d1qksa1 1.3.1.2.3 (9-135) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Paracoccus denitrificans}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaapp
>d1etpa1 1.3.1.3.1 (1-92) Cytochrome c4 {Pseudomonas stutzeri}
agdaeagqgkvavcgachgvdgnspapnfpklagqgeryllkqlqdikagstpgapegvg
rkvlemtgmldplsdqdlediaayfssqkgsv
>d1etpa2 1.3.1.3.1 (93-190) Cytochrome c4 {Pseudomonas stutzeri}
gyadpalakqgeklfrggkldqgmpactgchapngvgndlagfpklggqhaaytakqltd
fregnrtndgdtmimrgvaaklsnkdiealssyiqglh
>d1etpb1 1.3.1.3.1 (1-92) Cytochrome c4 {Pseudomonas stutzeri}
agdaeagqgkvavcgachgvdgnspapnfpklagqgeryllkqlqdikagstpgapegvg
rkvlemtgmldplsdqdlediaayfssqkgsv
>d1fcdc1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
eptaemltnncagchgthgnsvgpaspsiaqmdpmvfvevmegfksgeiastimgriakg
ystadfekmagyfkqqtyqp
>d1fcdc2 1.3.1.3.2 (81-174) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
akqsfdtaladtgaklhdkycekchveggkpladeedyhilagqwtpylqyamsdfreer
rpmekkmasklrellkaegdagldalfafyasqq
>d1fcdd1 1.3.1.3.2 (1-80) Flavocytochrome c sulfide dehydrogenase, FCSD, cytochrome subunit {Purple phototrophic bacterium (Cromatium vinosum)}
eptaemltnncagchgthgnsvgpaspsiaqmdpmvfvevmegfksgeiastimgriakg
ystadfekmagyfkqqtyqp
>d1enh__ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkraki
>d1hddc_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d1hddd_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d2hdda_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfknkrakikks
>d2hddb_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
krprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfknkrakik
>d3hdda_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikks
>d3hddb_ 1.4.1.1.1 Engrailed Homeodomain {Drosophila melanogaster}
rprtafsseqlarlkrefnenrylterrrqqlsselglneaqikiwfqnkrakikk
>d1akha_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleevfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1yrna_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleqvfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1akhb_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
tkpyrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrke
ktitiapeladllsgepl
>d1aplc_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
yrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrkekt
>d1apld_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
rghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrkekt
>d1mnmc_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
glvfnvvtqdminkstkpyrghrftkenvrileswfaknienpyldtkglenlmkntsls
riqiknwvsnrrrkekt
>d1mnmd_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
glvfnvvtqdminkstkpyrghrftkenvrileswfaknienpyldtkglenlmkntsls
riqiknwvsnrrrkekt
>d1yrnb_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
tkpyrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrke
ktitiapeladllsgepl
>d1lfb__ 1.4.1.1.4 Transcription factor LFB1 {Rat (Rattus rattus)}
rfkwgpasqqilfqayerqknpskeeretlveecnraeciqrgvspsqaqglgsnlvtev
rvynwfanrrkeeafrhk
>d2lfb__ 1.4.1.1.4 Transcription factor LFB1 {Rat (Rattus rattus)}
maridptkkgrrnrfkwgpasqqilfqayerqknpskeeretlveecnraeciqrgvsps
qaqglgsnlvtevrvynwfanrrkeeafrhklamdtykln
>d1cqta1 1.4.1.1.5 (102-161) Oct-1 POU Homeodomain {Human (Homo sapiens)}
rkkrtsietnirvaleksflenqkptseeitmiadqlnmekevirvwfcnrrqkekrinp
>d1cqtb1 1.4.1.1.5 (602-661) Oct-1 POU Homeodomain {Human (Homo sapiens)}
rkkrtsietnirvaleksflenqkptseeitmiadqlnmekevirvwfcnrrqkekrinp
>d1octc1 1.4.1.1.5 (102-161) Oct-1 POU Homeodomain {Human (Homo sapiens)}
rkkrtsietnirvaleksflenqkptseeitmiadqlnmekevirvwfcnrrqkekrinp
>d1pog__ 1.4.1.1.5 Oct-1 POU Homeodomain {Human (Homo sapiens)}
rrrkkrtsietnirvaleksflenqkptseeitmiadqlnmekevirvwfcnrrqkekri
di
>d1au7a1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7b1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1ftt__ 1.4.1.1.7 Thyroid transcription factor 1 homeodomain {Rat (Rattus rattus)}
mrrkrrvlfsqaqvyelerrfkqqkylsaperehlasmihltptqvkiwfqnhrykmkrq
akdkaaqq
>d1hdp__ 1.4.1.1.8 Oct-2 POU Homeodomain {Human (Homo sapiens)}
rrkkrtsietnvrfaleksflanqkptseeilliaeqlhmekevirvwfcnrrqkekrin
pcs
>d1ocp__ 1.4.1.1.9 Oct-3 POU Homeodomain {Mouse (Mus musculus)}
metlvqarkrkrtsienrvrwsletmflkcpkpslqqithianqlglekdvvrvwfcnrr
qkgkrss
>d1b72a_ 1.4.1.1.10 Homeobox protein hox-b1 {Human (Homo sapiens)}
artfdwmkvkrnppktakvsepglgspsglrtnfttrqltelekefhfnkylsrarrvei
aatlelnetqvkiwfqnrrmkqkkrere
>d1b72b_ 1.4.1.1.11 pbx1 {Human (Homo sapiens)}
rkrrnfnkqateilneyfyshlsnpypseeakeelakkcgitvsqvsnwfgnkrirykkn
igkfqeeaniyaa
>d1bw5__ 1.4.1.1.12 Insulin gene enhancer protein isl-1 {Rat (Rattus norvegicus)}
mkttrvrtvlnekqlhtlrtcyaanprpdalmkeqlvemtglsprvirvwfqnkrckdkk
rsimmk
>d1ahdp_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkke
nktkgepg
>d1hom__ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalclterqikiwfqnrrmkwkke
nktkgepg
>d1san__ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkkenktkge
pg
>d2hoa__ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkke
nktkgepg
>d9anta_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
rqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkken
>d9antb_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
rqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkken
>d1b8ia_ 1.4.1.1.14 Ultrabithorax (ubx) homeodomain {Drosophila melanogaster}
fypwmaiagtnglrrrgrqtytryqtlelekefhtnhyltrrrriemahalslterqiki
wfqnrrmklkkei
>d1b8ib_ 1.4.1.1.15 Extradenticle (exd) homeodomain {Drosophila melanogaster}
rrnfskqaseilneyfyshlsnpypseeakeelarkcgitvsqvsnwfgnkrirykkn
>d1ftz__ 1.4.1.1.16 Fushi Tarazu protein {Fruit fly (Drosophila melanogaster)}
mdskrtrqtytryqtlelekefhfnryitrrrridianalslserqikiwfqnrrmkskk
drtldsspeh
>d1nk2p_ 1.4.1.1.17 VND/NK-2 protein {Fruit fly (Drosophila melanogaster)}
asdglpnkkrkrrvlftkaqtyelerrfrqqrylsaperehlaslirltptqvkiwfqnh
ryktkraqnekgyeghp
>d1nk3p_ 1.4.1.1.17 VND/NK-2 protein {Fruit fly (Drosophila melanogaster)}
kkrkrrvlftkaqtyelerrfrqqrylsaperehlaslirltptqvkiwfqnhryktkra
qne
>d1qrya_ 1.4.1.1.17 VND/NK-2 protein {Fruit fly (Drosophila melanogaster)}
gshmsdglpnkkrkrrvlftkaqtyelerrfrqqrylsaperehltslirltptqvkiwf
qnhryktkraqnekgyeghp
>d1vnd__ 1.4.1.1.17 VND/NK-2 protein {Fruit fly (Drosophila melanogaster)}
asdglpnkkrkrrvlftkaqtyelerrfrqqrylsaperehlaslirltptqvkiwfqnh
ryktkraqnekgyeghp
>d1fjla_ 1.4.1.1.18 Paired protein {Fruit fly (Drosophila melanogaster)}
kqrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrkq
htsvs
>d1fjlb_ 1.4.1.1.18 Paired protein {Fruit fly (Drosophila melanogaster)}
qrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrk
>d1fjlc_ 1.4.1.1.18 Paired protein {Fruit fly (Drosophila melanogaster)}
kqrrsrttfsasqldelerafertqypdiytreelaqrtnlteariqvwfqnrrarlrk
>d1hcra_ 1.4.1.2.1 HIN recombinase (DNA-binding domain) {Synthetic}
grprainkheqeqisrllekghprqqlaiifgigvstlyryfpassikkrmn
>d1gdta1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1gdtb1 1.4.1.2.2 (141-183) gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1res__ 1.4.1.2.2 gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1ret__ 1.4.1.2.2 gamma,delta resolvase (C-terminal domain) {Escherichia coli}
grkrkidrdavlnmwqqglgashisktmniarstvykvinesn
>d1tc3c_ 1.4.1.2.3 Transposase tc3a1-65 {Caenorhabditis elegans}
prgsalsdteraqldvmkllnvslhemsrkisrsrhcirvylkdpvsygts
>d2ezk__ 1.4.1.2.4 Ibeta subdomain of the mu end DNA-binding domain of phage mu transposase {Bacteriophage mu}
miarptleahdydrealwskwdnasdsqrrlaekwlpavqaademlnqgistktafatva
ghyqvsastlrdkyyqvqkfakpdwaaalvdgr
>d2ezl__ 1.4.1.2.4 Ibeta subdomain of the mu end DNA-binding domain of phage mu transposase {Bacteriophage mu}
miarptleahdydrealwskwdnasdsqrrlaekwlpavqaademlnqgistktafatva
ghyqvsastlrdkyyqvqkfakpdwaaalvdgrgasrrn
>d2ezh__ 1.4.1.2.5 Transposase {Bacteriophage mu}
sefdedawqfliadylrpekpafrkcyerlelaarehgwsipsratafrriqqldeamvv
acreg
>d2ezi__ 1.4.1.2.5 Transposase {Bacteriophage mu}
mnvhksefdedawqfliadylrpekpafrkcyerlelaarehgwsipsratafrriqqld
eamvvacregehalm
>d1idy__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
mevkktswteeedrilyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1idz__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
mevkktswteeedrilyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbe__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
lgktrwtreedeklkklveqngtddwkvianylpnrtdvqcqhrwqkvlnpe
>d1mbf__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
lgktrwtreedeklkklveqngtddwkvianylpnrtdvqcqhrwqkvlnpe
>d1mbg__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
likgpwtkeedqrvielvqkygpkrwsviakhlkgrigkqcrerwhnhlnpe
>d1mbh__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
likgpwtkeedqrvielvqkygpkrwsviakhlkgrigkqcrerwhnhlnpe
>d1mbj__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1mbk__ 1.4.1.3.2 c-Myb, DNA-binding domain {Mouse (Mus musculus)}
vkktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msec1 1.4.1.3.2 (89-143) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
mlikgpwtkeedqrviklvqkygpkrwsviakhlkgrigkqcrerwhnhlnpevk
>d1msec2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1msfc1 1.4.1.3.2 (89-143) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
mlikgpwtkeedqrviklvqkygpkrwsviakhlkgrigkqcrerwhnhlnpevk
>d1msfc2 1.4.1.3.2 (144-193) c-Myb, DNA-binding domain {Mouse (Mus musculus)}
ktswteeedriiyqahkrlgnrwaeiakllpgrtdnaiknhwnstmrrkv
>d1a5j_1 1.4.1.3.3 (1-55) b-Myb DNA binding domain {Chicken (Gallus gallus)}
gipdlvkgpwtkeedqkvielvkkygtkqwtliakhlkgrlgkqcrerwhnhlnp
>d1a5j_2 1.4.1.3.3 (56-110) b-Myb DNA binding domain {Chicken (Gallus gallus)}
evkksswteeedriifeahkvlgnrwaeiakllpgrtdnavknhwnstikrkvdt
>d1ba5__ 1.4.1.4.1 DNA-binding domain of human telomeric protein, htrf1 {Human (Homo sapiens)}
rkrqawlweedknlrsgvrkygegnwskillhykfnnrtsvmlkdrwrtmkkl
>d6paxa_ 1.4.1.5.1 Pax-6 {Human (Homo sapiens)}
shsgvnqlggvfvngrplpdstrqrivelahsgarpcdisrilqvsngcvskilgryyat
gsirpraiggskprvatpevvskiaqykqecpsifaweirdrllsegvctndnipsvssi
nrvlrnlasekqq
>d1pdnc_ 1.4.1.5.2 Paired protein (prd) {Fruit fly (Drosophila melanogaster)}
qgrvnqlggvfingrplpnnirlkivemaadgirpcvisrqlrvshgcvskilnryqetg
sirpgviggskpriatpeienrieeykrsspgmfsweirekliregvcdrstapsvsais
rlv
>d1igna1 1.4.1.6.1 (360-445) DNA-binding domain of rap1 {Baker's yeast (Saccharomyces cerevisiae)}
kasftdeedefildvvrknptrrtthtlydeishyvpnhtgnsirhrfrvylskrleyvy
evdkfgklvrdddgnliktkvlppsi
>d1igna2 1.4.1.6.1 (446-594) DNA-binding domain of rap1 {Baker's yeast (Saccharomyces cerevisiae)}
krkfsadedytlaiavkkqfyrdlfqidpdtgrslitdedtptaiarrnmtmdpnhvpgs
epnfaayrtqsrrgpiareffkhfaeehaahtenawrdrfrkfllaygiddyisyyeaek
aqnrepepmknltnrpkrpgvptpgnyns
>d1ignb1 1.4.1.6.1 (360-445) DNA-binding domain of rap1 {Baker's yeast (Saccharomyces cerevisiae)}
kasftdeedefildvvrknptrrtthtlydeishyvpnhtgnsirhrfrvylskrleyvy
evdkfgklvrdddgnliktkvlppsi
>d1bw6a_ 1.4.1.7.1 DNA-binding domain of centromere binding protein B (CENP-B) {Human (Homo sapiens)}
mgpkrrqltfreksriiqeveenpdlrkgeiarrfnippstlstilknkrailase
>d1bl0a1 1.4.1.8.1 (9-62) MarA {Escherichia coli}
daitihsildwiednlesplslekvsersgyskwhlqrmfkketghslgqyirs
>d1bl0a2 1.4.1.8.1 (63-124) MarA {Escherichia coli}
rkmteiaqklkesnepilylaerygfesqqtltrtfknyfdvpphkyrmtnmqgesrflh
pl
>d1sfe_1 1.4.2.1.1 (93-176) Ada DNA repair protein {Escherichia coli}
gtafqqqvwqalrtipcgetvsyqqlanaigkpkavravasacaanklaivipchrvvrg
dgslsgyrwgvsrkaqllrreaen
>d1qnta1 1.4.2.1.2 (92-176) O6-alkylguanine-DNA alkyltransferase {Human (Homo sapiens) |A|}
esftrqvlwkllkvvkfgevisyqqlaalagnpkaaravggamrgnpvpilipchrvvcs
sgavgnysgglavkewllaheghrl
>d1mgta1 1.4.2.1.3 (89-169) O6-alkylguanine-DNA alkyltransferase {Pyrococcus kodakaraensis}
vtpfekkvyewltknvkrgsvitygdlakalntspravggamkrnpypivvpchrvvahd
gigyyssgieekkflleiegv
>d1c20a_ 1.4.3.1.1 DNA-binding domain from the dead ringer protein {Fruit fly (Drosophila melanogaster)}
gwsfeeqfkqvrqlyeinddpkrkeflddlfsfmqkrgtpinrlpimaksvldlyelynl
viargglvdvinkklwqeiikglhlpssitsaaftlrtqymkylypyecekknlstpael
qaaidgnr
>d1bia_1 1.4.4.1.1 (1-63) Biotin repressor, N-terminal domain {Escherichia coli}
mkdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgysl
pep
>d1bib_1 1.4.4.1.1 (2-63) Biotin repressor, N-terminal domain {Escherichia coli}
kdntvplkliallangefhsgeqlgetlgmsraainkhiqtlrdwgvdvftvpgkgyslp
ep
>d1lea__ 1.4.4.2.1 LexA repressor, N-terminal DNA-binding domain {Escherichia coli}
mkaltarqqevfdlirdhisqtgmpptraeiaqrlgfrspnaaeehlkalarkgvieivs
gasrgirllqee
>d1leb__ 1.4.4.2.1 LexA repressor, N-terminal DNA-binding domain {Escherichia coli}
mkaltarqqevfdlirdhisqtgmpptraeiaqrlgfrspnaaeehlkalarkgvieivs
gasrgirllqee
>d1aoy__ 1.4.4.3.1 Arginine repressor (ArgR), N-terminal DNA-binding domain {Escherichia coli}
mrssakqeelvkafkallkeekfssqgeivaalqeqgfdninqskvsrmltkfgavrtrn
akmemvyclpaelgvptt
>d1b4aa1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ab1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ac1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ad1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ae1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4af1 1.4.4.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1bera1 1.4.4.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d1berb1 1.4.4.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1cgpa1 1.4.4.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1cgpb1 1.4.4.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1runa1 1.4.4.4.1 (138-209) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvygtr
>d1runb1 1.4.4.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1ruoa1 1.4.4.4.1 (138-206) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsrftvgrilkmledqnlis
ahgktivvy
>d1ruob1 1.4.4.4.1 (138-209) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsrftvgrilkmledqnlis
ahgktivvygtr
>d2cgpc1 1.4.4.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d3gapa1 1.4.4.4.1 (138-208) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvygt
>d3gapb1 1.4.4.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1opc__ 1.4.4.5.1 OMPR C-terminal DNA-binding domain {Escherichia coli}
viafgkfklnlgtremfredepmpltsgefavlkalvshpreplsrdklmnlargreysa
mersidvqisrlrrmveedpahpryiqtvwglgyvfvpd
>d1smta_ 1.4.4.6.1 SmtB repressor {Cyanobacteria (Synechococcus), pcc7942}
elqaiapevaqslaeffavladpnrlrllsllarselcvgdlaqaigvsesavshqlrsl
rnlrlvsyrkqgrhvyyqlqdhhivalyqnaldhlqec
>d1smtb_ 1.4.4.6.1 SmtB repressor {Cyanobacteria (Synechococcus), pcc7942}
aiaselqaiapevaqslaeffavladpnrlrllsllarselcvgdlaqaigvsesavshq
lrslrnlrlvsyrkqgrhvyyqlqdhhivalyqnaldhlqe
>d1bm9a_ 1.4.4.7.1 Replication terminator protein (RTP) {Bacillus subtilis}
eekrsstgflvkqraflklymitmteqerlyglkllevlrsefkeigfkpnhtevyrslh
ellddgilkqikvkkegaklqevvlyqfkdyeaaklykkqlkveldrckkliekalsdnf
>d1bjaa_ 1.4.4.8.1 Transcription factor MotA, activation domain {Bacteriophage T4}
skvtyiikasndvlnektatilitiakkdfitaaevrevhpdlgnavvnsnigvlikkgl
veksgdgliitgeaqdiisnaatlyaqenapellk
>d1bjab_ 1.4.4.8.1 Transcription factor MotA, activation domain {Bacteriophage T4}
skvtyiikasndvlnektatilitiakkdfitaaevrevhpdlgnavvnsnigvlikkgl
veksgdgliitgeaqdiisnaatlyaqenapellk
>d1repc1 1.4.4.9.1 (15-143) RepE54 {Escherichia coli mini-F plasmid}
sprivqsndlteaayslsrdqkrmlylfvdqirksdgtlqehdgiceihvakyaeifglt
saeaskdirqalksfagkevvfyrpeedagdekgyesfpwfikpahspsrglysvhinpy
lipffiglq
>d1repc2 1.4.4.9.1 (144-246) RepE54 {Escherichia coli mini-F plasmid}
nrftqfrlsetkeitnpyamrlyeslcqyrkpdgsgivslkidwiieryqlpqsyqrmpd
frrrflqvcvneinsrtpmrlsyiekkkgrqtthivfsfrdit
>d1foka3 1.4.4.10.1 (287-386) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
vpkrvywemlatnltdkeyvrtrralileilikagslkieqiqdnlkklgfdevietien
dikglintgifieikgrfyqlkdhilqfvipnrgvtkqlv
>d2foka1 1.4.4.10.1 (5-143) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
irtfgwvqnpgkfenlkrvvqvfdrnskvhnevknikiptlvkeskiqkelvaimnqhdl
iytykelvgtgtsirseapcdaiiqatiadqgnkkgyidnwssdgflrwahalgfieyin
ksdsfvitdvglaysksad
>d2foka2 1.4.4.10.1 (144-286) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
gsaiekeilieaissyppairiltlledgqhltkfdlgknlgfsgesgftslpegilldt
lanampkdkgeirnnwegssdkyarmiggwldklglvkqgkkefiiptlgkpdnkefish
afkitgeglkvlrrakgstkftr
>d2foka3 1.4.4.10.1 (287-386) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
vpkrvywemlatnltdkeyvrtrralileilikagslkieqiqdnlkklgfdevietien
dikglintgifieikgrfyqlkdhilqfvipnrlgkpdlv
>d2fokb3 1.4.4.10.1 (287-378) Restriction endonuclease FokI, N-terminal (recognition) domain {Flavobacterium okeanokoites}
vpkrvywemlatnltdkeyvrtrralileilikagslkieqiqdnlkklgfdevietien
dikglintgifieikgrfyqlkdhilqfvipn
>d1hsta_ 1.4.4.11.1 Histone H5, globular domain {Chicken (Gallus gallus)}
shptysemiaaairaeksrggssrqsiqkyikshykvghnadlqiklsirrllaagvlkq
tkgvgasgsfrlak
>d1hstb_ 1.4.4.11.1 Histone H5, globular domain {Chicken (Gallus gallus)}
shptysemiaaairaeksrggssrqsiqkyikshykvghnadlqiklsirrllaagvlkq
tkgvgasgsfrlak
>d1ghc__ 1.4.4.11.2 Histone H1, globular domain {Chicken (Gallus gallus)}
magpsvtelitkavsaskerkglslaalkkalaaggydveknnsriklglkslvskgtlv
qtkgtgasgsfrlsk
>d2hfh__ 1.4.4.13.1 Genesis {Rat (Rattus norvegicus)}
mvkppysyialitmailqspqkkltlsgicefisnrfpyyrekfpawqnsirhnlslndc
fvkiprepgnpgkgnywtldpqsedmfdngsfl
>d1bby__ 1.4.4.14.1 DNA-binding domain from rap30 {Human (Homo sapiens)}
raradkqhvldmlfsafekhqyynlkdlvditkqpvvylkeilkeigvqnvkgihkntwe
lkpeyrhyq
>d2bby__ 1.4.4.14.1 DNA-binding domain from rap30 {Human (Homo sapiens)}
raradkqhvldmlfsafekhqyynlkdlvditkqpvvylkeilkeigvqnvkgihkntwe
lkpeyrhyq
>d1cf7a_ 1.4.4.15.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
srhekslgllttkfvsllqeakdgvldlklaadtlavrqkrriyditnvlegigliekks
knsiqwk
>d1cf7b_ 1.4.4.15.1 Cell cycle transcription factor e2f-dp {Human (Homo sapiens)}
gkglrhfsmkvcekvqrkgttsynevadelvseftnsnnhlaadsaydqknirrrvydal
nvlmamniiskekkeikwiglp
>d1qbja_ 1.4.4.16.1 Z-alpha domain of dsRNA-specific adenosine deaminase, ADAR1 {Human (Homo sapiens)}
siyqdqeqrilkfleelgegkattahdlsgklgtpkkeinrvlyslakkgklqkeagtpp
lwkia
>d1qbjb_ 1.4.4.16.1 Z-alpha domain of dsRNA-specific adenosine deaminase, ADAR1 {Human (Homo sapiens)}
yqdqeqrilkfleelgegkattahdlsgklgtpkkeinrvlyslakkgklqkeagtpplw
kia
>d1qbjc_ 1.4.4.16.1 Z-alpha domain of dsRNA-specific adenosine deaminase, ADAR1 {Human (Homo sapiens)}
siyqdqeqrilkfleelgegkattahdlsgklgtpkkeinrvlyslakkgklqkeagtpp
lwkiav
>d1qgpa_ 1.4.4.16.1 Z-alpha domain of dsRNA-specific adenosine deaminase, ADAR1 {Human (Homo sapiens)}
lsshfqelsiyqdqeqrilkfleelgegkattahdlsgklgtpkkeinrvlyslakkgkl
qkeagtpplwkiavsd
>d1flia_ 1.4.4.17.1 Fli-1 {Human (Homo sapiens)}
pgsgqiqlwqfllellsdsanascitwegtngefkmtdpdevarrwgerkskpnmnydkl
sralryyydknimtkvhgkryaykfdfhgiaqalqphp
>d1etd__ 1.4.4.17.2 ETS-1 transcription factor, residues 331-440 {Murine (Mus musculus)}
iqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrknkpkmnyeklsrglr
yyydkniihktagkryvyrfvcdlqsllgytpeelhamldvkpdad
>d2stta_ 1.4.4.17.3 ETS-1 transcription factor, residues 331-440 {Human (Homo sapiens)}
vipaaalagytgsgpiqlwqfllelltdkscqsfiswtgdgwefklsdpdevarrwgkrk
nkpkmnyeklsrglryyydkniihktagkryvyrfv
>d1puee_ 1.4.4.17.4 Transcription factor PU.1, residues 171-259 {Murine (Mus musculus)}
kirlyqflldllrsgdmkdsiwwvdkdkgtfqfsskhkealahrwgiqkgnrkkmtyekm
aralrnygktgevkkvkkkltyqfsgev
>d1puef_ 1.4.4.17.4 Transcription factor PU.1, residues 171-259 {Murine (Mus musculus)}
kirlyqflldllrsgdmkdsiwwvdkdkgtfqfsskhkealahrwgiqkgnrkkmtyekm
aralrnygktgevkkvkkkltyqfsgevl
>d1awca_ 1.4.4.17.5 GA binding protein (GABP) alpha {Mouse (Mus musculus)}
iqlwqfllelltdkdardciswvgdegefklnqpelvaqkwgqrknkptmnyeklsralr
yyydgdmickvqgkrfvykfvcdlktligysaaelnrlvieceqkklarm
>d1bc7c_ 1.4.4.17.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1bc8c_ 1.4.4.17.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1hks__ 1.4.4.18.1 Heat-shock transcription factor {Drosophila melanogaster}
gsgvpaflaklwrlvddadtnrlicwtkdgqsfviqnqaqfakellplnykhnnmasfir
qlnmygfhkitsidngglrfdrdeiefshpffkrnspflldqikrk
>d2hts__ 1.4.4.18.2 Heat-shock transcription factor {Milk yeast (Kluyveromyces lactis)}
arpafvnklwsmvndksnekfihwstsgesivvpnrerfvqevlpkyfkhsnfasfvrql
nmygwhkvqdvksgsndsrwefenerha
>d3hsf__ 1.4.4.18.2 Heat-shock transcription factor {Milk yeast (Kluyveromyces lactis)}
arpafvnklwsmvndksnekfihwstsgesivvpnrerfvqevlpkyfkhsnfasfvrql
nmygwhkvqdvksgsmlsnndsrwefenerha
>d3htsb_ 1.4.4.18.2 Heat-shock transcription factor {Milk yeast (Kluyveromyces lactis)}
marpafvnklwsmvndksnekfihwstsgesivvpnrerfvqevlpkyfkhsnfasfvrq
lnmygwhkvqdvksgsmlsnndsrwefener
>d1if1a_ 1.4.4.19.2 Interferon regulatory factor 1 (IRF-1) {Synthetic}
rmrpwlemqinsnqipgliwinkeemifqipwkhaakhgwdinkdaclfrswaihtgryk
agekepdpktwkanfrcamnslpdieevkdqsrnkgssavrvyrm
>d2irfg_ 1.4.4.19.3 Interferon regulatory factor-2, IRF-2 {Mouse (Mus musculus)}
rmrmrpwleeqinsntipglkwlnkekkifqipwmhaarhgwdvekdaplfrnwaihtgk
hqpgidkpdpktwkanfrcamnslpdieevkdrsikkgnnafrvyrmlp
>d1bi0_1 1.4.4.20.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi1_1 1.4.4.20.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi2a1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1bi2b1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1bi3a1 1.4.4.20.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1bi3b1 1.4.4.20.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d1ddna1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnb1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnc1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1ddnd1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dpra1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d1dprb1 1.4.4.20.1 (3-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
dlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrsl
qm
>d2dtr_1 1.4.4.20.1 (4-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
lvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdrslq
m
>d2tdx_1 1.4.4.20.1 (1-64) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
mkdlvdttemylrtiyeleeegvtplrariaerleqsgptvsqtvarmerdglvvvasdr
slqm
>d1b1ba1 1.4.4.20.2 (1-64) Iron-dependent regulator {Mycobacterium tuberculosis}
mnelvdttemylrtiydleeegvtplrariaerldqsgptvsqtvsrmerdgllrvagdr
hlel
>d1xgma1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgmb1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgna1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgnb1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgo_1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgsa1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1xgsb1 1.4.4.21.1 (195-271) Methionine aminopeptidase, insert domain {Pyrococcus furiosus}
gqvievpptliymyvrdvpvrvaqarfllakikreygtlpfayrwlqndmpegqlklalk
tlekagaiygypvlkei
>d1b59a1 1.4.4.21.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1b6a_1 1.4.4.21.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1bn5_1 1.4.4.21.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1boa_1 1.4.4.21.2 (375-448) Methionine aminopeptidase, insert domain {Human (Homo sapiens)}
hddmecshymknfdvghvpirlprtkhllnvinenfgtlafcrrwldrlgeskylmalkn
lcdlgivdpypplc
>d1qpma_ 1.4.4.22.1 mu transposase, DNA-binding domain {Bacteriophage mu}
ksiwcspqeimaadgmpgsvagvhyranvqgwtkrkkegvkggkaveydvmsmptkereq
viahlglst
>d1tns__ 1.4.4.22.1 mu transposase, DNA-binding domain {Bacteriophage mu}
melwvspkelanlpglpktsagviyvakkqgwqnrtragvkggkaieynanslpveakaa
lllrqgeietslgyfe
>d1tnt__ 1.4.4.22.1 mu transposase, DNA-binding domain {Bacteriophage mu}
melwvspkelanlpglpktsagviyvakkqgwqnrtragvkggkaieynanslpveakaa
lllrqgeietslgyfe
>d1aci__ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1fow__ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1fox__ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1foy__ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1qa6a_ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
ktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaamrmieg
tarsmgi
>d1qa6b_ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
ktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaamrmieg
tarsmgi
>d2fow__ 1.4.5.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1wjaa_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjab_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjba_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjbb_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjca_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjcb_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkg
>d1wjda_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjdb_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeehekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjea_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlk
>d1wjeb_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlk
>d1wjfa_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1wjfb_ 1.4.6.1.1 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 1, HIV-1}
fldgidkaqeecekyhsnwramasdfnlppvvakeivascdkcqlkgeamhgqvd
>d1aub__ 1.4.6.1.2 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 2, HIV-2}
flekiepaqeehekyhsnvkelshkfgipnlvarqivnscaqcqqk
>d1bdxa1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxb1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxc1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxd1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1cuk_1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavarlvalgykpqeasrmvskiarpdassetlirealraal
>d1hjp_1 1.5.1.1.1 (158-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
daeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bvsa1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsb1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsc1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsd1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvse1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsf1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsg1 1.5.1.1.2 (148-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
navrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1bvsh1 1.5.1.1.2 (147-203) DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
gnavrgsvvealvglgfaakqaeeatdqvldgelgkdgavatssalraalsllgktr
>d1dv0a_ 1.5.1.1.2 DNA helicase RuvA subunit, C-terminal domain {Mycobacterium leprae}
qekeaierlkalgfpeslviqayfaceknenlaanfllsqnfdde
>d1aua_1 1.5.2.1.1 (4-96) N-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
qqekeflesypqncppdalpgtpgnldsaqekalaelrklledagfierlddstllrflr
arkfdvqlakemfencekwrkdygtdtilqdfh
>d1b70b1 1.6.1.1.1 (1-38,152-190) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
mrvpfswlkayvpelespevleerlaglgfetdriervXeevvldlevtpnrpdalgllg
lardlhalgyalvepeaa
>d1b70b2 1.6.1.1.1 (400-474) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
ppeaipfrpeyanrllgtsypeaeqiailkrlgcrvegegptyrvtppshrldlrleedl
veevariqgyetipl
>d1b7yb1 1.6.1.1.1 (1-38,152-190) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
mrvpfswlkayvpelespevleerlaglgfetdriervXeevvldlevtpnrpdalgllg
lardlhalgyalvepeaa
>d1b7yb2 1.6.1.1.1 (400-474) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
ppeaipfrpeyanrllgtsypeaeqiailkrlgcrvegegptyrvtppshrldlrleedl
veevariqgyetipl
>d1pysb1 1.6.1.1.1 (1-38,152-190) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
mrvpfswlkayvpelespevleerlaglgfetdriervXeevvldlevtpnrpdalgllg
lardlhalgyalvepeaa
>d1pysb2 1.6.1.1.1 (400-474) Domains B1 and B5 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
ppeaipfrpeyanrllgtsypeaeqiailkrlgcrvegegptyrvtppshrldlrleedl
veevariqgyetipl
>d1d4ua1 1.6.1.2.1 (37-111) DNA repair factor XPA DNA- and RPA-binding domain, C-terminal subdomain {Human (Homo sapiens)}
dkhklitkteakqeyllkdcdlekrepplkfivkknphhsqwgdmklylklqivkrslev
wgsqealeeakevrq
>d1xpa_1 1.6.1.2.1 (134-210) DNA repair factor XPA DNA- and RPA-binding domain, C-terminal subdomain {Human (Homo sapiens)}
dkhklitkteakqeyllkdcdlekrepplkfivkknphhsqwgdmklylklqivkrslev
wgsqealeeakevrqen
>d2spca_ 1.7.1.1.1 Spectrin {Fruit fly (Drosophila melanogaster)}
qnldlqlymrdcelaeswmsareaflnadddanaggnvealikkhedfdkaingheqkia
alqtvadqliaqnhyasnlvdekrkqvlerwrhlkegliekrsrlgd
>d1cuna1 1.7.1.1.2 (7-115) Spectrin {Chicken (Gallus gallus)}
mvhqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqsvl
dtgkklsddntigkeeiqqrlaqfvdhwkelkqlaaargqrleesleyq
>d1cuna2 1.7.1.1.2 (116-219) Spectrin {Chicken (Gallus gallus)}
qfvanveeeeawinekmtlvasedygdtlaaiqgllkkheafetdftvhkdrvndvcang
edlikknnhhvenitakmkglkgkvsdlekaaaqrkakldensa
>d1quua1 1.7.1.1.3 (1-124) alpha-actinin {Human (Homo sapiens)}
gssneirrlerlehlaekfrqkasthetwaygkeqillqkdyesasltevrallrkheaf
esdlaahqdrveqiaaiaqelneldyhdavnvndrcqkicdqwdrlgtltqkrrealerm
ekll
>d1quua2 1.7.1.1.3 (125-248) alpha-actinin {Human (Homo sapiens)}
etidqlhlefakraapfnnwmegamedlqdmfivhsieeiqslitaheqfkatlpeadge
rqsimaiqnevekviqsynirisssnpystvtmdelrtkwdkvkqlvpirdqslqeelar
qhan
>d1br0a_ 1.7.2.1.1 Syntaxin 1-A N-terminal domain {Rat (Rattus norvegicus)}
drfmdeffeqveeirgfidkiaenveevkrkhsailaspnpdektkeeleelmsdikkta
nkvrsklksieqsieqeeglnrssadlrirktqhstlsrkfvevmseynatqsdyrersk
>d1e2aa_ 1.7.3.1.1 Enzyme IIa from lactose specific PTS, IIa-lac {Lactococcus lactis}
mnreemtllgfeivayagdarskllealkaaengdfakadslvveagsciaeahssqtgm
lareasgeelpysvtmmhgqdhlmttillkdvihhlielykr
>d1chua1 1.7.4.1.1 (423-533) L-aspartate oxidase {Escherichia coli}
desrvenpdervviqhnwhelrlfmwdyvgivrttkrleralrritmlqqeideyyahfr
vsnnllelrnlvqvaelivrcammrkesrglhftldypellthsgpsi
>d1fuma1 1.7.4.1.2 (443-575) Fumarate reductase flavoprotein subunit {Escherichia coli}
dggenwakirdemglameegcgiyrtpelmqktidklaelqerfkrvritdtssvfntdl
lytielghglnvaecmahsamarkesrgahqrldegcterddvnflkhtlafrdadgttr
leysdvkittlpp
>d1qlaa1 1.7.4.1.3 (458-655) Fumarate reductase flavoprotein subunit {Wolinella succinogenes}
kgtedvfkiknrmkdvmddnvgifrdgphleksvkeleelykksknvgiknkrlhanpel
eeayrvpmmlkvalcvakgaldrtesrgahnredypkrddinwlnrtlaswpnpeqtlpt
leyealdvnemeiapryrgygakgnyienplsvkrqeeidkiqseleaagkdrhaiqeal
mpyelpakykarnerlgd
>d1qsda_ 1.7.5.1.1 beta-Tubulin binding post-chaperonin cofactor Rbl2p {Baker's yeast (Saccharomyces cerevisiae)}
tqldikvkalkrltkeegyyqqelkdqeahvaklkedksvdpydlkkqeevlddtkrllp
tlyekirefkedleqflktyqgtedvsdarsaitsaqellds
>d1bdc__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
tadnkfnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaeakklndaqapka
>d1bdd__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
tadnkfnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaeakklndaqapka
>d1edi__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edj__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edk__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1edl__ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
aqhdeaqqnafyqvlnmpnlnadqrngfiqslkddpsqsanvlgeaqklndsqapk
>d1fc2c_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
fnkeqqnafyeilhlpnlneeqrngfiqslkddpsqsanllaea
>d1spzz_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
vdnkfnkeqqnafyeilhlpnlneeqrnafiqslkddpsqsanllaeakklndaqapk
>d2spza_ 1.8.1.1.1 Immunoglobulin-binding protein A modules {Staphylococcus aureus}
vdnkfnkeqqnafyeilhlpnlneeqrnafiqslkddpsqsanllaeakklndaqapk
>d1gab__ 1.8.1.2.1 An albumin-binding domain {Peptostreptococcus magnus}
tidqwllknakedaiaelkkagitsdfyfnainkaktveevnalkneilkaha
>d1prb__ 1.8.1.2.1 An albumin-binding domain {Peptostreptococcus magnus}
tidqwllknakedaiaelkkagitsdfyfnainkaktveevnalkneilkaha
>d1ebdc_ 1.9.1.1.1 E3-binding domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
iampsvrkyarekgvdirlvqgtgkngrvlkedidaflagg
>d1bal__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
yasleeqnndalspairrllaehnldasaikgtgvggrltredvekhlaka
>d1bbl__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
lspairrllaehnldasaikgtgvggrltredvekhl
>d2pdd__ 1.9.1.1.3 E3/E1 binding domain of dihydrolipoyl acetyltransferase {Bacillus stearothermophilus}
viampsvrkyarekgvdirlvqgtgkngrvlkedidaflagga
>d2pde__ 1.9.1.1.3 E3/E1 binding domain of dihydrolipoyl acetyltransferase {Bacillus stearothermophilus}
viampsvrkyarekgvdirlvqgtgkngrvlkedidaflagga
>d1erc__ 1.10.1.1.1 ER-1 {Euplotes raikovi}
daceqaaiqcvesaceslctegedrtgcymyiysncppyv
>d2erl__ 1.10.1.1.1 ER-1 {Euplotes raikovi}
daceqaaiqcvesaceslctegedrtgcymyiysncppyv
>d1erd__ 1.10.1.1.2 ER-2 {Euplotes raikovi}
dpmtceqamascehtmcgycqgplymtcigittdpecglp
>d1erp__ 1.10.1.1.3 ER-10 {Euplotes raikovi}
dlceqsalqcneqgchnfcspedkpgclgmvwnpelcp
>d1ery__ 1.10.1.1.4 ER-11 {Euplotes raikovi}
decanaaaqcsitlcnlycgplieiceltvmqnceppfs
>d1aca__ 1.11.1.1.1 Acyl-CoA binding protein {Bovine (Bos taurus)}
sqaefdkaaeevkhlktkpadeemlfiyshykqatvgdinterpgmldfkgkakwdawne
lkgtskedamkayidkveelkkkygi
>d2abd__ 1.11.1.1.1 Acyl-CoA binding protein {Bovine (Bos taurus)}
sqaefdkaaeevkhlktkpadeemlfiyshykqatvgdinterpgmldfkgkakwdawne
lkgtskedamkayidkveelkkkygi
>d1kdxa_ 1.12.1.1.1 Kix domain of CBP (creb binding protein) {Mouse (Mus musculus)}
gvrkgwhehvtqdlrshlvhklvqaifptpdpaalkdrrmenlvayakkvegdmyesans
rdeyyhllaekiykiqkelee
>d1lre__ 1.13.1.1.1 alpha-2-Macroglobulin receptor associated protein (RAP) domain 1 {Human (Homo sapiens)}
geefrmeklnqlwekaqrlhlppvrlaelhadlkiqerdelawkklkldgldedgekear
lirnlnvilakygldgkkdar
>d1nre__ 1.13.1.1.1 alpha-2-Macroglobulin receptor associated protein (RAP) domain 1 {Human (Homo sapiens)}
geefrmeklnqlwekaqrlhlppvrlaelhadlkiqerdelawkklkldgldedgekear
lirnlnvilakygldgkkdar
>d1qqva_ 1.14.1.1.1 Thermostable subdomain from chicken villin headpiece {Chicken (Gallus gallus)}
ptkletfpldvlvntaaedlprgvdpsrkenhlsdedfkavfgmtrsafanlplwkqqnl
kkekglf
>d1vii__ 1.14.1.1.1 Thermostable subdomain from chicken villin headpiece {Chicken (Gallus gallus)}
mlsdedfkavfgmtrsafanlplwkqqnlkkekglf
>d1tbaa_ 1.15.1.1.1 TAF(II)230 TBP-binding fragment {Fruit fly (Drosophila melanogaster)}
egsigngldltgilfgnidsegrllqdddgegrggtgfdaelrenigslsklgldsmlle
vidlkea
>d1ail__ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilk
>d1ns1a_ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilkees
>d1ns1b_ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilkees
>d1a32__ 1.16.1.2.1 Ribosomal protein S15 {Bacillus stearothermophilus}
ltqerkreiieqfkvhendtgspevqiailteqinnlnehlrvhkkdhhsrrgllkmvgk
rrrllaylrnkdvaryreiveklgl
>d1ab3__ 1.16.1.2.2 Ribosomal protein S15 {Thermus thermophilus}
pitkeekqkviqefarfpgdtgstevqvalltlrinrlsehlkvhkkdhhshrgllmmvg
qrrrllrylqredperyralieklgirg
>d1r1ba_ 1.16.1.3.1 Multifunctional Glu-Pro-tRNA synthase (EPRS) second repeated element {Chinese hamster (Cricetulus griseus)}
mvydkiaaqgevvrklkaekapkakvteavecllslkaeykektgkeyvpglehhh
>d1hp8__ 1.17.1.1.1 p8-MTCP1 {Human (Homo sapiens)}
mpqkdpcqkqaceiqkclqansymeskcqaviqelrkccaqypkgrsvvcsgfekeeeen
ltrksask
>d2hp8__ 1.17.1.1.1 p8-MTCP1 {Human (Homo sapiens)}
mpqkdpcqkqaceiqkclqansymeskcqaviqelrkccaqypkgrsvvcsgfekeeeen
ltrksask
>d2end__ 1.18.1.1.1 T4 endonuclease V {bacteriophage T4, (Escherichia coli)}
trinltlvseladqhlmaeyrelprvfgavrkhvangkrvrdfkisptfilgaghvtffy
dkleflrkrqieliaeclkrgfnikdttvqdisdipqefrgdyipheasiaisqarldek
iaqrptwykyygkaiya
>d2lisa_ 1.19.1.1.1 Lysin {Red abalone (Haliotis rufescens)}
hyvepkflnkafevalkvqiiagfdrglvkwlrvhgrtlstvqkkalyfvnrrymqthwa
nymlwinkkidalgrtpvvgdytrlgaeigrridmayfydflkdknmipkylpymeeinr
mrpadvpvkym
>d1bmfg_ 1.20.1.1.1 ATP syntase (F1-ATPase), gamma subunit {Bovine (Bos taurus)}
atlkditrrlksikniqkitksmkmvaaakyaraerelkparvygvgslalyekadiktp
edkkkhliigvssdrglcgaihssvakqmkseaanlaaagkevkiigvgdkirsilhrth
sdqflvtfkevgrrpptfgdasvialellnsgyefdegsiifnrfrsvisykteekpifs
ldtissaesmsiyddidadvlrnyqeyslaniiyyslkesttseqsarmtamdnasknas
emidkltltfnrtrqavitkelieiisgaaal
>d1lbu_1 1.21.1.1.1 (1-83) Zn2+ DD-carboxypeptidase, N-terminal domain {Streptomyces albus G}
dgcytwsgtlsegssgeavrqlqirvagypgtgaqlaidgqfgpatkaavqrfqsaygla
adgiagpatfnkiyqlqdddctp
>d1aab__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
gkgdpkkprgkmssyaffvqtsreehkkkhpdasvnfsefskkcserwktmsakekgkfe
dmakadkaryeremktyippkge
>d1ckta_ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
kprgkmssyaffvqtcreehkkkhpdasvnfsefskkcserwktmsakekgkfedmakad
karyeremkty
>d1hme__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
fkdpnapkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekka
aklkekyekdiaayrak
>d1hmf__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
fkdpnapkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekka
aklkekyekdiaayrak
>d1hsm__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d1hsn__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d1nhm__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d1nhn__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
napkrppsafflfcseyrpkikgehpglsigdvakklgemwnntaaddkqpyekkaaklk
ekyekdiaayrakgkpdaa
>d2ezda_ 1.22.1.1.2 HMG1, domains A and B {Human (Homo sapiens), HMG-I(Y)}
vptpkrprgrpkgsknkgaak
>d2ezea_ 1.22.1.1.2 HMG1, domains A and B {Human (Homo sapiens), HMG-I(Y)}
vptpkrprgrpkgsknkgaaktrkt
>d1hma__ 1.22.1.1.3 HMG-D {Drosophila melanogaster}
sdkpkrplsaymlwlnsaresikrenpgikvtevakrggelwramkdkseweakaakakd
dydravkefeang
>d1qrva_ 1.22.1.1.3 HMG-D {Drosophila melanogaster}
sdkpkrplsaymlwlnsaresikrenpgikvtevakrggelwramkdkseweakaakakd
dydravkefeang
>d1qrvb_ 1.22.1.1.3 HMG-D {Drosophila melanogaster}
dkpkrplsaymlwlnsaresikrenpgikvtevakrggelwramkdkseweakaakakdd
ydravkefean
>d1cg7a_ 1.22.1.1.4 NHP6a {Baker's yeast (Saccharomyces cerevisiae)}
mvtprepkkrttrkkkdpnapkralsaymffanenrdivrsenpditfgqvgkklgekwk
altpeekqpyeakaqadkkryesekelynatla
>d1hrya_ 1.22.1.1.5 SRY {Human (Homo sapiens)}
drvkrpmnafivwsrdqrrkmalenprmrnseiskqlgyqwkmlteaekwpffqeaqklq
amhrekypnykyr
>d1hrza_ 1.22.1.1.5 SRY {Human (Homo sapiens)}
drvkrpmnafivwsrdqrrkmalenprmrnseiskqlgyqwkmlteaekwpffqeaqklq
amhrekypnykyr
>d2lefa_ 1.22.1.1.7 Lymphoid enhancer-binding factor, LEF1 {Mouse (Mus musculus)}
mhikkplnafmlymkemranvvaestlkesaainqilgrrwhalsreeqakyyelarker
qlhmqlypgwsardnygkkkkrkrek
>d1hioa_ 1.23.1.1.1 Histone H2A {Chicken (Gallus gallus), erythrocytes}
ksrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeilelagnaardnk
ktriiprhlqlairndeelnkllgkvtiaqggvlp
>d2hioa_ 1.23.1.1.1 Histone H2A {Chicken (Gallus gallus), erythrocytes}
ksrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeilelagnaardnk
ktriiprhlqlairndeelnkllgkvtiaqggvlpniqavl
>d1aoic_ 1.23.1.1.2 Histone H2A {African clawed frog (Xenopus laevis)}
gkqggktrakaktrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeil
elagnaardnkktriiprhlqlavrndeelnkllgrvtiaqggvlpniqsvllpk
>d1hiob_ 1.23.1.1.3 Histone H2B {Chicken (Gallus gallus), erythrocytes}
sysiyvykvlkqvhpdtgisskamgsmnsfvndiferiaglasrlahynkrstitsreiq
tavrlllpgelakhavsegtkavtkhtssk
>d2hiob_ 1.23.1.1.3 Histone H2B {Chicken (Gallus gallus), erythrocytes}
sysiyvykvlkqvhpdtgisskamgimnsfvndiferiageasrlahynkrstitsreiq
tavrlllpgelakhavsegtkavtkytssk
>d1aoid_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1aoih_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1hioc_ 1.23.1.1.5 Histone H3 {Chicken (Gallus gallus), erythrocytes}
pgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssavmalqeaseaylvg
lfedtnlcaihakrvtimpkdielarrirgera
>d2hioc_ 1.23.1.1.5 Histone H3 {Chicken (Gallus gallus), erythrocytes}
pgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssavmalqeaseaylvg
lfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoia_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
phryrpgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssavmalqease
aylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoie_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
latkaarksapatggvkkphryrpgtvalreirryqkstellirklpfqrlvreiaqdfk
tdlrfqssavmalqeaseaylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1hiod_ 1.23.1.1.7 Histone H4 {Chicken (Gallus gallus), erythrocytes}
qgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtytehakrktvtamdv
vyalkrqgrtlygfgg
>d2hiod_ 1.23.1.1.7 Histone H4 {Chicken (Gallus gallus), erythrocytes}
niqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtytehakrktvtam
dvvyalkrqertlygfgg
>d1aoib_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
kvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtytehakrk
tvtamdvvyalkrqgrtlygfgg
>d1aoif_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
krhrkvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtyteh
akrktvtamdvvyalkrqgrtlygfgg
>d1b67a_ 1.23.1.2.1 Histone A {Methanothermus fervidus}
gelpiapigriiknagaervsddarialakvleemgeeiaseavklakhagrktikaedi
elarkmfk
>d1b67b_ 1.23.1.2.1 Histone A {Methanothermus fervidus}
elpiapigriiknagaervsddarialakvleemgeeiaseavklakhagrktikaedie
larkm
>d1hta__ 1.23.1.2.1 Histone A {Methanothermus fervidus}
mgelpiapigriiknagaervsddarialakvleemgeeiaseavklakhagrktikaed
ielarkmf
>d1a7w__ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfk
>d1b6wa_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
elpiapigriikdagaervsddaritlakileexgrdiaseaiklarhagrktikaedie
lavrrfk
>d1bfma_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfmb_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1tafa_ 1.23.1.3.1 TAF(II)42 {Fruit fly (Drosophila melanogaster)}
pkdaqvimsilkelnvqeyeprvvnqlleftfryvtsilddakvyanharkktidlddvr
latevtld
>d1tafb_ 1.23.1.3.2 TAF(II)62 {Fruit fly (Drosophila melanogaster)}
mlygssisaesmkviaesigvgslsddaakelaedvsiklkrivqdaakfmnhakrqkls
vrdidmslkv
>d1bh8a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh9a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh8b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>d1bh9b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>d1diog_ 1.24.1.1.1 Diol dehydratase, gamma subunit {Klebsiella oxytoca}
sarvsdyplankhpewvktatnktlddftlenvlsnkvtaqdmritpetlrlqasiakda
grdrlamnferaaeltavpddrileiynalrpyrstkeellaiaddlesryqakicaafv
reaatlyverkklkgdd
>d1mtyg_ 1.24.2.1.1 Methane monooxygenase hydrolase, gamma subunit {Methylococcus capsulatus}
lgihsndtrdawvnkiahvntlekaaemlkqfrmdhttpfrnsyeldndylwieakleek
vavlkarafnevdfrhktafgedaksvldgtvakmnaakdkweaekihigfrqaykppim
pvnyfldgerqlgtrlmelrnlnyydtpleelrkqrgvrvvh
>d1mhyg_ 1.24.2.1.2 Methane monooxygenase hydrolase, gamma subunit {Methylosinus trichosporium}
akrepihdnsirteweakiakltsvdqatkfiqdfrlaytspfrksydidvdyqyierki
eeklsvlkteklpvadlitkattgedaaaveatwiakikaakskyeaeaihiefrqlykp
pvlpvnvflrtdaalgtvlmeirntdyygtpleglrkergvkvlhlq
>d1om2a_ 1.24.3.1.1 Mitochondrial import receptor subunit Tom20 {Rat (Rattus norvegicus)}
raglsklpdlkdaeavqkffleeiqlgeellaqgdyekgvdhltnaiavcgqpqqllqvl
qqtlpppvfqmlltklptisqrivsaqslgeddve
>d1bz4a_ 1.25.1.1.1 Apolipoprotein E3 {Human (Homo sapiens)}
sgqrwelalgrfwdylrwvqtlseqvqeellssqvtqelralmdetmkelkaykseleeq
ltpvaeetrarlskelqaaqarlgadmedvcgrlvqyrgevqamlgqsteelrvrlashl
rklrkrllrdaddlqkrlavyqag
>d2asr__ 1.25.2.1.1 Aspartate receptor, ligand-binding domain {Escherichia coli}
ksfvvsnqlreqqgeltstwdlmlqtrinlsrsavrmmmdssnqqsnakvelldsarktl
aqaathykkfksmaplpemvatsrnidekyknyytaltelidyldygntgayfaqptqgm
qnamgerfaqyalsseklyrdi
>d2liga_ 1.25.2.1.2 Aspartate receptor, ligand-binding domain {Salmonella typhimurium}
mggllfsslqhcqqgfvisnelrqqqseltstwdlmlqtrinlsrsaarmmmdasnqqss
aktdllqnakttlaqaaahyanfknmtplpamaeasanvdekyqryqaalaeliqfldng
nmdayfaqptqgmqnalgealgnyarvsenlyrqtfd
>d256ba_ 1.25.3.1.1 Cytochrome b562 {Escherichia coli}
adlednmetlndnlkviekadnaaqvkdaltkmraaaldaqkatppkledkspdspemkd
frhgfdilvgqiddalklanegkvkeaqaaaeqlkttrnayhqkyr
>d2ccya_ 1.25.3.2.1 Cytochrome c' {Rhodospirillum molischianum}
qskpedllklrqglmqtlksqwvpiagfaagkadlpadaaqraenmamvaklapigwakg
tealpngetkpeafgsksaeflegwkalatestklaaaakagpdalkaqaaatgkvckac
heefkqd
>d1bbha_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1cgo__ 1.25.3.2.4 Cytochrome c' {Alcaligenes}
xfakpedavkyrqsaltlmashfgrmtpvvkgqapydaaqikanvevlktltalpwaafg
pgteggdarpeiwsdaasfkqkqqafqdnivklsaaadagdldklraafgdvgasckach
dayrk
>d1jafa_ 1.25.3.2.5 Cytochrome c' {Rhodocyclus gelatinosus}
qfqkpgdaieyrqsaftlianhfgrvaamaqgkapfdakvaaenialvstlsklpltafg
pgtdkghgteakpavwsdaagfkaaadkfaaavdkldaagktgdfaqikaavgetggack
gchdkfke
>d1cpq__ 1.25.3.2.6 Cytochrome c' {Rhodobacter capsulatus}
adtkevleareayfkslggsmkamtgvakafdaeaakveaaklekilatdvaplfpagts
stdlpgqteakaaiwanmddfgakgkamheaggaviaaanagdgaafgaalqklggtcka
chddyreed
>d1a7va_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d2hmza_ 1.25.4.1.1 Hemerythrin {Sipunculid worm (Themiste dyscrita)}
gfpipdpycwdisfrtfytivddehktlfngilllsqadnadhlnelrrctgkhflneqq
lmqasqyagyaehkkahddfihkldtwdgdvtyaknwlvnhiktidfkyrgki
>d1hrb__ 1.25.4.1.2 Hemerythrin {Phascolopsis gouldi}
gfpipdpyvwdpsfrtfysiiddehktlfngifhlaiddnadnlgelrrctgkhflnqev
lmeasqyqfydehkkehdgfinaldnwkgdvkwakawlvnhiktidfkykgki
>d2mhr__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewlvnhikgtdfkykgkl
>d2tmvp_ 1.25.5.1.1 Tobacco mosaic virus coat protein {Tobacco mosaic virus, Vulgare strain}
sysittpsqfvflssawadpielinlctnalgnqfqtqqartvvqrqfsevwkpspqvtv
rfpdsdfkvyrynavldplvtallgafdtrnriievenqanpttaetldatrrvddatva
irsainnlivelirgtgsynrssfesssglvwts
>d1cgme_ 1.25.5.1.2 Cucumber green mottle mosaic virus {Cucumber green mottle mosaic virus, watermelon strain}
xaynpitpskliafsasyvpvrtllnflvasqgtafqtqagrdsfreslsalpssvvdin
srfpdagfyaflngpvlrpifvsllsstdtrnrvievvdpsnpttaeslnavkrtddast
aaraeidnliesiskgfdvydrasfeaafsvvwseattska
>d1rmva_ 1.25.5.1.3 Ribgrass mosaic virus {Ribgrass mosaic virus}
synitnsnqyqyfaavwaeptpmlnqcvsalsqsyqtqagrdtvrqqfanllstivapnq
rfpdtgfrvyvnsavikplyealmksfdtrnriieteeesrpsasevanatqrvddatva
irsqiqlllnelsnghgymnraefeailpwttapat
>d1buca1 1.25.6.1.1 (233-383) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
gkgfkiammtldggrigvaaqalgiaeaaladaveyskqrvqfgkplckfqsisfkladm
kmqieaarnlvykaackkqegkpftvdaaiakrvasdvamrvtteavqifggygyseeyp
varhmrdakitqiyegtnevqlmvtggallr
>d3mdda1 1.25.6.1.2 (242-395) Medium chain acyl-CoA dehydrogenase {Pig (Sus scrofa)}
gagfkiamgtfdktrppvaagavglaqraldeatkyalerktfgkllaehqgisflladm
amkvelarlsyqraaweidsgrrntyyasiakayaadianqlatdavqvfggngfnteyp
veklmrdakiyqiyegtaqiqriiiarehigryk
>d1ivha1 1.25.6.1.4 (242-392) Isovaleryl-CoA dehydrogenase {Human (Homo sapiens)}
kgvyvlmsgldlerlvlaggplglmqavldhtipylhvreafgqkighfqlmqgkmadmy
trlmacrqyvynvakacdeghctakdcagvilysaecatqvaldgiqcfggngyindfpm
grflrdaklyeigagtsevrrlvigrafnad
>d1nsgb_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
vailwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdl
meaqewcrkymksgnvkdltqawdlyyhvfrris
>e1avo.1a 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.1b 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.2c 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.3e 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.4g 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.5i 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.6k 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.7m 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>d2a0b__ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
sksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghk
ikgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1c02a_ 1.25.9.2.1 Phosphorelay protein ypd1 {Yeast (Saccharomyces cerevisiae)}
stipseiinwtilneiismddddsdfskgliiqfidqaqttfaqmqrqldgeknlteldn
lghflkgssaalglqriawvceriqnlgrkmqhffpnktelvntlsdksiinginidedd
eeikiqvddkdensiyliliakalnqsrlefklarielskyyntnl
>d1ryt_1 1.26.1.1.1 (2-147) Rubrerythrin, N-terminal domain {Desulfovibrio vulgaris}
kslkgsrtekniltafagesqarnrynyfggqakkdgfvqisdifaetadqerehakrlf
kfleggdleivaafpagiiadthanliasaagehheytemypsfariareegyeeiarvf
asiavaeefhekrfldfarnikegrv
>d1bcfa_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d2fha__ 1.26.1.1.3 (Apo)ferritin {Human (Homo sapiens), H chain}
tsqvrqnyhqdseaainrqinlelyasyvylsmsyyfdrddvalknfakyflhqsheere
haeklmklqnqrggriflqdiqkpdcddwesglnamecalhleknvnqsllelhklatdk
ndphlcdfiethylneqvkaikelgdhvtnlrkmgapesglaeylfdkhtlg
>d1dpsa_ 1.26.1.1.6 Dodecameric ferritin homolog DPS {Escherichia coli}
skatnllytrndvsdsekkatvellnrqviqfidlslitkqahwnmrganfiavhemldg
frtalidhldtmaeravqlggvalgttqvinsktplksypldihnvqdhlkeladryaiv
andvrkaigeakdddtadiltaasrdldkflwfiecnie
>d1qgha_ 1.26.1.1.7 Dodecameric ferritin homolog DPS {Listeria innocua}
vdtkeflnhqvanlnvftvkihqihwymrghnfftlhekmddlysefgeqmdevaerlla
iggspfstlkeflenasveeapytkpktmdqlmedlvgtlellrdeykqgieltdkegdd
vtndmliafkasidkhiwmfkaflgkaple
>d1mtyb_ 1.26.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {Methylococcus capsulatus}
errrgltdpemaavilkalpeapldgnnkmgyfvtprwkrlteyealtvyaqpnadwiag
gldwgdwtqkfhggrpswgnettelrtvdwfkhrdplrrwhapyvkdkaeewrytdrflq
gysadgqiramnptwrdefinrywgaflfneyglfnahsqgarealsdvtrvslafwgfd
kidiaqmiqlergflakivpgfdestavpkaewtngevyksarlaveglwqevfdwnesa
fsvhavydalfgqfvrreffqrlaprfgdnltpffinqaqtyfqiakqgvqdlyynclgd
dpefsdynrtvmrnwtgkwleptiaalrdfmglfaklpagttdkeeitaslyrvvddwie
dyasridfkadrdqivkavlaglk
>d1mtyd_ 1.26.1.2.1 Methane monooxygenase hydrolase, beta and alpha subunits {Methylococcus capsulatus}
aanraptsvnaqevhrwlqsfnwdfknnrtkyatkykmanetkeqfkliakeyarmeavk
derqfgslqvaltrlnagvrvhpkwnetmkvvsnflevgeynaiaatgmlwdsaqaaeqk
ngylaqvldeirhthqcayvnyyfakngqdpaghndarrtrtigplwkgmkrvfsdgfis
gdavecslnlqlvgeacftnplivavtewaaangdeitptvflsietdelrhmangyqtv
vsiandpasakylntdlnnafwtqqkyftpvlgmlfeygskfkvepwvktwdrwvyedwg
giwigrlgkygvesprslkdakqdaywahhdlyllayalwptgffrlalpdqeemewfea
nypgwydhygkiyeewrargcedpssgfiplmwfiennhpiyidrvsqvpfcpslakgas
tlrvheyngemhtfsdqwgermwlaeperyecqnifeqyegrelseviaelhglrsdgkt
liaqphvrgdklwtlddikrlncvfknpvkaf
>d1xika_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1r2fa_ 1.26.1.2.4 Ribonucleotide reductase R2 {Salmonella typhimurium}
isainwnkiqddkdlevwnrltsnfwlpekvplsndipawqtlsaaeqqltirvftgltl
ldtiqniagapslmadaitpheeavlsnisfmeavharsyssifstlcqtkevdaayaws
eenpplqrkaqiilahyvsdeplkkkiasvflesflfysgfwlpmyfssrgkltntadli
rliirdeavhgyyigykyqialqklsaiereelklfaldllmelydneirytealyaetg
wvndvkaflcynankalmnlgyealfppemadvnpailaalsp
>d1xsm__ 1.26.1.2.5 Ribonucleotide reductase R2 {Mouse (Mus musculus)}
npsvedepllrenprrfvvfpieyhdiwqmykkaeasfwtaeevdlskdiqhwealkpde
rhfishvlaffaasdgivnenlverfsqevqvtearcfygfqiamenihsemysllidty
ikdpkereylfnaietmpcvkkkadwalrwigdkeatygervvafaavegiffsgsfasi
fwlkkrglmpgltfsnelisrdeglhcdfaclmfkhlvhkpaeqrvreiitnavrieqef
ltealpvkligmnctlmkqyiefvadrlmlelgfnkifrvenpfdfme
>d1afra_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1bgc__ 1.27.1.1.2 Granulocyte-colony stimulating factor (G-CSF) {Bovine (Bos taurus)}
slpqsfllkcleqvrkiqadgaelqerlcaahklchpeelmllrhslgipqaplsscssq
slqlrgclnqlhgglflyqgllqalagispelaptldtlqldvtdfatniwlqmedlgaa
pavqptqgamptftsafqrraggvlvasqlhrflelayrglryla
>d1alu__ 1.27.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1lki__ 1.27.1.1.5 Leukemia inhibitory factor (LIF) {Mouse (Mus musculus)}
natcairhpchgnlmnqiknqlaqlngsanalfisyytaqgepfpnnveklcapnmtdfp
sfhgngtektklvelyrmvaylsasltnitrdqkvlnptavslqvklnatidvmrgllsn
vlcrlcnkyrvghvdvppvpdhsdkeafqrkklgcqllgtykqvisvvvqaf
>d1huw__ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
fptiplsrladnawlradrlnqlafdtyqefeeayipkeqihsfwwnpqtslcpsesipt
psnkeetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeg
iqtlmgrleallknygllycfnkdmskvstylrtvqcrsvegscgf
>d1cnt1_ 1.27.1.1.7 Ciliary neurotrophic factor (CNTF) {Human (Homo sapiens)}
phrrdlcsrsiwlarkirsdltaltesyvkhqglnkninldsadgmpvastdqwseltea
erlqenlqayrtfhvllarlledqqvhftptegdfhqaihtlllqvaafayqieelmill
eykiprneadgmpinvgdgglfekklwglkvlqelsqwtvrsihdlrfisshqtgip
>d1ax8__ 1.27.1.1.8 Leptin (obesity protein) {Human (Homo sapiens)}
iqkvqddtktliktivtrindishtqsvsskqkvtgldfipglhpiltlskmdqtlavyq
qiltsmpsrnviqisndlenlrdllhvlafskschlpeasgletldslggvleasgyste
vvalsrlqgslqdmlwqldlspgc
>d1eera_ 1.27.1.2.1 Erythropoietin {Human (Homo sapiens)}
apprlicdsrvlerylleakeaekittgcaehcslnekitvpdtkvnfyawkrmevgqqa
vevwqglallseavlrgqallvkssqpweplqlhvdkavsglrslttllralgaqkeais
nsdaasaaplrtitadtfrklfrvysnflrgklklytgeacrtgdr
>d2gmfa_ 1.27.1.2.2 Granulocyte-macrophage colony-stimulating factor (GM-CSF) {Human (Homo sapiens)}
rspspstqpwehvnaiqearrllnlsrdtaaemnetvevisemfdlqeptclqtrlelyk
qglrgsltklkgpltmmashykqhcpptpetscatqiitfesfkenlkdfllvipfdcwe
p
>d1rcb__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
hkcditlqeiiktlnslteqktlcteltvtdifaaskntteketfcraatvlrqfyshhe
kdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeanqstlenflerlktim
rekyskcss
>d1hula_ 1.27.1.2.4 Interleukin-5 {Human (Homo sapiens)}
iptsalvketlallsthrtllianetlripvpvhknhqlcteeifqgigtlesqtvqggt
verlfknlslikkyidgqkkkcgeerrrvnqfldylqeflgvmntewi
>d1hmca_ 1.27.1.2.5 Macrophage colony-stimulating factor (M-CSF) {Human (Homo sapiens)}
seycshmigsghlqslqrlidsqmetscqitfefvdqeqlkdpvcylkkafllvqdimed
tmrfrdntpnaiaivqlqelslrlkscftkdyeehdkacvrtfyetplqllekvknvfne
tknlldkdwnifskncnnsfaecssqgh
>d3inkc_ 1.27.1.2.6 Interleukin-2 (IL-2) {Human (Homo sapiens)}
stkktqlqlehllldlqmilnginnyknpkltrmltfkfympkkatelkhlqcleeelkp
leevlnlaqsknfhlrprdlisninvivlelkgsettfmceyadetativeflnrwitfa
qsiistlt
>d1jli__ 1.27.1.2.7 Interleukin-3 (IL-3) {Human (Homo sapiens)}
ancsimideiihhlkrppnplldpnnlnsedmdilmernlrtpnllafvravkhlenasa
iesilknllpclplataaptrhpihikdgdwnefrrkltfylktlenaqaqq
>d2ilk__ 1.27.1.3.1 Interleukin-10 (cytokine synthesis inhibitory factor, CSIF) {Human (Homo sapiens)}
tqsenscthfpgnlpnmlrdlrdafsrvktffqmkdqldnlllkeslledfkgylgcqal
semiqfyleevmpqaenqdpdikahvnslgenlktlrlrlrrchrflpcenkskaveqvk
nafnklqekgiykamsefdifinyieaymtmkirn
>d1au1a_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1rmi__ 1.27.1.3.4 Interferon-beta {Mouse (Mus musculus)}
inykqlqlqertnirkcqelleqlngkinltyradfkipmemtekmqksytafaiqemlq
nvflvfrnnfsstgwnetivvrlldelhqqtvflktvleekqeerltwemsstalhlksy
ywrvqrylklmkynsyawmvvraeifrnfliirrltrnfq
>d1rh2a_ 1.27.1.3.5 Interferon-alpha 2b {Human (Homo sapiens)}
thslgsrrtlmllaqmrrislfsclkdrhdfgfpqeefgnqfqkaetipvlhemiqqifn
lfstkdssaawdetlldkfytelyqqlndleacviqgvgvtetplmnedsilavrkyfqr
itlylkekkyspcawevvraeimrsfslstnlqe
>d1b5l__ 1.27.1.3.7 Interferon-tau {Sheep (Ovis aries)}
cylsrklmldarenlklldrmnrlsphsclqdrkdfglpqemvegdqlqkdqafpvlyem
lqqsfnlfytehssaawdttlleqlctglqqqldhldtcrgqvmgeedselgnmdpivtv
kkyfqgiydylqekgysdcaweivrvemmraltvsttlqkrltk
>d1d9ca_ 1.27.1.3.8 Interferon-gamma {Bovine (Bos taurus)}
qgqffreienlkeyfnasspdvakggplfseilknwkdesdkkiiqsqivsfyfklfenl
kdnqviqrsmdiikqdmfqkflngssekledfkkliqipvddlqiqrkainelikvmndl
s
>d1higa_ 1.27.1.3.9 Interferon-gamma {Human (Homo sapiens)}
qdpyvkeaenlkkyfnaghsdvadngtlflgilknwkeesdrkimqsqivsfyfklfknf
kddqsiqksvetikedmnvkffnsnkkkrddfekltnysvtdlnvqrkaiheliqvmael
spa
>d2rig__ 1.27.1.3.10 Interferon-gamma {Rabbit (Oryctolagus cuniculus)}
qdtltretehlkaylkantsdvanggplflnilrnwkeesdnkiiqsqivsfyfklfdnl
kdhevikksmesikedifvkffnsnltkmddfqnltrisvddrlvqrkavselsnvlnf
>d1a8h_1 1.28.1.1.1 (349-500) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
laddlgnlvqrtramlfrfaegripepvageelaegtglagrlrplvrelkfhvaleeam
ayvkalnryinekkpwelfkkepeearavlyrvveglriasilltpampdkmaelrralg
lkeevrleeaerwglaeprpipeeapvlfpkk
>d1qqta1 1.28.1.1.2 (389-548) Methionyl-tRNA synthetase (MetRS) {Escherichia coli}
vvnlasrnagfinkrfdgvlaseladpalyktftdaaevigeawesrefgkavreimala
dlanryvdeqapwvvakqagrdadlqaicsmginlfrvlmtylkpvlpklteraeaflnt
eltwdgiqqpllghkvnpfkalynridmrqvealveaske
>d1ile_1 1.28.1.1.3 (642-821) Isoleucyl-tRNA synthetase (IleRS) {Thermus thermophilus}
yfltlwnvysffvtyanldrpdlknppppekrpemdrwllarmqdliqrvtealeaydpt
tsaralrdfvvedlsqwyvrrnrrrfwknedaldreaayatlyealvlvatlaapftpfl
aevlwqnlvrsvrleakesvhladwpeadpaladealvaqmravlkvvdlaraaraksgv
>d1qu2a1 1.28.1.1.4 (645-917) Isoleucyl-tRNA synthetase (IleRS) {Staphylococcus aureus}
yrkirntlrfmlgnindfnpdtdsipesellevdryllnrlreftastinnyenfdylni
yqevqnfinvelsnfyldygkdilyieqrdshirrsmqtvlyqilvdmtkllapilvhta
eevwshtphvkeesvhladmpkvvevdqalldkwrtfmnlrddvnraletarnekvigks
leakvtiasndkfnasefltsfdalhqlfivsqvkvvdklddqatayehgdiviehadge
kcercwnysedlgavdelthlcprcqqvvkslv
>d1bs2a1 1.28.1.1.5 (484-607) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
dtgpylqyahsrlrsvernasgitqekwinadfsllkepaakllirllgqypdvlrnaik
thepttvvtylfklthqvsscydvlwvagqteelatarlalygaarqvlyngmrllgltp
verm
>d1acp__ 1.29.1.1.1 Acyl carrier protein {Escherichia coli}
stieervkkiigeqlgvkqeevtnnasfvedlgadsldtvelvmaleeefdteipdeeae
kittvqaaidyinghqa
>d1af8__ 1.29.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {Streptomyces coelicolor, A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d2af8__ 1.29.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {Streptomyces coelicolor, A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d1ayi__ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkq
>d1cei__ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
lknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdnrd
dspegivkeikewraangkpgfkqg
>d1unka_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d1unkb_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d1unkc_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d1unkd_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d7ceia_ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkqg
>d1imy__ 1.29.2.1.2 ImmE8 {Escherichia coli}
melknsisdytetefkkiiediincegdekkqddnlehfisvtehpsgsdliyypegnnd
gspeavikeikewraangksgfkqg
>d1imz__ 1.29.2.1.2 ImmE8 {Escherichia coli}
melknsisdytetefkkiiediincegdekkqddnlehfisvtehpsgsdliyypegnnd
gspeavikeikewraangksgfkqg
>d1bxia_ 1.29.2.1.3 ImE9 protein {Escherichia coli}
lkasisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegddd
spsgivntvqqwraangksgfkq
>d1imp__ 1.29.2.1.3 ImE9 protein {Escherichia coli}
melkhsisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegd
ddspsgivntvkqwraangksgfkqg
>d1imq__ 1.29.2.1.3 ImE9 protein {Escherichia coli}
melkhsisdyteaeflqlvtticnadtsseeelvklvthfeemtehpsgsdliyypkegd
ddspsgivntvkqwraangksgfkqg
>d1eia_1 1.29.3.1.1 (148-222) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
pkaqnirqgakepypefvdrllsqikseghpqeiskfltdtltiqnaneecrnamrhlrp
edtleekmyacrdig
>d2eiaa1 1.29.3.1.1 (148-222) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
pkaqnirqgakepypefvdrllsqikseghpqeiskfltdtltiqnaneecrnamrhlrp
edtleekmyacrdig
>d2eiab1 1.29.3.1.1 (148-220) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
pkaqnirqgakepypefvdrllsqikseghpqeiskfltdtltiqnaneecrnamrhlrp
edtleekmyacrd
>d1qrjb1 1.29.3.1.2 (131-214) HTLV-I capsid protein {Human t-cell leukemia virus, type I, HTLV-I}
pswasilqgleepyhafverlnialdnglpegtpkdpilrslaysnankecqkllqargh
tnsplgdmlracqtwtpkdktkvl
>d1a43__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtacq
>d1a8o__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
dirqgpkepfrdyvdrfyktlraeqasqevknwxtetllvqnanpdcktilkalgpgatl
eexxtacqg
>d1aum__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
ldirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgpgat
leemmtacqg
>d1baj__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtac
>d1bmx__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
csildirqgpkepfrdyvdrfyktlraeqas
>d1d1da1 1.29.3.1.4 (151-230) RSV capsid protein {Rous sarcoma virus, RSV}
gpwaditqgpsesfvdfanrlikavegsdlppsarapviidcfrqksqpdiqqliraaps
tlttpgeiikyvldrqkiap
>d1ffh_1 1.30.1.1.1 (2-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
fqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreealg
kqvlesltpaevilatvyealkealgg
>d1ng1_1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevardfvervreeal
gkqvlesltpaevilatvyealkealgg
>d2ffha1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreeal
gkqvlesltpaevilatvyealkealgg
>d2ffhb1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreeal
gkqvlesltpaevilatvyealkealgg
>d2ffhc1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreeal
gkqvlesltpaevilatvyealkealgg
>d2ng1_1 1.30.1.1.1 (2-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
fqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevtrdfvervreealg
kqvlesltpaevilatvyealkealgg
>d3ng1a1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevardfvervreeal
gkqvlesltpaevilatvyealkealgg
>d3ng1b1 1.30.1.1.1 (1-88) Signal sequence recognition protein Ffh {Thermus aquaticus}
mfqqlsarlqeaigrlrgrgriteedlkatlreirralmdadvnlevardfvervreeal
gkqvlesltpaevilatvyealkealgg
>d1fts_1 1.30.1.1.2 (201-284) Signal recognition particle receptor, FtsY {Escherichia coli}
rsllktkenlgsgfislfrgkkidddlfeeleeqlliadvgvettrkiitnltegasrkq
lrdaealygllkeemgeilakvde
>d1b91a_ 1.30.2.1.1 P300/CAF histone acetyltransferase bromodomain {human (Homo sapiens)}
gshmskeprdpdqlystlksilqqvkshqsawpfmepvkrteapgyyevirspmdlktms
erlknryyvskklfmadlqrvftnckeynapeseyykcanilekfffskikeaglidk
>d1b6q__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldpdeqadiceslhdhadelyrsclarf
>d1gtoa_ 1.31.1.1.1 ROP protein {Escherichia coli}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfgddg
en
>d1gtob_ 1.31.1.1.1 ROP protein {Escherichia coli}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfg
>d1gtoc_ 1.31.1.1.1 ROP protein {Escherichia coli}
gtkqektalnmarfirsqtltlleklnelgadeqadiceslhdhadelyrsclarfg
>d1nkd__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneladaadeqadiceslhdhadelyrsclarfg
>d1ropa_ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldadeqadiceslhdhadelyrsclarf
>d1rpo__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneladaadeqadiceslhdhadelyrsclarfgd
d
>d1rpra_ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldadeqadiceslhdhadelyrsclarfgddg
enl
>d1rprb_ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldadeqadiceslhdhadelyrsclarfgddg
enl
>d1joya_ 1.31.2.1.1 EnvZ histidine kinase {Escherichia coli}
maagvkqladdrtllmagvshdlrtpltrirlatemmseqdgylaesinkdieecnaiie
qfidylr
>d1joyb_ 1.31.2.1.1 EnvZ histidine kinase {Escherichia coli}
maagvkqladdrtllmagvshdlrtpltrirlatemmseqdgylaesinkdieecnaiie
qfidylr
>d1b3qa1 1.31.2.1.2 (293-354) Histidine kinase CheA {Thermotoga maritima}
sqtvrvdiekldnlmdlmgelviarsriletlkkynikeldeslshlsritldlqnvvmk
ir
>d1b3qb1 1.31.2.1.2 (293-354) Histidine kinase CheA {Thermotoga maritima}
sqtvrvdiekldnlmdlmgelviarsriletlkkynikeldeslshlsritldlqnvvmk
ir
>d1r2aa_ 1.32.1.1.1 Dimerization-anchoring domain of cAMP-dependent type II PK regulatory subunit {Mouse (Mus musculus)}
hmghiqippgltellqgytvevlrqqppdlvdfaveyftrlrearr
>d1r2ab_ 1.32.1.1.1 Dimerization-anchoring domain of cAMP-dependent type II PK regulatory subunit {Mouse (Mus musculus)}
hmghiqippgltellqgytvevlrqqppdlvdfaveyftrlrearr
>d1ytfb1 1.33.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
snaeasrvyeiivesvvnevredfenagideqtlqdlkniwqkklt
>d1ytfd1 1.33.1.1.1 (5-54) Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
gyyelyrrstignslvdaldtlisdgrieaslamrvletfdkvvaetlkd
>d1ecia_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
gvipkkiwetvcptvepwakkcsgdiatyikrecgkl
>d1ecib_ 1.34.1.1.1 Ectatomin, A & B chains {Ant (Ectatomma tuberculatum), venom}
wstivklticptlksmakkcegsiatmikkkcdk
>d1b0na1 1.35.1.1.1 (74-108) SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
ldseweklvrdamtsgvskkqfrefldyqkwrksq
>d1b0nb1 1.35.1.1.1 SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
feldqewvelmveakeanispeeirkyllln
>d1cqta2 1.36.1.1.1 (2-75) Oct-1 {Human (Homo sapiens)}
epsdleeleqfaktfkqrriklgftqgdvglamgklygndfsqttisrfealnlsfknmc
klkpllekwlndae
>d1cqtb2 1.36.1.1.1 (505-575) Oct-1 {Human (Homo sapiens)}
dleeleqfaktfkqrriklgftqgdvglamgklygndfsqttisrfealnlsfknmcklk
pllekwlndae
>d1octc2 1.36.1.1.1 (5-75) Oct-1 {Human (Homo sapiens)}
dleeleqfaktfkqrriklgftqgdvglamgklygndfsqttisrfealnlsfknmcklk
pllekwlndae
>d1pou__ 1.36.1.1.1 Oct-1 {Human (Homo sapiens)}
dleeleqfaktfkqrriklgftqgdvglamgklygndfsqttisrfealnlsfknmcklk
pllekwlndae
>d1au7a2 1.36.1.1.2 (5-76) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleeaeq
>d1au7b2 1.36.1.1.2 (5-74) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleea
>d1llia_ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
kkpltqeqledarrlkaiyekkknelglsqesladklgmgqsgigalfnginalnaynaa
llakilkvsveefspsiareiyemyeavs
>d1llib_ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
stkkkpltqeqledarrlkaiyekkknelglsqesladklgmgqsgigalfnginalnay
naallakilkvsveefspsiareiyemyeavs
>d1lmb3_ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
pltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnaynaall
akilkvsveefspsiareiyemyeavs
>d1lmb4_ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
stkkkpltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnay
naallakilkvsveefspsiareiyemyeavs
>d1lrp__ 1.36.1.2.1 lambda C1 repressor, DNA-binding domain {Bacteriophage lambda (Escherichia coli)}
kkpltqeqledarrlkaiyekkknelglsqesvadkmgmgqsgvgalfnginalnaynaa
llakilkvsveefspsiareiyemyeavs
>d1perl_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1perr_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1pra__ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngtsdsnvr
>d1r63__ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1r69__ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1rpel_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1rper_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d2or1l_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d2or1r_ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskriqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d2r63__ 1.36.1.2.2 434 C1 repressor, DNA-binding domain {Phage 434 (Escherichia coli)}
sissrvkskmiqlglnqaelaqkvgttqqsieqlengktkrprflpelasalgvsvdwll
ngt
>d1zug__ 1.36.1.2.3 cro 434 {Bacteriophage 434}
mqtlserlkkrrialkmtqtelatkagvkqqsiqlieagvtkrprflfeiamalncdpvw
lqygtkrgkaa
>d2cro__ 1.36.1.2.3 cro 434 {Bacteriophage 434}
mqtlserlkkrrialkmtqtelatkagvkqqsiqlieagvtkrprflfeiamalncdpvw
lqygt
>d3crol_ 1.36.1.2.3 cro 434 {Bacteriophage 434}
mqtlserlkkrrialkmtqtelatkagvkqqsiqlieagvtkrprflfeiamalncdpvw
lqygtk
>d3cror_ 1.36.1.2.3 cro 434 {Bacteriophage 434}
mqtlserlkkrrialkmtqtelatkagvkqqsiqlieagvtkrprflfeiamalncdpvw
lqyg
>d1adr__ 1.36.1.2.4 p22 C2 repressor, DNA-binding domain {Bacteriophage p22 (Salmonella)}
mntqlmgerirarrkklkirqaalgkmvgvsnvaisqwersetepngenllalskalqcs
pdyllkgdlsqtnvay
>d1copd_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1cope_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
nkktta
>d1d1la_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpwps
n
>d1d1ma_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgev
kpwps
>d1d1mb_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgev
kpwps
>d1orc__ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgevkp
fpsn
>d2orc__ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgev
kpfpsnkktta
>d3orca_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
eqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkdgevk
pfpsn
>d4croa_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d4crob_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d4croc_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d4crod_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d4croe_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d4crof_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
qritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsnk
ktta
>d5croa_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
n
>d5crob_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
n
>d5croc_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
n
>d5croo_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
meqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfps
>d6croa_ 1.36.1.2.5 cro lambda repressor {Bacteriophage lambda (Escherichia coli)}
eqritlkdyamrfgqtktakdlgvyqsainkaihagrkifltinadgsvyaeevkpfpsn
>d1neq__ 1.36.1.2.6 Ner {Bacteriophage mu}
csnekardwhradviaglkkrklslsalsrqfgyapttlanalerhwpkgeqiianalet
kpeviwpsryqage
>d1ner__ 1.36.1.2.6 Ner {Bacteriophage mu}
csnekardwhradviaglkkrklslsalsrqfgyapttlanalerhwpkgeqiianalet
kpeviwpsryqage
>d1b0na2 1.36.1.3.1 (1-68) SinR repressor, DNA-binding domain {Bacillus subtilis}
migqrikqyrkekgyslselaekagvaksylssiernlqtnpsiqflekvsavldvsvht
lldekhet
>d1bdha1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1bdia1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1pnra1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1pru__ 1.36.1.4.1 Purine repressor (PurR), N-terminal domain {Escherichia coli}
matikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkv
>d1prv__ 1.36.1.4.1 Purine repressor (PurR), N-terminal domain {Escherichia coli}
matikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkv
>d1qp0a1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qp4a1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qp7a1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1qpza1 1.36.1.4.1 (2-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
atikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1qqaa1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1qqba1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1vpwa1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarsmkvnh
>d1weta1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1zaya1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puaa1 1.36.1.4.1 (2-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
atikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puba1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puca1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puda1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puea1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2pufa1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d2puga1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1cjga_ 1.36.1.4.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
sl
>d1cjgb_ 1.36.1.4.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
sl
>d1lbga1 1.36.1.4.2 (1-60) Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgb1 1.36.1.4.2 (1-60) Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgc1 1.36.1.4.2 (1-60) Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lbgd1 1.36.1.4.2 (1-60) Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqqlagkq
>d1lcca_ 1.36.1.4.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lcda_ 1.36.1.4.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnr
>d1lqc__ 1.36.1.4.2 Lac repressor (LacR), N-terminal domain {Escherichia coli}
mkpvtlydvaeyagvsyqtvsrvvnqashvsaktrekveaamaelnyipnrvaqql
>d1uxc__ 1.36.1.4.3 Fructose repressor (FruR), N-terminal domain {Escherichia coli}
mkldeiarlagvsrttasyvingkakqyrvsdktvekvmavvrehnyhpn
>d1uxd__ 1.36.1.4.3 Fructose repressor (FruR), N-terminal domain {Escherichia coli}
mkldeiarlagvsrttasyvingkakqyrvsdktvekvmavvrehnyhpnavaaglrlq
>d1a6i_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srldkskvinsalellnevgieglttrklaqklgveqptlywhvknkralldalaveila
rhhdys
>d1bj0_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjya1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjyb1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1bjz_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1ork_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d2tct_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
arlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d2trt_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
arlnresvidaalellnetgidglttrklaqklgieqptlywhvknkralldalaveila
rhhdys
>d1a04a1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1a04b1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1rnl_1 1.37.1.2.1 (155-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
qltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavwvhqer
if
>d2ffha2 1.38.1.1.1 (319-418) Signal sequence binding protein Ffh {Thermus aquaticus}
eapksakelsledflkqmqnlkrlgpfseilgllpgvpqglkvdekaikrleaivlsmtp
eerkdprilngsrrkriakgsgtsvqevnrfikafeemkalmkslek
>d1qb2a_ 1.38.1.1.2 SRP54M {Human (Homo sapiens)}
qftlrdmyeqfqnimkmgpfsqilgmipgfgtdfmskgneqesmarlkklmtimdsmndq
eldstdgakvfskqpgriqrvargsgvstrdvqelltqytkfaqmvk
>d1sknp_ 1.39.1.1.1 Binding domain of Skn-1 {Caenorhabditis elegans}
grqskdeqlasdnelpvsafqisemslselqqvlkneslseyqrqlirkirrrgknkvaa
rtcrqrrtdrhdkm
>d1hloa_ 1.40.1.1.1 Max protein {Human (Homo sapiens)}
nddievesdadkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiq
ymrrknhthqqdiddlkrqn
>d1hlob_ 1.40.1.1.1 Max protein {Human (Homo sapiens)}
sdadkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknh
thqqdiddlkrqn
>d1an2a_ 1.40.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an2c_ 1.40.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1mdya_ 1.40.1.1.3 Myod B/HLH domain {Mouse (Mus musculus)}
melkrkttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyie
glqallrd
>d1mdyb_ 1.40.1.1.3 Myod B/HLH domain {Mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1mdyc_ 1.40.1.1.3 Myod B/HLH domain {Mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1mdyd_ 1.40.1.1.3 Myod B/HLH domain {Mouse (Mus musculus)}
ttnadrrkaatmrerrrlskvneafetlkrstssnpnqrlpkveilrnairyieglqall
rd
>d1an4a_ 1.40.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an4b_ 1.40.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1a0aa_ 1.40.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0ab_ 1.40.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1am9a_ 1.40.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslk
>d1am9b_ 1.40.1.1.6 SREBP-1a {Human (Homo sapiens)}
srgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnqk
lkqenlslrtavhks
>d1am9c_ 1.40.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslkdl
>d1am9d_ 1.40.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhks
>d1b1ga_ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1boc__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekyadkegdgnqlskeelklllqtefpsllkgmstldelfeeldkngdg
evsfeefqvlvkkisq
>d1bod__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekydkegdgqlskeelklllqtefpsllkgmstldelfeeldkngdgev
sfeefqvlvkkisq
>d1cdn__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1clb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d2bca__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d2bcb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d3icb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkgpstldelfeeldkngdge
vsfeefqvlvkkisq
>d4icb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekyaakegdpnqlskeelklllqtefpsllkgpstldelfeeldkngdg
evsfeefqvlvkkisq
>d5icb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkgpstldelfeeldkngdge
vsfeefqvlvkkisq
>d6icb__ 1.41.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
mkspeelkgifekyaakegdpnqlskeelklllqtefpsllkgpstldelfeeldkngdg
evsfeefqvlvkkisq
>d1cb1__ 1.41.1.1.2 Calbindin D9K {Porcine (Sus scrofa)}
saqkspaelksifekyaakegdpnqlskeelkqliqaefpsllkgprtlddlfqeldkng
dgevsfeefqvlvkkisq
>d1a03a_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1a03b_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnpa_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1cnpb_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d2cnpa_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d2cnpb_ 1.41.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1b4ca_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1b4cb_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1qlka_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1qlkb_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1syma_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1symb_ 1.41.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1cfpa_ 1.41.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1cfpb_ 1.41.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
mselekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldsdgdgecdfqefmafvamittacheffehe
>d1mho__ 1.41.1.2.3 Calcyclin (S100) {Bovine (Bos taurus), s100b}
selekavvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmetl
dsdgdgecdfqefmafvamittacheff
>d1uwoa_ 1.41.1.2.4 Calcyclin (S100) {Human (Homo sapiens), s100b}
selekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmetl
dndgdgecdfqefmafvamvttacheffehe
>d1uwob_ 1.41.1.2.4 Calcyclin (S100) {Human (Homo sapiens), s100b}
selekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmetl
dndgdgecdfqefmafvamvttacheffehe
>d1a4pa_ 1.41.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmkq
>d1a4pb_ 1.41.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1bt6a_ 1.41.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1bt6b_ 1.41.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1psra_ 1.41.1.2.6 Calcyclin (S100) {Human (Homo sapiens), psoriasin s100a7}
sntqaersiigmidmfhkytrrddkidkpslltmmkenfpnflsacdkkgtnyladvfek
kdknedkkidfseflsllgdiatdyhkqshgaapcsggsq
>d1sra__ 1.41.1.3.1 C-terminal (EC) domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
ppcldseltefplrmrdwlknvlvtlyerdednnlltekqklrvkkihenekrleagdhp
vellardfeknynmyifpvhwqfgqldqhpidgylshtelaplraplipmehcttrffet
cdldndkyialdewagcfgikqkdidkdlvi
>d1rro__ 1.41.1.4.1 Oncomodulin {Rat (Rattus norvegicus), Sprague-dawley strain}
sitdilsaediaaalqecqdpdtfepqkffqtsglskmsasqvkdifrfidndqsgyldg
delkyflqkfqsdareltesetkslmdaadndgdgkigadefqemvhs
>d1cdp__ 1.41.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
xafagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiidqdksgfie
edelklflqnfkadaraltdgetktflkagdsdgdgkigvdeftalvka
>d1pvaa_ 1.41.1.4.3 Parvalbumin {Pike (Esox lucius)}
xaakdllkaddikkaldavkaegsfnhkkffalvglkamsandvkkvfkaidadasgfie
eeelkfvlksfaadgrdltdaetkaflkaadkdgdgkigidefetlvhea
>d2pvba_ 1.41.1.4.3 Parvalbumin {Pike (Esox lucius)}
sfaglkdadvaaalaacsaadsfkhkeffakvglaskslddvkkafyvidqdksgfieed
elklflqnfspsaraltdaetkafladgdkdgdgmigvdefaamika
>d5pal__ 1.41.1.4.4 Parvalbumin {Leopard shark (Triakis semifasciata)}
pmtkvlkaddinkaisafkdpgtfdykrffhlvglkgktdaqvkevfeildkdqsgfiee
eelkgvlkgfsahgrdlndtetkallaagdsdhdgkigadefakmvaqa
>d1a75a_ 1.41.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
agiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfieede
lklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1bu3__ 1.41.1.4.6 Parvalbumin {Silver hake (Merluccius bilinearis)}
afsgiladadvaaalkaceaadsfnykaffakvgltaksaddikkaffvidqdksgfiee
delklflqvfsagaraltdaetkaflkagdsdgdgaigvdewaalvka
>d1rtp1_ 1.41.1.4.7 Parvalbumin {Rat (Rattus rattus)}
smtdllsaedikkaigaftaadsfdhkkffqmvglkkksaddvkkvfhildkdksgfiee
delgsilkgfssdardlsaketktlmaagdkdgdgkigveefstlvaes
>d1avsa_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
qaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevd
edgsgtidfeeflvmmvrqmk
>d1avsb_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
qqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieev
dedgsgtidfeeflvmmvrqmk
>d1blq__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1ctaa_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctab_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctda_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ctdb_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
xkseeelanafrifdknadgyidieelgeilratg
>d1ncx__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkedakgkseeelancfrifdknadgfidieelge
ilratgehvteediedlmkdsdknndgridfdeflkmmegvq
>d1pona_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
kseeelanafrifdknadgyidieelgeilratg
>d1ponb_ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
vteediedlmkdsdknndgridfdeflkmmegvq
>d1skt__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1smg__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkalgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1tnp__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1tnq__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d1zac__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
asmtdqqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeelda
iieevdedgsgtidfeeflvmmvrqmkeda
>d2ctn__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
adiykaaveqlteeqknefkaafdifvlgaedgsistkelgkvmrmlgqnptpeelqemi
devdedgsgtvdfdeflvmmvrsmkdds
>d3ctn__ 1.41.1.5.1 Troponin C {Chicken (Gallus gallus)}
kddskgkteeelsdlfrmfdknadgyidleelkimlqatgetiteddieelmkdgdknnd
gridydeflefmkgve
>d1trf__ 1.41.1.5.2 Troponin C {Turkey (Meleagris gallopavo)}
aflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevdedgsg
tidfeeflvmmvrqmk
>d1ap4__ 1.41.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d1mxlc_ 1.41.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d1spy__ 1.41.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d2scpa_ 1.41.1.5.5 Sarcoplasmic calcium-binding protein {Sandworm (Nereis diversicolor)}
sdlwvqkmktyfnridfdkdgaitrmdfesmaerfakesemkaehakvlmdsltgvwdnf
ltavaggkgidettfinsmkemvknpeaksvvegplplffravdtnednnisrdeygiff
gmlgldktmapasfdaidtnndgllsleefviagsdffmndgdstnkvfwgplv
>d2sas__ 1.41.1.5.6 Sarcoplasmic calcium-binding protein {Amphioxus (Branchiostoma lanceolatum)}
glndfqkqkikftfdffldmnhdgsiqdndfedmmtrykevnkgslsdadyksmqasled
ewrdlkgradinkddvvsweeylamwektiatcksvadlpawcqnripflfkgmdvsgdg
ivdleefqnycknfqlqcadvpavynvitdggkvtfdlnrykelyyrlltspaadagntl
mgqkp
>d1cll__ 1.41.1.5.7 Calmodulin {Human (Homo sapiens)}
lteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngti
dfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevde
mireadidgdgqvnyeefvqmmta
>d1ak8__ 1.41.1.5.8 Calmodulin {Bovine (Bos taurus)}
madqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadg
ngtidfpefltmmark
>d1cmf__ 1.41.1.5.8 Calmodulin {Bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1cmg__ 1.41.1.5.8 Calmodulin {Bovine (Bos taurus)}
mkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgq
vnyeefvqmmtak
>d1trca_ 1.41.1.5.8 Calmodulin {Bovine (Bos taurus)}
dseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgqvnye
efvqmmta
>d1trcb_ 1.41.1.5.8 Calmodulin {Bovine (Bos taurus)}
dseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevdemireadidgdgqvnye
efvqmmta
>d1osa__ 1.41.1.5.13 Calmodulin {Paramecium tetraurelia}
aeqlteeqiaefkeafalfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpeflslmarkmkeqdseeelieafkvfdrdgnglisaaelrhvmtnlgekltdde
vdemireadidgdghinyeefvrmmvsk
>d1wdcb_ 1.41.1.5.15 Myosin Essential Chain {Bay scallop (Aequipecten irradians)}
lpqkqiqemkeafsmidvdrdgfvskedikaiseqlgrapddkeltamlkeapgplnftm
flsifsdklsgtdseetirnafamfdeqetkklnieyikdllenmgdnfnkdemrmtfke
apveggkfdyvkftamikgsge
>d1br1b_ 1.41.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fseeqtaefkeafqlfdrtgdgkilysqcgdvmralgqnptnaevmkvlgnpksdemnlk
tlkfeqflpmmqtiaknkdqgcfedyveglrvfdkegngtvmgaeirhvlvtlgekmtee
eveqlvaghedsngcinyeelvrmvlsg
>d2mysb_ 1.41.1.5.16 Myosin Essential Chain {Chicken (Gallus gallus)}
fdeteiedfkeaftvidqnadgiidkddlretfaamgrlnvkneeldamikeasgpinft
vfltmfgeklkgadpedvimgafkvldpdgkgsikksfleellttgggrftpeeiknmwa
afppdvagnvdyknicyvithgeda
>d1wdcc_ 1.41.1.5.17 Myosin Regulatory Chain {Bay scallop (Aequipecten irradians)}
lsqdeiddlkdvfelfdfwdgrdgavdafklgdvcrclginprnedvfavggthkmgeks
lpfeeflpayeglmdceqgtfadymeafktfdregqgfisgaelrhvltalgerlsdedv
deiikltdlqedlegnvkyedfvkkvmagpyp
>d2mysc_ 1.41.1.5.18 Myosin Regulatory Chain {Chicken (Gallus gallus)}
aaaddfkeafllfdrtgdakitasqvgdiaralgqnptnaeinkilgnpskeemnaaait
feeflpmlqaaannkdqgtfedfveglrvfdkegngtvmgaelrhvlatlgekmteeeve
elmkgqedsngcinyeafvkhimsv
>d1auib_ 1.41.1.5.20 Calcineurin regulatory subunit (B-chain) {Human (Homo sapiens)}
syplemcshfdadeikrlgkrfkkldldnsgslsveefmslpelqqnplvqrvidifdtd
gngevdfkefiegvsqfsvkgdkeqklrfafriydmdkdgyisngelfqvlkmmvgnnlk
dtqlqqivdktiinadkdgdgrisfeefcavvggldihkkmvvdv
>d1rec__ 1.41.1.5.22 Recoverin {Bovine (Bos taurus)}
lskeileelqlntkfteeelsswyqsflkecpsgritrqefqtiyskffpeadpkayaqh
vfrsfdansdgtldfkeyvialhmtsagktnqklewafslydvdgngtisknevleivta
ifkmispedtkhlpedentpekraekiwgffgkkdddkltekefiegtlankeilrliqf
epqkvkeklk
>d1jbaa_ 1.41.1.5.23 Guanylate cyclase activating protein 2, GCAP-2 {Bovine (Bos taurus)}
gqqfsweeaeengavgaadaaqlqewykkfleecpsgtlfmhefkrffkvpdneeatqyv
eamfrafdtngdntidfleyvaalnlvlrgtlehklkwtfkiydkdrngcidrqelldiv
esiyklkkacsveveaeqqgklltpeevvdrifllvdengdgqlslnefvegarrdkwvm
kmlqmdlnp
>d1dgua_ 1.41.1.5.25 Calium- and integrin-binding protein, CIB {Human (Homo sapiens)}
skellaeyqdltfltkqeillahrrfcellpqeqrsvesslraqvpfeqilslpelkanp
fkericrvfstspakdslsfedfldllsvfsdtatpdikshyafrifdfdddgtlnredl
srlvncltgegedtrlsasemkqlidnileesdidrdgtinlsefqhvisrspdfassfk
ivl
>d1qjta_ 1.41.1.6.1 Eps15 {Mouse (Mus musculus)}
lsltqlssgnpvyekyyrqveagntgrvlaldaaaflkksglpdlilgkiwdladtdgkg
vlskqeffvalrlvacaqnglevslsslslavppprfhd
>d1eh2__ 1.41.1.6.2 Eps15 {Human (Homo sapiens)}
pwavkpedkakydaifdslspvngflsgdkvkpvllnsklpvdilgrvwelsdidhdgml
drdefavamflvycalekepvpmslppalvppskr
>d1djga1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djha1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djia1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djwa1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djxa1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djxb1 1.41.1.7.1 (158-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
nkmnfkelkdflkelniqvddgyarkifrecdhsqtdsledeeietfykmltqraeidra
feeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetakaqrqmtkdgflm
yllsadgnafslahrrvyqdm
>d1djya1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1djza1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1qasa1 1.41.1.7.1 (205-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
ykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslieryepseta
kaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1qasb1 1.41.1.7.1 (206-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
kmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetak
aqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1qata1 1.41.1.7.1 (206-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
kmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetak
aqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1qatb1 1.41.1.7.1 (206-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
kmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslieryepsetak
aqrqmtkdgflmyllsadgnafslahrrvyqdm
>d2isda1 1.41.1.7.1 (200-298) Phosphoinositide-specific phospholipase C, isozyme D1 (PLC-D!) {Rat (Rattus norvegicus)}
eietfykmltqraeidrafeeaagsaetlsverlvtflqhqqreeeagpalalslierye
psetakaqrqmtkdgflmyllsadgnafslahrrvyqdm
>d1alva_ 1.41.1.7.4 Calpain small (regulatory) subunit (domain VI) {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1dkva1 1.41.1.7.5 (515-700) Calpain large subunit, C-terminal domain (domain IV) {Human (Homo sapiens)}
eieanleefdiseddiddgvrrlfaqlagedaeisafelqtilrrvlakrqdiksdgfsi
etckimvdmldsdgsgklglkefyilwtkiqkyqkiyreidvdrsgtmnsyemrkaleea
gfkmpcqlhqvivarfaddqliidfdnfvrclvrletlfkifkqldpentgtieldlisw
lcfsvl
>d1b47a1 1.41.1.7.6 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47b1 1.41.1.7.6 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47c1 1.41.1.7.6 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d2cbla1 1.41.1.7.6 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1c3za_ 1.41.2.1.1 Thp12-carrier protein {Yellow meal worm (Tenebrio molitor) |A|}
etpreklkqhsdackaesgvseeslnkvrnreevddpklkehafcilkragfidasgefq
ldhiktkfkensehpekvddlvakcavkkdtpqhssadffkcvhdnrs
>d1cpo_1 1.41.3.1.1 (1-119) Cloroperoxidase {Fungus (Caldariomyces fumago)}
epgsgigypydnntlpyvapgptdsrapcpalnalanhgyiphdgraisretlqnaflnh
mgiansvielaltnafvvceyvtgsdcgdslvnltllaephafehdhsfsrkdykqgva
>d1cpo_2 1.41.3.1.1 (120-298) Cloroperoxidase {Fungus (Caldariomyces fumago)}
nsndfidnrnfdaetfqtsldvvagkthfdyadmneirlqreslsneldfpgwfteskpi
qnvesgfifalvsdfnlpdndenplvridwwkywftnesfpyhlgwhppspareiefvts
assavlaasvtstpsslpsgaigpgaeavplsfastmtpfllatnapyyaqdptlgpnd
>d1bkra_ 1.42.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1aoa_1 1.42.1.1.2 (121-251) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
yseeekyafvnwinkalendpdcrhvipmnpntddlfkavgdgivlckminlsvpdtide
rainkkkltpfiiqenlnlalnsasaigchvvnigaedlragkphlvlgllwqiikiglf
adielsrneal
>d1aoa_2 1.42.1.1.2 (260-375) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
tleelmklspeelllrwanfhlensgwqkinnfsadikdskayfhllnqiapkgqkegep
ridinmsgfnetddlkraesmlqqadklgcrqfvtpadvvsgnpklnlafvanlfn
>d1bhda_ 1.42.1.1.3 Utrophin {Human (Homo sapiens)}
lqqtnsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkms
pierlehafskaqtylgieklldpedvavrlpdkksiimyltslfevl
>d1qaga1 1.42.1.1.3 (31-151) Utrophin {Human (Homo sapiens)}
dvqkktftkwinarfsksgkppindxftdlkdgrklldllegltgtslpkergstrvhal
nnvnrvlqvlhqnnvelvniggtdivdgnhkltlgllwsiilhwqvkdvxkdvxsdlqqt
n
>d1a26_1 1.43.1.1.1 (662-796) Domain of poly(ADP-ribose) polymerase {Chicken (Gallus gallus)}
ksklakpiqdlikmifdvesmkkamvefeidlqkmplgklskrqiqsaysilnevqqavs
dggsesqildlsnrfytliphdfgmkkppllsnleyiqakvqmldnlldievaysllrgg
nedgdkdpidinyek
>d1ycqa_ 1.44.1.1.1 MDM2 {African clawed frog (Xenopus laevis)}
eklvqptplllsllksagaqketftmkeviyhlgqyimakqlydekqqhivhcsndplge
lfgvqefsvkeprrlyamisrnlvsanv
>d1ycra_ 1.44.1.1.2 MDM2 {Human (Homo sapiens)}
etlvrpkplllkllksvgaqkdtytmkevlfylgqyimtkrlydekqqhivycsndllgd
lfgvpsfsvkehrkiytmiyrnlvv
>d1arqa_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arqb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arra_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arrb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1b28a_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegriga
>d1b28b_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegriga
>d1baza_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
skmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bazb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bazc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bazd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bdta_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdtb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdtc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdtd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdva_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdvb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdvc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkeg
>d1bdvd_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1myka_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1mykb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmlqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1myla_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegr
>d1mylb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1mylc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myld_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkkegri
>d1myle_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfkk
>d1mylf_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqfnlrwprevldlvrkvaeengmsvnsyiyqlvmesfk
>d1para_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1parb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1parc_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1pard_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1qtga_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqflnrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1qtgb_ 1.45.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqflnrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1mnta_ 1.45.1.1.2 Mnt repressor {Bacteriophage p22 (Salmonella)}
arddphfnfrmpmevreklkfraeangrsmnsellqivqdalskpspvtgyrndaerlad
eqselv
>d1mntb_ 1.45.1.1.2 Mnt repressor {Bacteriophage p22 (Salmonella)}
arddphfnfrmpmevreklkfraeangrsmnsellqivqdalskpspvtgyrndaerlad
eqselv
>d1b01a_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d1b01b_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d2cpga_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgq
>d2cpgb_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkgqer
>d2cpgc_ 1.45.1.2.1 Transcriptional repressor CopG {Streptococcus agalactiae}
mkkrltitlsesvlenlekmaremglsksamisvalenykkg
>d1cmba_ 1.45.1.2.2 Met repressor, MetR {Escherichia coli}
aewsgeyispyaehgkkseqvkkitvsiplkvlkiltdertrrqvnnlrhatnsellcea
flhaftgqplpddadlrkersdeipeaakeimremginpetwey
>d1a23_1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a24_1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2j_1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2la1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2lb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2ma1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2mb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1a1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1b1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acva1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acvb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7a1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7b1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7c1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7d1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7e1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bq7f1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsba1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1dsbb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvja1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvjb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvka1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1fvkb1 1.46.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1bed_1 1.46.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain {Vibrio cholerae}
gnmgqamskayatmialevedkmvpvmfnrihtlrkppkdeqelrqifldegidaakfda
ayng
>d2gsta1 1.47.1.1.1 (85-217) Glutathione S-transferase {Rat (Rattus rattus), class mu}
lcgeteeeriradivenqvmdnrmqlimlcynpdfekqkpeflktipekmklyseflgkr
pwfagdkvtyvdflaydildqyhifepkcldafpnlkdflarfeglkkisaymkssryls
tpifsklaqwsnk
>d1glqa1 1.47.1.1.2 (79-209) Glutathione S-transferase {Mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d3gtub1 1.47.1.1.6 (85-224) Glutathione S-transferase {Human (Homo sapiens), class mu}
rkhnmcgeteeekirvdiienqvmdfrtqlirlcyssdheklkpqyleelpgqlkqfsmf
lgkfswfagekltfvdfltydildqnrifdpkcldefpnlkafmcrfealekiaaylqsd
qfckmpinnkmaqwgnkpvc
>d1gsua1 1.47.1.1.8 (85-217) Glutathione S-transferase {Chicken (Gallus gallus), class mu}
mcgetevekqrvdvlenhlmdlrmafarlcyspdfeklkpayleqlpgklrqlsrflgsr
swfvgdkltfvdflaydvldqqrmfvpdcpelqgnlsqflqrfealekisaymrsgrfmk
apifwytalwnnk
>d1gsea1 1.47.1.1.9 (81-222) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lygkdikeralidmyiegiadlgemilllpvcppeekdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1gula1 1.47.1.1.9 (81-220) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lfgknlkertlidmyvegtldllellimhpflkpddqqkevvnmaqkaiiryfpvfekil
rghgqsflvgnqlsladvillqtilaleekipnilsafpflqeytvklsniptikrflep
gskkkpppdeiyvrtvynif
>d1b48a1 1.47.1.1.10 (80-222) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvrivlkf
>d1ljra1 1.47.1.1.11 (80-244) Glutathione S-transferase {Human (Homo sapiens), class theta}
tpdhwypsdlqararvheylgwhadcirgtfgiplwvqvlgpligvqvpeekvernrtam
dqalqwledkflgdrpflagqqvtladlmaleelmqpvalgyelfegrprlaawrgrvea
flgaelcqeahsiilsileqaakktlptpspeayqamllriarip
>d1pd211 1.47.1.1.12 (76-199) Glutathione S-transferase {Rat (Rattus norvegicus), class sigma}
dlagkteleqcqvdavvdtlddfmslfpwaeenqdlkertfndlltrqaphllkdldtyl
gdkewfignyvtwadfywdicsttllvlkpdllgiyprlvslrnkvqaipaisawilkrp
qtkl
>d2gsq_1 1.47.1.1.13 (76-202) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus), class sigma}
ldgktslekyrvdeitetlqdifndvvkikfapeaakeavqqnyeksckrlapflegllv
sngggdgffvgnsmtladlhcyvalevplkhtpellkdcpkivalrkrvaecpkiaaylk
krpvrdf
>d1duga1 1.47.1.1.14 (81-234) Glutathione S-transferase {Schistosoma japonicum}
lggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchkt
ylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyiaw
plqgwqatfgggdhppksdpqqhhlggakqagdv
>d2fhea1 1.47.1.1.15 (81-216) Glutathione S-transferase {Fasciola hepatica}
igttseerarvsmiegaavdlrqgisrisyqpkfeqlkegylkdlpttmkmwsdflgknp
ylrgtsvshvdfmvyealdairylephcldhfpnlqqfmsriealpsikaymesnrfikw
plngwhaqfgggdapp
>d1gnwa1 1.47.1.1.16 (86-211) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
lqtdsknisqyaimaigmqvedhqfdpvasklafeqifksiyglttdeavvaeeeaklak
vldvyearlkefkylagetftltdlhhipaiqyllgtptkklfterprvnewvaeitkrp
asekvq
>d1axda1 1.47.1.1.17 (81-210) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalm
>d1aw9_1 1.47.1.1.18 (83-217) Glutathione S-transferase {Maize (Zea mays), type III}
gtdllpatasaaklevwleveshhfypnasplvfqllvrpllggapdaavvdkhaeqlak
vldvyeahlarnkylagdeftladanhasyllylsktpkaglvaarphvkawweaivarp
afqktvaaiplpppp
>d1a0fa1 1.47.1.1.19 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1pmt_1 1.47.1.1.20 (81-201) Glutathione S-transferase {Proteus mirabilis}
nliappkaleryhqiewlnflasevhkgysplfssdtpesylpvvknklkskfvyindvl
skqkcvcgdhftvadaylftlsqwaphvaldltdlshlqdylariaqrpnvhsalvtegl
i
>d1bmta1 1.48.1.1.1 (651-740) Methionine synthase domain {Escherichia coli}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1bmtb1 1.48.1.1.1 (651-740) Methionine synthase domain {Escherichia coli}
qaewrswevnkrleyslvkgitefieqdteearqqatrpieviegplmdgmnvvgdlfge
gkmflpqvvksarvmkqavaylepfieask
>d1azya1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1azyb1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1otp_1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1tpt_1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d2tpt_1 1.48.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1brwa1 1.48.2.1.2 (1-70) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
mrmvdliakkrdgkaltkeeiewivrgytngdipdyqmsalamaiyfrgmteeetaaltm
amvqsgemld
>d1brwb1 1.48.2.1.2 (1001-1070) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
mrmvdliakkrdgkaltkeeiewivrgytngdipdyqmsalamaiyfrgmteeetaaltm
amvqsgemld
>d1bf5a1 1.49.1.1.1 (136-316) STAT-1, coiled coil domain {Human (Homo sapiens)}
ldkqkeldskvrnvkdkvmcieheiksledlqdeydfkcktlqnrehlllkkmylmldnk
rkevvhkiiellnvteltqnalindelvewkrrqqsaciggppnacldqlqnwftivaes
lqqvrqqlkkleeleqkytyehdpitknkqvlwdrtfslfqqliqss
>d1bg1a1 1.49.1.1.2 (136-321) STAT3b {Mouse (Mus musculus)}
vvtekqqmleqhlqdvrkrvqdleqkmkvvenlqddfdfnyktlksqgdmqdlngnnqsv
trqkmqqleqmltaldqmrrsivselagllsameyvqktltdeeladwkrrqqiaciggp
pnicldrlenwitslaesqlqtrqqikkleelqqkvsykgdpivqhrpmleerivelfrn
lmksaf
>d2cbla2 1.50.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1de4c1 1.50.2.1.1 (609-756) Transferrin receptor ectodomain, C-terminal domain {Human (Homo sapiens)}
ldyerynsqllsfvrdlnqyradikemglslqwlysargdffratsrlttdfgnaektdr
fvmkklndrvmrveyhflspyvspkespfrhvfwgsgshtlpallenlklrkqnngafne
tlfrnqlalatwtiqgaanalsgdvwdi
>d1cfaa_ 1.51.1.1.1 C5a anaphylotoxin {Human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgasvnndetceqraarislgprcikafteccvvasq
lranishkdmc
>d1kjs__ 1.51.1.1.1 C5a anaphylotoxin {Human (Homo sapiens)}
mlqkkieeiaakykhsvvkkccydgacvnndetceqraarislgprcikafteccvvasq
lranishkdmqlgr
>d1c5a__ 1.51.1.1.2 C5a anaphylotoxin {Pig (Sus scrofa domestica)}
mlqkkieeeaakykyamlkkccydgayrnddetceeraarikigpkcvkafkdccyianq
vraeqs
>d1occh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d1occu_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d1ocoh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d1ocou_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d1ocrh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
kiknyqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpi
swvstwddrraegtfpgki
>d1ocru_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
kiknyqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpi
swvstwddrraegtfpgki
>d1oczh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d1oczu_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
yqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpiswvs
twddrraegtfpgki
>d2occh_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
kiknyqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpi
swvstwddrraegtfpgki
>d2occu_ 1.52.1.1.1 Cytochrome c oxidase subunit h {Bovine (Bos taurus)}
kiknyqtapfdsrfpnqnqtrncwqnyldfhrcekamtakggdvsvcewyrrvykslcpi
swvstwddrraegtfpgki
>d1hyp__ 1.53.1.1.1 Soybean hydrophobic protein {Soybean (Glycine max)}
pscpdlsiclnilggslgtvddccaligglgdieaivclciqlralgilnlnrnlqliln
scgrsypsnatcprt
>d1bwoa_ 1.53.1.1.2 Plant non-specific lipid-transfer protein (ns-LTP) {Wheat (Triticum aestivum), L. seeds}
idcghvdslvrpclsyvqggpgpsgqccdgvknlhnqarsqsdrqsacnclkgiargihn
lnednarsippkcgvnlpytislnidcsrv
>d1be2__ 1.53.1.1.3 Plant non-specific lipid-transfer protein (ns-LTP) {Barley (Hordeum vulgare)}
lncgqvdskmkpcltyvqggpgpsgeccngvrdlhnqaqssgdrqtvcnclkgiargihn
lnlnnaasipskcnvnvpytispdidcsriy
>d1afh__ 1.53.1.1.4 Plant non-specific lipid-transfer protein (ns-LTP) {Maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1mzl__ 1.53.1.1.4 Plant non-specific lipid-transfer protein (ns-LTP) {Maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1mzm__ 1.53.1.1.4 Plant non-specific lipid-transfer protein (ns-LTP) {Maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1bv2__ 1.53.1.1.5 Plant non-specific lipid-transfer protein (ns-LTP) {Rice (Oryza sativa)}
itcgqvnsavgpcltyarggagpsaaccsgvrslkaaasttadrrtacnclknaargikg
lnagnaasipskcgvsvpytisasidcsrvs
>d1rzl__ 1.53.1.1.5 Plant non-specific lipid-transfer protein (ns-LTP) {Rice (Oryza sativa)}
itcgqvnsavgpcltyarggagpsaaccsgvrslkaaasttadrrtacnclknaargikg
lnagnaasipskcgvsvpytisasidcsrvs
>d1hssa_ 1.53.1.2.1 0.19 alpha-amylase inhibitor {Wheat (Triticum aestivum)}
mcypgqafqvpalpacrpllrlqcngsqvpeavlrdccqqlahisewcrcgalysmldsm
ykehgaqegqagtgafprcrrevvkltaasitavcrlpivvdasgdgayvckdvaaypda
>d1tmqb_ 1.53.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri), seeds}
svgtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceav
rilmdgvvtssgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsl
>d1bea__ 1.53.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>e1pnb.1a 1.53.1.3.1 Napin BNIb {Rape (Brassica napus)}
qpqkcqrefqqeqhlracqqwirqqlagspf
>e1pnb.1b 1.53.1.3.1 Napin BNIb {Rape (Brassica napus)}
qsgpqqgpwlreqccnelyqedqvcvcptlkqaaksvrvqgqhgpfqstriyqiaknlpn
vcnmkqigtcpfiai
>d1a1ua_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1uc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1aie__ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfemfrelnealelkdaqag
>d1c26a_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqag
>d1olga_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olgd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olha_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1olhd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1pesa_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1pesd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1peta_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1petd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
geyftlqirgrerfemfrelnealelkdaqa
>d1saea_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saeb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saec_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saed_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safa_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1safd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saga_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sagd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saha_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sahd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saia_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saib_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saic_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1said_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saja_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sajd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1saka_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sakd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sala_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1salb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1salc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1sald_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3saka_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakb_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakc_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d3sakd_ 1.54.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
kkkpldgeyftlqirgrerfemfrelnealelkdaqagkepg
>d1adt_1 1.55.1.1.1 (176-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
pivsawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltft
snktfvtmmgrflqaylqsfaevtykhhep
>d1adua1 1.55.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adub1 1.55.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adva1 1.55.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1advb1 1.55.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1anv_1 1.55.1.1.1 (179-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
sawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnk
tfvtmmgrflqaylqsfaevtykhhep
>d1ihfa_ 1.56.1.1.1 Integration host factor (IHF) {Escherichia coli}
altkaemseylfdklglskrdakelvelffeeirralengeqvklsgfgnfdlrdknqrp
grnpktgedipitarrvvtfrpgqklksrvenaspk
>d1ihfb_ 1.56.1.1.1 Integration host factor (IHF) {Escherichia coli}
mtkselierlatqqshipaktvedavkemlehmastlaqgerieirgfgsfslhyraprt
grnpktgdkvelegkyvphfkpgkelrdraniyg
>d1hnr__ 1.56.1.1.2 DNA-binding domain of H1 protein, (H-NS) {Escherichia coli}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1hns__ 1.56.1.1.2 DNA-binding domain of H1 protein, (H-NS) {Escherichia coli}
aqrpakysyvdengetktwtgqgrtpavikkamdeqgkslddflikq
>d1huea_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1hueb_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1huua_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1huub_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1huuc_ 1.56.1.1.3 HU protein {Bacillus stearothermophilus}
mnktelinavaetsglskkdatkavdavfdsitealrkgdkvqligfgnfevreraarkg
rnpqtgeemeipaskvpafkpgkalkdavk
>d1b8za_ 1.56.1.1.4 HU protein {Thermotoga maritima}
mnkkelidrvakkagakkkdvklildtiletitealakgekvqivgfgsfevrkaaarkg
vnpqtrkpitiperkvpkfkpgkalkekvk
>d1b8zb_ 1.56.1.1.4 HU protein {Thermotoga maritima}
mnkkelidrvakkagakkkdvklildtiletitealakgekvqivgfgsfevrkaaarkg
vnpqtrkpitiperkvpkfkpgkalkekvk
>d1wtua_ 1.56.1.1.5 Transcription factor 1, TF1 {Phage SPO1 (Bacillus subtilis)}
mnktelikaiaqdteltqvsvskmlasfekittetvakgdkvqltgflnikpvarqarkg
fnpqtqealeiapsvgvsvkpgeslkkaaeglkyedfak
>d1wtub_ 1.56.1.1.5 Transcription factor 1, TF1 {Phage SPO1 (Bacillus subtilis)}
mnktelikaiaqdteltqvsvskmlasfekittetvakgdkvqltgflnikpvarqarkg
fnpqtqealeiapsvgvsvkpgeslkkaaeglkyedfak
>d1alo_1 1.57.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 {Desulfovibrio gigas}
qpenlhplqkawvlhggaqcgfcspgfivsakglldtnadpsredvrdwfqkhrnacrct
gykplvdavmdaaavingkkpetdlefkmpadgriwgskyprptavakvtgtl
>d1qj2a1 1.57.1.1.2 (82-161) Carbon monoxide (CO) dehydrogenase iron-sulfur protein, C-domain {Pseudomonas carboxydovorans}
apdgtlsalqegfrmmhglqcgyctpgmimrshrllqenpspteaeirfgiggnlcrctg
yqnivkaiqyaaakingvpf
>d1qj2g1 1.57.1.1.2 (82-161) Carbon monoxide (CO) dehydrogenase iron-sulfur protein, C-domain {Pseudomonas carboxydovorans}
apdgtlsalqegfrmmhglqcgyctpgmimrshrllqenpspteaeirfgiggnlcrctg
yqnivkaiqyaaakingvpf
>d1bg8a_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8b_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8c_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1dj8a_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1dj8b_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1dj8c_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1dj8d_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1dj8e_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1dj8f_ 1.58.1.1.1 Protein HNS-dependent expression A; HdeA {Escherichia coli}
nkkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactq
dkqanfkdkvkgewdkikk
>d1af7_1 1.59.1.1.1 (11-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
svllqmtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgryl
smleanqnsaewqafinaltt
>d1bc5a1 1.59.1.1.1 (16-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
mtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgrylsmlea
nqnsaewqafinaltt
>d1bqv__ 1.60.1.1.1 Ets-1 transcription factor pointed domain {Mouse (Mus musculus)}
mecadvplltpsskemmsqalkatfsgftkeqqrlgipkdprqwtethvrdwvmwavnef
slkgvdfqkfcmsgaalcalgkecflelapdfvgdilwehleilqkedvk
>d1b0xa_ 1.60.1.2.1 EphA4 receptor tyrosine kinases {Mouse (Mus musculus)}
fsavvsvgdwlqaikmdrykdnftaagyttleavvhmsqddlarigitaithqnkilssv
qamrtqmqqmhg
>d1b4fa_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fb_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
trpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkki
lnsiqvmraqmnqiqsv
>d1b4fc_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fd_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqs
>d1b4fe_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4ff_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsve
>d1b4fg_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqi
>d1b4fh_ 1.60.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsv
>d1sgg__ 1.60.1.2.3 EphB2 receptor {Chicken (Gallus gallus)}
ytsfntvdewldaikmsqykesfasagfttfdivsqmtvedilrvgvtlaghqkkilnsi
qvmraqm
>d1coka_ 1.60.1.2.4 C-terminal domain of p73 {Human (Homo sapiens)}
yhadpslvsfltglgcpncieyftsqglqsiyhlqnltiedlgalkipeqyrmtiwrglq
dlkqghdy
>d1bdxa2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxb2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxc2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxd2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1cuk_2 1.60.2.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1hjp_2 1.60.2.1.1 (65-140) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlf
>d1bvsa2 1.60.2.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgpv
>d1bvsb2 1.60.2.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgp
>d1bvsc2 1.60.2.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgpv
>d1bvsd2 1.60.2.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgp
>d1bvse2 1.60.2.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgpv
>d1bvsf2 1.60.2.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgp
>d1bvsg2 1.60.2.1.2 (64-134) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgpv
>d1bvsh2 1.60.2.1.2 (64-133) DNA helicase RuvA subunit, middle domain {Mycobacterium leprae}
daenrdlflallsvsgvgprlamatlavhdaaalrqaladsdvasltrvpgigrrgaeri
vleladkvgp
>d1tfr_1 1.60.3.1.1 (183-305) T4 RNase H {Bacteriophage T4}
gsaeidcmtkilkgdkkdnvasvkvrsdfwftrvegertpsmktsiveaiandreqakvl
lteseynrykenlvlidfdyipdniasnivnyynsyklpprgkiysyfvkaglskltnsi
nef
>d1bgxt1 1.60.3.1.2 (174-289) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
lrpdqwadyraltgdesdnlpgvkgigektarklleewgsleallknldrlkpairekil
ahmddlklswdlakvrtdlplevdfakrrepdrerlraflerlefgsllhefglle
>d1xo1a1 1.60.3.1.3 (186-290) T5 5'-exonuclease {Bacteriophage T5}
vddveqfislkaimgdlgdnirgvegigakrgyniirefgnvldiidqlplpgkqkyiqn
lnaseellfrnlilvdlptycvdaiaavgqdvldkftkdileiae
>d1a77_1 1.60.3.1.4 (209-316) Flap endonuclease-1 {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1b43a1 1.60.3.1.5 (220-339) Fen-1 nuclease {Pyrococcus furiosus}
ltreklielailvgtdynpggikgiglkkaleivrhskdplakfqkqsdvdlyaikeffl
nppvtdnynlvwrdpdeegilkflcdehdfseervknglerlkkaiksgkqstleswfkr
>d1coo__ 1.60.4.1.1 C-terminal domain of RNA polymerase alpha subunit {Escherichia coli}
fdpillrpvddleltvrsanclkaeaihyigdlvqrtevellktpnlgkkslteikdvla
srglslgmrlenwppasiade
>d1doqa_ 1.60.4.1.2 C-terminal domain of RNA polymerase alpha subunit {Thermus thermophilus}
eqeeeldlpleelglstrvlhslkeegiesvrallalnlkdlknipgigersleeikeal
ekkgftlke
>d1qcka_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d1qckb_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezxa_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezxb_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezya_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezyb_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezza_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d2ezzb_ 1.60.5.1.1 Barrier-to-autointegration factor, BAF {Human (Homo sapiens)}
mttsqkhrdfvaepmgekpvgslagigevlgkkleergfdkayvvlgqflvlkkdedlfr
ewlkdtcganakqsrdcfgclrewcdafl
>d1bmy__ 1.60.6.1.1 MRF-2 DNA-binding domain {Human (Homo sapiens)}
radeqaflvalykymkerktpieripylgfkqinlwtmfqaaqklggyetitarrqwkhi
ydelggnpgstsaatctrrhyerlilpyerfikgeedkplppikprk
>d1b22a_ 1.60.7.1.1 DNA repair protein Rad51, N-terminal domain {Human (Homo sapiens)}
eeesfgpqpisrleqcginandvkkleeagfhtveavayapkkelinikgiseakadkil
aeaaklvpmg
>d1d8ba_ 1.60.8.1.1 HRDC domain from RecQ helicase {Baker's yeast (Saccharomyces cerevisiae)}
elnnlrmtyerlrelslnlgnrmvppvgnfmpdsilkkmaailpmndsafatlgtvedky
rrrfkyfkatiadlskkrsse
>d4crxa1 1.60.9.1.1 (20-129) Cre recombinase {Bacteriophage P1}
sdevrknlmdmfrdrqafsehtwkmllsvcrswaawcklnnrkwfpaepedvrdyllylq
arglavktiqqhlgqlnmlhrrsglprpsdsnavslvmrrirkenvdage
>d1a0p_1 1.60.9.1.2 (3-100) Recombinase XerD {Escherichia coli}
qdlarieqfldalwleknlaentlnayrrdlsmmvewlhhrgltlataqsddlqallaer
leggykatssarllsavrrlfqylyrekfreddpsahl
>d1bpxa1 1.60.10.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1bpya1 1.60.10.1.1 (10-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
tlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtki
aekideflatgklrklekirqd
>d1bpza1 1.60.10.1.1 (5-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
kapqetlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpg
vgtkiaekideflatgklrklekirqd
>d1zqaa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqba1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqca1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqda1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqea1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqfa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqga1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqha1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqia1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqja1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqka1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqla1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqma1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqna1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqoa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqpa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqqa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqra1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqsa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zqta1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icea1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icfa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icga1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icha1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icia1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icja1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icka1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icla1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icma1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icna1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icoa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icpa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icqa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icra1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icsa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icta1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icua1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d7icva1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icaa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icba1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icca1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icea1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icfa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icga1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icha1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icia1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icja1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icka1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icla1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icma1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icna1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icoa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icpa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icqa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icra1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icsa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icta1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icua1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icva1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icwa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icxa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icya1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d8icza1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icaa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icba1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icca1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icea1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icfa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icga1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icha1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icia1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icja1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icka1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icla1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icma1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icna1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icoa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icpa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icqa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icra1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icsa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icta1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icua1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icva1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icwa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icxa1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d9icya1 1.60.10.1.1 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Human (Homo sapiens)}
etlnggitdmltelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1bno__ 1.60.10.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d1bnp__ 1.60.10.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d1bpd_1 1.60.10.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1bpe_1 1.60.10.1.2 (12-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
nggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtkiae
kideflatgklrklekirrd
>d1dk2a_ 1.60.10.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
skrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakk
lpgvgtkiaekideflatgklrklek
>d1dk3a_ 1.60.10.1.2 DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
mskrkapqetlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeak
klpgvgtkiaekideflatgklrklek
>d2bpfa1 1.60.10.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d2bpga1 1.60.10.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d2bpgb1 1.60.10.1.2 (9-91) DNA polymerase beta, N-terminal (8 kD)-domain {Rat (Rattus norvegicus)}
etlnggitdmlvelanfeknvsqaihkynayrkaasviakyphkiksgaeakklpgvgtk
iaekideflatgklrklekirqd
>d1zyma1 1.60.11.1.1 (22-144) Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain {Escherichia coli}
deividrkkisadqvdqeverflsgrakasaqletiktkagetfgeekeaifeghimlle
deeleqeiialikdkhmtadaaaheviegqasaleelddeylkeraadvrdigkrllrni
lgl
>d1hiwa_ 1.61.1.1.1 HIV-1 matrix protein (HIV-1 MA, HIVp17, p17, MA) {Human immunodeficiency virus, type 1, HIV-1}
vlsggeldkwekirlrpggkkqyklkhivwasrelerfavnpglletsegcrqilgqlqp
slqtgseelrslyntiavlycvhqridvkdtkealdkieeeqnkskkkaqqaaad
>d1ed1a_ 1.61.1.1.2 SIV matrix antigen {Simian immunodeficiency virus}
svlsgkkadelekirlrpggkkkymlkhvvwaaneldrfglaesllenkegcqkilsvla
plvptgsenlkslyntvcviwcihaeekvkhteeakqivqrhlvvetgtaetmp
>d1jvr__ 1.61.1.2.1 HTLV-II matrix protein {Human t-cell leukemia virus type II, TTLV-II}
hmgqihglsptpipkaprglsthhwlnflqaayrlqpgpsdfdfqqlrrflklalktpiw
lnpidysllaslipkgypgrvveiinilvknqvspsapaapvptpicptttpppppppsp
eahvpppyveptttqcf
>d1bax__ 1.61.1.3.1 Mason-pfizer monkey virus matrix protein {Simian mason-pfizer virus, MPMV}
mgqelsqheryveqlkqalktrgvkvkyadllkffdfvkdtcpwfpqegtidikrwrrvg
dcfqdyyntfgpekvpvtafsywnlikelidkke
>d1a6s__ 1.61.1.4.1 GAG polyprotein M-domain {Rous sarcoma virus, RSV}
geavikvissacktycgktspskkeigamlsllqkegllmspsdlyspgswdpitaalsq
ramilgksgelktwglvlgalkaaree
>d1qgta_ 1.62.1.1.1 Hepatitis B viral capsid (hbcag) {Hepatitis B virus, HBV}
mdidpykefgatvellsflpsdffpsvrdlldtasalyrealespehcsphhtalrqail
cwgelmtlatwvgnnledpasrdlvvnyvntnmglkirqllwfhiscltfgretvleylv
sfgvwirtppayrppnapilst
>d1aep__ 1.63.1.1.1 Apolipophorin-III {African locust (Locusta migratoria)}
niaeavqqlnhtivnaahelhetlglptpdealnllteqanafktkiaevttslkqeaek
hqgsvaeqlnafarnlnnsihdaatslnlqdqlnslqsaltnvghqwqdiatktqasaqe
awapvqsalqeaaektkeaaanlqnsiqsavqk
>d1nkl__ 1.64.1.1.1 NK-lysin {Pig (Sus scrofa)}
gyfcescrkiiqkledmvgpqpnedtvtqaasqvcdklkilrglckkimrsflrriswdi
ltgkkpqaicvdikicke
>d1qdma1 1.64.1.2.1 (1s-104s) (Pro)phytepsin {Barley (Hordeum vulgare)}
vvsqecktivsqygqqildlllaetqpkkicsqvglctfdgtrgvsagirsvvddepvks
nglradpmcsacemavvwmqnqlaqnktqdlildyvnqlcnrlp
>d1bo9a_ 1.65.1.1.1 Annexin I {Human (Homo sapiens)}
tfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpldetlkkal
tghleevvlallk
>d1axn__ 1.65.1.1.2 Annexin III {Human (Homo sapiens)}
sasiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkey
qaaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttr
tsrqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaq
ilykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedll
laivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygysly
saiksdtsgdyeitllkicggdd
>d1a8a__ 1.65.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1aeia_ 1.65.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1azsc1 1.66.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gfngdgekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdf
dfppefyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrc
r
>d1tada1 1.66.1.1.1 (57-177) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
ysleeclefiaiiygntlqsilaivramttlniqygdsarqddarklmhmadtieegtmp
kemsdiiqrlwkdsgiqacfdraseyqlndsagyylsdlerlvtpgyvpteqdvlrsrvk
t
>d1cipa1 1.66.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1ezm_1 1.67.1.1.1 (154-298) Elastase {Pseudomonas aeruginosa}
iyrgqsggmneafsdmageaaefymrgkndfligydikkgsgalrymdqpsrdgrsidna
sqyyngidvhhssgvynrafyllanspgwdtrkafevfvdanryywtatsnynsgacgvi
rsaqnrnysaadvtrafstvgvtcp
>d1trla_ 1.67.1.1.2 Thermolysin {Bacillus thermoproteolyticus}
vvgigrdklgkifyraltqyltptsnfsqlraaavqsatdlygstsqevasvkqafdavg
vk
>d1trlb_ 1.67.1.1.2 Thermolysin {Bacillus thermoproteolyticus}
vvgigrdklgkifyraltqyltptsnfsqlraaavqsatdlygstsqevasvkqafdavg
vk
>d8tlne1 1.67.1.1.2 (156-316) Thermolysin {Bacillus thermoproteolyticus}
iyqnesgaineaisdifgtlvefyanknpdweigedvytpgisgdslrsmsdpakygdpd
hyskrytgtqdnggvhinsgiinkaaylisqggthygvsvvgigrdklgkifyraltqyl
tptsnfsqlraaavqsatdlygstsqevasvkqafdavgvk
>d1bqba1 1.67.1.1.4 (155-301) Aureolysin {Staphylococcus aureus}
anleykdqsgalnesfsdvfgyfvddedflmgedvytpgkegdalrsmsnpeqfgqpshm
kdyvytekdnggvhtnsgipnkaaynviqaigkskseqiyyralteyltsnsnfkdlkda
lyqaakdlyeqqtaeqvyeawnevgve
>d1tyae1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d1tybe1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d1tyc_1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d1tyde1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d2ts1_1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d3ts1_1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairis
>d4ts1a1 1.68.1.1.1 (228-319) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealrqairya
>d4ts1b1 1.68.1.1.1 (228-313) Tyrosyl-tRNA synthetase, middle domain {Bacillus stearothermophilus, nca 1503}
gtkfgktesgtiwldkektspyefyqfwintddrdvirylkyftflskeeiealeqelre
apekraaqktlaeevtklvhgeealr
>d1bmfa1 1.69.1.1.1 (380-510) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
tramkqvagtmklelaqyrevaafaqfgsdldaatqqllsrgvrltellkqgqyspmaie
eqvaviyagvrgyldklepskitkfenaflshvisqhqallgkirtdgkiseesdaklke
ivtnflagfea
>d1bmfd1 1.69.1.1.1 (358-475) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
mdpnivgsehydvargvqkilqdykslqdiiailgmdelseedkltvsrarkiqrflsqp
fqvaevftghlgklvplketikgfqqilageydhlpeqafymvgpieeavakadklae
>d1skyb1 1.69.1.1.3 (372-502) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
ikamkkvagtlrldlaayreleafaqfgsdldkatqanvargartvevlkqdlhqpipve
kqvliiyaltrgflddipvedvrrfekefylwldqngqhllehirttkdlpneddlnqai
eafkktfvvsq
>d1skye1 1.69.1.1.3 (357-470) C-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
eivgeehyqvarkvqqtlerykelqdiiailgmdelsdedklvvhrarriqfflsqnfhv
aeqftgqpgsyvpvketvrgfkeilegkydhlpedrfrlvgrieevvekakamg
>d1abv__ 1.70.1.1.1 N-terminal domain of the delta subunit of the F1F0-ATP synthase {Escherichia coli}
sefitvarpyakaafdfavehqsverwqdmlafaaevtkneqmaellsgalapetlaesf
iavcgeqldengqnlirvmaengrlnalpdvleqfihlravseat
>d1ak4c_ 1.71.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d2eiaa2 1.71.1.1.2 (17-147) EIAV capsid protein p26 {Equine infectious anemia virus, EIAV}
prgyttwvntiqtngllneasqnlfgilsvdctseemnafldvvpgqagqkqilldaidk
iaddwdnrhplpnaplvappqgpipmtarfirglgvprerqmepafdqfrqtyrqwiiea
msegikvmigk
>e1qrj.1b 1.71.1.1.3 (16-130) HTLV-I capsid protein {Human t-cell leukemia virus type i, HTLV-I}
qmkdlqaikqevsqaapgspqfmqtirlavqqfdptakdlqdllqylcsslvaslhhqql
dsliseaetrgitgynplagplrvqannpqqqglrreyqqlwlaafaalpgsakd
>d1d1da2 1.71.1.1.4 (11-150) RSV capsid protein {Rous sarcoma virus, RSV}
wtplepklitrladtvrtkglrspitmaevealmsspllphdvtnlmrvilgpapyalwm
dawgvqlqtviaaatrdprhpangqgrgertnldrlkgladgmvgnpqgqaallrpgelv
aitasalqafrevarlaepa
>d1vin_1 1.72.1.1.2 (181-308) Cyclin A {Bovine (Bos taurus)}
dihtylremevkckpkvgymkkqpditnsmrailvdwlvevgeeyklqnetlhlavnyid
rflssmsvlrgklqlvgtaamllaskfeeiyppevaefvyitddtytkkqvlrmehlvlk
vlafdlaa
>d1vin_2 1.72.1.1.2 (309-432) Cyclin A {Bovine (Bos taurus)}
ptinqfltqyflhqqpanckveslamflgelslidadpylkylpsviaaaafhlalytvt
gqswpeslvqktgytletlkpclldlhqtylrapqhaqqsirekyknskyhgvsllnppe
tlnl
>d1jkw_1 1.72.1.1.3 (11-161) Cyclin H (mcs2) {Human (Homo sapiens)}
wtfsseeqlarlradanrkfrckavangkvlpndpvflepheemtlckyyekrllefcsv
fkpamprsvvgtacmyfkrfylnnsvmeyhpriimltcaflackvdefnvsspqfvgnlr
esplgqekaleqileyellliqqlnfhlivh
>d1jkw_2 1.72.1.1.3 (162-287) Cyclin H (mcs2) {Human (Homo sapiens)}
npyrpfegflidlktrypilenpeilrktaddflnrialtdayllytpsqialtailssa
sragitmesylseslmlkenrtclsqlldimksmrnlvkkyepprseevavlkqkldrch
saelal
>d1bu2a1 1.72.1.1.4 (22-148) Viral cyclin {Herpes virus saimiri}
rvlnnlklrelllpkftslweiqtevtvdnrtilltwmhllcesfeldksvfplsvsild
rylckkqgtkktlqkigaacvligskirtvkpmtvskltylscdcftnlelinqekdile
alkwdte
>d1bu2a2 1.72.1.1.4 (149-250) Viral cyclin {Herpes virus saimiri}
avlatdfliplcnalkipedlwpqlyeaasttickaliqpniallspglicaggllttie
tdntncrpwtcyledlssilnfstntvrtvkdqvseafslyd
>d1c9ba1 1.72.1.2.1 (110-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
sdrammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacr
qegvprtfkeicavsriskkeigrcfklilkaletsvd
>d1c9be1 1.72.1.2.1 (110-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
sdrammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacr
qegvprtfkeicavsriskkeigrcfklilkaletsvd
>d1c9bi1 1.72.1.2.1 (110-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
sdrammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacr
qegvprtfkeicavsriskkeigrcfklilkaletsvd
>d1c9bm1 1.72.1.2.1 (110-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
sdrammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacr
qegvprtfkeicavsriskkeigrcfklilkaletsvd
>d1c9bq1 1.72.1.2.1 (110-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
sdrammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacr
qegvprtfkeicavsriskkeigrcfklilkaletsvd
>d1tfb_1 1.72.1.2.1 (111-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
srammnafkeittmadrinlprnivdrtnnlfkqvyeqkslkgrandaiasaclyiacrq
egvprtfkeicavsriskkeigrcfklilkaletsvd
>d1vola1 1.72.1.2.1 (113-207) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
ammnafkeittmadrinlprnkvdrtnnlfrqayeqkslkgrandaiasaclyiacrqeg
vprtfkeicavsriskkeigrcfklilkaletsvd
>d1vola2 1.72.1.2.1 (208-316) Transcription factor IIB (TFIIB), core domain {Human (Homo sapiens)}
littgdfmsrfcsnlclpkqvqmaathiarkaveldlvpgrspisvaaaaiymasqasae
krtqkeigdiagvadvtirqsyrliyprapdlfptdfkfdtpvdklpql
>d1aisb1 1.72.1.2.2 (1108-1205) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
nlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacvyaacrllk
vprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1aisb2 1.72.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1d3ub1 1.72.1.2.2 (1100-1205) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
mvsdaaernlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacv
yaacrllkvprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1d3ub2 1.72.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1guxa_ 1.72.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
ntiqqlmmilnsasdqpsenlisyfnnctvnpkesilkrvkdigyifkekfakavgqgcv
eigsqryklgvrlyyrvmesmlkseeerlsiqnfskllndnifhmsllacalevvmatys
rstsqnldsgtdlsfpwilnvlnlkafdfykviesfikaegnltremikhlercehrime
slawlsdsplfdlikqsk
>d1guxb_ 1.72.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
tslslfykkvyrlaylrlntlcerllsehpelehiiwtlfqhtlqneyelmrdrhldqim
mcsmygickvknidlkfkiivtaykdlphavqetfkrvlikeeeydsiivfynsvfmqrl
ktnilqyastrpptlspiphi
>d1hus__ 1.73.1.1.1 Ribosomal protein S7 {Bacillus stearothermophilus}
rdvlpdpiynsklvtrlinkixidgkkskaqkilytafdiirertgkdpxevfeqalknv
xpvlevrarrvgganyqvpvevrpdrrvslglrwlvqyarlrnektxeerlaneixdaan
ntgaavkkredthkxaean
>d1rss__ 1.73.1.1.2 Ribosomal protein S7 {Thermus thermophilus}
lqpdlvygdvlvtafinkimrdgkknlaarifydackiiqektgqeplkvfkqavenvkp
rmevrsrrvgganyqvpmevsprrqqslalrwlvqaanqrperraavriahelmdaaegk
ggavkkkedvermaeanrayahyrw
>d1bi0_2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi1_2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi2a2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi2b2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi3a2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1bi3b2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeaxrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d1ddna2 1.74.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnb2 1.74.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnc2 1.74.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1ddnd2 1.74.1.1.1 (65-120) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvl
>d1dpra2 1.74.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d1dprb2 1.74.1.1.1 (65-136) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgld
>d2dtr_2 1.74.1.1.1 (65-140) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeacrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelgv
>d2tdx_2 1.74.1.1.1 (65-139) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
tptgrtlatavmrkhrlaerlltdiigldinkvhdeadrwehvmsdeverrlvkvlkdvs
rspfgnpipgldelg
>d1b1ba2 1.74.1.1.2 (65-140) Iron-dependent regulator {Mycobacterium tuberculosis}
tekgralaiavmrkhrlaerllvdviglpweevhaeacrwehvmsedverrlvkvlnnpt
tspfgnpipglvelgv
>d1ngr__ 1.75.1.1.1 p75 low affinity neurotrophin receptor {Rat (Rattus norvegicus)}
gnlysslpltkreevekllngdtwrhlagelgyqpehidsftheacpvrallaswgaqds
atldallaalrriqradiveslcse
>d1ddf__ 1.75.1.1.2 Fas {Human (Homo sapiens)}
metvainlsdvdlskyittiagvmtlsqvkgfvrkngvneakideikndnvqdtaeqkvq
llrnwhqlhgkkeaydtlikdlkkanlctlaekiqtiilkditsdsensnfrneiqslvl
ehhhhhh
>d1a1w__ 1.75.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkylclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1a1z__ 1.75.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkglclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1fada_ 1.75.1.1.4 FADD (Mort1) {Mouse (Mus musculus)}
aappgeaylqvafdivcdnvgrdwkrlarelkvseakmdgieekyprslservreslkvw
knaekknasvaglvkalrtcrlnlvadlveeaqes
>d3crd__ 1.75.1.1.5 Raidd CARD domain {Human (Homo sapiens)}
meardkqvlrslrlelgaevlveglvlqylyqegiltenhiqeinaqttglrktmllldi
lpsrgpkafdtfldslqefpwvreklkkareeamtdlpag
>d1c15a_ 1.75.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
mdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraamlikmi
lkkdndsyvsfynallhegykdlaallhdgipvvsss
>d1cwwa_ 1.75.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
gplgsmdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraam
likmilkkdndsyvsfynallhegykdlaallhdgipvvsss
>d1cy5a_ 1.75.1.1.6 Apoptotic protease activating factor 1, APAF-1 {Human (Homo sapiens)}
mdakarncllqhrealekdiktsyimdhmisdgfltiseeekvrneptqqqraamlikmi
lkkdndsyvsfynallhegykdlaallhdgipv
>d1d2za_ 1.75.1.1.7 Pelle death domain {Drosophila melanogaster}
ldntmairllplpvraqlcahldaldvwqqlatavklypdqveqissqkqrgrsasnefl
niwggqynhtvqtlfalfkklklhnamrlikdyvsedlhkyi
>d1d2zb_ 1.75.1.1.8 Tube death domain {Drosophila melanogaster}
lsskysrntelrrvedndiyrlakildenscwrklmsiipkgmdvqacsgagclnfpaei
kkgfkytaqdvfqideaanrlppdqsksqmmidewktsgklnerptvgvllqllvqaelf
saadfvaldflnestparpvdgpgalisle
>d1baq__ 1.76.1.1.1 Antitermination factor NusB {Escherichia coli}
mkpaarrrarecavqalyswqlsqndiadveyqflaeqdvkdvdvlyfrellagvatnta
yldglmkpylsrlleelgqvekavlrialyelskrsdvpykvaineaielaksfgaedsh
kfvngvldkaapvirpnkk
>d1b79a_ 1.77.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1qc7a_ 1.78.1.1.1 FliG C-terminal domain {Thermotoga maritima}
mfvfedilklddrsiqlvlrevdtrdlalalkgasdelkekifknmskraaallkdeley
mgpvrlkdveeaqqkiiniirrleeageiviargggeelim
>d1qc7b_ 1.78.1.1.1 FliG C-terminal domain {Thermotoga maritima}
mfvfedilklddrsiqlvlrevdtrdlalalkgasdelkekifknmskraaallkdeley
mgpvrlkdveeaqqkiiniirrleeageiv
>d1crka1 1.79.1.1.1 (1-98) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), mitochondria}
tvhekrklfppsadypdlrkhnncmaecltpaiyaklrdkltpngysldqciqtgvdnpg
hpfiktvgmvagdeesyevfaeifdpvikarhngydpr
>d1qh4a1 1.79.1.1.2 (2-102) Creatine kinase, N-terminal domain {Chicken (Gallus gallus), brain-type}
pfsnshnllkmkysvddeypdlsvhnnhmakvltldlykklrdrqtssgftlddviqtgv
dnpghpfimtvgcvagdeesyevfkelfdpviedrhggykp
>d2crka1 1.79.1.1.3 (8-102) Creatine kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
nkyklnykseeeypdlskhnnhmakvltpdlykklrdketpsgftlddviqtgvdnpghp
fimtvgcvagdeesytvfkdlfdpiiqdrhggfkp
>d1bg0_1 1.79.1.1.4 (2-95) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
vdqatldkleagfkklqeasdcksllkkhltkdvfdsiknkktgmgatlldviqsgvenl
dsgvgiyapdaesyrtfgplfdpiiddyhggfkl
>d1al01_ 1.80.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1lla_1 1.81.1.1.1 (2-109) Hemocyanin, N-terminal domain {Limulus polyphemus}
lhdkqirichlfeqlssatvigdgdkhkhsdrlknvgklqpgaifscfhpdhleearhly
evfweagdfndfieiakeartfvneglfafaaevavlhrddckglyvp
>d1hc2_1 1.81.1.1.2 (5-135) Hemocyanin, N-terminal domain {Spiny lobster (Panulirus interruptus)}
tgnaqkqqdinhlldkiyeptkypdlkdiaenfnplgdtsiyndhgaavetlmkelndhr
lleqrhwyslfntrqrkealmlfavlnqckewycfrsnaayfrermnegefvyalyvsvi
hsklgdgivlp
>d1lla_2 1.82.1.1.1 (110-379) Hemocyanin, middle domain {Limulus polyphemus}
pvqeifpdkfipsaaineafkkahvrpefdespilvdvqdtgnildpeyrlayyredvgi
nahhwhwhlvypstwnpkyfgkkkdrkgelfyymhqqmcarydcerlsngmhrmlpfnnf
deplagyaphlthvasgkyysprpdglklrdlgdieisemvrmrerildsihlgyvised
gshktldelhgtdilgalvessyesvnheyygnlhnwghvtmarihdpdgrfheepgvms
dtstslrdpifynwhrfidnifheykntlk
>d1hc2_2 1.82.1.1.2 (136-398) Hemocyanin, middle domain {Spiny lobster (Panulirus interruptus)}
plyqitphmftnsevidkaysakmtqkpgtfnvsftgtkknreqrvayfgedigmnihhv
twhmdfpfwwedsygyhldrkgelffwvhhqltarfdferlsnwldpvdelhwdriireg
fapltsykyggefpvrpdnihfedvdgvahvhdleitesriheaidhgyitdsdghtidi
rqpkgiellgdiiesskyssnvqyygslhntahvmlgrqgdphgkfnlppgvmehfetat
rdpsffrlhkymdnifkkhtdsf
>d1bt3a_ 1.82.1.2.1 Catechol oxidase {Sweet potato (Ipomoea batatas)}
apiqapeiskcvvppadlppgavvdnccppvasnivdyklpavttmkvrpaahtmdkdai
akfakavelmkalpaddprnfyqqalvhcaycnggydqvnfpdqeiqvhnswlffpfhrw
ylyfyerilgkligdpsfglpfwnwdnpggmvlpdflndstsslydsnrnqshlppvvvd
lgyngadtdvtdqqritdnlalmykqmvtnagtaelflgkayragdapspgagsietsph
ipihrwvgdprntnnedmgnfysagrdiafychhsnvdrmwtiwqqlagkprkrdytdsd
wlnatflfydengqavkvrigdsldnqkmgykyaktplpwl
>d1dbha1 1.83.1.1.1 (198-404) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
eqtyydlvkafxaeirqyirelnliikvfrepfvsnsklfsandvenifsrivdihelsv
kllghiedtvextdegsphplvgscfedlaeelafdpyesyardilrpgfhdrflsqlsk
pgaalylqsigegfkeavqyvlprlllapvyhclhyfellkqleeksedqedkeclkqai
tallnvqsgxekicskslakrrlsesa
>d1by1a_ 1.83.1.1.2 beta-pix {Human (Homo sapiens) |A|}
mkgfdttainksyynvvlqnileteneyskelqtvlstylrplqtseklssanisylmgn
leeicsfqqmlvqsleectklpeaqqrvggcflnlmpqmktlyltycanhpsavnvlteh
seelgefmetkgasspgilvlttglskpfmrldkyptllkelerhmedyhtdrqdiqksm
aafknlsaqcqevrkrkelelqilteair
>d1boua_ 1.84.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1mroa1 1.85.1.1.1 (270-549) Alpha chain {Methanobacterium thermoautotrophicum}
rxargenepggvpfgyladicqssrvnyedpvrvsldvvatgamlydqiwlgsymsggvg
ftqyataaytdnilddftyfgkeyvedkyglceapnnmdtvldvatevtfygleqyeeyp
alledqfggsxraavvaaaagcstafatgnaqtglsgwylsmylhkeqhsrlgfyxydlq
dqxgasnvfsirgdeglplelrgpnypnyamnvghqgeyagisqaphaargdafvfnplv
kiafaddnlvfdftnvrgefakgalrefepageralitpa
>d1mrob1 1.85.1.1.2 (189-443) Beta chain {Methanobacterium thermoautotrophicum}
gyalrnimvnhvvaatlkntlqaaalstileqtamfemgdavgafermhllglayqgmna
dnlvfdlvkangkegtvgsviadlveraledgvikvekeltdykvygtddlamwnayaaa
glmaatmvnqgaaraaqgvsstllyyndliefetglpsvdfgkvegtavgfsffshsiyg
gggpgifngnhivtrhskgfaipcvaaamaldagtqmfspeatsglikevfsqvdefrep
lkyvveaaaeiknei
>d1bgf__ 1.86.1.1.1 Transcription factor STAT-4 N-domain {Mouse (Mus musculus)}
ggsqwnqvqqleikfleqvdqfyddnfpmeirhllaqwietqdwevasnnetmatillqn
lliqldeqlgrvskeknlllihnlkrirkvlqgkfhgnpmhvavvisnclreerrilaaa
nmpi
>d1agre_ 1.87.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
vsqeevkkwaeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspk
akkiynefisvqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflk
srfyldlt
>d1cmza_ 1.87.1.1.2 Galpha interacting protein, GaIP {Human (Homo sapiens)}
pspeevqswaqsfdklmhspagrsvfraflrteyseenmlfwlaceelkaeanqhvvdek
arliyedyvsilspkevsldsrvreginkkmqepsahtfddaqlqiytlmhrdsyprfls
sptyrall
>d1a9xa1 1.88.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1aru__ 1.89.1.1.2 Peroxidase {Arthromyces ramosus}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1ryc__ 1.89.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1apxa_ 1.89.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d7atja_ 1.89.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvn
>e1mhl.1a 1.89.1.2.1 Myeloperoxidase {Human (Homo sapiens)}
cpeqdkyrtitgmcnnrrsptlgasnrafvrwlpaeyedgfslpygwtpgvkrngfpval
aravsneivrfptdqltpdqerslmfmqwgqlldhdldftpepa
>e1mhl.1c 1.89.1.2.1 Myeloperoxidase {Human (Homo sapiens)}
vncetscvqqppcfplkippndpriknqadcipffrscpacpgsnitirnqinaltsfvd
asmvygseeplarnlrnmsnqlgllavnqrfqdngrallpfdnlhddpclltnrsaripc
flagdtrssempeltsmhtlllrehnrlatelkslnprwdgerlyqearkivgamvqiit
yrdylplvlgptamrkylptyrsyndsvdprianvftnafryghtliqpfmfrldnryqp
mepnprvplsrvffaswrvvleggidpilrglmatpaklnrqnqiavdeirerlfeqvmr
igldlpalnmqrsrdhglpgynawrrfcglpqpetvgqlgtvlrnlklarklmeqygtpn
nidiwmggvseplkrkgrvgpllaciigtqfrklrdgdrfwwenegvfsmqqrqalaqis
lpriicdntgittvsknnifmsnsyprdfvncstlpalnlaswrea
>d1cqea1 1.89.1.2.3 (74-583) Prostaglandin H2 synthase-1 {Sheep (Ovis aries)}
iwtwlrttlrpspsfihfllthgrwlwdfvnatfirdtlmrlvltvrsnlipspptynia
hdyiswesfsnvsyytrilpsvprdcptpmgtkgkkqlpdaeflsrrfllrrkfipdpqg
tnlmfaffaqhfthqffktsgkmgpgftkalghgvdlghiygdnlerqyqlrlfkdgklk
yqmlngevyppsveeapvlmhyprgippqsqmavgqevfgllpglmlyatiwlrehnrvc
dllkaehptwgdeqlfqtarliligetikivieeyvqqlsgyflqlkfdpellfgaqfqy
rnriamefnqlyhwhplmpdsfrvgpqdysyeqflfntsmlvdygvealvdafsrqpagr
igggrnidhhilhvavdvikesrvlrlqpfneyrkrfgmkpytsfqeltgekemaaelee
lygdidalefypglllekchpnsifgesmiemgapfslkgllgnpicspeywkastfgge
vgfnlvktatlkklvclntktcpyvsfhvp
>d1aa7a_ 1.90.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
mslltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgil
gfvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsys
agalascmgliynrmgavttevafglvcatceqiadsq
>d2abk__ 1.91.1.1.1 Endonuclease III {Escherichia coli}
mnkakrleiltrlrennphpttelnfsspfelliavllsaqatdvsvnkataklypvant
paamlelgvegvktyiktiglynskaeniiktcrilleqhngevpedraalealpgvgrk
tanvvlntafgwptiavdthifrvcnrtqfapgknveqveekllkvvpaefkvdchhwli
lhgrytciarkprcgsciiedlceykekvdi
>d1mun__ 1.91.1.2.1 Catalytic domain of MutY {Escherichia coli}
mqasqfsaqvldwydkygrktlpwqidktpykvwlsevmlqqtqvatvipyferfmarfp
tvtdlanapldevlhlwtglgyyararnlhkaaqqvatlhggkfpetfeevaalpgvgrs
tagailslslgkhfpilngnvkrvlarcyavsgwpgkkevenklwslseqvtpavgverf
nqammdlgamictrskpkcslcplqngciaaannswalypgkkpk
>d1mpga1 1.91.1.3.1 (100-282) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), 2 C-terminal domains {Escherichia coli}
aarpglrlpgcvdafeqgvrailgqlvsvamaakltarvaqlygerlddfpeyicfptpq
rlaaadpqalkalgmplkraealihlanaalegtlpmtipgdveqamktlqtfpgigrwt
anyfalrgwqakdvflpddylikqrfpgmtpaqirryaerwkpwrsyallhiwytegwqp
dea
>d1gln_1 1.92.1.1.1 (306-468) Anticodon-binding (C-terminal) domain of glutamyl-tRNA synthetase (GluRS) {Thermus thermophilus}
dleklrwmngkyirevlsleevaervkpflreaglsweseaylrravelmrprfdtlkef
pekarylftedypvsekaqrkleeglpllkelyprlraqeewteaaleallrgfaaekgv
klgqvaqplraaltgsletpglfeilallgkeralrrlerala
>d1rlr_1 1.93.1.1.1 (10-221) R1 subunit of ribonucleotide reductase, N-terminal domain {Escherichia coli}
rdgsterinldkihrvldwaaeglhnvsisqvelrshiqfydgiktsdihetiikaaadl
isrdapdyqylaarlaifhlrkkaygqfeppalydhvvkmvemgkydnhlledyteeefk
qmdtfidhdrdmtfsyaavkqlegkylvqnrvtgeiyesaqflyilvaaclfsnypretr
lqyvkrfydavstfkislptpimsgvrtptrq
>d1qnf_1 1.94.1.1.2 (205-475) FAD-binding (C-terminal) domain of DNA photolyase {Anacystis nidulans}
pvepgetaaiarlqefcdraiadydpqrnfpaeagtsglspalkfgaigirqawqaasaa
halsrsdearnsirvwqqelawrefyqhalyhfpsladgpyrslwqqfpwenrealftaw
tqaqtgypivdaamrqltetgwmhnrcrmivasfltkdliidwrrgeqffmqhlvdgdla
annggwqwsassgmdpkplrifnpasqakkfdatatyikrwlpelrhvhpkdlisgeitp
ierrgypapivnhnlrqkqfkalynqlkaai
>d2pgd_1 1.95.1.1.1 (177-473) 6-phosphogluconate dehydrogenase (6PGD) {Sheep (Ovis orientalis aries)}
gaghfvkmvhngieygdmqliceayhlmkdvlglghkemakafeewnkteldsflieita
silkfqdadgkhllpkirdsagqkgtgkwtaisaleygvpvtligeavfarclsslkder
iqaskklkgpqnipfegdkksfledirkalyaskiisyaqgfmllrqaatefgwtlnygg
ialmwrggciirsvflgkikdafdrnpglqnlllddffksavencqdswrraistgvqag
ipmpcfttalsfydgyrhamlpanliqaqrdyfgahtyellakpgqfihtnwtghgg
>d1pgja1 1.95.1.1.2 (179-478) 6-phosphogluconate dehydrogenase (6PGD) {Trypanosoma brucei}
gagscvkmyhnsgeyailqiwgevfdilramglnndevaavledwksknflksymldisi
aaarakdkdgsyltehvmdrigskgtglwsaqealeigvpapslnmavvsrqftmykter
qanasnapgitqspgytlknkspsgpeikqlydsvciaiiscyaqmfqclremdkvhnfg
lnlpatiatfragcilqgyllkpmteafeknpnisnlmcafqteiraglqnyrdmvalit
sklevsipvlsaslnyvtamftptlkygqlvslqrdvfgrhgyervdkdgresfqwpelq
>d1yvei1 1.95.1.2.1 (308-595) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) {Spinach (Spinacia oleracea)}
leqeyksdifgergillgavhgiveclfrrytesgmsedlaykntvecitgvisktistk
gmlalynslseegkkdfqaaysasyypsmdilyecyedvasgseirsvvlagrrfyekeg
lpafpmgkidqtrmwkvgekvrsvrpagdlgplypftagvyvalmmaqieilrkkghsys
eiinesvieavdslnpfmhargvsfmvdncsttarlgsrkwaprfdyilsqqalvavdng
apinqdlisnflsdpvheaigvcaqlrpsvdisvtadadfvrpelrqa
>d2hdha1 1.95.1.3.1 (204-304) Short chain L-3-hydroxyacyl CoA dehydrogenase {Human (Homo sapiens)}
gfivnrllvpylxeairlyergdaskedidtaxklgagypxgpfelldyvgldttkfivd
gwhexdaenplhqpspslnklvaenkfgkktgegfykykaa
>d3hdha1 1.95.1.3.2 (204-302) Short chain L-3-hydroxyacyl CoA dehydrogenase {Pig (Sus scrofa)}
gfivnrllvpylieavrlyergdaskedidtamklgagypmgpfelldyvgldttkfiid
gwhemdsqnplfqpspamnklvaenkfgkktgegfykyk
>d3hdhc1 1.95.1.3.2 (204-295) Short chain L-3-hydroxyacyl CoA dehydrogenase {Pig (Sus scrofa)}
gfivnrllvpylieavrlyergdaskedidtamklgagypmgpfelldyvgldttkfiid
gwhemdsqnplfqpspamnklvaenkfgkktg
>d1bg6_1 1.95.1.4.1 (188-359) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
nvlhtsltnvnavmhplptllnaarcesgtpfqyylegitpsvgslaekvdaeriaiaka
fdlnvpsvcewykesygqspatiyeavqgnpayrgiagpinlntryffedvstglvplse
lgravnvptplidavldlisslidtdfrkegrtleklglsgltaagirsave
>d1utg__ 1.96.1.1.1 Uteroglobin {Rabbit (Oryctolagus cuniculus)}
gicprfahvienlllgtpssyetslkefepddtmkdagmqmkkvldslpqttrenimklt
ekivksplcm
>d2utga_ 1.96.1.1.1 Uteroglobin {Rabbit (Oryctolagus cuniculus)}
gicprfahvienlllgtpssyetslkefepddtmkdagmqmkkvldslpqttrenimklt
ekivksplcm
>d2utgb_ 1.96.1.1.1 Uteroglobin {Rabbit (Oryctolagus cuniculus)}
gicprfahvienlllgtpssyetslkefepddtmkdagmqmkkvldslpqttrenimklt
ekivksplcm
>d1ccd__ 1.96.1.1.2 Clara cell 17kDa protein {Rat (Rattus rattus)}
ssdicpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivk
ltekiltsplceqdlrv
>d1utra_ 1.96.1.1.2 Clara cell 17kDa protein {Rat (Rattus rattus)}
icpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivklte
kiltsplc
>d1utrb_ 1.96.1.1.2 Clara cell 17kDa protein {Rat (Rattus rattus)}
icpgflqvlealllgsesnyeaalkpfnpasdlqnagtqlkrlvdtlpqetrinivklte
kiltsplc
>d1gai__ 1.97.1.1.1 Glucoamylase {Aspergillus awamori, variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsivatg
>d1cem__ 1.97.1.2.1 CelA cellulase {Clostridium thermocellum}
agvpfntkypygptsiadnqsevtamlkaewedwkskritsngaggykrvqrdastnydt
vsegmgyglllavcfneqalfddlyryvkshfngnglmhwhidannnvtshdggdgaatd
adedialalifadkqwgssgainygqeartlinnlynhcvehgsyvlkpgdrwggssvtn
psyfapawykvyaqytgdtrwnqvadkcyqiveevkkynngtglvpdwctasgtpasgqs
ydykydatrygwrtavdyswfgdqrakancdmltkffardgakgivdgytiqgskisnnh
nasfigpvaaasmtgydlnfakelyretvavkdseyygyygnslrlltllyitgnfpnpl
sdl
>d1tf4a1 1.97.1.2.2 (1-460) Endo/exocellulase:cellobiose E-4, N-terminal domain {Thermomonospora fusca}
epafnyaealqksmffyeaqrsgklpennrvswrgdsglndgadvgldltggwydagdhv
kfgfpmaftatmlawgaiespegyirsgqmpylkdnlrwvndyfikahpspnvlyvqvgd
gdadhkwwgpaevmpmerpsfkvdpscpgsdvaaetaaamaassivfadddpayaatlvq
hakqlytfadtyrgvysdcvpagafynswsgyqdelvwgaywlykatgddsylakaeyey
dflsteqqtdlrsyrwtiawddksygtyvllaketgkqkyiddanrwldywtvgvngqrv
pyspggmavldtwgalryaantafvalvyakviddpvrkqryhdfavrqinyalgdnprn
ssyvvgfgnnpprnphhrtahgswtdsiaspaenrhvlygalvggpgspndaytddrqdy
vanevatdynagfssalamlveeyggtpladfppteepdg
>d1clc_1 1.97.1.2.3 (135-575) CelD cellulase {Clostridium thermocellum}
amnvyedafktamlgmyllrcgtsvsatyngihyshgpchtndayldyingqhtkkdstk
gwhdagdynkyvvnagitvgsmflawehfkdqlepvaleipeknnsipdfldelkyeidw
iltmqypdgsgrvahkvstrnfggfimpenehderffvpwssaatadfvamtamaarifr
pydpqyaekcinaakvsyeflknnpanvfanqsgfstgeyatvsdaddrlwaaaemwetl
gdeeylrdfenraaqfskkieadfdwdnvanlgmftyllserpgknpalvqsikdsllst
adsivrtsqnhgygrtlgttyywgcngtvvrqtmilqvankispnndyvnaaldaishvf
grnyynrsyvtglginppmnphdrrsgadgiwepwpgylvgggwpgpkdwvdiqdsyqtn
eiainwnaaliyalagfvnyn
>d1fce__ 1.97.1.2.4 Processive endocellulase CelF {Clostridium cellulolyticum}
asspankvyqdrfesmyskikdpangyfseqgipyhsietlmveapdyghvttseamsyy
mwleamhgrfsgdftgfdkswsvteqyliptekdqpntsmsrydankpatyapefqdpsk
ypspldtsqpvgrdpinsqltsaygtsmlygmhwildvdnwygfgaradgtskpsyintf
qrgeqestwetipqpcwdehkfggqygfldlftkdtgtpakqfkytnapdadaravqaty
wadqwakeqgksvstsvgkatkmgdylrysffdkyfrkigqpsqagtgydaahyllswyy
awgggidstwswiigsshnhfgyqnpfaawvlstdanfkpkssngasdwaksldrqlefy
qwlqsaegaiaggatnswngryeavpsgtstfygmgyvenpvyadpgsntwfgmqvwsmq
rvaelyyktgdarakklldkwakwingeikfnadgtfqipstidwegqpdtwnptqgytg
nanlhvkvvnygtdlgcasslantltyyaaksgdetsrqnaqklldamwnnysdskgist
veqrgdyhrfldqevfvpagwtgkmpngdviksgvkfidirskykqdpewqtmvaalqag
qvptqrlhrfwaqsefavangvyailfpd
>d1dl2a_ 1.97.2.1.1 Class I alpha-1;2-mannosidase, catalytic domain {Baker's yeast (Saccharomyces cerevisiae)}
gagemrdriesmfleswrdyskhgwgydvygpiehtshnmprgnqplgwiivdsvdtlml
mynsstlyksefeaeiqrsehwindvldfdidaevnvfettirmlggllsayhlsdvlev
gnktvylnkaidlgdrlalaflstqtgipyssinlhsgqavknhadggasstaefttlqm
efkylayltgnrtywelvervyeplyknndllntydglvpiytfpdtgkfgastirfgsr
gdsfyeyllkqyllthetlyydlyrksmegmkkhllaqskpsslwyigereqglhgqlsp
kmdhlvcfmggllasgsteglsihearrrpffslslerksdwdlakgitdtcyqmykqss
sglapeivvfndgnikqdgwwrssvgdffvkpldrhnlqrpetvesimfmyhlshdhkyr
ewgaeiatsffentcvdcndpklrrftslsdcitlptkksnnmesfwlaetlkylyilfl
defdltkvvfnteahpfpvldeeilksqslttgwsl
>d1qaza_ 1.97.3.1.1 Alginate lyase A1-III {Sphingomonas, sp. A1}
gshpfdqavvkdptasyvdvkarrtflqsgqlddrlkaalpkeydctteatpnpqqgemv
iprrylsgnhgpvnpdyepvvtlyrdfekisatlgnlyvatgkpvyatcllnmldkwaka
dallnydpksqswyqvewsaataafalstmmaepnvdtaqrervvkwlnrvarhqtsfpg
gdtsccnnhsywrgqeatiigviskddelfrwglgryvqamglinedgsfvhemtrheqs
lhyqnyamlpltmiaetasrqgidlyaykengrdihsarkfvfaavknpdlikkyasepq
dtrafkpgrgdlnwieyqrarfgfadelgfmtvpifdprtggsatllaykp
>d1cb8a1 1.97.3.2.1 (26-335) Chondroitinase AC, N-terminal domain {Flavobacterium heparinum}
gtaelimkrvmldlkkplrnmdkvaeknlntlqpdgswkdvpykddamtnwlpnnhllql
etiiqayiekdshyygddkvfdqiskafkywydsdpksrnwwhneiatpqalgemlilmr
ygkkpldealvhkltermkrgepekktganktdialhyfyralltsdeallsfavkelfy
pvqfvhyeeglqydysylqhgpqlqissygavfitgvlklanyvrdtpyalsteklaifs
kyyrdsylkairgsymdfnvegrgvsrpdilnkkaekkrllvakmidlkhteewadaiar
tdstvaagyk
>d5eau_1 1.97.4.1.1 (21-220) 5-Epi-aristolochene synthase, N-terminal domain {Tobacco (Nicotiana tabacum)}
spslwgdqflsfsidnqvaekyakeiealkeqtrnmllatgmkladtlnlidtierlgis
yhfekeiddildqiynqnsncndlctsalqfrllrqhgfnispeifskfqdengkfkesl
asdvlgllnlyeashvrthaddiledalafstihlesaaphlksplreqvthaleqclhk
gvprvetrffissiydkeqs
>d2sqca1 1.97.4.2.1 (8-36,308-630) Squalene-hopene cyclase {Alicyclobacillus acidocaladarius}
apayartldraveyllscqkdegywwgplXispvwdtglavlalraaglpadhdrlvkag
ewlldrqitvpgdwavkrpnlkpggfafqfdnvyypdvcdtavvvwalntlrlpderrrr
damtkgfrwivgmqssnggwgaydvdntsdlpnhipfsdfgevtdppsedvtahvlecfg
sfgyddawkvirraveylkreqkpdgswfgrwgvnylygtgavvsalkavgidtrepyiq
kaldwveqhqnpdggwgedcrsyedpayagkgastpsqtawalmaliaggraeseaarrg
vqylvetqrpdggwdepyytgtgfpgdfylgytmyrhvfptlalgrykqaier
>d2sqca2 1.97.4.2.1 (37-307) Squalene-hopene cyclase {Alicyclobacillus acidocaladarius}
lsnvtmeaeyvllchildrvdrdrmekirryllheqredgtwalypggppdldttieayv
alkyigmsrdeepmqkalrfiqsqggiessrvftrmwlalvgeypwekvpmvppeimflg
krmplniyefgswaratvvalsivmsrqpvfplperarvpelyetdvpprrrgakggggw
ifdaldralhgyqklsvhpfrraaeiraldwllerqagdgswggiqppwfyalialkild
mtqhpafikgweglelygveldyggwmfqas
>d1d8db_ 1.97.4.3.1 Protein farnesyltransferase, beta-subunit {Rat (Rattus norvegicus)}
pvwseplyslrpeharerlqddsvetvtsieqakveekiqevfssykfnhlvprlvlqre
khfhylkrglrqltdayecldasrpwlcywilhslelldepipqivatdvcqflelcqsp
dggfgggpgqyphlaptyaavnalciigteeaynvinrekllqylyslkqpdgsflmhvg
gevdvrsaycaasvasltniitpdlfegtaewiarcqnweggiggvpgmeahggytfcgl
aalvilkkerslnlksllqwvtsrqmrfeggfqgrcnklvdgcysfwqagllpllhralh
aqgdpalsmshwmfhqqalqeyilmccqcpagglldkpgksrdfyhtcyclsglsiaqhf
gsgamlhdvvmgvpenvlqpthpvynigpdkviqatthflqkpvpgf
>d1c3d__ 1.97.4.4.1 C3D, a C3 fragment and ligand for complement receptor 2 {Human (Homo sapiens)}
mldaerlkhlivtpsgageqnmigmtptviavhyldeteqwekfglekrqgalelikkgy
tqqlafrqpssafaafvkrapstwltayvvkvfslavnliaidsqvlcgavkwlilekqk
pdgvfqedapvihqemigglrnnnekdmaltafvlislqeakdiceeqvnslpgsitkag
dfleanymnlqrsytvaiagyalaqmgrlkgpllnkflttakdknrwedpgkqlynveat
syallallqlkdfdfvppvvrwlneqryygggygstqatfmvfqalaqyqkdap
>d1csh__ 1.98.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1aj8a_ 1.98.1.1.3 Citrate synthase {Pyrococcus furiosus}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielrr
>d1phb__ 1.99.1.1.1 Cytochrome P450 {Pseudomonas putida}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqelierperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1bu7a_ 1.99.1.1.2 Cytochrome P450 {Bacillus megaterium}
tikempqpktfgelknlpllntdkpvqalmkiadelgeifkfeapgrvtrylssqrlike
acdesrfdknlsqalkfvrdfagdglftswtheknwkkahnillpsfsqqamkgyhammv
diavqlvqkwerlnadehievpedmtrltldtiglcgfnyrfnsfyrdqphpfitsmvra
ldeamnklqranpddpaydenkrqfqedikvmndlvdkiiadrkasgeqsddllthmlng
kdpetgeplddeniryqiitfliaghettsgllsfalyflvknphvlqkaaeeaarvlvd
pvpsykqvkqlkyvgmvlnealrlwptapafslyakedtvlggeyplekgdelmvlipql
hrdktiwgddveefrperfenpsaipqhafkpfgngqracigqqfalheatlvlgmmlkh
fdfedhtnyeldiketltlkpegfvvkakskkipl
>d2rom__ 1.99.1.1.3 Cytochrome P450-NOR, nitric reductase {Fungus (Fusarium oxysporum)}
apsfpfsrasgpeppaefaklratnpvsqvklfdgslawlvtkhkdvcfvatseklskvr
trqgfpelsasgkqaakakptfvdmdppehmhqrsmveptftpeavknlqpyiqrtvddl
leqmkqkgcangpvdlvkefalpvpsyiiytllgvpfndleyltqqnairtngsstarea
saanqelldylailveqrlvepkddiisklcteqvkpgnidksdavqiaflllvagnatm
vnmialgvatlaqhpdqlaqlkanpslapqfveelcryhtasalaikrtakedvmigdkl
vranegiiasnqsanrdeevfenpdefnmnrkwppqdplgfgfgdhrciaehlakaeltt
vfstlyqkfpdlkvavplgkinytplnrdvgivdlpvif
>d1oxa__ 1.99.1.1.4 Cytochrome P450-ERYF {Saccarapolyspora erythraea}
atvpdlesdsfhvdwystyaelretapvtpvrflgqdawlvtgydeakaalsdlrlssdp
kkkypgvevefpaylgfpedvrnyfatnmgtsdppthtrlrklvsqeftvrrveamrprv
eqitaelldevgdsgvvdivdrfahplpikvicellgvdeaargafgrwsseilvmdper
aeqrgqaarevvnfildlverrrtepgddllsalisvqddddgrlsadeltsialvllla
gfeasvsligigtylllthpdqlalvradpsalpnaveeilryiappetttrfaaeevei
ggvaipqystvlvangaanrdpsqfpdphrfdvtrdtrghlsfgqgihfcmgrplakleg
evalralfgrfpalslgidaddvvwrrslllrgidhlpvrldg
>d1cpt__ 1.99.1.1.5 Cytochrome P450-TERP {Pseudomonas}
mdaratipehiartvilpqgyaddeviypafkwlrdeqplamahiegydpmwiatkhadv
mqigkqpglfsnaegseilydqnneafmrsisggcphvidsltsmdppthtayrgltlnw
fqpasirkleenirriaqasvqrlldfdgecdfmtdcalyyplhvvmtalgvpeddeplm
lkltqdffgveaarrfhetiatfydyfngftvdrrscpkddvmsllanskldgnyiddky
inayyvaiataghdttssssggaiiglsrnpeqlalaksdpaliprlvdeavrwtapvks
fmrtaladtevrgqnikrgdrimlsypsanrdeevfsnpdefditrfpnrhlgfgwgahm
clgqhlaklemkiffeellpklksvelsgpprlvatnfvggpknvpirftka
>d1f36a_ 1.100.1.1.1 FIS protein {Escherichia coli}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1f36b_ 1.100.1.1.1 FIS protein {Escherichia coli}
vltvstvnsqdqvtqkplrdsvkqalenyfaqlngqdvndlyelvlaeveqplldmvmqy
trgnqtraalmmginrgtlrkklkkygmn
>d1fiaa_ 1.100.1.1.1 FIS protein {Escherichia coli}
qkplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmgi
nrgtlrkklkkygmn
>d1fiab_ 1.100.1.1.1 FIS protein {Escherichia coli}
kplrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmgin
rgtlrkklkkygmn
>d1fipa_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqalldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d1fipb_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqalldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d3fisa_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d3fisb_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmginr
gtlrkklkkygmn
>d4fisa_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmginr
gtlckklkkygmn
>d4fisb_ 1.100.1.1.1 FIS protein {Escherichia coli}
plrdsvkqalknyfaqlngqdvndlyelvlaeveqplldmvmqytrgnqtraalmmginr
gtlckklkkygmn
>d1ntca_ 1.100.1.1.2 DNA-binding domain of NTRC {Salmonella typhimurium}
mdlpgelfeastpdspshlppdswatllaqwadralrsghqnllseaqpelertllttal
rhtqghkqeaarllgwgaatltaklkelgme
>d1ntcb_ 1.100.1.1.2 DNA-binding domain of NTRC {Salmonella typhimurium}
mdlpgelfeastpdspshlppdswatllaqwadralrsghqnllseaqpelertllttal
rhtqghkqeaarllgwgaatltaklkelgme
>d1jhga_ 1.101.1.1.1 Trp repressor {Escherichia coli}
saamaeqrhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriieellrgems
qrelknelgagiatitrgsnslkaapvelrqwleevllksd
>d1troc_ 1.101.1.1.1 Trp repressor {Escherichia coli}
amaeerhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriveellrgemsqr
elknelgagiatitrgsnslkaapvelrqwleevllksd
>d1troe_ 1.101.1.1.1 Trp repressor {Escherichia coli}
aeerhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriveellrgemsqrel
knelgagiatitrgsnslkaapvelrqwleevllksd
>d1trog_ 1.101.1.1.1 Trp repressor {Escherichia coli}
spysaamaeerhqewlrfvdllknayqndlhlpllnlmltpderealgtrvriveellrg
emsqrelknelgagiatitrgsnslkaapvelrqwleevll
>d1iiea_ 1.102.1.1.1 MHC class II-associated invariant chain ectoplasmic trimerization domain {Human (Homo sapiens)}
ygnmtedhvmhllqnadplkvypplkgsfpenlrhlkntmetidwkvfeswmhhwllfem
srhsleqkptdappk
>d1iieb_ 1.102.1.1.1 MHC class II-associated invariant chain ectoplasmic trimerization domain {Human (Homo sapiens)}
ygnmtedhvmhllqnadplkvypplkgsfpenlrhlkntmetidwkvfeswmhhwllfem
srhsleqkptdappk
>d1iiec_ 1.102.1.1.1 MHC class II-associated invariant chain ectoplasmic trimerization domain {Human (Homo sapiens)}
ygnmtedhvmhllqnadplkvypplkgsfpenlrhlkntmetidwkvfeswmhhwllfem
srhsleqkptdappk
>d1aora1 1.103.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1b25a1 1.103.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1vns__ 1.104.1.1.1 Vanadium-containing chloroperoxidase {Curvularia inaequalis}
vtpiplpkidepeeyntnyilfwnhvglelnrvthtvggpltgpplsaralgmlhlaihd
ayfsicpptdfttflspdtenaayrlpspngandarqavagaalkmlsslymkpveqpnp
npganisdnayaqlglvldrsvleapggvdresasfmfgedvadvffallndprgasqeg
yhptpgrykfddepthpvvlipvdpnnpngpkmpfrqyhapfygkttkrfatqsehflad
ppglrsnadetaeyddavrvaiamggaqalnstkrspwqtaqglywaydgsnligtpprf
ynqivrriavtykkeedlansevnnadfarlfalvdvactdagifswkekwefefwrpls
gvrddgrpdhgdpfwltlgapatntndipfkppfpaypsghatfggavfqmvrryyngrv
gtwkddepdniaidmmiseelngvnrdlrqpydptapiedqpgivrtrivrhfdsawelm
fenaisriflgvhwrfdaaaardiliptttkdvyavdnngatvfqnvediryttrgtred
eeglfpiggvplgieiadeifnnglkptppeiqp
>d1sig__ 1.105.1.1.1 sigma70 subunit fragment from RNA polymerase {Escherichia coli}
megeidiakriedginqvqcsvaeypeaitylleqynrveaeearlsdlitgfvdpnaee
dlaptathvgselsqedldddededeedgdddsadddnsidpelarekfaelraqyvvtr
dtikakgrshataqeeilklsevfkqfrlvpkqfdylvnsmrvmmdrvrtqerlimklcv
eqckmpkknfitlftgnetsdtwfnaaiamnkpwseklhdvseevhralqklqqieeetg
ltieqvkdinrrmsigeakarrakkemveanlrlvisiakkytnrglqfldliqegnigl
mkavdkfeyrrgykfstyatwwirqaitrsiadq
>d1dg3a1 1.106.1.1.1 (284-583) Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain {Human (Homo sapiens)}
ggiqvngprleslvltyvnaissgdlpcmenavlalaqiensaavqkaiahyeqqmgqkv
qlpteslqelldlhrdsereaievfirssfkdvdhlfqkelaaqlekkrddfckqnqeas
sdrcsgllqvifspleeevkagiyskpggyrlfvqklqdlkkkyyeeprkgiqaeeilqt
ylkskesmtdailqtdqtltekekeievervkaesaqasakmlhemqrkneqmmeqkers
yqehlkqltekmendrvqllkeqertlalklqeqeqllkegfqkesrimkneiqdlqtkm
>d1bvp11 1.107.1.1.1 (1-120,255-349) Bluetongue virus coat protein vp7 (BTV-10 vp7), alpha-helical domain {Bluetongue virus}
mdtiaaraltvmracatlqearivleanvmeilgiainryngltlrgvtmrptslaqrne
mffmcldmmlsaaginvgpispdytqhmatigvlatpeipftteaaneiarvtgetstwg
Xktlnqypaltaeifnvysfrdhtwhglrtailnrttlpnmlppifppndrdsiltllll
stladvytvlrpefaihgvnpmpgpltraiaraayv
>d1tx4a_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
plpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvrevqq
kynmglpvdfdqynalhlpavilktflrelpeplltfdlyphvvgflnidesqrvpatlq
vlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlkainp
intftkflldhqgelf
>d1pbwa_ 1.108.1.1.2 p85 alpha subunit RhoGAP domain {Human (Homo sapiens)}
lpdlaeqfappdiapplliklveaiekkglecstlyrtqsssnlaelrqlldcdtpsvdl
emidvhvladafkrylldlpnpvipaavysemislapevqsseeyiqllkklirspsiph
qywltlqyllkhffklsqtssknllnarvlseifspmlfrfsaassdntenlikvieili
stew
>d1wer__ 1.108.1.2.1 p120GAP domain {Human (Homo sapiens)}
mpeeeysefkelilqkelhvvyalshvcgqdrtllasillriflhekleslllctlndre
ismedeattlfrattlastlmeqymkatatqfvhhalkdsilkimeskqscelspsklek
nedvntnlthllnilselvekifmaseilpptlryiygclqksvqhkwptnttmrtrvvs
gfvflrlicpailnprmfniisdspspiaartlilvaksvqnlanlvefgakepymegvn
pfiksnkhrmimfldelgnvpelpdttehsrtdlsrdlaalheicvahsdelrtlsnerg
aqqhvlkkllaitellqqkqnqyt
>d1nf1a_ 1.108.1.2.2 GAP related domain of neurofibromin {Human (Homo sapiens)}
erlvelvtmmgdqgelpiamalanvvpcsqwdelarvlvtlfdsrhllyqllwnmfskev
eladsmqtlfrgnslaskimtfcfkvygatylqklldpllrivitssdwqhvsfevdptr
lepsesleenqrnllqmtekffhaiissssefppqlrsvchclyqvvsqrfpqnsigavg
samflrfinpaivspyeagildkkpppiierglklmskilqsianhvlftkeehmrpfnd
fvksnfdaarrffldiasdcptsdavnhslsfisdgnvlalhrllwnnqekigqylssnr
dhkavgrrpfdkmatllaylgppe
>d1bkds_ 1.109.1.1.1 Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
rlpsadvyrfaepdseeniifeegipiikagtviklierltyhmyadpnfvrtflttyrs
fckpqellsliierfeipeprfrkeyiqpvqlrvlnvcrhwvehhfydferdayllqrme
efigtvrgkamkkwvesitkiiqrkkitfqsspptvewhisrpghietfdlltlhpieia
rqltllesdlyravqpselvgsvwtkedkeinspnllkmirhttnltlwfekcivetenl
eervavvsriieilqvfqelnnfngvlevvsamnsspvyrldhtfeqipsrqkkileeah
elsedhykkylaklrsinppcvpffgiyltnilkteegnpevlkrhgkelinfskrrkva
eitgeiqqyqnqpyclrvesdikrffenlnpmgnsmekeftdylfnksleieprnpkplp
rfpkkysyplkspgvrpsn
>d3bct__ 1.110.1.1.1 beta-Catenin {Mouse (Mus musculus)}
qxvsaivrtxqntndvetarctagtlhnlshhregllaifksggipalvkxlgspvdsvl
fyaittlhnlllhqegakxavrlagglqkxvallnktnvkflaittdclqilaygnqesk
liilasggpqalvnixrtytyekllwttsrvlkvlsvcssnkpaiveaggxqalglhltd
psqrlvqnclwtlrnlsdaatkqegxegllgtlvqllgsddinvvtcaagilsnltcnny
knkxxvcqvggiealvrtvlragdreditepaicalrhltsrhqeaexaqnavrlhyglp
vvvkllhppshwplikatvglirnlalcpanhaplreqgaiprlvqllvrahqdtqrgvr
xeeivegctgalhilardvhnrivirglntiplfvqllyspieniqrvaagvlcelaqdk
eaaeaieaegatapltellhsrnegvatyaaavlfr
>d1qgra_ 1.110.1.1.3 Importin beta {Human (Homo sapiens)}
melitilektvspdrleleaaqkfleraavenlptflvelsrvlanpgnsqvarvaaglq
iknsltskdpdikaqyqqrwlaidanarrevknyvlhtlgtetyrpssasqcvagiacae
ipvnqwpelipqlvanvtnpnstehmkestleaigyicqdidpeqlqdksneiltaiiqg
mrkeepsnnvklaatnallnsleftkanfdkeserhfimqvvceatqcpdtrvrvaalqn
lvkimslyyqymetymgpalfaitieamksdidevalqgiefwsnvcdeemdlaieasea
aeqgrppehtskfyakgalqylvpiltqtltkqdendddddwnpckaagvclmllatcce
ddivphvlpfikehiknpdwryrdaavmafgcilegpepsqlkplviqamptlielmkdp
svvvrdtaawtvgricellpeaaindvylapllqclieglsaeprvasnvcwafsslaea
ayeaadvaddqeepatyclsssfelivqkllettdrpdghqnnlrssayeslmeivknsa
kdcypavqkttlvimerlqqvlqmeshiqstsdriqfndlqsllcatlqnvlrkvqhqda
lqisdvvmasllrmfqstagsggvqedalmavstlvevlggeflkymeafkpflgiglkn
yaeyqvclaavglvgdlcralqsniipfcdevmqlllenlgnenvhrsvkpqilsvfgdi
alaiggefkkylevvlntlqqasqaqvdksdydmvdylnelrescleaytgivqglkgdq
envhpdvmlvqprvefilsfidhiagdedhtdgvvacaagligdlctafgkdvlklvear
pmihelltegrrsktnkaktlarwatkelrklknqa
>d1qbkb_ 1.110.1.1.4 Karyopherin beta2 {Human (Homo sapiens)}
yewkpdeqglqqilqllkesqspdttiqrtvqqkleqlnqypdfnnylifvltklksede
ptrslsglilknnvkahfqnfpngvtdfikseclnnigdsspliratvgilittiaskge
lqnwpdllpklcslldsedyntcegafgalqkicedsaeildsdvldrplnixipkflqf
fkhsspkirshavacvnqfiisrtqalxlhidsftenlfalagdeepevrknvcralvxl
levrmdrllphxhniveyxlqrtqdqdenvaleacefwltlaeqpickdvlvrhlpklip
vlvngxkysdidiillkgdveedetipdseqdirprfhrsrtvaqqhdedgieeeddddd
eiddddtisdwnlrkcsaaaldvlanvyrdellphilpllkellfhhewvvkesgilvlg
aiaegcxqgxipylpeliphliqclsdkkalvrsitcwtlsryahwvvsqppdtylkplx
tellkrildsnkrvqeaacsafatleeeactelvpylayildtlvfafskyqhknllily
daigtladsvghhlnkpeyiqxlxppliqkwnxlkdedkdlfplleclssvatalqsgfl
pycepvyqrcvnlvqktlaqaxlnnaqpdqyeapdkdfxivaldllsglaeglggnieql
varsniltlxyqcxqdkxpevrqssfallgdltkacfqhvkpciadfxpilgtnlnpefi
svcnnatwaigeisiqxgiexqpyipxvlhqlveiinrpntpktllentaitigrlgyvc
pqevapxlqqfirpwctslrnirdneekdsafrgictxisvnpsgviqdfiffcdavasw
inpkddlrdxfckilhgfknqvgdenwrrfsdqfplplkerlaafygv
>d1bk5a_ 1.110.1.1.5 Karyopherin alpha {Baker's yeast (Saccharomyces cerevisiae)}
lpqmtqqlnsddmqeqlsatvkfrqilsrehrppidvviqagvvprlvefmrenqpemlq
leaawaltniasgtsaqtkvvvdadavplfiqllytgsvevkeqaiwalgnvagdstdyr
dyvlqcnamepilglfnsnkpslirtatwtlsnlcrgkkpqpdwsvvsqalptlakliys
mdtetlvdacwaisylsdgpqeaiqavidvripkrlvellshestlvqtpalravgnivt
gndlqtqvvinagvlpalrlllsspkenikkeacwtisnitagnteqiqavidanlippl
vkllevaeyktkkeacwaisnassgglqrpdiirylvsqgcikplcdlleiadnriievt
ldalenilkmgeadkearglninenadfiekaggmekifncqqnendkiyekaykiiety
fg
>d1b3ua_ 1.110.1.2.1 Constant regulatory domain of protein phosphatase 2a, pr65alpha {Human (Homo sapiens)}
aaadgddslypiavlidelrnedvqlrlnsikklstialalgvertrsellpfltdtiyd
edevllalaeqlgtfttlvggpeyvhcllppleslatveetvvrdkaveslraishehsp
sdleahfvplvkrlaggdwftsrtsacglfsvcyprvssavkaelrqyfrnlcsddtpmv
rraaasklgefakvleldnvkseiipmfsnlasdeqdsvrllaveacvniaqllpqedle
alvmptlrqaaedkswrvrymvadkftelqkavgpeitktdlvpafqnlmkdceaevraa
ashkvkefcenlsadcrenvimsqilpcikelvsdanqhvksalasvimglspilgkdnt
iehllplflaqlkdecpevrlniisnldcvnevigirqlsqsllpaivelaedakwrvrl
aiieympllagqlgveffdeklnslcmawlvdhvyaireaatsnlkklvekfgkewahat
iipkvlamsgdpnylhrmttlfcinvlsevcgqdittkhmlptvlrmagdpvanvrfnva
kslqkigpildnstlqsevkpilekltqdqdvdvkyfaqealtvlsla
>d1b89a_ 1.110.1.3.1 Clathrin heavy chain proximal leg segment {Bovine (Bos taurus)}
rlaeleefingpnnahiqqvgdrcydekmydaakllynnvsnfgrlastlvhlgeyqaav
dgarkanstrtwkevcfacvdgkefrlaqxcglhivvhadeleelinyyqdrgyfeelit
xleaalglerahxgxftelailyskfkpqkxrehlelfwsrvnipkvlraaeqahlwael
vflydkyeeydnaiitxxnhptdawkegqfkdiitkvanvelyyraiqfylefkplllnd
llxvlsprldhtravnyfskvkqlplvkpylrsvqnhnnksvneslnnlfiteedyqalr
tsidaydnfdnislaqrlekheliefrriaaylfkg
>d1lrv__ 1.110.1.4.1 Leucine-rich repeat variant {Azotobacter vinelandii}
tpigdcrvcsfrmsllltgrctpgdacvavesgrqidrffrnnphlavqyladpfwerra
iavryspvealtplirdsdevvrravayrlpreqlsalmfdedrevritvadrlpleqle
qmaadrdylvrayvvqrippgrlfrfmrdedrqvrklvakrlpeeslglmtqdpepevrr
ivasrlrgddllellhdpdwtvrlaavehaslealreldepdpevrlaiagrl
>d1qmma1 1.110.1.5.1 (525-725) Phoshoinositide 3-kinase (PI3K) helical domain {Pig (Sus scrofa)}
aaseetlafqrqlnaligydvtdvsnvhddeleftrrrlvtprmaevagrdpklyamhpw
vtskplpeyllkkitnncvfivihrsttsqtikvsaddtpgtilqsfftkmakkkslmdi
pesqnerdfvlrvcgrdeylvgetpiknfqwvrqclkngeeihlvldtppdpaldevrke
ewplvddctgvtgyheqltihgkdhesvftvslwdcdrkfrvkirgidipvlprtadltv
fveaniqygqqvlcqrrtspkpfteevlwnvwlefsikikdlpkgallnlqiycgkapal
sgktsaempspeskgkaqllyyvnlllidhrfllrhgeyvlhmwqlsgkgedqgsfnadk
ltsatnpdkensmsisilldnychpialpkhrptpdpegdrvraempnqlrkqleaiiat
dplnpltaedkellwhfryeslkdpkaypklfssvkwgqqeivaktyqllakrevwdqsa
ldvgltmqlldcnfsdenvraiavqklesledddvlhyllqlvqavkfepyhdsalarfl
lkrglrnkrighflfwflrseiaqsrhyqqrfavileaylrgcg
>d1ycsb1 1.110.2.1.1 (327-456) 53BP2 {Human (Homo sapiens)}
plallldsslegefdlvqriiyevddpslpndegitalhnavcaghteivkflvqfgvnv
naadsdgwtplhcaascnnvqvckflvesgaavfamtysdmqtaadkceemeegytqcsq
flygvqekmg
>d1awcb_ 1.110.2.1.2 GA bindinig protein (GABP) beta 1 {Mouse (Mus musculus)}
dlgkklleaaragqddevrilmangapfttdwlgtsplhlaaqyghfsttevllragvsr
dartkvdrtplhmaaseghanivevllkhgadvnakdmlkmtalhwatehnhqevvelli
kygadvhtqskfcktafdisidngnedlaeilq
>d1bd8__ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
ragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqgas
pnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsfl
aaesdlhrrdargltplelalqrgaqdlvdilqghm
>d1ihba_ 1.110.2.1.4 p18ink4C(ink6) {Human (Homo sapiens)}
wgnelasaaargdleqltsllqnnvnvnaqngfgrtalqvmklgnpeiarrlllrganpd
lkdrtgfavihdaaragfldtlqtllefqadvniednegnlplhlaakeghlrvveflvk
htasnvghrnhkgdtacdlarlygrnevvslmqang
>d1bi7b_ 1.110.2.1.5 Cell cycle inhibitor p16ink4A {Human (Homo sapiens)}
epsadwlataaargrveevralleaganpnapnsygrrpiqvmmmgsarvaellllhgae
pncadpatltrpvhdaaregfldtlvvlhragarldvrdawgrlpvdlaeelghrdvary
lraaa
>d1iknd_ 1.110.2.1.7 I-kappa-B-alpha {Human (Homo sapiens)}
dgdsflhlaiiheekaltmevirqvkgdlaflnfqnnlqqtplhlavitnqpeiaeallg
agcdpelrdfrgntplhlaceqgclasvgvltqscttphlhsilkatnynghtclhlasi
hgylgivellvslgadvnaqepcngrtalhlavdlqnpdlvslllkcgadvnrvtyqgys
pyqltwgrpstriqqqlgqltlenlqmlpesedeesydtes
>d1myo__ 1.110.2.1.8 Myotrophin {Rat (Rattus norvegicus)}
mcdkefmwalkngdldevkdyvakgedvnrtleggrkplhyaadcgqleileflllkgad
inapdkhhitpllsavyeghvscvklllskgadktvkgpdgltaleatdnqaikallq
>d1sw6a_ 1.110.2.1.9 Swi6 ankyrin-repeat fragment {Baker's yeast (Saccharomyces cerevisiae)}
gpiitfthdltsdflssplkimkalpspvvndneqkmkleaflqrllfpeiqemptslnn
dssnrnseggssnqqqqhvsfdsllqevndafpntqlnlnipvdehgntplhwltsianl
elvkhlvkhgsnrlygdnmgesclvkavksvnnydsgtfealldylypcliledsmnrti
lhhiiitsgmtgcsaaakyyldilmgwivkkqnrpiqsgtnekeskpndkngerkdsile
nldlkwiianmlnaqdsngdtclniaarlgnisivdalldygadpfianksglrpvdfga
g
>d1dcqa1 1.110.2.1.10 (369-522) Pyk2-associated protein beta {Mouse (Mus musculus)}
adtaaklhslceavktrdifgllqayadgvdltekiplanghepdetalhlavrsvdrts
lhivdflvqnsgnldkqtgkgstalhyccltdnaeclklllrgkasieianesgetpldi
akrlkhehceelltqalsgrfnshvhveyewrll
>d1pbv__ 1.110.3.1.1 Exchange factor ARNO {Human (Homo sapiens)}
anegsktlqrnrkmamgrkkfnmdpkkgiqflvenellqntpeeiarflykgeglnktai
gdylgereelnlavlhafvdlheftdlnlvqalrqflwsfrlpgeaqkidrmmeafaqry
clcnpgvfqstdtcyvlsfavimlntslhnpnvrdkpglerfvamnrgineggdlpeell
rnlydsirnepfkip
>d1qsaa1 1.110.5.1.1 (1-450) 70 KDa soluble lytic transglycosylase (SLT70), superhelical domain {Escherichia coli}
dsldeqrsryaqikqawdnrqmdvveqmmpglkdyplypyleyrqitddlmnqpavtvtn
fvranptlppartlqsrfvnelarredwrgllafspekpgtteaqcnyyyakwntgqsee
awqgakelwltgksqpnacdklfsvwrasgkqdplaylerirlamkagntglvtvlagqm
padyqtiasaiislannpntvltfarttgatdftrqmaavafasvarqdaenarlmipsl
aqaqqlnedqiqelrdivawrlmgndvtdeqakwrddaimrsqstslierrvrmalgtgd
rrglntwlarlpmeakekdewrywqadlllergreaeakeilhqlmqqrgfypmvaaqri
geeyelkidkapqnvdsaltqgpemarvrelmywnldntarsewanlvkskskteqaqla
ryafnnqwwdlsvqatiagklwdhleerfp
>d1d8da_ 1.110.6.1.1 Protein farnesyltransferase, alpha-subunit {Rat (Rattus norvegicus)}
flsldsptyvlyrdraewadidpvpqndgpspvvqiiysekfrdvydyfravlqrderse
rafkltrdaielnaanytvwhfrrvllrslqkdlqeemnyiiaiieeqpknyqvwhhrrv
lvewlkdpsqelefiadilnqdaknyhawqhrqwviqefrlwdnelqyvdqllkedvrnn
svwnqrhfvisnttgysdravlerevqytlemiklvphnesawnylkgilqdrglsrypn
llnqlldlqpshsspyliaflvdiyedmlenqcdnkedilnkalelceilakekdtirke
ywryigrslqskhsresdipasv
>d1qjba_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlwtsdt
>d1a17__ 1.110.8.1.1 Protein phosphatase 5 {Human (Homo sapiens)}
ppadgalkraeelktqandyfkakdyenaikfysqaielnpsnaiyygnrslaylrtecy
gyalgdatraieldkkyikgyyrraasnmalgkfraalrdyetvvkvkphdkdakmkyqe
cnkivkqkaferaiagdehkrsvvdsldiesmtiedeys
>d1qqea_ 1.110.8.1.2 Vesicular transport protein sec17 {Yeast (Saccharomyces cerevisiae)}
isdpvellkraekkgvpssgfmklfsgsdsykfeeaadlcvqaatiyrlrkelnlagdsf
lkaadyqkkagnedeagntyveaykcfksggnsvnavdslenaiqifthrgqfrrganfk
felgeilendlhdyakaidcyelagewyaqdqsvalsnkcfikcadlkaldgqyieasdi
ysklikssmgnrlsqwslkdyflkkglcqlaatdavaaartlqegqsedpnfadsresnf
lkslidavnegdseqlsehckefdnfmrldkwkitilnkikesiqqqedd
>d1bpoa1 1.110.9.1.1 (331-487) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlagaeelfarkfnalfaqgnyseaakvaanapkg
ilrtpdtirrfqsvpaqpgqtspllqyfgilldqgqlnkyeslelcrpvlqqgrkqllek
wlkedklecseelgdlvksvdptlalsvylranvpnk
>d1c9ia1 1.110.9.1.1 (331-357) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnl
>d1c9ib1 1.110.9.1.1 (331-358) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnla
>d1c9la1 1.110.9.1.1 (331-359) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlag
>d1c9lb1 1.110.9.1.1 (331-359) Clathrin heavy-chain linker domain {Rat (Rattus norvegicus)}
eeniipyitnvlqnpdlalrmavrnnlag
>d2occe_ 1.110.10.1.1 Cytochrome c oxidase subunit E {Bovine (Bos taurus)}
hetdeefdarwvtyfnkpdidawelrkgmntlvgydlvpepkiidaalracrrlndfasa
vrilevvkdkagphkeiypyviqelrptlnelgistpeelgldkv
>d1yge_1 1.111.1.1.1 (150-839) Lipoxigenase, C-terminal domain {Soybean (Glycine max), isozyme L1}
vpsetpaplvsyreeelkslrgngtgerkeydriydydvyndlgnpdkseklarpvlggs
stfpyprrgrtgrgptvtdpntekqgevfyvprdenlghlkskdaleigtkslsqivqpa
fesafdlkstpiefhsfqdvhdlyeggiklprdvistiiplpvikelyrtdgqhilkfpq
phvvqvsqsawmtdeefaremiagvnpcvirgleefppksnldpaiygdqsskitadsld
ldgytmdealgsrrlfmldyhdifmpyvrqinqlnsaktyatrtilflredgtlkpvaie
lslphsagdlsaavsqvvlpakegvestiwllakayvivndscyhqlmshwlnthaamep
fviathrhlsvlhpiyklltphyrnnmninalarqslinangiiettflpskysvemssa
vyknwvftdqalpadlikrgvaikdpstphgvrlliedypyaadgleiwaaiktwvqeyv
plyyardddvkndselqhwwkeavekghgdlkdkpwwpklqtledlvevcliiiwiasal
haavnfgqypygglimnrptasrrllpekgtpeyeeminnhekaylrtitsklptlisls
vieilsthasdevylgqrdnphwtsdskalqafqkfgnklkeieeklvrrnndpslqgnr
lgpvqlpytllypsseegltfrgipnsisi
>d1lox_1 1.111.1.2.1 (113-663) 15-Lipoxygenase {Rabbit (Oryctolagus cuniculus)}
tgcttvgdpqglfqkhreqeleerrklyqwgswkeglilnvagskltdlpvderfledkk
idfeaslawglaelalknslnilapwktlddfnrifwcgrsklarrvrdswqedslfgyq
flnganpmllrrsvqlparlvfppgmeelqaqlekelkagtlfeadfalldnikanvily
cqqylaaplvmlklqpdgklmpmviqlhlpkigssppplflptdppmvwllakcwvrssd
fqvhelnshllrghlmaevftvatmrclpsihpvfklivphlrytleinvrarnglvsdf
gifdqimstgggghvqllqqagafltyrsfcppddladrgllgvessfyaqdalrlweii
sryvqgimglyyktdeavrddlelqswcreiteiglqgaqkqgfptslqsvaqachfvtm
ciftctgqhssihlgqldwftwvpnapctmrlpppttkdatletvmatlpnlkqsslqms
ivwqlgrdqpimvplgqhqeeyfsgpepravlekfreelaimdkeievrnekldipyeyl
rpsivensvai
>d1c1ka_ 1.112.1.1.1 gene 59 helicase assembly protein {Bacteriophage T4}
miklrmpaggeryidgksvyklylmikqhmngkydvikynwcmrvsdaayqkrrdkyffq
klsekyklkelalifisnlvanqdawigdisdadalvfyreyigrlkqikfkfeedirni
yyfskkvevsafkeifeynpkvqssyifkllqsniisfetfilldsflniidkhdeqtdn
lvwnnysiklkayrkilnidsqkaknvfietvkscky
>d1a5t_1 1.113.1.1.1 (167-330) delta prime subunit of DNA polymerase III, C-terminal domain {Escherichia coli}
ppeqyavtwlsrevtmsqdallaalrlsagspgaalalfqgdnwqaretlcqalaysvps
gdwysllaalnheqaparlhwlatllmdalkrhhgaaqvtnvdvpglvaelanhlspsrl
qailgdvchireqlmsvtginrellitdlllriehylqpgvvlp
>d2tct_2 1.114.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1lbd__ 1.115.1.1.1 Retinoid-X receptor (RXR-alpha) {Human (Homo sapiens)}
sanedmpverileaelavepktetyveanmglnpsspndpvtnicqaadkqlftlvewak
riphfselplddqvillragwnelliasfshrsiavkdgillatglhvhrnsahsagvga
ifdrvltelvskmrdmqmdktelgclraivlfnpdskglsnpaevealrekvyasleayc
khkypeqpgrfaklllrlpalrsiglkclehlfffkligdtpidtflmemleaphqmt
>d2lbd__ 1.115.1.1.2 Retinoic acid receptor (RAR-gamma) {Human (Homo sapiens)}
lspqleelitkvskahqetfpslcqlgkyttnssadhrvqldlglwdkfselatkciiki
vefakrlpgftglsiadqitllkaacldilmlrictrytpeqdtmtfsdgltlnrtqmhn
agfgpltdlvfafagqllplemddtetgllsaiclicgdrmdleepekvdklqeplleal
rlyarrrrpsqpymfprmlmkitdlrgistkgaeraitlkmeipgpmppliremlenp
>d1a28a_ 1.115.1.1.3 Progesterone receptor {Human (Homo sapiens)}
qlipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrn
lhiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltm
wqipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqk
gvvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkil
agmvkpllfhk
>d3erda_ 1.115.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqhqrlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
dahrlh
>d2prga_ 1.115.1.1.5 Peroxisome proliferator activated receptor gamma, PPAR-RXR {Human (Homo sapiens)}
esadlralakhlydsyiksfpltkakarailtgkttdkspfviydmnslmmgedkikfkh
itplqeqskevairifqgcqfrsveavqeiteyaksipgfvnldlndqvtllkygvheii
ytmlaslmnkdgvlisegqgfmtreflkslrkpfgdfmepkfefavkfnalelddsdlai
fiaviilsgdrpgllnvkpiediqdnllqalelqlklnhpessqlfakllqkmtdlrqiv
tehvqllqvikktetdmslhpllqeiykdly
>d1db1a_ 1.115.1.1.6 Vitamin D nuclear receptor {Human (Homo sapiens)}
lrpklseeqqriiailldahhktydptysdfcqfrppvrvndgggsvtlelsqlsmlphl
adlvsysiqkvigfakmipgfrdltsedqivllkssaievimlrsnesftmddmswtcgn
qdykyrvsdvtkaghslelieplikfqvglkklnlheeehvllmaicivspdrpgvqdaa
lieaiqdrlsntlqtyircrhpppgshllyakmiqkladlrslneehskqyrclsfqpec
smkltplvlevfg
>d1bsxa_ 1.115.1.1.7 Thyroid hormone receptor beta (TR-beta) {Human (Homo sapiens)}
kpeptdeeweliktvteahvatnaqgshwkqkrkflpedigqapivnapeggkvdleafs
hftkiitpaitrvvdfakklpmfcelpcedqiillkgccmeimslraavrydpesetltl
ngemavtrgqlkngglgvvsdaifdlgmslssfnlddtevallqavllmssdrpglacve
riekyqdsfllafehyinyrkhhvthfwpkllmkvtdlrmigachasrflhmkvecptel
fpplflevfed
>d1ah7__ 1.116.1.1.1 Bacterial phosholipase C {Bacillus cereus}
wsaedkhkegvnshlwivnraidimsrnttlvkqdrvaqlnewrtelengiyaadyenpy
ydnstfashfydpdngktyipfakqaketgakyfklagesyknkdmkqaffylglslhyl
gdvnqpmhaanftnlsypqgfhskyenfvdtikdnykvtdgngywnwkgtnpeewihgaa
vvakqdysgivndntkdwfvkaavsqeyadkwraevtpmtgkrlmdaqrvtagyiqlwfd
tygdr
>d1ca1_1 1.116.1.1.2 (1-249) Alpha-toxin, N-terminal domain {Clostridium perfringens}
wdgkidgtgthamivtqgvsilendlsknepesvrknleilkenmhelqlgstypdydkn
aydlyqdhfwdpdtdnnfskdnswylaysipdtgesqirkfsalaryewqrgnykqatfy
lgeamhyfgdidtpyhpanvtavdsaghvkfetfaeerkeqykintvgcktnedfyadil
knkdfnawskeyargfaktgksiyyshasmshswddwdyaakvtlansqkgtagyiyrfl
hdvsegndp
>d1ak0__ 1.116.1.2.1 P1 nuclease {Penicillium citrinum}
wgalghatvayvaqhyvspeaaswaqgilgsssssylasiaswadeyrltsagkwsaslh
fidaednpptncnvdyerdcgssgcsisaianytqrvsdsslssenhaealrflvhfigd
mtqplhdeayavggnkinvtfdgyhdnlhsdwdtympqkligghalsdaeswaktlvqni
esgnytaqaigwikgdnisepittatrwasdanalvctvvmphgaaalqtgdlyptyyds
vidtielqiakggyrlanwineih
>d1bm0a1 1.117.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1bm0a2 1.117.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1bm0a3 1.117.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1fura_ 1.118.1.1.2 Fumarase {Escherichia coli}
vrsekdsmgaidvpadklwgaqtqrslehfristekmptslihalaltkraaakvnedlg
llseekasairqaadevlagqhddefplaiwqtgsgtqsnmnmnevlanrasellggvrg
merkvhpnddvnksqssndvfptamhvaallalrkqlipqlktltqtlneksrafadivk
igrtnlqdatpltlgqeisgwvamlehnlkhieyslphvaelalggtavgtglnthpeya
rrvadelavitcapfvtapnkfealatcdalvqahgalkglaaslmkiandvrwlasgpr
cgigeisipenepgssimpgkvnptqcealtmlccqvmgndvainmggasgnfelnvfrp
mvihnflqsvrlladgmesfnkhcavgiepnrerinqllneslmlvtalnthigydkaae
iakkahkegltlkaaalalgylseaefdswvrpeqm
>d1auwa_ 1.118.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1c3ca_ 1.118.1.1.7 Adenylosuccinate lyase {(Thermotoga maritima)}
veryslspmkdlwteeakyrrwlevelavtrayeelgmipkgvterirnnakidvelfkk
ieektnhdvvafvegigsmigedsrffhygltssdvldtanslalveagkilleslkefc
dvlwevanrykhtptigrthgvhaeptsfglkvlgwysemkrnvqrleraieevsygkis
gavgnyanvppeveekalsylglkpepvstqvvprdrhafylstlaivaagieriaveir
hlqrtevleveepfrkgqrgssamphkknpitcerltglsrmmrayvdpslenialwher
dishssveryvfpdatqtlyymivtatnvvrnmkvneermkknidltkglvfsqrvllkl
iekgltrkeaydivqrnalktwnsekhfleylledeevkklvtkeeleelfdisyylkhv
dhiferfek
>d1b8fa_ 1.118.1.2.1 Histidine ammonia-lyase (HAL) {Pseudomonas putida}
teltlkpgtltlaqlraihaapvrlqldasaapaidasvacveqiiaedrtaygintgfg
llastriashdlenlqrslvlshaagigapldddlvrlimvlkinslsrgfsgirrkvid
alialvnaevyphiplkgsvgasgdlaplahmslvllgegkarykgqwlsatealavagl
epltlaakeglallngtqastayalrglfyaedlyaaaiacgglsveavlgsrspfdari
heargqrgqidtaacfrdllgdssevslshknadkvqdpyslrcqpqvmgacltqlrqaa
evlgieanavsdnplvfaaegdvisggnfhaepvamaadnlalaiaeigslserrislmm
dkhmsqlppflvenggvnsgfmiaqvtaaalasenkalshphsvdslptsanqedhvsma
paagkrlwemaentrgvlaiewlgacqgldlrkglktsaklekarqalrsevahydrdrf
fapdiekavellakgsltgllpagvlpsl
>d1uby__ 1.119.1.1.1 Farnesyl diphosphate synthase {Chicken (Gallus gallus)}
spvvverereefvgffpqivrdltedgighpevgdavarlkevlqynapggkcnrgltvv
aayrelsgpgqkdaeslrcalavgwcielfqaaslvaddimdqsltrrgqlcwykkegvg
ldaindsfllessvyrvlkkycrqrpyyvhllelflqtayqtelgqmldlitapvskvdl
shfseerykaivkyktafysfylpvaaamymvgidskeehenakaillemgeyfqiqddy
ldcfgdpaltgavgtdiqdnkcswlvvqclqrvtpeqrqllednygrkepekvakvkely
eavgmraafqqyeessyrrlqeliekhsnrlpkeiflglaqkiykrqk
>d5eau_2 1.119.1.2.1 (221-548) 5-Epi-aristolochene synthase, C-terminal domain {Tobacco (Nicotiana tabacum)}
knnvllrfakldfnllqmlhkqelaqvsrwwkdldfvttlpyardrvvecyfwalgvyfe
pqysqarvmlvktismisivddtfdaygtvkeleaytdaiqrwdineidrlpdymkisyk
aildlykdyekelssagrshivchaiermkevvrnynvestwfiegytppvseylsnala
tttyyylattsylgmksateqdfewlsknpkileasviicrviddtatyeveksrgqiat
gieccmrdygistkeamakfqnmaetawkdinegllrptpvstefltpilnlarivevty
ihnldgythpekvlkphiinllvdsiki
>d1ps1a_ 1.119.1.3.1 Pentalenene synthase {Streptomyces UC5319}
qdvdfhiplpgrqspdharaeaeqlawprslglirsdaaaerhlrggyadlasrfyphat
gadldlgvdlmswfflfddlfdgprgenpedtkqltdqvaaaldgplpdtappiahgfad
iwrrtcegmtpawcarsarhwrnyfdgyvdeaesrfwnapcdsaaqylamrrhtigvqpt
vdlaeragrfevphrvfdsavmsamlqiavdvnlllndiaslekeeargeqnnmvmilrr
ehgwsksrsvshmqnevrarleqylllesclpkvgeiyqldtaerealeryrtdavrtvi
rgsydwhrssg
>d1oela1 1.120.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndagvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtvaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1a6da1 1.120.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1ecma_ 1.121.1.1.1 Chorismate mutase domain of P-protein {Escherichia coli}
npllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgk
ahhldahyitrlfqliiedsvltqqallqqh
>d1ecmb_ 1.121.1.1.1 Chorismate mutase domain of P-protein {Escherichia coli}
pllalrekisaldekllallaerrelavevgkakllshrpvrdidrerdllerlitlgka
hhldahyitrlfqliiedsvltqqallqqhlnkin
>d5csma_ 1.121.1.2.1 Allosteric chorismate mutase {Baker's yeast (Saccharomyces cerevisiae)}
mdftkpetvlnlqnirdelvrmedsiifkfiershfatcpsvyeanhpgleipnfkgsfl
dwalsnleiahsrirrfespdetpffpdkiqksflpsinypqilapyapevnyndkikkv
yiekiipliskrdgddknnfgsvatrdieclqslsrrihfgkfvaeakfqsdiplytkli
kskdvegimknitnsaveekilerltkkaevygvdpterrierrispeylvkiykeivip
itkeveveyllrrlee
>d1pprm1 1.122.1.1.1 (1-156) Peridinin-chlorophyll protein {Dinoflagellate (Amphidinium carterae)}
deigdaakklgdasyafakevdwnngiflqapgklqplealkaidkmivmgaaadpkllk
aaaeahhkaigsisgpngvtsradwdnvnaalgrviasvpenmvmdvydsvskitdpkvp
aymkslvngadaekayegflafkdvvkksqvtsaag
>d1pprm2 1.122.1.1.1 (157-312) Peridinin-chlorophyll protein {Dinoflagellate (Amphidinium carterae)}
patvpsgdkigvaaqqlseasypflkeidwlsdvymkplpgvsaqqslkaidkmivmgaq
adgnalkaaaeahhkaigsidatgvtsaadyaavnaalgrviasvpkstvmdvynamagv
tdtsiplnmfskvnpldanaaakafytfkdvvqaaq
>d1qq8a_ 1.123.1.1.1 Heme oxygenase-1 (HO-1) {Human (Homo sapiens)}
pqdlsealkeatkevhtqaenaefmrnfqkgqvtrdgfklvmaslyhiyvaleeeiernk
espvfapvyfpeelhrkaaleqdlafwygprwqevipytpamqryvkrlhevgrtepell
vahaytrylgdlsggqvlkkiaqkaldlpssgeglafftfpniasatkfkqlyrsrmnsl
emtpavrqrvieeaktafllniqlfeelqellth
>d1poc__ 1.124.1.1.1 Phospholipase A2 {European honeybee (Apis mellifera)}
iiypgtlwcghgnkssgpnelgrfkhtdaccrthdmcpdvmsageskhgltntashtrls
cdcddkfydclknsadtissyfvgkmyfnlidtkcyklehpvtgcgertegrclhytvdk
skpkvyqwfdlrky
>d1poa__ 1.124.1.2.1 Snake phospholipase A2 {Taiwan cobra (Naja naja atra)}
nlyqfknmiqctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckggnnacaaavcdcdrlaaicfagapyndndyninlkarc
>d1bjja_ 1.124.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycgwggqgkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1jiaa_ 1.124.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
hllqfrkmikkmtgkepvvsyafygcycgsggrgkpkdatdrccfvhdccyekvtgcdpk
wddytyswkngtivcggddpckkevcecdkaaaicfrdnlktykkrymaypdilcsskse
kc
>d1ppa__ 1.124.1.2.5 Snake phospholipase A2 {Eastern cottonmouth snake (Agkistridon piscivorus)}
svlelgkmilqetgknaitsygsygcncgwghrgqpkdatdrccfvhkccykkltdcnhk
tdrysyswknkaiiceeknpclkemcecdkavaiclrenldtynkkykayfklkckkpdt
c
>d1vapa_ 1.124.1.2.5 Snake phospholipase A2 {Eastern cottonmouth snake (Agkistridon piscivorus)}
nlfqfeklikkmtgksgmlwysaygcycgwggqgrpkdatdrccfvhdccygkvtgcnpk
mdiytysvdngnivcggtnpckkqicecdraaaicfrdnlktydsktywkypkknckees
epc
>d1cl5a_ 1.124.1.2.6 Snake phospholipase A2 {Snake (Daboia russelli pulchella)}
sllefgkmileetgklaipsyssygcycgwggkgtpkdatdrccfvhdccygnlpdcnpk
sdrykykrvngaivcekgtscenricecdkaaaicfrqnlntyskkymlypdflckgelk
c
>d1ae7__ 1.124.1.2.7 Snake phospholipase A2 {Mainland tiger snake (Notechis scutatus scutatus), notexin}
nlvqfsyliqcanhgkrptwhymdygcycgaggsgtpvdeldrcckihddcydeagkkgc
fpkmsaydyycgengpycrnikkkclrfvcdcdveaafcfakapynnanwnidtkkrcq
>d1vip__ 1.124.1.2.9 Snake phospholipase A2 {Russell's viper (Vipera russelli)}
nlfqfaemivkmtgknplssysdygcycgwggkgkpqdatdrccfvhdccyekvksckpk
lslysysfqnggivcgdnhsckravcecdrvaatcfrdnlntydkkyhnyppsqctgteq
c
>d1aokb_ 1.124.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfakmingklgafsvwnyisygcycgwggqgtpkdatdrccfvhdccygrvrgcnpk
laiyyysfkkgnivcgknngclrdicecdrvaancfhqnkntynanykflsssrcrqtge
kc
>d1vpi__ 1.124.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfgdmilqktgkeavhsyaiygcycgwggqgraqdatdrccfaqdccygrvndcnpk
tatytysfengdivcgdndlclravcecdraaaiclgenvntydknyeyysishcteese
qc
>d1kvoa_ 1.124.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1une__ 1.124.1.2.12 Phospholipase A2 {Bovine (Bos taurus), pancreas}
alwqfngmikckipsseplldfnnygcycglggsgtpvddldrccqthdncykqakklds
ckvlvdnpytnnysyscsnneitcssennaceaficncdrnaaicfskvpynkehknldk
knc
>d1buna_ 1.124.1.2.14 beta2-bungarotoxin, phospholipase A2 chain {Many-banded krait (elapid) (Bungarus multicinctus)}
nlinfmemirytipcektwgeyadygcycgaggsgrpidaldrccyvhdncygdaekkhk
cnpktqsysykltkrtiicygaagtcarivcdcdrtaalcfgnseyieghknidtarfcq
>d1beo__ 1.125.1.1.1 beta-cryptogein {Phytophthora cryptogea}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bxm__ 1.125.1.1.1 beta-cryptogein {Phytophthora cryptogea}
rgtctatqqtaayhtlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntm
ikkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1b2nb_ 1.126.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1b2nd_ 1.126.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d4aahb_ 1.126.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrianaks
sgnfvfdvk
>d4aahd_ 1.126.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrianaks
sgnfvfdvk
>d1a0rg_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
pviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedk
npfke
>d1b9xb_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1b9yb_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1gg2g_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1gotg_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
ltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedknpfke
>d1gp2g_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
siaqarklveqlkmeanidrikvskaaadlmayceahakedplltpvpasenpf
>d1tbge_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
apviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1tbgf_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
apviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfk
>d1tbgg_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
apviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfk
>d1tbgh_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
apviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfk
>d2trcg_ 1.126.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1hfes_ 1.126.3.1.1 Fe-only hydrogenase smaller subunit {Desulfovibrio vulgaris}
vkqikdymldringvygadakfpvrasqdntqvkalyksylekplghkshdllhthwfdk
skgvkelttagklpnprasefegpypye
>d1hfet_ 1.126.3.1.1 Fe-only hydrogenase smaller subunit {Desulfovibrio vulgaris}
vkqikdymldringvygadakfpvrasqdntqvkalyksylekplghkshdllhthwfdk
skgvkelttagklpnprasefegpypye
>d2prgc_ 1.126.4.1.1 Nuclear receptor coactivator Src-1 {Human (Homo sapiens)}
qtshklvqlltttaeqqlrhadidtsckdvlsctgtsnsasanssggscpsshsslterh
kilhrllqegspsdit
>d1aqe__ 1.127.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvertfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d2cy3__ 1.127.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
adapgddyvisapegmkakpkgdkpgalqktvpfphtkhatvecvqchhtleadggavkk
cttsgchdslefrdkanakdiklvenafhtqcidchkalkkdkkptgptacgkchttn
>d3cyr__ 1.127.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
apavpnkpvevkgsqktvmfphaphekvecvtchhlvdgkesyakcgssgchddltakkg
ekslyyvvhakgelkhtsclachskvvaekpelkkdltgcakskchp
>d2ctha_ 1.127.1.1.2 Cytochrome c3 {Desulfovibrio vulgaris}
apkapadglkmeatkqpvvfnhsthksvkcgdchhpvngkedyrkcgtagchdsmdkkdk
sakgyyhvmhdkntkfkscvgchvevagadaakkkdltgckkskche
>d1wad__ 1.127.1.1.3 Cytochrome c3 {Desulfovibrio gigas}
vdvpadgakidfiaggeknltvvfnhsthkdvkcddchhdpgdkqyagcttdgchnildk
adksvnswykvvhdakggakptcischkdkagddkelkkkltgckgsachp
>d1new__ 1.127.1.2.1 Cytochrome c551.5 {Desulfuromonas acetoxidans}
advvtyenkkgnvtfdhkahaeklgcdachegtpakiaidkksahkdacktchksnngpt
kcggchik
>d2new__ 1.127.1.2.1 Cytochrome c551.5 {Desulfuromonas acetoxidans}
advvtyenkkgnvtfdhkahaeklgcdachegtpakiaidkksahkdacktchksnngpt
kcggchik
>d19hca_ 1.127.1.3.1 Nine-haem cytochrome c {Desulfovibrio desulfuricans atcc 27774}
aaleptdsgapsaivmfpvgekpnpkgaamkpvvfnhlihekkiadcetchhtgdpvscs
tchtvegkaegdyitldramhatdiaarakgntptscvschqsetkerrecagchaittp
kddeawcatchditpsmtpsemqkgiagtllpgdnealaaetvlaeatvapvspmlapyk
vvidaladkyepsdfthrrhltslmesikddklaqafhdkpeilcatchhrsplsltppk
cgschtkeidaadpgrpnlmaayhlecmgchkgmavarprdtdcttchkaaa
>d6prcc_ 1.127.1.4.1 Photosynthetic reaction centre (cytochrome subunit) {Rhodopseudomonas viridis}
cfepppatttqtgfrglsmgevlhpatvkakkerdaqyppalaavkaegppvsqvyknvk
vlgnlteaeflrtmtaitewvspqegctychdennlaseakypyvvarrmlemtraintn
wtqhvaqtgvtcytchrgtplppyvryleptlplnnretpthvervetrsgyvvrlakyt
aysalnydpftmflandkrqvrvvpqtalplvgvsrgkerrplsdayatfalmmsisdsl
gtnctfchnaqtfeswgkkstpqraiawwgirmvrdlnmnylaplnaslpasrlgrqgea
pqadcrtchqgvtkplfgasrlkdypelgpik
>d1fgja_ 1.127.1.5.1 Hydroxylamine oxidoreductase, HAO {Nitrosomonas europaea}
distvpdetydalkldrgkatpketyealvkrykdpahgagkgtmgdywepiaisiymdp
ntfykppvspkevaerkdcvechsdetpvwvrawkrsthanldkirnlksddplyykkgk
leevennlrsmgklgeketlkevgcidchvdvnkkdkadhtkdirmptadtcgtchlref
aereserdtmvwpngqwpagrpshaldytaniettvwatmpqrevaegctmchtnqnkcd
nchtrhefsaaesrkpeacatchsgvdhnnweaytmskhgklaemnrdkwnwevrlkdaf
skggqnaptcaachmeyegeythnitrktrwanypfvpgiaenitsdwsearldswvltc
tqchserfarsyldlmdkgtleglakyqeanaivhkmyedgtltgqktnrpnppepekpg
fgiftqlfwskgnnpaslelkvlemgennlakmhvglahvnpggwtytegwgpmnrayve
iqdeytkmqelsalqarvn
>d1bvb__ 1.127.1.5.2 Cytochrome c554 {Nitrosomonas europaea}
adapfegrkkcsschkaqaqswkdtahakameslkpnvkkeakqkakldpakdytqdkdc
vgchvdgfgqkggytiespkpmltgvgceschgpgrnfrgdhrksgqafeksgkktprkd
lakkgqdfhfeercsachlnyegspwkgakapytpftpevdakytfkfdemvkevkamhe
hyklegvfegepkfkfhdefqasakpakkgk
>d1ddca_ 1.127.1.5.3 Dimeric di-heme split-soret cytochrome c {Desulfovibrio desulfuricans, ATCC 27774}
rfdqvggafgwkphkldpkecaqvaydgywykgfgcgfgafysivglmgekygapynqfp
famleankggisdwgtiygalygaaatfslfwgrkevhpmvnelfrwyevtklpifnpgd
aaqgvkgdlpmsasdsvlchisvskwcyenkieatskqrseragrltadaafkaaeiint
kidqgkdfkstfpmqasvsscgechmtkgndanwakgimdctpchsgtaatqnkfvnh
>d1qdba_ 1.127.1.5.4 Cytochrome c nitrite reductase {Sulfurospirillum deleyianum}
giagkekseewakyyprqfdswkktkeydsftdmlakdpalviawsgyafskdynsprgh
yyalqdnvnslrtgapvdaktgplptacwtckspdvprlieedgeleyftgkwakygsqi
vnvigcanchddktaelkvrvphlnrglqaaglktfeesthqdkrtlvcaqchveyyfkk
tewkdakgadktamvvtlpwangvgkdgnagvegmikyydeinfsdwthnisktpmlkaq
hpgfefwksgihgqkgvscadchmpytqegsvkysdhqvkenpldsmdqscmnchreses
klrgivhqkyerkeflnkvafdnigkahletgkaieagasdeelkevrklirhgqfkadm
aiaahgnyfhapeetlrllaagsddaqkarlllvkilakhgvmdyiapdfdtkdkaqkla
kvdiaalaaekmkfkqtleqewkkeakakgranpelykdvdtindgksswnkk
>d1qjda1 1.127.1.5.5 (1-102) Flavocytochrome c3 (respiratory fumarate reductase), N-terminal domain {Shewanella frigidimarina |A|}
adnlaefhvqnqecdschtpdgelsndsltyentqcvschgtlaevaettkhehynahas
hfpgevactschsaheksmvycdschsfdfnmpyakkwlrde
>d1d4ca1 1.127.1.5.6 (1-102) Flavocytochrome c3 (respiratory fumarate reductase), N-terminal domain {Shewanella putrefaciens}
apevladfhgemggcdschvsdkggvtndnlthengqcvschgdlkelaaaapkdkvsph
kshligeiactschkgheksvaycdachsfgfdmpfggkwer
>d1neu__ 2.1.1.1.1 Myelin membrane adhesion molecule P0 {Rat (Rattus norvegicus)}
ivvytdrevygavgsqvtlhcsfwssewvsddisftwryqpeggrdaisifhyakgqpyi
devgtfkeriqwvgdpswkdgsivihnldysdngtftcdvknppdivgktsqvtlyvfe
>d1kacb_ 2.1.1.1.2 Coxsackie virus and adenovirus receptor (Car), domain 1 {Human (Homo sapiens)}
gittpeemiekakgetaylpckftlspedqgpldiewlispadnqkvdqviilysgdkiy
ddyypdlkgrvhftsndlksgdasinvtnlqlsdigtyqckvkkapgvankkihlvvlvk
psga
>d1qfoa_ 2.1.1.1.3 N-terminal domain of sialoadhesin {Mouse (Mus musculus)}
twgvsspknvqglsgscllipcifsypadvpvsngitaiwyydysgkrqvvihsgdpklv
dkrfrgraelmgnmdhkvcnlllkdlkpedsgtynfrfeisdsnrwldvkgttvtvtt
>d1akjd_ 2.1.1.1.4 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1bqhg_ 2.1.1.1.5 CD8 {Mouse (Mus musculus)}
kpqapelrifpkkmdaelgqkvdlvcevlgsvsqgcswlfqnsssklpqptfvvymassh
nkitwdeklnssklfsamrdtnnkyvltlnkfskenegyyfcsvisnsvmyfssvvpvlq
kv
>d1cdu_1 2.1.1.1.6 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsvltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cdy_1 2.1.1.1.6 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkspsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1wioa2 2.1.1.1.6 (179-291) CD4 {Human (Homo sapiens)}
fqkassivykkegeqvefsfplaftvekltgsgelwwqaerassskswitfdlknkevsv
krvtqdpklqmgkklplhltlpqalpqyagsgnltlaleaktgklhqevnlvv
>d3cd4_1 2.1.1.1.6 (1-97) CD4 {Human (Homo sapiens)}
kkvvlgkkgdtveltctasqkksiqfhwknsnqikilgnqgsfltkgpsklndradsrrs
lwdqgnfpliiknlkiedsdtyicevedqkeevqllv
>d1cid_1 2.1.1.1.7 (1-105) CD4 {Rat (Rattus rattus)}
tsitayksegesaefsfplnlgeeslqgelrwkaekapssqswitfslknqkvsvqksts
npkfqlsetlpltlqipqvslqfagsgnltltldrgilyqevnlv
>d1hnf_1 2.1.1.1.8 (4-104) CD2, first domain {Human (Homo sapiens)}
tnaletwgalgqdinldipsfqmsddiddikwektsdkkkiaqfrkeketfkekdtyklf
kngtlkikhlktddqdiykvsiydtkgknvlekifdlkiqe
>d1a64a_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a64b_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6pa_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6pb_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a7ba_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bb_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bc_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bd_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1cdca_ 2.1.1.1.9 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilangdl
kiknltrddsgtynvtvystngtrildkaldlrile
>d1hnga1 2.1.1.1.9 (2-99) CD2, first domain {Rat (Rattus rattus)}
dsgtvwgalghginlnipnfqmtddidevrwergstlvaefkrkmkpflksgafeilang
dlkiknltrddsgtynvtvystngtrilnkaldlrile
>d1ccza1 2.1.1.1.10 (1-93) CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
fsqqiygvvygnvtfhvpsnvplkevlwkkqkdkvaelensefrafssfknrvyldtvsg
sltiynltssdedeyemespnitdtmkfflyvl
>d1ci5a1 2.1.1.1.10 (1-95) CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
ssqqiygvkygnvtfhvpsnqplkevlwkkqkdkvaelensefrafssfknrvyldtksg
sltiynltssdedeyemespnitdsmkfflyvges
>d1qa9b_ 2.1.1.1.10 CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
ssqqiygvkygnvtfhvpsnqplkevlwkkqkdkvaelensefrafssfknrvyldtksg
sltiynltssdedeyemespnitdsmkfflyvges
>d1qa9d_ 2.1.1.1.10 CD2-binding domain of CD58, first domain {Human (Homo sapiens)}
ssqqiygvkygnvtfhvpsnqplkevlwkkqkdkvaelensefrafssfknrvyldtksg
sltiynltssdedeyemespnitdsmkfflyvges
>d1igta1 2.1.1.1.11 (1-108) Immunoglobulin (variable domains of L and H chains) {Intact IgG2a antibody Mab231 (mouse), kappa L chain}
divltqspsslsaslgdtititchasqninvwlswyqqkpgnipklliykasnlhtgvps
rfsgsgsgtgftltisslqpediatyycqqgqsypltfgggtkleikr
>d1igyb1 2.1.1.1.12 (2-113) Immunoglobulin (variable domains of L and H chains) {Intact IgG1 antibody Mab61.1.3 (mouse), kappa L chain}
vklqesgaelarpgasvkmsckasgytfttytihwikqrpgqglewigyinpssvytnyn
qrfkdkatltrdrssntanihlssltsddsavyycvregevpywgqgttvtvss
>d8faba1 2.1.1.1.13 (3-105) Immunoglobulin (variable domains of L and H chains) {Fab HIL (human), lambda L chain}
eltqppsvsvspgqtaritcsanalpnqyaywyqqkpgrapvmviykdtqrpsgipqrfs
sstsgttvtltisgvqaedeadyycqawdnsasifgggtkltv
>d8fabb1 2.1.1.1.13 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab HIL (human), lambda L chain}
avklvqagggvvqpgrslrlsciasgftfsnygmhwvrqapgkglewvaviwyngsrtyy
gdsvkgrftisrdnskrtlymqmnslrtedtavyycardpdiltafsfdywgqgvlvtvs
s
>d7fabh1 2.1.1.1.14 (1-116) Immunoglobulin (variable domains of L and H chains) {Fab NEW (human), lambda L chain}
avqleqsgpglvrpsqtlsltctvsgtsfddyywtwvrqppgrglewigyvfytgttlld
pslrgrvtmlvntsknqfslrlssvtaadtavyycarnliaggidvwgqgslvtvs
>d7fabl1 2.1.1.1.14 (1-103) Immunoglobulin (variable domains of L and H chains) {Fab NEW (human), lambda L chain}
asvltqppsvsgapgqrvtisctgsssnigaghnvkwyqqlpgtapkllifhnnarfsvs
ksgtsatlaitglqaedeadyycqsydrslrvfgggtkltvlr
>d1a3rh1 2.1.1.1.16 (2-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytkyd
pkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssakt
tap
>d1a3rl1 2.1.1.1.16 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkradaapt
>d1bbjl1 2.1.1.1.17 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
diqmtqspaslsvsvgetvtitcraseniysnlawyqqkqgkspqllvyaatnladgvps
rfsgsgsgtqyslkinslqsedfgsyycqhfwgtpytfgggtrleikra
>d1hilb1 2.1.1.1.18 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 17/9 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgfsfssygmswvrqtpdkrlewvatisngggytyy
pdsvkgrftisrdnakntlylqmsslksedsamyycarrerydengfaywgqgtlvtvs
>d1dfbh1 2.1.1.1.20 (1-126) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
evqlvesggglvqpgrslrlscaasgftfndyamhwvrqapgkglewvsgiswdsssigy
adsvkgrftisrdnaknslylqmnslraedmalyycvkgrdyydsggyftvafdiwgqgt
mvtvss
>d1dfbl1 2.1.1.1.20 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab 3D6 (human), kappa L chain}
diqmtqspstlsasvgdrvtitcrasqsisrwlawyqqkpgkvpklliykasslesgvps
rfsgsgsgteftltisslqpddfatyycqqynsysfgpgtkvdikr
>d1igfh1 2.1.1.1.21 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab B13I2 (mouse), kappa L chain}
evqlvesggdlvkpggslklscaasgftfsrcamswvrqtpekrlewvagissggsytfy
pdtvkgrfiisrnnarntlslqmsslrsedtaiyyctryssdpfyfdywgqgttltvss
>d1igjb1 2.1.1.1.22 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 26-10 (mouse), kappa L chain}
vqlqqsgpelvkpgasvrmsckssgyiftdfymnwvrqshgksldyigyispysgvtgyn
qkfkgkatltvdkssstaymelrsltsedsavyycagssgnkwamdywghgasvtvssa
>d1igmh_ 2.1.1.1.23 Immunoglobulin (variable domains of L and H chains) {Fv POT (human) Ig-M, kappa L chain}
evhllesggnlvqpggslrlscaasgftfnifvmswvrqapgkglewvsgvfgsggntdy
adavkgrftitrdnskntlylqmnslraedtaiyycakhrvsyvltgfdswgqgtlvtvs
sgsasaptl
>d1igml_ 2.1.1.1.23 Immunoglobulin (variable domains of L and H chains) {Fv POT (human) Ig-M, kappa L chain}
diqmtqspsslsasvgdrvtitcqasqdisnylawyqqkpgkapelriydasnletgvps
rfsgsgsgtdftftisslqpediatyycqqyqnlpltfgpgtkvdikrtvaapsv
>d1indh1 2.1.1.1.24 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab Cha255 (mouse), lambda L chain}
evtlvesggdsvkpggslklscaasgftlsgetmswvrqtpekrlewvattlsgggftfy
sasvkgrftisrdnaqnnlylqlnslrsedtalyfcashrfvhwghgtlvtvsa
>d2fb4h1 2.1.1.1.26 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab KOL (human), lambda L chain}
evqlvqsgggvvqpgrslrlscsssgfifssyamywvrqapgkglewvaiiwddgsdqhy
adsvkgrftisrndskntlflqmdslrpedtgvyfcardgghgfcssascfgpdywgqgt
pvtvssa
>d2fb4l1 2.1.1.1.26 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab KOL (human), lambda L chain}
qsvltqppsasgtpgqrvtiscsgtssnigsstvnwyqqlpgmapklliyrdamrpsgvp
drfsgsksgasaslaigglqsedetdyycaawdvslnayvfgtgtkvtvlg
>d2fbjh1 2.1.1.1.27 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab J539 (mouse), kappa L chain}
evkllesggglvqpggslklscaasgfdfskywmswvrqapgkglewigeihpdsgtiny
tpslkdkfiisrdnaknslylqmskvrsedtalyycarlhyygynaywgqgtlvtvsa
>d2fbjl1 2.1.1.1.27 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab J539 (mouse), kappa L chain}
eivltqspaitaaslgqkvtitcsasssvsslhwyqqksgtspkpwiyeisklasgvpar
fsgsgsgtsysltintmeaedaaiyycqqwtyplitfgagtklelkrad
>d1fgvh_ 2.1.1.1.28 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscatsgytfteytmhwmrqapgkglewvaginpknggtsy
adsvkgrftisvdkskntlylqmnslraedtavyycarwrglnygfdvryfdvwgqgtlv
tvss
>d1fgvl_ 2.1.1.1.28 Immunoglobulin (variable domains of L and H chains) {Fab H52 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdinnylnwyqqkpgkapklliyytstlesgvps
rfsgsgsgtdytltisslqpedfatyycqqgntlpptfgagtkveik
>d1mcph1 2.1.1.1.29 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
evklvesggglvqpggslrlscatsgftfsdfymewvrqppgkrlewiaasrnkgnkytt
eysasvkgrfivsrdtsqsilylqmnalraedtaiyycarnyygstwyfdvwgagttvtv
s
>d2imn__ 2.1.1.1.29 Immunoglobulin (variable domains of L and H chains) {Fab MCPC603 (human), kappa L chain}
divmtqspsslsvsagervtmsckssqsllykdgknflawyqqkpgqppklliygastre
sgvpdrftgsgsgtdftltissvqaedlavyycqndhsypltfgagtklelkr
>d1fvca_ 2.1.1.1.30 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
diqmtqspsslsasvgdrvtitcrasqdvntavawyqqkpgkapklliysasflysgvps
rfsgsrsgtdftltisslqpedfatyycqqhyttpptfgqgtkveikrt
>d1fvcb_ 2.1.1.1.30 Immunoglobulin (variable domains of L and H chains) {Fab 4D5 (synthetic, humanised version), kappa L chain}
evqlvesggglvqpggslrlscaasgfnikdtyihwvrqapgkglewvariyptngytry
adsvkgrftisadtskntaylqmnslraedtavyycsrwggdgfyamdywgqgtlvtvss
>d1ggbh1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
qvqlqesgpgilqpsqtlsltcsfsgfslstygmgvswirqpsgkglewlahifwdgdkr
ynpslksrlkiskdtsnnqvflkitsvdtadtatyycvqegyiywgqgtsvtvs
>d1ggbl1 2.1.1.1.31 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 50.1 (mouse), kappa L chain}
divltqspgslavslgqratiscrasesvdddgnsflhwyqqkpgqppklliyrssnlis
gipdrfsgsgsrtdftltinpveaddvatyycqqsnedpltfgagtkleik
>d1ai1h1 2.1.1.1.32 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1ai1l1 2.1.1.1.32 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1mfa_1 2.1.1.1.34 (1l-111l) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
qivvtqesalttspgetvtltcrsstgtvtsgnhanwvqekpdhlftgligdtnnrapgv
parfsgsligdkaaltitgaqpedeaiyfcalwsnnhwifgggtkltvlgq
>d1mfa_2 2.1.1.1.34 (251h-367h) Immunoglobulin (variable domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
evqvqqsgtvvarpgasvkmsckasgytftnywmhwikqrpgqglewigaiypgnsatfy
nhkfraktkltavtstttaymelssltsedsavyyctrgghgyygdywgqgasltvs
>d1nbvh1 2.1.1.1.35 (1-122) Immunoglobulin (variable domains of L and H chains) {Fab BV04-01 (mouse), kappa L chain}
evqpvetggglvqpkgslklscaasgfsfntnamnwvrqapgkglewvarirsksnnyat
yyadsvkdrftisrddsqnmlylqmnnlktedtamyycvrdqtgtawfaywgqgtlvtvs
aa
>d1teth1 2.1.1.1.36 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab TE33 (mouse), kappa L chain}
qiqlvqsgpelktpgetvrisckasgytfttygmswvkqtpgkgfkwmgwintysgvpty
addfkgrfafsletsastaylqinnlknedtatyfcarrswyfdvwgtgttvtvs
>d1flrh1 2.1.1.1.37 (1-118) Immunoglobulin (variable domains of L and H chains) {Fab 4-4-20 (mouse), kappa L chain}
evkldetggglvqpgrpmklscvasgftfsdywmnwvrqspekglewvaqirnkpynyet
yysdsvkgrftisrddskssvylqmnnlrvedmgiyyctgsyygmdywgqgtsvtvss
>d6fabh1 2.1.1.1.38 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 36-71 (mouse), kappa L chain}
evqlqqsgvelvragssvkmsckasgytftsnginwvkqrpgqglewigynnpgngyiay
nekfkgkttltvdkssstaymqlrsltsedsavyfcarseyyggsykfdywgqgttltvs
s
>d1gigh1 2.1.1.1.39 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab HC19 (mouse), lambda L chain}
qvqlkesgpglvapsqslsitctvsgfllisngvhwvrqppgkglewlgviwaggntnyn
salmsrvsiskdnsksqvflkmkslqtddtamyycardfydydvfyyamdywgqgtsvtv
>d1figh1 2.1.1.1.41 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
dvqlqqsgpelekpgasvkisckasgfslpghninwivqrngkslewignidpyyggtnf
npkfkgkatltvdkssstlymhltslqsedsavyycarrrdgnygftywgqgtlvtvsa
>d1figl1 2.1.1.1.41 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 1F7 (mouse), kappa L chain}
envltqspaimsaspgekvtmacrasssvsstylhwyqqksgaspklliystsnlasgvp
arfsgsgsgtsysltissveaedaatyycqqysgypltfgagtklelkr
>d1a2ya_ 2.1.1.1.43 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1a2yb_ 2.1.1.1.43 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1cica1 2.1.1.1.44 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
divmtqshkfmstsvgdrvsitckasqdvriavawyqqkpgqspklliywastrhtgvpd
rftgsgsgtdftltisnvqsedladyfcqhcgsypftfgsgtkleik
>d1jhlh_ 2.1.1.1.45 Immunoglobulin (variable domains of L and H chains) {Fv D11.15 (mouse), kappa L chain}
qvqlqqsgaelvrpgasvklsckasgytfisywinwvkqrpgqglewigniypsdsytny
nqkfkdkatltvdkssstaymqlssptsedsavyyctrddnygamdywgqgttvtv
>d1jhll_ 2.1.1.1.45 Immunoglobulin (variable domains of L and H chains) {Fv D11.15 (mouse), kappa L chain}
dieltqspsylvaspgetitincrasksiskslawyqekpgktnnlliysgstlqsgips
rfsgsgsgtdftltisslepedfamyicqqhneypwtfgggtkleikr
>d1bqll1 2.1.1.1.46 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab HyHEL-5 (mouse), kappa L chain}
divltqspaimsaspgekvtmtcsasssvnymywyqqksgtspkrwiydtsklasgvpvr
fsgsgsgtsysltissmetedaatyycqqwgrnptfgggtkleikr
>d2jelh1 2.1.1.1.48 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab JE142 (mouse), kappa L chain}
qvqlaqsgpelvrpgvsvkisckgsgytfttyamhwvkqshakslewiglistysgytny
nqkfkgkatmtvdkssstaymelarltsedsaiyycarvmgeqyfdvwgagttvivss
>d1ncbh1 2.1.1.1.49 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab NC41 (mouse), kappa L chain}
qiqlvqsgpelkkpgetvkisckasgytftnygmnwvkqapgkglewmgwintntgepty
geefkgrfafsletsastanlqinnlknedkatffcargednfgslsdywgqgttltvss
>d1ncbl1 2.1.1.1.49 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab NC41 (mouse), kappa L chain}
divmtqspkfmstsvgdrvtitckasqdvstavvwyqqkpgqspklliywastrhigvpd
rfagsgsgtdytltissvqaedlalyycqqhysppwtfgggtkleikr
>d1forh1 2.1.1.1.50 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
qgqlqqsgaelvrpgssvkisckasgyafssfwvnwvkqrpgqglewigqiypgdgdnky
ngkfkgkatltadkssttaymqlysltsedsavyfcarsgnypyamdywgqgtsvtvssa
>d1forl1 2.1.1.1.50 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 17-Ia (mouse), kappa L chain}
qivltqspaimsafpgekvtitcsatssvnymhwfqqkpgtspklwiysssnlasgvpar
fsgsgsgtsysltisrmeaedaatyycqqrssypitfgsgtkleikr
>d1rmfh1 2.1.1.1.55 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab R6.5 (mouse), kappa L chain}
qvqlqqsgpelvrpgvsvkisckgsgytfidyaihwvkeshakslewigvisaysgdtny
nqkfkgkatmtvdkssntaylelarltsedsaiyycarggwlllsfdywgqgttltvss
>d1fpth1 2.1.1.1.56 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab C3(?), neutralizing type 1 poliovirus, (mouse), kapppa L chain}
qvqlqqsgaelvrpgtsvkvsckasgyaftnyliqwikqrpgqglewigvinpgsggtdy
nanfkgkatltadksssivymqlssltsddsavyfcardfydydvgfdywgqgttltvss
>d1ikfh1 2.1.1.1.57 (1-126) Immunoglobulin (variable domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
evklvesggglvqpggslklscatsgftfsdyymywvrqnsekrlewvafisngggsafy
adivkgrftisrdnakntlylqmsrlksedtamyyctrhtlydtlygnypvwfadwgqgt
lvtvsa
>d1ikfl1 2.1.1.1.57 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab, anti-cyclosporin A, (mouse), kappa L chain}
diqmtqttsslsaslgdrvtiscrasqdistylnwyqqkpdgtvkllifytsrlrsgvps
rfsgsgsgtdysltisnleqediatyfcqqgsripptfgggtkleil
>d1igcl1 2.1.1.1.60 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab MoPC21 (mouse), kappa L chain}
nivmtqspksmsmsvgervtltckasenvvtyvswyqqkpeqspklliygasnrytgvpd
rftgsgsatdftltissvqaedladyhcgqgnsypytfgggtkleikr
>d1ibgh1 2.1.1.1.61 (2-113) Immunoglobulin (variable domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
vhlvqsgpglvapsqslsitctvsgfslttygvhwfrqppgkglewlgliwaggntdyns
almsrlsinkdnsksqvflkmnslqaddtamyycarfrfasyydyavdywgqgtsvtvss
>d1ibgl1 2.1.1.1.61 (2-107) Immunoglobulin (variable domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
ivltqspaslavslgqratiscrasksvstsgyshihwyqqkpgqppklliylasilesg
vparfsgsgsgtdftlnihpveeedaatyycqhsreypltfgagtelelk
>d1a14h_ 2.1.1.1.63 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvrmsckasgytftnynmywvkqspgqglewigifypgngdtsy
nqkfkdkatltadkssntaymqlssltsedsavyycarsggsyrydggfdywgqgttvtv
>d1a14l_ 2.1.1.1.63 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
dieltqttsslsaslgdrvtiscrasqdisnylnwyqqnpdgtvklliyytsnlhsevps
rfsgsgsgtdysltisnleqediatyfcqqdftlpftfgggtaa
>d1bm3h1 2.1.1.1.64 (1-125) Immunoglobulin (variable domains of L and H chains) {Anti-integrin Fab OPG2 (mouse), kappa L chain}
evqlvqsggglvnpgrslklscaasgftfssygmswvrqtpekrlewvaaisgggtyihy
pdsvkgrftisrdnaknnlylqmsslrsedtalyyctrhpfyrydggnyyamdhwgqgts
vtvsa
>d1nsnl1 2.1.1.1.65 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab N10 (mouse), kappa L chain}
divltqspsslavslgqratiscrasqsvstssfrymhwyqqkpgqpprllikyasnles
gvparfsgsgsgtdftlnihpveeedtatyycqhsweipytfgggtkleik
>d1iail1 2.1.1.1.66 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
divmtqshkfmstsvgdrvsitckasqdvstavawyqqkpgqspklliysasyqytgvpd
rftgsgsrtdftftinsvqaedlavyychqhystpftfgsgtkleikr
>d1iaim1 2.1.1.1.67 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1plgh1 2.1.1.1.68 (1-117) Immunoglobulin (variable domains of L and H chains) {Polysialic acid-binding Fab (mouse), kappa L chain}
qiqlqqsgpelvrpgasvkisckasgytftdyyihwvkqrpgeglewigwiypgsgntky
nekfkgkatltvdtssstaymqlssltsedsavyfcarggkfamdywgqgtsvtvss
>d1gafl1 2.1.1.1.69 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeingylgwlqqkpdgtikrliyaastlhsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1vgeh1 2.1.1.1.71 (1-122) Immunoglobulin (variable domains of L and H chains) {Fab TR1.9 (mouse/human), kappa L chain}
qvklleqsgaevkkpgasvkvsckasgysftsyglhwvrqapgqrlewmgwisagtgntk
ysqkfrgrvtftrdtsattaymglsslrpedtavyycardpygggksefdywgqgtlvtv
ss
>d1vgel1 2.1.1.1.71 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TR1.9 (mouse/human), kappa L chain}
elvmtqspsslsasvgdrvniacrasqgissalawyqqkpgkaprlliydasnlesgvps
rfsgsgsgtdftltisslqpedfaiyycqqfnsypltfgggtkveik
>d1ucbh1 2.1.1.1.73 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CBR96 (mouse/human), kappa L chain}
evnlvesggglvqpggslkvscvtsgftfsdyymywvrqtpekrlewvayisqggditdy
pdtvkgrftisrdnaknslylqmsrlksedtamyycarglddgawfaywgqgtlvtvsv
>d1dvfc_ 2.1.1.1.75 Immunoglobulin (variable domains of L and H chains) {Fv E5.2 (mouse), kappa L chain}
diqltqspsslsaslgdrvtiscrasqdisnylnwyqqkpdgtvklliyytsrlhsgvps
rfsgsgsgtdysltisnleqediatyfcqqgntlpwtfgggtkleik
>d1dvfd_ 2.1.1.1.75 Immunoglobulin (variable domains of L and H chains) {Fv E5.2 (mouse), kappa L chain}
qvqlqqsgtelvksgasvklsctasgfnikdthmnwvkqrpeqglewigridpangniqy
dpkfrgkatitadtssntaylqlsltsedtavyycatkviyyqgrgamdywgqgttltvs
>d1ghfh1 2.1.1.1.76 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab GH1002 (mouse), kappa L chain}
vqlqqsgpelkkpgetvkiscklwytftdygmnwvkqapgkglkwmgwiqtnteeptyga
efkgrfafsletsaftaykqinnlknedmatyfcarveagfdywaqgttltvss
>d1nldh1 2.1.1.1.77 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain}
qvklqqsgpglvqpsqslsitctvsgfsltcygvhwvrqspgkglewlgviwsggdtdyn
aafisrlsitkdnsksqvffkmnslqpndraiyycarrggdfwgqgttvtvs
>d1kelh1 2.1.1.1.78 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab 28B4 (mouse), kappa L chain}
evklvesggglgqpggslrlscatsgftftdyyfnwarqppgkalewlgfirnkakgytt
eysasvkgrftisrdnsqgilylqmntlraedsatyycarwgsyamdywgqgtsv
>d1osph1 2.1.1.1.79 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 184.1 (mouse), kappa L chain}
evqlqesgpslvkpsqtlsltcsvtgepitsgfwdwirkfpgnklefmgyirygggtyyn
pslkspisitrdtsknhyylqlnsvvtedtatyycarsrdyygssgfafwgegtlvtvsa
a
>d1ospl1 2.1.1.1.79 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 184.1 (mouse), kappa L chain}
diqmsqssssfsvslgdrvtitckasediysrlawyqqkpgnaprllisgatsletwvps
rfsgsdsgkdytlsitslqtedvatyfcqqywsppptfgggtkleikr
>d1clol1 2.1.1.1.80 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (mouse), kappa L chain}
qtvlsqspailsaspgekvtmtcrasssvtyihwyqqkpgsspkswiyatsnlasgvpar
fsgsgsgtsysltisrveaedaatyycqhwsskpptfgggtkleik
>d1ad0a1 2.1.1.1.81 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0b1 2.1.1.1.81 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1miml1 2.1.1.1.82 (1-105) Immunoglobulin (variable domains of L and H chains) {Fab CHI621 (mouse), kappa L chain}
qivstqspaimsaspgekvtmtcsasssrsymqwyqqkpgtspkrwiydtsklasgvpar
fsgsgsgtsysltissmeaedaatyychqrssytfgggtkleikr
>d1qkzh1 2.1.1.1.85 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab MN14C11.6 (mouse), kappa L chain}
dvklvesggglvkpgrslklscaasgftfsdyymfwvrqtpeqrlewvatisdggaytyy
pdsvkgrftisrdnaknnlylqmnslksedtgmyycardpleyygmdywgqgtsvavss
>d1pskh1 2.1.1.1.86 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab against a ganglioside (mouse), kappa L chain}
evqlqqsgpelvkpgasvkiscktsgytftkytmhwvkqshgkslewigdinpnnggtny
nqkfkgtatltvhkssttaymelrsltsedsavyyctsksfdywgqgttltvss
>d1pskl1 2.1.1.1.86 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab against a ganglioside (mouse), kappa L chain}
qivltqspaimsaspgekvtitcsasssvsnihwfqqkpgtfpklwiyststlasgvpgr
fsgsgsgtsysltisrmgaedaatyycqqrsgypftfgsgtkleik
>d1yejh1 2.1.1.1.87 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab D2.3 (mouse), kappa L chain}
emqlqqsgaellrpgtsvklscktsgyiftsywihwvkqrsgqglewiariypgtgstyy
nekfkgkatltadkssstaymqlstlksedsavyfctrwgfipvredyvmdywgqgtlvt
vss
>d1yejl1 2.1.1.1.87 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab D2.3 (mouse), kappa L chain}
divmtqspltlsvtigqpasisckssqsllysngktylnwllqrpgqspkrlihlvskld
sgvpdritgsgsgtdftlkisrveaadlgvyycvqgthfpytfgggtkleil
>d1cfvh_ 2.1.1.1.90 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1hyxh1 2.1.1.1.91 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 6D9 (mouse), kappa L chain}
evkllesggglvkpggslklscaasgftfsnyamswvrqtpekrlewvvsissggsiyyl
dsvkgrftvsrdnarnilylqmtslrsedtamyfcarvshydgsrdwyfdvwgagtsvtv
ss
>d2hrph1 2.1.1.1.92 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dvqlvesggglvqpggsrklscaasgftfmrfgmhwvrqapekglewvayissgsstiyy
adtvkgrftisrdnpkntlflqmtslrsedtalyycarsggierydgtyyvmdywgqgts
vtvss
>d2hrpl1 2.1.1.1.92 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab F11.2.32 (mouse), kappa L chain}
dtvltqspaslavslgqratiscrasesvdyygksfmnwfqqkpgqppklliyaasnqgs
gvparfsgsgsgtdfslhihpmeeddsamyfcqqskevpwtfgggtkleik
>d2ap2b_ 2.1.1.1.93 Immunoglobulin (variable domains of L and H chains) {scFv C219, (mouse sequence-based), kappa L chain}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
sg
>d1nfde1 2.1.1.1.94 (2-107) Immunoglobulin (variable domains of L and H chains) {Fab H57 (hamster), lambda(?) L chain}
yeliqpssasvtvgetvkitcsgdqlpknfaywfqqksdknillliymdnkrpsgiperf
sgstsgttatltisgaqpedeaayyclssygdnndlvfgsgtqltvlr
>d1nfdf1 2.1.1.1.94 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab H57 (hamster), lambda(?) L chain}
evylvesggdlvqpgsslkvscaasgftfsdfwmywvrqapgkglewvgriknipnnyat
eyadsvrgrftisrddsrnsiylqmnrlrvddtaiyyctragrfdhfdywgqgtmvtvss
a
>d2h1ph1 2.1.1.1.95 (301-420) Immunoglobulin (variable domains of L and H chains) {Fab 2H1 (mouse), kappa L chain}
dvklvesggglvklggslklscaasgftfssyflswvrqtpekrlelvatinsngdktyh
pdtmkgrftisrdnakntlylqmsslksedtalyycarrdssaslyfdywgqgttltvss
>d1aqkh1 2.1.1.1.96 (2-123) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
vqlvesgggvvqpgrslrlscaasgftfnnyaihwvrqapgkglewvafisydgsknyya
dsvkgrftisrdnskntlflqmnslrpedtaiyycarvlfqqlvlyapfdiwgqgtmvtv
ss
>d1aqkl1 2.1.1.1.96 (2-111) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
nvltqppsvsgapgqrvtisctgsnsnigagftvhwyqhlpgtapkllifantnrpsgvp
drfsgsksgtsaslaitglqaedeadyycqsydsslsarfgggtrltvlg
>d1d5ih1 2.1.1.1.97 (1-113) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab az-28, chimeric (mouse V domains/human C1 domains)}
qvqlqqsgaelmkpgasvkisckatgytfssywiewvkqrpghglewigeilpgsgstny
nekfkgkatftadtssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1d5il1 2.1.1.1.97 (1-107) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab az-28, chimeric (mouse V domains/human C1 domains)}
dikmtqspssmyaslgervtitckasqdinsylswfqqkpgkspktliyranrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1ar1d_ 2.1.1.1.98 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
dieltqtpvslsasvgetvtitcraseniysylawyqqkqgkspqflvynaktlgegvps
rfsgsgsgtqfslkinsllpedfgsyycqhhygtppltfgggtkleik
>d1ae6l1 2.1.1.1.99 (1-106a) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
divmtqaapsvpvtpgeslsiscrssksllhsngdtflywflqrpgqspqlliyrmsnla
sgvpdrfsgsgsgtaftlrvsrveaedvgvyycmqhleypftfgagtklelk
>d1ad9a1 2.1.1.1.100 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9b1 2.1.1.1.100 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1fgnh1 2.1.1.1.101 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1fgnl1 2.1.1.1.101 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1jrhh1 2.1.1.1.102 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A6 (mouse), kappa L chain}
avklqesgpgilkpsqtlsltcsfsgfslttygmgvgwirqssgkglewlahiwwdddky
ynpslksrltiskdtsrnqvflkitsvatadtatyycarrapfygnhamdywgqgttvtv
ss
>d1jrhl1 2.1.1.1.102 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A6 (mouse), kappa L chain}
svemtqspssfsvslgdrvtitckasediynrlawyqqkpgnaprllisgatsletevps
rfsgsgsgkdytlsitslqtedvatyycqqywstwtfgggtkleik
>d1gpol1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab M41 (artifitial design)}
dieltqspatlsvtpgnsvsiscrasqslvnedgntylfwyqqkshesprllikyasqsi
sgipsrfsgsgsgtdftlsinsvetedlavyfcqqitdwpftfgggtkleik
>d1kb5h1 2.1.1.1.104 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Desire-1 (mouse), kappa L chain}
evqlqqsgpelekpgasvkisckasgysftgynmnwvkqsngkslewignidpyyggisy
nqkfkgratltvdkssstaymqlksltsedsavyycarsrtdlyyfdywgqgttltvss
>d1a3lh1 2.1.1.1.106 (1-113) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
evqleesgpelvrpgtsvkisckasgytftnywlgwvkqrpghgfewigdiypggvyttn
nekfrgkailtadtssstaymqlssltsedsavyfcaraggyytggdywgqgtsvtvss
>d1a3ll1 2.1.1.1.106 (1-107) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
divltqaafsnpvtlgasasiscrssksllnsngiihmywylqkpgqspqlliyqmskla
sgapdrfsgsgsgtdftlrisrveaedvgvyycaqnlelpytfgggtkleik
>d1ay1l1 2.1.1.1.107 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1bgxh1 2.1.1.1.107 (5-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
qesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdynpsl
ksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1dsfh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Anticancer Fv B1}
qlvesggglvkpggslklscaasgfifsdnymywvrqtpekclewvatisdggtyidysd
svkgrftisrdnaknnlylqmsslrsedtgmyycgrspiyydyapftywgqgtlvtvsa
>d1a6ta1 2.1.1.1.109 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6tb1 2.1.1.1.109 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6wh_ 2.1.1.1.110 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1gc1h1 2.1.1.1.111 (1-129) Immunoglobulin (variable domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
qvqllesgaevkkpgssvkvsckasgdtfirysftwvrqapgqglewmgriitildvahy
aphlqgrvtitadkststvylelrnlrsddtavyfcagvyegeadegeydnngflkhwgq
gtlvtvtsa
>d1gc1l1 2.1.1.1.111 (1-109) Immunoglobulin (variable domains of L and H chains) {HIV-1 neutralizing Fab 17B (human), kappa L chain}
eleltqspatlsvspgeratlscrasesvssdlawyqqkpgqaprlliygastratgvpa
rfsgsgsgaeftltisslqsedfavyycqqynnwpprytfgqgtrleik
>d12e8h1 2.1.1.1.112 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
evqlqqsgaevvrsgasvklsctasgfnikdyyihwvkqrpekglewigwidpeigdtey
vpkfqgkatmtadtssntaylqlssltsedtavyycnaghdydrgrfpywgqgtlvtvsa
a
>d12e8l1 2.1.1.1.112 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
divmtqsqkfmstsvgdrvsitckasqnvgtavawyqqkpgqspklmiysasnrytgvpd
rftgsgsgtdftltisnmqsedladyfcqqyssypltfgagtklelk
>d1adql1 2.1.1.1.113 (2-107) Immunoglobulin (variable domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
yvltqppsvsvapgqtaritcggnnigsksvhwyqqkpgqapvlvvyddsdrppgiperf
sgsnsgntatltisrveagdeadyycqvwdsssdhavfgggtkltvlg
>d2hmid1 2.1.1.1.114 (1-123) Immunoglobulin (variable domains of L and H chains) {Fab 28 against HIV-1 RT (mouse), kappa L chain}
qitlkesgpgivqpsqpfrltctfsgfslstsgigvtwirqpsgkglewlatiwwdddnr
ynpslksrltvskdtsnnqaflnmmtvetadtaiyycaqsaitsvtdsamdhwgqgtsvt
vss
>d1bvka_ 2.1.1.1.115 Immunoglobulin (variable domains of L and H chains) {Humanized anti-lysozyme Fv HuLys11 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcrasgnihnylawyqqkpgkapklliyytttladgvps
rfsgsgsgtdytftisslqpediatyycqhfwstprtfgqgtkveikr
>d1a0qh1 2.1.1.1.116 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
vqlqesdaelvkpgasvkisckasgytftdhvihwvkqkpeqglewigyispgngdikyn
ekfkgkatltadkssstaymqlnsltsedsavylckrgyygrsnvdywgqgttltvssa
>d1a0ql1 2.1.1.1.116 (2-108) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
ieltqspsslsaslggkvtitckasqdikkyigwyqhkpgkqprllihytstllpgipsr
frgsgsgrdysfsisnlepediatyyclqyynlrtfgggtkleikr
>d1oakl1 2.1.1.1.117 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab NMC-4 (mouse), kappa L chain}
diqmtqspsslsaslgdrvtiscsasqdinkylnwyqqkpdgavkllifytsslhsgvps
rfsgsgsgtdysltisnlepediatyycqqyeklpwtfgggtklevk
>d1qfuh1 2.1.1.1.118 (1-113) Immunoglobulin (variable domains of L and H chains) {Influenza virus hemagglutinin-neutralizing Fab (mouse), kappa L chain}
qvqlqqpgaelvrpgasvklsckasgytlttywmnwfkqrpdqglewigridpydsethy
nqkfkdkailtvdrssstaymqlssltsedsavyyctrflqittiiygmdywgqgtsvtv
ss
>d35c8l1 2.1.1.1.119 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
divltqspaimsaslgervtmtctasssvsssnlhwyqqkpgsspklwiystsnlasgvp
arfsgsgsgtsysltissmeaedaatyychqyhrspytfgggtkleik
>d1a5fh1 2.1.1.1.120 (1-120) Immunoglobulin (variable domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
evalqqsgaelvkpgasvklscaasgftikdaymhwvkqkpeqglewigridsgssntny
dptfkgkatitaddssntaylqmssltsedtavyycarvglsywyamdywgqgtsvtvss
>d1axth1 2.1.1.1.121 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
evkleesggglvqpggsmklscvvsgltfsrfwmswvrqspekglewvaeirlksdnyat
hyaesvkgkftisrddsksrlylqmnslrtedtgiyyckiyfysfsywgqgtlvtvsa
>d1b2wh1 2.1.1.1.122 (2-117) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
vqlvqsgggvvqpgrslklsclasgyiftsswinwvkqrpgrglewigridpsdgevhyn
qdfkdrftisrdkskntlylqmnslrpedtavyycargflpwfadwgqgtlvtvss
>d1b2wl1 2.1.1.1.122 (1-107) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
diqmtqspstlsasvgdrvtitckasenvdtyvswyqqkpgkapklliygasnrytgvps
rfsgsgsgtdftltisslqpddfatyycgqsynypftfgqgtkvevk
>d1bfob1 2.1.1.1.123 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1ce1h1 2.1.1.1.124 (1-121) Immunoglobulin (variable domains of L and H chains) {Therapeutic CAMPATH-1H fab (rat), kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgftftdfymnwvrqppgrglewigfirdkakgytt
eynpsvkgrvtmlvdtsknqfslrlssvtaadtavyycareghtaapfdywgqgslvtvs
s
>d1ce1l1 2.1.1.1.124 (1-107) Immunoglobulin (variable domains of L and H chains) {Therapeutic CAMPATH-1H fab (rat), kappa L chain}
diqmtqspsslsasvgdrvtitckasqnidkylnwyqqkpgkapklliyntnnlqtgvps
rfsgsgsgtdftftisslqpediatyyclqhisrprtfgqgtkveik
>d1bj1h1 2.1.1.1.126 (1-123) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
evqlvesggglvqpggslrlscaasgytftnygmnwvrqapgkglewvgwintytgepty
aadfkrrftfsldtskstaylqmnslraedtavyycakyphyygsshwyfdvwgqgtlvt
vss
>d1bj1j1 2.1.1.1.126 (1-107) Immunoglobulin (variable domains of L and H chains) {VEGF neutralizing Fab-12 (mouse), kappa L chain}
diqmtqspsslsasvgdrvtitcsasqdisnylnwyqqkpgkapkvliyftsslhsgvps
rfsgsgsgtdftltisslqpedfatyycqqystvpwtfgqgtkveik
>d1bogb1 2.1.1.1.128 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-p24 (HIV-1) Fab CB 4-1 (mouse), kappa L chain}
qdqlqqsgaelvrpgasvklsckalgyiftdyeihwvkqtpvhglewiggihpgssgtay
nqkfkgkatltadkssttafmelssltsedsavyyctrkdywgqgtlvtvsa
>d1f58h1 2.1.1.1.129 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
dvqlqqsgpdlvkpsqslsltctvtgysitsgyswhwirqfpgnklewmgyihysagtny
npslksrisitrdtsknqfflqlnsvttedtatyycareeampygnqayyyamdcwgqgt
tvtvss
>d1f58l1 2.1.1.1.129 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
divltqspaslavslgqratisckasqgvdfdgasfmnwyqqkpgqppkllifaastles
giparfsgrgsgtdftlnihpveeedaatyycqqshedpltfgagtklelk
>d2mpah1 2.1.1.1.130 (1-121) Immunoglobulin (variable domains of L and H chains) {Bactericidal Fab MN12H2, (mouse), kappa L chain}
evnlqqsgtvlarpgasvrmsckasgysftsywlhwikqrpgqglewiggiypgnrdtry
tqrfkdkakltavtsantaymelssltnedsavyycsiiyfdyadfimdywgqgttvtvs
s
>d1wejh1 2.1.1.1.131 (1-112) Immunoglobulin (variable domains of L and H chains) {Anti-cytochrome c Fab E8, (mouse), kappa L chain}
evqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpekglewigridpasgntky
dpkfqdkatitadtssntaylqlssltsedtavyycagydygnfdywgqgtt
>d2pcpb1 2.1.1.1.134 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 6B5, (mouse), kappa L chain}
evqlqqsgpelvkpgasvkmsckasgytftdyyihwnkqshgkslewigyiypnnggngy
nhkfkgkatltvdkssstaymdvrtltsedsavyycgrstwddfdywgqgttltvss
>d1cf8l1 2.1.1.1.136 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
divltqsptimsvspgekvtltcsasssvssnyvywyqqkpgsspkvwiystsnlasgvp
arfsgsgsgtsysltissmeaedaasyfclqwssfpytfgggtklelk
>d1c12a1 2.1.1.1.137 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
dieltqspssmsvslgdtvsitchasqgissnigwlqqkpgksfkgliyhgtnledgvps
rfsgsgsgadysltisslesedfadyycvqyvqfpftfgsgtkleik
>d1c12b1 2.1.1.1.137 (301-413) Immunoglobulin (variable domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
qvqlqesgpglvkpsqslsltctvtgysitsdyawnwirqfpgnklewmgyisysgstsy
spslksrisltrdtsknqfflqlnsvttedtatyycvtsltwllrrkrsywgqgttvtvs
s
>d1dlfh_ 2.1.1.1.138 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
evkleesggglvqpggsmklscatsgftfsdawmdwvrqspekglewvaeirnkannhat
yyaesvkgrftisrddskrrvylqmntlraedtgiyyctgiyyhypwfaywgqgtlvtvs
>d1dlfl_ 2.1.1.1.138 Immunoglobulin (variable domains of L and H chains) {Anti-dansyl Fv, (mouse), kappa L chain}
dvvmtqtplslpvslgnqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpftfgsgtkleikr
>d43c9a_ 2.1.1.1.139 Immunoglobulin (variable domains of L and H chains) {Sterolytic and amidolytic Fv 43c9, (mouse), kappa L chain}
dvvmtqtpsslamsvgqkvtmsckssqsllnisnqknylawyqqkpgqspkllvyfastr
esgvpdrfigsgsgtdftltissvqaedqadyfcqqhyraprtfgggtkleik
>d43c9b_ 2.1.1.1.139 Immunoglobulin (variable domains of L and H chains) {Sterolytic and amidolytic Fv 43c9, (mouse), kappa L chain}
gqvqlvesgpglvapsqslsitctvsgislsrynvhwvrqspgkglewlgmiwgggsiey
npalksrlsiskdnsksqiflkmnslqtddsamyycvsygyggdrfsywgqgtlvtvs
>d1bz7a1 2.1.1.1.140 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab R24, (mouse), kappa L chain}
diqmtqitsslsvslgdrviiscrasqdignflnwyqqkpdgslklliyytsrlqsgvps
rfsgwgsgtdysltisnleeediatffcqqgktlpytfgggtkleik
>d1ct8a1 2.1.1.1.141 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 7C8, (mouse), kappa L chain}
elvmtqtpatlsvtpgdsvslscrasqsvsnklhwyqqkshesprllikfasqsipgips
rfsgsgsgsdftlsinsvetedfgiyfchqthgrpltfgagtklelk
>d1ct8b1 2.1.1.1.141 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 7C8, (mouse), kappa L chain}
qvkllesgavlvkpgasvklscktsgftfsssyinwlkqkpgqslewiawiyagsggtvy
nqhftdkarltvdtssstaymqfsslttedsaiyycaryrydegfaywgqgtlvtvsa
>d1c5da1 2.1.1.1.142 (1-106) Immunoglobulin (variable domains of L and H chains) {Fab against the main immunogenic region of the human muscle acetylcholine receptor, (rat), kappa L chain}
diqmtqsppslsaslgdkvtitcqasqdinkyiawyqqkpgkaprqlirytsilvlgtps
rfsgsgsgrdfsfsisnvasediasyyclqygnlytfgagtkleik
>d1c5db1 2.1.1.1.142 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab against the main immunogenic region of the human muscle acetylcholine receptor, (rat), kappa L chain}
evkllesgpglvqpsqtlsltctvsgfplttngvswvrqppgkglewiaaissggspyyn
salksrlsinrdtsksqvflkmnslqtedtaiyfctredgwnyfdywgpgtmvtvss
>d1cl7h1 2.1.1.1.143 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab 1696, (mouse), kappa L chain}
qiqlqqsgpelkkpgetvkisckatnyaftdysmhwvkqapggdlkyvgwintetdeptf
addfkgrfafsldtststaflqinnlknedtatyfcvrdrhdygeiftywgqgttvtvss
>d1dqqa1 2.1.1.1.144 (1-107) Immunoglobulin (variable domains of L and H chains) {Anti-lysozyme Fab HYHEL-63, (mouse), kappa L chain}
divltqspatlsvtpgdsvslscrasqsisnnlhwyqqkshesprllikyasqsisgips
rfsgsgsgtdftlsinsvetedfgmyfcqqsnswpytfgggtkleik
>d1dqqb1 2.1.1.1.144 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-lysozyme Fab HYHEL-63, (mouse), kappa L chain}
evqlqesgpslvkpsqtlsltcsvtgdsvtsdywswirkfpgnkleymgyisysgstyyh
pslksrisitrdtsknqyylqlnsvttedtatyycaswggdvwgagttvtvss
>d1vhp__ 2.1.1.1.145 Immunoglobulin (variable domains of L and H chains) {VH-P8 domain (human), camelized monomer}
evqlvesggglvqpggslrlscaasgftfssyamswvrqapgkereivsavsgsggstyy
adsvkgrftisrdnskntlylqmnslraedtavyycarlkkyafdywgqgtlvtvss
>d1mela_ 2.1.1.1.146 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-lysozyme antibody}
vqlqasgggsvqaggslrlscaasgytigpycmgwfrqapgkeregvaainmgggityya
dsvkgrftisqdnakntvyllmnslepedtaiyycaadstiyasyyecghglstggygyd
swgqgtqvtvss
>d1bzqk_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Camel (Camelus dromedarius), anti-RNase A antibody}
qvqlvesggglvqaggslrlscaasgyaytyiymgwfrqapgkeregvaamdsggggtly
adsvkgrftisrdkgkntvylqmdslkpedtatyycaaggyelrdrtygqwgqgtqvtvs
srgr
>d1hcv__ 2.1.1.1.148 Immunoglobulin (variable domains of L and H chains) {Llama (Lama glama), VH domain}
vqlqesggglvqaggslrlscaasgrtgstydmgwfrqapgkeresvaainwdsartyya
ssvrgrftisrdnakktvylqmnslkpedtavytcgageggtwdswgqgtqvtvss
>d1bwwa_ 2.1.1.1.150 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitcqasqdiikylnwyqqkpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d2rhe__ 2.1.1.1.151 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (lambda) dimer RHE (human)}
esvltqppsasgtpgqrvtisctgsatdigsnsviwyqqvpgkapklliyyndllpsgvs
drfsasksgtsaslaisglesedeadyycaawndsldepgfgggtkltvlgqpk
>d1wtla_ 2.1.1.1.153 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer WAT (human)}
diqmtqspsslsasvgdrvtitcrasqditnyvnwfqqrpgqapkvliygasiletgvps
rfsgsgsgtdftftisslqpediatyycqqydtlpltfgggtkvdikr
>d1b0wa_ 2.1.1.1.154 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1qaca_ 2.1.1.1.155 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) domain LEN (human)}
divmtqspdslavslgeratinckssqsvlyssnsknylawyqqkpgqppklliywastr
esgvpdrfsgsgsgtdftltisslqaedvavyyclqyystpysfgqgtkleikr
>d1lila1 2.1.1.1.156 (2-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones lambda L chain dimer CLE (human)}
yevtqppslsvspgqtaritcsgeklgdayvcwyqqrpgqspvvviyqdnrrpsgiperf
sgsssgntatltisgtqtldeadyycqvwdsnasvvfgggtkltvlg
>d1mcoh1 2.1.1.1.157 (1-117) Immunoglobulin (variable domains of L and H chains) {Intact antibody (lambda) MCG (human)}
plvlqesgpglvkpsealsltctvsgdsintilyywswirqppgkglewigyiyysgsty
gnpslksrvtisvntsknqfysklssvtaadtavyycarvplvvnpwgqgtlvtvss
>d1dcla1 2.1.1.1.158 (1-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
psaltqppsasgslgqsvtisctgtssnvggynyvswyqqhagkapkviiyevnkrpsgv
pdrfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1mcww1 2.1.1.1.159 (1-111) Immunoglobulin (variable domains of L and H chains) {Heterologous L chain dimer MCG-WEIR hybrid (human)}
xsaltqpasvsgspgqsitvscaghtsdvadsnsiswfqqhpdkapklliyavtfrpsgi
plrfsgsksgntasltisgllpddeadyfcmsylsdasfvfgsgtkvtvlr
>d1b6da1 2.1.1.1.160 (1-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
diqmtqspsslsasvgdrvtitcqasqdisrylrwyqqkpgkapkllihaassletgvps
rfsgsgsgtdfsftisslqpedlatyycqqydnlpltfgggtkveik
>d1d9ka_ 2.1.1.1.161 T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qvrqspqsltvwegettilncsyedstfdyfpwyrqfpgkspalliaislvsnkkedgrf
tiffnkrekklslhitdsqpgdsatyfcaatgsfnkltfgagtrlavspy
>d1kb5a_ 2.1.1.1.161 T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qqvrqspqsltvwegetailncsyedstfnyfpwyqqfpgegpallisirsvsdkkedgr
ftiffnkrekklslhitdsqpgdsatyfcaaryqggralifgtgttvsvspgsad
>d1nfda1 2.1.1.1.161 (1-117) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
dsvtqteglvtvteglpvklnctyqttyltiaffwyvqylneapqvllksstdnkrtehq
gfhatlhkssssfhlqkssaqlsdsalyycalseggnykyvfgagtrlkviah
>d1tcra1 2.1.1.1.161 (1-117) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
qsvtqpdarvtvsegaslqlrckysysatpylfwyvqyprqglqlllkyysgdpvvqgvn
gfeaefsksnssfhlrkasvhwsdsavyfcavsgfasaltfgsgtkvivlpy
>d1ac6a_ 2.1.1.1.162 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ao7d_ 2.1.1.1.162 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
keveqnsgplsvpegaiaslnctysdrgsqsffwyrqysgkspelimsiysngdkedgrf
taqlnkasqyvsllirdsqpsdsatylcavttdswgklqfgagtqvvvtpdiqnp
>d1b88a_ 2.1.1.1.162 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1bd2d1 2.1.1.1.162 (1-117) T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
qqvkqnspslsvqegrisilncdytnsmfdyflwykkypaegptflisissikdknadgr
ftvflnksakhlslhivpsqpgdsavyfcaamegaqklvfgqgtrltinpn
>d1bec_1 2.1.1.1.163 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1kb5b_ 2.1.1.1.163 T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
vtlleqnprwrlvprgqavnlrcilknsqypwmswyqqdlqkqlqwlftlrspgdkevks
lpgadylatrvtdtelrlqvanmsqgrtlyctcsaapdwgasaetlyfgsgtrltvl
>d1nfdb1 2.1.1.1.163 (1-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dsgvvqsprhiikekggrsvltcipisghsnvvwyqqtlgkelkfliqhyekverdkgfl
psrfsvqqfddyhsemnmsaleledsamyfcasslrwgdeqyfgpgtrltvle
>d1bd2e1 2.1.1.1.164 (3-118) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcassypgggfyeqyfgpgtrltvte
>d1tvda_ 2.1.1.1.165 T-cell antigen receptor {Human (Homo sapiens), delta-chain}
dkvtqsspdqtvasgsevvllctydtvysnpdlfwyrirpdysfqfvfygddsrsegadf
tqgrfsvkhiltqkafhlvispvrtedsatyycaftlppptdklifgkgtrvtvep
>d1ah1__ 2.1.1.1.166 Immunoreceptor CTLA-4 (CD152), N-terminal fragment {Human (Homo sapiens)}
amhvaqpavvlassrgiasfvceyaspgkatevrvtvlrqadsqvtevcaatymmgnelt
flddsictgtssgnqvnltiqglramdtglyickvelmypppyylgigngtqiyvidpep
cpdsdqepk
>d1frta1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d3frua1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d3frub1 2.1.1.2.1 Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
iqktpqiqvysrhppengkpnflncyvsqfhppqieiellkngkkipniemsdlsfskdw
sfyilahteftptetdvyacrvkhvtlkepktvtwdrdm
>d3fruc1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d3frue1 2.1.1.2.1 (179-269) Fc (IgG) receptor, alpha-3 domain and beta subunit {Rat (Rattus norvegicus)}
keppsmrlkarpgnsgssvltcaafsfyppelkfrflrnglasgsgncstgpngdgsfha
wsllevkrgdehhyqcqveheglaqpltvdl
>d1bmg__ 2.1.1.2.2 Class I MHC, beta2-microglobulin and alpha-3 domain {Bovine (Bos taurus)}
iqrppkiqvysrhppedgkpnylncyvygfhppqieidllkngekikseqsdlsfskdws
fyllshaeftpnskdqyscrvkhvtleqprivkwdrdl
>d1hlaa1 2.1.1.2.3 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d1duza1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1duzb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1hhka1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d3hlaa1 2.1.1.2.4 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-A2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpl
>d1hsba1 2.1.1.2.6 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-aw68}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwvavvvpsgqeqrytchvqheglpkpl
>d2hlaa1 2.1.1.2.6 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-aw68}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwvavvvpsgqeqrytchvqheglpkpl
>d1agda1 2.1.1.2.7 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1qqda1 2.1.1.2.10 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-CW4}
aehpkthvthhpvsdheatlrcwalgfypaeitltwqwdgedqtqdtelvetrpagdgtf
qkwaavvvpsgeeqrytchvqheglpepltlrw
>d1mhea1 2.1.1.2.11 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-E}
leppkthvthhpisdheatlrcwalgfypaeitltwqqdgeghtqdtelvetrpagdgtf
qkwaavvvpsgeeqrytchvqheglpepvtlrw
>d1de4a1 2.1.1.2.12 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d2mhaa1 2.1.1.2.13 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
tdspkahvthhsrpedkvtlrcwalgfypaditltwqlngeeliqdmelvetrpagdgtf
qkwasvvvplgkeqyytchvyhqglpepl
>d2mhac1 2.1.1.2.13 (182-270) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
tdspkahvthhsrpedkvtlrcwalgfypaditltwqlngeeliqdmelvetrpagdgtf
qkwasvvvplgkeqyytchvyhqglpepl
>d2vaaa1 2.1.1.2.13 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2KB}
tdspkahvthhsrpedkvtlrcwalgfypaditltwqlngeeliqdmelvetrpagdgtf
qkwasvvvplgkeqyytchvyhqglpepltlrw
>d1hoca1 2.1.1.2.14 (182-272) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DB}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpepltl
>d1mhca1 2.1.1.2.15 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H2M3}
adppkahvahhprpkgdvtlrcwalgfypaditltwqkdeedltqdmelvetrpsgdgtf
qkwaavvvpsgeeqrytcyvhheglteplalkwrs
>d1mhcb1 2.1.1.2.15 Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H2M3}
iqktpqiqvysrhppengkpnilncyvtqfhpphieiqmlkngkkipkvemsdmsfskdw
sfyilahteftptetdtyacrvkhdsmaepktvywdrdm
>d1ld9a1 2.1.1.2.16 (182-268) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2LD}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpe
>d1ld9d1 2.1.1.2.16 (182-268) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2LD}
tdspkahvthhprskgevtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgtf
qkwasvvvplgkeqnytcrvyheglpe
>d1qo3a1 2.1.1.2.17 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus), H-2DD}
tdppkahvthhrrpegdvtlrcwalgfypaditltwqlngeeltqemelvetrpagdgtf
qkwasvvvplgkeqkytchveheglpepltlrwg
>d1zaga1 2.1.1.2.18 (184-277) Zinc-alpha-2-glycoprotein, ZAG {Human (Homo sapiens)}
qdppsvvvtshqapgekkklkclaydfypgkidvhwtragevqepelrgdvlhngngtyq
swvvvavppqdtapyschvqhsslaqplvvpwea
>d1b3ja1 2.1.1.2.19 (181-274) MHC I homolog {Human (Homo sapiens) Mic-a}
tvppmvnvtrseasegnitvtcrasgfypwnitlswrqdgvslshdtqqwgdvlpdgngt
yqtwvatricqgeeqrftcymehsgnhsthpvps
>d1c16a1 2.1.1.2.20 (181-276) MHC I homolog {Mouse (Mus musculus) t22}
rsdppkahvtrhprpegdvtlrcwalgfypaditltwqlngeeltqdmelvetrpagdgt
fqkwaavvvplgkeqsytchvyheglpeplilrwgg
>d1igtb3 2.1.1.2.21 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antibody Mab231 (mouse), kappa L chain}
pcppckcpapnllggpsvfifppkikdvlmislspivtcvvvdvseddpdvqiswfvnnv
evhtaqtqthredynstlrvvsalpiqhqdwmsgkefkckvnnkdlpapiertiskpkg
>d1igtb4 2.1.1.2.21 (363-474) Immunoglobulin (constant domains of L and H chains) {Intact IgG2a antibody Mab231 (mouse), kappa L chain}
svrapqvyvlpppeeemtkkqvtltcmvtdfmpediyvewtnngktelnykntepvldsd
gsyfmysklrvekknwvernsyscsvvheglhnhhttksfsr
>d1igyb3 2.1.1.2.22 (236-361) Immunoglobulin (constant domains of L and H chains) {Intact IgG1 antibody Mab61.1.3 (mouse), kappa L chain}
gckpcictvpevssvfifppkpkdtllitvtpkvtcvvvdiskddpevqfswfvdnvevh
taqtqpreeqfnstfrvvsalpimhqdwlngkefkcrvnsaafpapiektisktkg
>d8faba2 2.1.1.2.23 (106-208) Immunoglobulin (constant domains of L and H chains) {Fab HIL (human), lambda L chain}
lgqpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspikagvetttps
kqsnnkyaassylsltpeqwkshrsyscqvthegstvektvap
>d8fabb2 2.1.1.2.23 (122-223) Immunoglobulin (constant domains of L and H chains) {Fab HIL (human), lambda L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepks
>d1a3rh2 2.1.1.2.26 (120-228) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
svyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d2fbjh2 2.1.1.2.36 (119-220) Immunoglobulin (constant domains of L and H chains) {Fab J539 (mouse), kappa L chain}
esarnptiypltlppalssdpviigclihdyfpsgtmnvtwgksgkdittvnfppalasg
grytmsnqltlpavecpegesvkcsvqhdsnpvqeldvncsg
>d1mfbl2 2.1.1.2.43 (112-212) Immunoglobulin (constant domains of L and H chains) {Fab SE155-4 (mouse), lambda L chain}
pksspsvtlfppsseeletnkatlvctitdfypgvvtvdwkvdgtpvtqgmettqpskqs
nnkymassyltltarawerhssyscqvtheghtvekslsra
>d1teth2 2.1.1.2.45 (113-213) Immunoglobulin (constant domains of L and H chains) {Fab TE33 (mouse), kappa L chain}
sakttppsvyplapgsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdlytls
ssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1cicb2 2.1.1.2.53 (118-217) Immunoglobulin (constant domains of L and H chains) {Anti-idiotope (D1.3) Fab E225, (mouse), kappa L chain}
alttppsvyplapgcgdttgssvtlgclvkgyfpepvtvtwnsgslsssvhtfpallqsg
lytmsssvtvpsstwpsetvtcsvahpassttvdkkleps
>d2jelh2 2.1.1.2.56 (114-226) Immunoglobulin (constant domains of L and H chains) {Fab JE142 (mouse), kappa L chain}
aattppsvyplapgsggqgnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlaad
lytlsssvtvpssprpsetvtcnvahpasstkvdkkiapg
>d2gfbb2 2.1.1.2.59 (120-227) Immunoglobulin (constant domains of L and H chains) {Fab CNJ206 (mouse), kappa L chain}
svyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkieprg
>d1eapb2 2.1.1.2.60 (125-221) Immunoglobulin (constant domains of L and H chains) {Fab 17E8 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgglsssvhtfpallqsg
lytmsssvtvpgggwpsatvtcsvahpassttvdkkl
>d1rmfh2 2.1.1.2.63 (120-216) Immunoglobulin (constant domains of L and H chains) {Fab R6.5 (mouse), kappa L chain}
akttapsvtplapvcgdttgssvtlgvlvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkki
>d1ibgh2 2.1.1.2.67 (114-223) Immunoglobulin (constant domains of L and H chains) {Fab 40-50 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtsgclvkgyfpepvtvtwnsgslsssvhtfpallqsg
lytmsssvtvpsstwpsqtvtcsvahpassttvdkkl
>d1iaih2 2.1.1.2.71 (122-219) Immunoglobulin (constant domains of L and H chains) {Fab 730.1.4 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtssttpsqsitcnvahpasstkvdkkid
>d1iaii2 2.1.1.2.72 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1vgel2 2.1.1.2.76 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab TR1.9 (mouse/human), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1yuhb2 2.1.1.2.77 (119-218) Immunoglobulin (constant domains of L and H chains) {Fab anti-nitrophenol (mouse/human), lambda L chain}
aattppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgalssgvhtfpavlqsd
lytlsssvtvpastwpsgtvtcnvahpasstavdkkivpr
>d1clzh2 2.1.1.2.79 (115-231) Immunoglobulin (constant domains of L and H chains) {Fab MBR96 (mouse), kappa L chain}
tttapsvyplvpgcsdtsgssvtlgclvkgyfpepvtvkwnygalssgvrtvssvlqsgf
yslsslvtvpsstwpsqtvicnvahpasktelikriepr
>d1nldh2 2.1.1.2.81 (113-215) Immunoglobulin (constant domains of L and H chains) {Fab1583, against an epitope of gp41 of HIV-1, (mouse), kappa L chain}
sasttapsvyplapvsgdqtnssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqs
dlytlsssvtvtsspwpsetitcnvahpasstkvdkkieprgc
>d1osph2 2.1.1.2.83 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 184.1 (mouse), kappa L chain}
kttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhtfpallqsgl
ytmsssvtvpsstwpsqtvtcsvahpassttvdkkle
>d1ad0b2 2.1.1.2.85 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1pskh2 2.1.1.2.90 (115-209) Immunoglobulin (constant domains of L and H chains) {Fab against a ganglioside (mouse), kappa L chain}
akttapsvyplapvcgdttgsavtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdk
>d1nfde2 2.1.1.2.96 (108-215) Immunoglobulin (constant domains of L and H chains) {Fab H57 (hamster), lambda(?) L chain}
gpksspkvtvfppspeelrtnkatlvclvndfypgsatvtwkangatindgvkttkpskq
gqnymtssylsltadqwkshnrvscqvthegetvekslspaecl
>d1nfdf2 2.1.1.2.96 (115-228) Immunoglobulin (constant domains of L and H chains) {Fab H57 (hamster), lambda(?) L chain}
tttapsvyplapacdsttsttdtvtlgclvkgyfpepvtvswnsgaltsgvhtfpsvlhs
glyslsssvtvpsstwpkqpitcnvahpasstkvdkkiepr
>d1jrhh2 2.1.1.2.103 (114-221) Immunoglobulin (constant domains of L and H chains) {Fab A6 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdk
>d1a4kb2 2.1.1.2.106 (120-213) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkvep
>d1a4kh2 2.1.1.2.106 (120-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a3lh2 2.1.1.2.107 (114-227) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivp
>d1ay1h2 2.1.1.2.108 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bgxh2 2.1.1.2.108 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1a6tb2 2.1.1.2.109 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1adqh2 2.1.1.2.112 (114-223b) Immunoglobulin (constant domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
gsasaptlfplvscensnpsstvavgclaqdflpdsitfswkyknnsdisstrgfpsvlr
ggkyaatsqvllpskdvmqgtnehvvckvqhpngnkekdvpl
>d1a5fh2 2.1.1.2.118 (121-217) Immunoglobulin (constant domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvsvptstetvtcnvahapsstkvdkkivpr
>d1bfoa2 2.1.1.2.121 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfob2 2.1.1.2.121 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1f58h2 2.1.1.2.127 (114-230) Immunoglobulin (constant domains of L and H chains) {Anti-gp120 (HIV-1) Fab 58.2, (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1wejh2 2.1.1.2.129 (113-223) Immunoglobulin (constant domains of L and H chains) {Anti-cytochrome c Fab E8, (mouse), kappa L chain}
ltvssaettppsvyplapgtaalkssmvtlgclvkgyfpepvtvtwnsgslssgvhtfpa
vlqsdlytltssvtvpsstwpsqtvtcnvahpasstkvdkkivprncggdc
>d1sm3h2 2.1.1.2.131 (114-213) Immunoglobulin (constant domains of L and H chains) {Tumor-specific Fab SM3, (mouse), lambda L chain}
akttpptvyplapgsnaasqsmvtlgclvkgyfpepvtvtwnsgslasgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdakivpr
>d2pcpb2 2.1.1.2.132 (114-226) Immunoglobulin (constant domains of L and H chains) {Fab 6B5, (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtssprpsetvtcnvahpasstkvdkkiv
>d1cf8h2 2.1.1.2.134 (114-215) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 19A4 (mouse), kappa L chain}
akttppsvyplapgcgdttgssvtlgclvkgyfpesvtvtwnsgslsssvhafpallqsd
lytmsssvtvpsstwpsqtvtcsvahpassttvdkklepkdc
>d1c12b2 2.1.1.2.135 (414-513) Immunoglobulin (constant domains of L and H chains) {Fab directed agains the musk odorant traseolide, (mouse), kappa L chain}
astkgpsvyplapgskaaasmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkivpe
>d1bz7b2 2.1.1.2.136 (123-217) Immunoglobulin (constant domains of L and H chains) {Fab R24, (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqsg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdk
>d1r24b2 2.1.1.2.136 (123-217) Immunoglobulin (constant domains of L and H chains) {Fab R24, (mouse), kappa L chain}
atttapsvyplvpgcsdtsgssvtlgclvkgyfpgpvtvkwnygalssgvrtvssvlqsg
fyslsslvtvpsstwpsqtvicnvahpasktdlik
>d1r24d2 2.1.1.2.136 (123-217) Immunoglobulin (constant domains of L and H chains) {Fab R24, (mouse), kappa L chain}
atttapsvyplvpgcsdtsgssvtlgclvkgyfpgpvtvkwnygalssgvrtvssvlqsg
fyslsslvtvpsstwpsqtvicnvahpasktdlik
>d1c5da2 2.1.1.2.138 (107-213) Immunoglobulin (constant domains of L and H chains) {Fab against the main immunogenic region of the human muscle acetylcholine receptor, (rat), kappa L chain}
radaaptvsifppsteqlatggasvvclmnnfyprdisvkwkidgterrdgvldsvtdqd
skdstysmsstlsltkadyeshnlytcevvhktssspvvksfnrnec
>d1c5db2 2.1.1.2.138 (118-215) Immunoglobulin (constant domains of L and H chains) {Fab against the main immunogenic region of the human muscle acetylcholine receptor, (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkklerr
>e1cl7.1i 2.1.1.2.139 Immunoglobulin (constant domains of L and H chains) {Fab 1696, (mouse), kappa L chain}
smvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdlytlsssvtvpssprpsetv
tcnvahpasstkvdkkivprdc
>d1dqqa2 2.1.1.2.140 (108-214) Immunoglobulin (constant domains of L and H chains) {Anti-lysozyme Fab HYHEL-63, (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1dqqb2 2.1.1.2.140 (114-221) Immunoglobulin (constant domains of L and H chains) {Anti-lysozyme Fab HYHEL-63, (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkki
>d1adqa1 2.1.1.2.146 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvsqedpqvqfnwyvdgvqvhnaktkpreqqfn
styrvvsvltvlhqnwldgkeykckvsnkglpssiektiskakg
>d1adqa2 2.1.1.2.146 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsqeemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflysrltvdksrwqegnvfscsvmhealhnhytqkslsl
>d1pfc__ 2.1.1.2.148 Immunoglobulin (constant domains of L and H chains) {Fc (guinea pig)}
rtiskakgppripevyllppprnelskkkvsltcmitgfypadinvewdssepsdykntp
pvfdtdgsfflysrlkvdtdawnngesftcsvmhealpnhviqksisrspg
>d1cqka_ 2.1.1.2.149 Immunoglobulin (constant domains of L and H chains) {Fc MAK33 (mouse)}
paapqvytipppleqmakdlvsltcmitdffpeditvewqwngqpaenykntqpimdtdg
syfvysklnvqksnweagntftcsvlheglhnhhtekslsh
>d1nfda2 2.1.1.2.150 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyqlkdprsqdstlclftdfdsqinvpktmesgtfitdktvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d1nfdc2 2.1.1.2.150 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyqlkdprsqdstlclftdfdsqinvpktmesgtfitdktvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d1tcra2 2.1.1.2.150 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyalkdprsqdstlclftdfdsqinvpktmesgtfitdatvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d2ckba2 2.1.1.2.150 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyalkdprsqdstlclftdfdsqinvpktmesgtfitdatvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d2ckbc2 2.1.1.2.150 (118-213) T-cell antigen receptor {Mouse (Mus musculus), alpha-chain}
iqnpepavyalkdprsqdstlclftdfdsqinvpktmesgtfitdatvldmkamdsksng
aiawsnqtsftcqdifketnatypssdvpc
>d1bd2d2 2.1.1.2.151 (118-203) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtf
>d1qrnd2 2.1.1.2.151 (118-206) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdkdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtffps
>d1qsed2 2.1.1.2.151 (118-206) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtffps
>d1qsfd2 2.1.1.2.151 (118-206) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtffps
>d1bec_2 2.1.1.2.152 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1qrne2 2.1.1.2.153 (119-246) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
lknvfppevavfepsaeeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpqp
lkeqpalndsryalssrlrvsatfwqnprnhfrcqvqfyglsendewtqdrakpvtqivs
aeawgrad
>d1cd1a1 2.1.1.2.154 (186-279) CD1, beta2-microglobulin and alpha-3 domain {Mouse (Mus musculus)}
qekpvawlssvpssahghrqlvchvsgfypkpvwvmwmrgdqeqqgthrgdflpnadetw
ylqatldveageeaglacrvkhsslggqdiilyw
>d1hdma1 2.1.1.2.155 (94-196) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dm}
srgfpiaevftlkplefgkpntlvcfvsnlfppmltvnwhdhsvpvegfgptfvsavdgl
sfqafsylnftpepsdifscivthepdrytaiaywvprnalps
>d1hdmb1 2.1.1.2.155 (88-185) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dm}
trppsvqvakttpfntrepvmlacyvwgfypaevtitwrkngklvmhssahktaqpngdw
tyqtlshlaltpsygdtytcvvehigapepilrdwtpg
>d1aqda1 2.1.1.2.156 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefd
>d1aqdb1 2.1.1.2.156 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1iaka1 2.1.1.2.159 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA i-ak}
atneapqatvfpkspvllgqpntlicfvdnifppvinitwlrnsksvtdgvyetsffvnr
dysfhklsyltfipsdddiydckvehwgleepvlkhwepe
>d1iakb1 2.1.1.2.159 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA i-ak}
rleqpsvvislsrtealnhhntlvcsvtdfypakikvrwfrngqeetvgvsstqlirngd
wtfqvlvmlemtprrgevytchvehpsltspitvewra
>d1ieaa1 2.1.1.2.161 (82-182) Class II MHC, C-terminal domains of alpha and beta chains {Mouse I-EK}
danvapevtvlsrspvnlgepnilicfidkfsppvvnvtwlrngrpvtegvsetvflprd
dhlfrkfhyltflpstddfydcevdhwgleeplrktwefee
>d1ieab1 2.1.1.2.161 (93-188) Class II MHC, C-terminal domains of alpha and beta chains {Mouse I-EK}
rrveptvtvyptktqplehhnllvcsvsdfypgnievrwfrngkeektgivstglvrngd
wtfqtlvmletvpqsgevytcqvehpsltdpvtvew
>d2iadb1 2.1.1.2.162 (94-188) Class II MHC, C-terminal domains of alpha and beta chains {Mouse I-AD}
rleqpnvaislsrtealnhhntlvcsvtdfypakikvrwfrngqeetvgvsstqlirngd
wtfqvlvmlemtphqgevytchvehpslkspitvew
>d1vcaa1 2.1.1.3.1 (91-199) Second domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fpkdpeihlsgpleagkpitvkcsvadvypfdrleidllkgdhlmksqefledadrksle
tkslevtftpviedigkvlvcraklhidemdsvptvrqavkelqvyisp
>d1iam_1 2.1.1.3.2 (83-185) Second domain of intercellular cell adhesion molecule-1 (ICAM-1) {Human (Homo sapiens)}
ywtpervelaplpswqpvgkqltlrcqveggapraqltvvllrgekelkrepavgepaev
tttvlvrrdhhgaqfscrteldlrpqglelfentsapyqlqtf
>d1zxq_1 2.1.1.3.3 (87-192) Second domain of intercellular cell adhesion molecule-2 (ICAM-2) {Human (Homo sapiens)}
pprqviltlqptlvavgksftiecrvptvepldsltlflfrgnetlhyetfgkaapapqe
atatfnstadredghrnfsclavldlmsrggnifhkhsapkmleiy
>d1cdh_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdi_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdj_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdu_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cdy_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1gc1c2 2.1.1.3.4 (98-181) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvlafqk
>d1wioa3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wioa4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1wiob3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wiob4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1wipa3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wipa4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1wipb3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wipb4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1wiqa3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wiqa4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d1wiqb3 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1wiqb4 2.1.1.3.4 (292-363) CD4 {Human (Homo sapiens)}
mratqlqknltcevwgptspklmlslklenkeakvskrekavwvlnpeagmwqcllsdsg
qvllesnikvlp
>d3cd4_2 2.1.1.3.4 (98-178) CD4 {Human (Homo sapiens)}
fgltansdthllqgqsltltlesppgsspsvqcrsprgkniqggktlsvsqlelqdsgtw
tctvlqnqkkvefkidivvla
>d1cid_2 2.1.1.3.5 (106-177) CD4 {Rat (Rattus rattus)}
vmkvtqpdsntltcevmgptspkmrlilkqenqearvsrqekviqvqapeagvwqcllse
geevkmdskiqv
>d1hnf_2 2.1.1.3.6 (105-182) CD2, second domain {Human (Homo sapiens)}
rvskpkiswtcinttltcevmngtdpelnlyqdgkhlklsqrvithkwttslsakfkcta
gnkvskessvepvscpek
>d1hnga2 2.1.1.3.7 (100-176) CD2, second domain {Rat (Rattus rattus)}
mvskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkcka
vnrvsqesemevvncpe
>d1hngb2 2.1.1.3.7 (100-176) CD2, second domain {Rat (Rattus rattus)}
mvskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkcka
vnrvsqesemevvncpe
>d1ccza2 2.1.1.3.8 (94-171) CD2-binding domain of CD58, second domain {Human (Homo sapiens)}
emvskpmiywecsnatltcevlegtdvelklyqgkehlrslrqktmsyqwtnlrapfkck
avnrvsqesemevvncpe
>d1vcaa2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fkiettpesrylaqigdsvsltcsttgcespffswrtqidsplngkvtnegttstltmnp
vsfgnehsylctatcesrklekgiqveiys
>d1vcab2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fkiettpesrylaqigdsvsltcsttgcespffswrtqidsplngkvtnegttstltmnp
vsfgnehsylctatcesrklekgiqveiys
>d1vsca2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fkiettpesrylaqigdsvsltcsttgcespffswrtqidsplngkvtnegttstltmnp
vsfgnehsylctatcesrklekgiqveiys
>d1vscb2 2.1.1.4.1 (1-90) N-terminal domain of vascular cell adhesion molecule-1 (VCAM-1) {Human (Homo sapiens)}
fkiettpesrylaqigdsvsltcsttgcespffswrtqidsplngkvtnegttstltmnp
vsfgnehsylctatcesrklekgiqveiys
>d1d3la2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {Human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1iam_2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {Human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1ic1a2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {Human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1ic1b2 2.1.1.4.2 (1-82) N-terminal domain of intracellular adhesion molecule-1, ICAM-1 {Human (Homo sapiens)}
qtsvspskvilprggsvlvtcstscdqpkllgietplpkkelllpgnnrkvyelsnvqed
sqpmcysncpdgqstaktfltv
>d1zxq_2 2.1.1.4.3 (1-86) N-terminal domain of intracellular adhesion molecule-2, ICAM-2 {Human (Homo sapiens)}
kvfevhvrpkklavepkgslevncsttcnqpevggletslnkilldeqaqwkhylvsnis
hdtvlqchftcsgkqesmnsnvsvyq
>d2ncm__ 2.1.1.4.4 Neural cell adhesion molecule (NCAM) {Human (Homo sapiens)}
rvlqvdivpsqgeisvgeskfflcqvagdakdkdiswfspngeklspnqqrisvvwnddd
sstltiynaniddagiykcvvtaedgtqseatvnvkifq
>d3ncma_ 2.1.1.4.4 Neural cell adhesion molecule (NCAM) {Human (Homo sapiens)}
yvmfknaptpqefkegedavivcdvvsslpptiiwkhkgrdvilkkdvrfivlsnnylqi
rgikktdegtyrcegrilargeinfkdiqviv
>d1bqsa1 2.1.1.4.5 (1-90) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
vkplqveppepvvavalgasrqltcrlacadrgasvqwrgldtslgavqsdtgrsvltvr
naslsaagtrvcvgscggrtfqhtvqllvy
>d1bqsa2 2.1.1.4.5 (91-209) Mucosal addressin cell adhesion molecule-1 (MADCAM-1) {Human (Homo sapiens)}
afpnqltvspaalvpgdpevactahkvtpvdpnalsfsllvggqelegaqalgpevqeee
eepqgdedvlfrvterwrlpplgtpvppalycqatmrlpglelshrqaipvlhsptspe
>d1tlk__ 2.1.1.4.6 Telokin {Turkey (Meleagris gallopavo)}
vaeekphvkpyftktildmdvvegsaarfdckvegypdpevmwfkddnpvkesrhfqidy
deegncsltisevcgdddakytckavnslgeatctaellvetm
>d1nct__ 2.1.1.4.7 Titin {Human (Homo sapiens), module M5}
skttlaariltkprsmtvyegesarfscdtdgepvptvtwlrkgqvlstsarhqvtttky
kstfeissvqasdegnysvvvensegkqeaeftltiqk
>d1ncu__ 2.1.1.4.7 Titin {Human (Homo sapiens), module M5}
skttlaariltkprsmtvyegesarfscdtdgepvptvtwlrkgqvlstsarhqvtttky
kstfeissvqasdegnysvvvensegkqeaeftltiqk
>d1tnm__ 2.1.1.4.7 Titin {Human (Homo sapiens), module M5}
riltkprsmtvyegesarfscdtdgepvptvtwlrkgqvlstsarhqvtttkykstfeis
svqasdegnysvvvensegkqeaeftltiqk
>d1tnn__ 2.1.1.4.7 Titin {Human (Homo sapiens), module M5}
riltkprsmtvyegesarfscdtdgepvptvtwlrkgqvlstsarhqvtttkykstfeis
svqasdegnysvvvensegkqeaeftltiqk
>d1koa_1 2.1.1.4.8 (6265-6361) Twitchin {Nematode (Caenorhabditis elegans)}
qprfivkpygtevgegqsanfycrviassppvvtwhkddrelkqsvkymkryngndyglt
inrvkgddkgeytvraknsygtkeeivflnvtrhsep
>d1wit__ 2.1.1.4.8 Twitchin {Nematode (Caenorhabditis elegans)}
lkpkiltasrkikikagfthnlevdfigapdptatwtvgdsgaalapellvdakssttsi
ffpsakradsgnyklkvknelgedeaifevivq
>d1wiu__ 2.1.1.4.8 Twitchin {Nematode (Caenorhabditis elegans)}
lkpkiltasrkikikagfthnlevdfigapdptatwtvgdsgaalapellvdakssttsi
ffpsakradsgnyklkvknelgedeaifevivq
>d1tit__ 2.1.1.4.9 Twitchin {Human (Homo sapiens), Ig repeat 27}
lievekplygvevfvgetahfeielsepdvhgqwklkgqpltaspdceiiedgkkhilil
hncqlgmtgevsfqaanaksaanlkvkel
>d1tiu__ 2.1.1.4.9 Twitchin {Human (Homo sapiens), Ig repeat 27}
lievekplygvevfvgetahfeielsepdvhgqwklkgqpltaspdceiiedgkkhilil
hncqlgmtgevsfqaanaksaanlkvkel
>d1iray1 2.1.1.4.10 (1-101) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
dkckereekiilvssaneidvrpcplnpnehkgtitwykddsktpvsteqasrihqhkek
lwfvpakvedsghyycvvrnssyclrikisakfvenepnlc
>d1iray2 2.1.1.4.10 (102-204) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
ynaqaifkqklpvagdgglvcpymeffknennelpklqwykdckpllldnihfsgvkdrl
ivmnvaekhrgnytchasytylgkqypitrviefitleenkpt
>d1iray3 2.1.1.4.10 (205-311) Type-1 interleukin-1 receptor {Human (Homo sapiens)}
rpvivspanetmevdlgsqiqlicnvtgqlsdiaywkwngsvideddpvlgedyysvenp
ankrrstlitvlniseiesrfykhpftcfaknthgidaayiqliypv
>d1cvsc_ 2.1.1.4.11 Fibroblast growth factor receptor, FGFR {Human (Homo sapiens), FGFR1}
mpvapywtspekmekklhavpaaktvkfkcpssgtpqptlrwlkngkefkpdhriggykv
ryatwsiimdsvvpsdkgnytciveneygsinhtyqldvversphrpilqaglpanktva
lgsnvefmckvysdpqphiqwlkhievngskigpdnlpyvqilktagvnttdkemevlhl
rnvsfedageytclagnsiglshhsawltvl
>d1djsa1 2.1.1.4.12 (147-250) Fibroblast growth factor receptor, FGFR {Human (Homo sapiens), FGFR2}
tlepegapywtntekxekrlhavpaantvkfrcpaggnpxptxrwlkngkefkqehrigg
ykvrnqhwslixesvvpsdkgnytcvveneygsinhtyhldvve
>d1djsa2 2.1.1.4.12 (251-362) Fibroblast growth factor receptor, FGFR {Human (Homo sapiens), FGFR2}
rsphrpilqaglpanastvvggdvefvckvysdaqphiqwikhvekngskygpdglpylk
vlkaagvnttdkeievlyirnvtfedageytclagnsigisfhsawltvlpa
>d1biha1 2.1.1.4.13 (5-98) Hemolin {Moth (Hyalophora cecropia)}
kypvlkdqpaevlfrennptvleciiegndqgvkyswkkdgksynwqehnaalrkdegsl
vflrpqasdeghyqcfaetpagvassrvisfrkt
>d1biha2 2.1.1.4.13 (99-209) Hemolin {Moth (Hyalophora cecropia)}
yliaspakthektpiegrpfqldcvlpnaypkplitwkkrlsgadpnadvtdfdrritag
pdgnlyftivtkedvsdiykyvctaknaavdeevvlveyeikgvtkdnsgy
>d1biha3 2.1.1.4.13 (210-306) Hemolin {Moth (Hyalophora cecropia)}
kgepvpqyvskdmmakagdvtmiycmygsnpmgypnyfkngkdvngnpedritrhnrtsg
krllfkttlpedegvytcevdngvgkpqkhslkltvv
>d1biha4 2.1.1.4.13 (307-395) Hemolin {Moth (Hyalophora cecropia)}
sapkyeqkpekvivvkqgqdvtipckvtglpapnvvwshnakplsggratvtdsglvikg
vkngdkgyygcratnehgdkyfetlvqvn
>d1bihb4 2.1.1.4.13 (307-395) Hemolin {Moth (Hyalophora cecropia)}
sapkyeqkpekvivvkqgqdvtipckvtglpapnvvwshnakplsggratvtdsglvikg
vkngdkgyygcratnehgdkyfetlvqvn
>d1fltx_ 2.1.1.4.14 Second domain of the Flt-1 receptor {Human (Homo sapiens)}
grpfvemyseipeiihmtegrelvipcrvtspnitvtlkkfpldtlipdgkriiwdsrkg
fiisnatykeiglltceatvnghlyktnylthrqt
>d1wwwx_ 2.1.1.4.15 NGF binding domain of trkA receptor {Human (Homo sapiens)}
vsfpasvqlhtavemhhwcipfsvdgqpapslrwlfngsvlnetsfifteflepaanetv
rhgclrlnqpthvnngnytllaanpfgqasasimaafmdnp
>d1wwbx_ 2.1.1.4.16 Ligand binding domain of trkB receptor {Human (Homo sapiens)}
vhfaptitflesptsdhhwcipftvkgnpkpalqwfyngailneskyictkihvtnhtey
hgclqldnpthmnngdytliakneygkdekqisahfmgwpgid
>d1wwca_ 2.1.1.4.17 NT3 binding domain of trkC receptor {Human (Homo sapiens)}
tvyypprvvsleepelrlehciefvvrgnppptlhwlhngqplreskiihveyyqegeis
egcllfnkpthynngnytliaknplgtanqtinghflkepfpvde
>d1gof_1 2.1.1.5.1 (538-639) Galactose oxidase, C-terminal domain {Dactylium dendroides}
gnlatrpkitrtstqsvkvggritistdssiskaslirygtathtvntdqrripltltnn
ggnsysfqvpsdsgvalpgywmlfvmnsagvpsvastirvtq
>d1qba_1 2.1.1.5.2 (781-885) Bacterial chitobiase, c-terminal domain {Serratia marcescens}
gethfvdtqalekdwlrfanilgqrelakldkggvayrlpvpgarvaggkleanialpgl
gieystdggkqwqrydakakpavsgevqvrsvspdgkrysraekv
>d1svb_1 2.1.1.5.3 (303-395) Envelope glycoprotein, domain III (C-terminal) {Tick-borne encephalitis virus, TBE}
tytmcdktkftwkraptdsghdtvvmevtfsgtkpcripvravahgspdvnvamlitpnp
tienngggfiemqlppgdniiyvgelshqwfqk
>d1cdg_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgt_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgu_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cgv_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgw_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgx_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cgy_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxe_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxf_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxh_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxi_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1cxka1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d1cxla1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d1d3ca1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d1tcma1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d1tcmb1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d2cxg_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
tatptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipa
vaggnynikvanaagtasnvydnfev
>d2dij_1 2.1.1.5.4 (497-583) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
atptighvgpmmakpgvtitidgrgfgsskgtvyfgttavsgaditswedtqikvkipav
aggnynikvanaagtasnvydnfevls
>d3cgt_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ttptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtipsv
aagnyavkvaasgvnsnaynnftilt
>d4cgt_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ttptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtipsv
aagnyavkvaasgvnsnaynnftilt
>d5cgt_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ttptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtipsv
aagnyavkvaasgvnsnaynnftilt
>d6cgt_1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d7cgt_1 2.1.1.5.4 (496-581) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ttptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtipsv
aagnyavkvaasgvnsnaynnftilt
>d8cgta1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d9cgta1 2.1.1.5.4 (495-579) Cyclodextrin glycosyltransferase, domain E {Bacillus circulans, different strains}
ettptighvgpvmgkpgnvvtidgrgfgstkgtvyfgttavtgaaitswedtqikvtips
vaagnyavkvaasgvnsnaynnfti
>d1cyg_1 2.1.1.5.5 (492-574) Cyclodextrin glycosyltransferase, domain E {Bacillus stearothermophilus}
estpiighvgpmmgqvghqvtidgegfgtntgtvkfgttaanvvswsnnqivvavpnvsp
gkynitvqsssgqtsaaydnfev
>d1pama1 2.1.1.5.6 (497-582) Cyclodextrin glycosyltransferase, domain E {Alkalophilic bacillus, sp. 1011}
ttpiignvgpmmakpgvtitidgrgfgsgkgtvyfgttavtgadivawedtqiqvkipav
pggiydirvanaagaasniydnfevl
>d1pamb1 2.1.1.5.6 (497-582) Cyclodextrin glycosyltransferase, domain E {Alkalophilic bacillus, sp. 1011}
ttpiignvgpmmakpgvtitidgrgfgsgkgtvyfgttavtgadivawedtqiqvkipav
pggiydirvanaagaasniydnfevl
>d1a47_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1ciu_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1bvza1 2.1.1.5.8 (1-120) Alpha-amylase II (TVAII), N-terminal domain {Thermoactinomyces vulgaris, r-47}
mlleaifheakgsyaypisetqlrvrlrakkgdvvrcevlyadryaspeeelahalagka
gsderfdyfeallecstkrvkyvflltgpqgeavyfgetgfsaerskagvfqyayihrse
>d1bf2_1 2.1.1.5.9 (1-162) Isoamylase, N-terminal domain {Pseudomonas amyloderamosa}
ainsmslgasydaqqanitfrvyssqatrivlylysagygvqesatytlspagsgvwavt
vpvssikaagitgavyygyrawgpnwpyasnwgkgsqagfvsdvdangdrfnpnkllldp
yaqevsqdplnpsnqngnvfasgasyrttdsgiyapkgvvlv
>d1lla_3 2.1.1.5.10 (380-628) Hemocyanin, C-terminal domain {Horseshoe crab (Limulus polyphemus), hemolymph}
pydhdvlnfpdiqvqdvtlharvdnvvhtfmreqelelkhginpgnarsikaryyhldhe
pfsyavnvqnnsasdkhatvriflapkydelgneikadelrrtaieldkfktdlhpgknt
vvrhsldssvtlshqptfedllhgvglnehkseycscgwpshllvpkgnikgmeyhlfvm
ltdwdkdkvdgsesvacvdavsycgardhkypdkkpmgfpfdrpihtehisdfltnnmfi
kdikikfhe
>d1hc2_3 2.1.1.5.11 (399-653) Hemocyanin, C-terminal domain {Spiny lobster (Panulirus interruptus)}
ppythdnlefsgmvvngvaidgelitffdefqyslinavdsgeniedveinarvhrlnhn
eftykitmsnnndgerlatfriflcpiednngitltldearwfcieldkffqkvpsgpet
iersskdssvtvpdmpsfqslkeqadnavngghdldlsayerscgipdrmllpkskpegm
efnlyvavtdgdkdteghngghdyggthaqcgvhgeaypdnrplgyplerripdervidg
vsnikhvvvkivhhl
>d1clc_2 2.1.1.5.12 (35-134) CelD cellulase, N-terminal domain {Clostridium thermocellum}
ietkvsaakitenyqfdsrirlnsigfipnhskkatiaancstfyvvkedgtivytgtat
smfdndtketvyiadfssvneegtyylavpgvgksvnfki
>d1edqa1 2.1.1.5.13 (24-132) Chitinase A, N-terminal domain {Serratia marcescens}
aapgkptiawgntkfaivevdqaataynnlvkvknaadvsvswnlwngdtgttakvllng
keawsgpstgssgtanfkvnkggryqmqvalcnadgctasdateivvad
>d1f13a1 2.1.1.5.14 (5-190) Transglutaminase factor XIII, N-terminal domain {Human (Homo sapiens), blood}
rtafggrravppnnsnaaeddlptvelqgvvprgvnlqeflnvtsvhlfkerwdtnkvdh
htdkyennklivrrgqsfyvqidfsrpydprrdlfrveyvigrypqenkgtyipvpivse
lqsgkwgakivmredrsvrlsiqsspkcivgkfrmyvavwtpygvlrtsrnpetdtyilf
npwced
>d1eut_1 2.1.1.5.15 (403-505) Sialidase, "linker" domain {Micromonospora viridifaciens}
gicapftipdvalepgqqvtvpvavtnqsgiavpkpslqldaspdwqvqgsveplmpgrq
akgqvtitvpagttpgryrvgatlrtsagnasttftvtvglld
>d1ksr__ 2.1.1.5.16 F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
adpeksyaegpgldggecfqpskfkihavdpdgvhrtdggdgfvvtiegpapvdpvmvdn
gdgtydvefepkeagdyvinltldgdnvngfpktvtvkpa
>d1qfha1 2.1.1.5.16 (646-749) F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
kpapsaehsyaegeglvkvfdnapaeftifavdtkgvartdggdpfevaingpdglvvda
kvtdnndgtygvvydapvegnynvnvtlrgnpiknmpidvkcie
>d1qfha2 2.1.1.5.16 (750-857) F-actin cross-linking gelation factor (ABP-120), one repeat (ROD 4) {Slime mold (Dictyostelium discoideum), different domains}
gangedssfgsftftvaaknkkgevktyggdkfevsitgpaeeitldaidnqdgtytaay
slvgngrfstgvklngkhiegspfkqvlgnpgkknpevksftttrtan
>d1rhoa_ 2.1.1.5.17 Rho GDP-dissociation inhibitor 1, RhoGDI {Human (Homo sapiens)}
vavsadpnvpnvvvtgltlvcssapgpleldltgdlesfkkqsfvlkegveyrikisfrv
nreivsgxkyiehtyrkgvkidktdyxvgsygpraeeyefltpveeapkgxlargsysik
srftdddktdhlswewnltikkdwk
>d1cf1a1 2.1.1.5.19 (10-182) Arrestin {Bovine (Bos taurus)}
hvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvsltcafrygq
edidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypflltfpdylpcs
vmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqhapr
>d1cf1a2 2.1.1.5.19 (183-393) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtakesfqdenfvfeefarqnlkdageyke
>d1a02n1 2.1.1.5.20 (577-678) Transcription factor NFATC, C-terminal domain {Human (Homo sapiens)}
lpmverqdtdsclvyggqqmiltgqnftseskvvftekttdgqqiwemeatvdkdksqpn
mlfveipeyrnkhirtpvkvnfyvingkrkrsqpqhftyhpv
>d1a3qa1 2.1.1.5.22 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1bfs__ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
asnlkivrmdrtagcvtggeeiyllcdkvqkddiqirfyeeeenggvwegfgdfsptdvh
rqfaivfktpkykdvnitkpasvfvqlrrksdletsepkpflyype
>d1bfta_ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1a9v__ 2.1.1.5.26 Major mite allergen {House-dust mite (Dermatophagoides pteronyssinus), Der p 2}
sqvdvkdcanheikkvlvpgchgsepciihrgkpfqleavfeanqntktakieikasidg
levdvpgidpnachymkcplvkgqqydikytwnvpkiapksenvvvtvkvmgddgvlaca
iathakird
>d1soxa1 2.1.1.5.27 (344-466) Sulfite oxidase, C-terminal domain {Chicken (Gallus gallus)}
elpvqsavtqprpgaavppgeltvkgyawsgggrevvrvdvsldggrtwkvarlmgdkap
pgrawawalweltvpveagteleivckavdssynvqpdsvapiwnlrgvlstawhrvrvs
vqd
>d2hft_1 2.1.2.1.1 (1-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
sgttntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdlt
deivkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d2hft_2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywksssqekg
efrsgkktaktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>e1dan.1t 2.1.2.1.1 Extracellular region of human tissue factor {Human (Homo sapiens)}
tvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdeivk
dvkqtylarvfsypa
>d1a21a1 2.1.2.1.2 (4-106) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
tgraynltwkstnfktilewepksidhvytvqistrlenwkskcfltaetecdltdevvk
dvgqtymarvlsyparngnttgfpeeppfrnspeftpyldtnl
>d1a21a2 2.1.2.1.2 (107-208) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
gqptiqsfeqvgtklnvtvqdartlvrrngtflslravfgkdlnytlyywrasstgkkta
ttntneflidvdkgenycfsvqavipsrkrkqrspesltect
>d1fna__ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
levvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatisglkpgvd
ytitvyavtgrgdspasskpisinyrtei
>d1fnf_1 2.1.2.1.3 (1142-1235) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
plspptnlhleanpdtgvltvswersttpditgyritttptngqqgnsleevvhadqssc
tfdnlspgleynvsvytvkddkesvpisdtiipa
>d1fnf_2 2.1.2.1.3 (1236-1326) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
vppptdlrftnigpdtmrvtwapppsidltnflvryspvkneedvaelsispsdnavvlt
nllpgteyvvsvssvyeqhestplrgrqktg
>d1fnf_3 2.1.2.1.3 (1327-1415) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
ldsptgidfsditansftvhwiapratitgyrirhhpehfsgrpredrvphsrnsitltn
ltpgteyvvsivalngreesplligqqst
>d1fnf_4 2.1.2.1.3 (1416-1509) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
vsdvprdlevvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatis
glkpgvdytitvyavtgrgdspasskpisinyrt
>d1fnha1 2.1.2.1.3 (3-92) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
paptdlkftqvtptslsaqwtppnvqltgyrvrvtpkektgpmkeinlapdsssvvvsgl
mvatkyevsvyalkdtltsrpaqgvvttle
>d1fnha2 2.1.2.1.3 (93-182) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
nvspprrarvtdatettitiswrtktetitgfqvdavpangqtpiqrtikpdvrsytitg
lqpgtdykiylytlndnarsspvvidasta
>d1fnha3 2.1.2.1.3 (183-271) Fibronectin, different Fn3 modules {Human (Homo sapiens)}
idapsnlrflattpnsllvswqppraritgyiikyekpgspprevvprprpgvteatitg
lepgteytiyvialknnqksepligrkkt
>d1ttf__ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
vsdvprdlevvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatis
glkpgvdytitvyavtgrgdspasskpisinyrt
>d1ttg__ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
vsdvprdlevvaatptslliswdapavtvryyritygetggnspvqeftvpgskstatis
glkpgvdytitvyavtgrgdspasskpisinyrt
>d2fnba_ 2.1.2.1.3 Fibronectin, different Fn3 modules {Human (Homo sapiens)}
mrgsevpqltdlsfvditdssiglrwtplnsstiigyritvvaagegipifedfvdssvg
yytvtglepgidydisvitlinggesapttltqqt
>d1mfn_1 2.1.2.1.4 (1-92) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
gldsptgfdssditansftvhwvaprapitgyiirhhaehsvgrprqdrvppsrnsitlt
nlnpgteyvvsiiavngreesppligqqatvs
>d1mfn_2 2.1.2.1.4 (93-184) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
diprdleviastptsllisweppavsvryyritygetggnspvqeftvpgskstatinni
kpgadytitlyavtgrgdspasskpvsinykt
>d2mfn_1 2.1.2.1.4 (1-92) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
gldsptgfdssditansftvhwvaprapitgyiirhhaehsvgrprqdrvppsrnsitlt
nlnpgteyvvsiiavngreesppligqqatvs
>d2mfn_2 2.1.2.1.4 (93-184) Fibronectin, different Fn3 modules {Mouse (Mus musculus)}
diprdleviastptsllisweppavsvryyritygetggnspvqeftvpgskstatinni
kpgadytitlyavtgrgdspasskpvsinykt
>d1qr4a1 2.1.2.1.5 (1-87) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
dnpkdlevsdptettlslrwrrpvakfdryrltyvspsgkknemeipvdstsfilrglda
gteytislvaekgrhkskpttikgstv
>d1qr4a2 2.1.2.1.5 (88-175) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
vgspkgisfsditensatvswtpprsrvdsyrvsyvpitggtpnvvtvdgsktrtklvkl
vpgvdynvniisvkgfeesepisgilkt
>d1qr4b1 2.1.2.1.5 (1-87) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
dnpkdlevsdptettlslrwrrpvakfdryrltyvspsgkknemeipvdstsfilrglda
gteytislvaekgrhkskpttikgstv
>d1qr4b2 2.1.2.1.5 (88-175) Tenascin, a Fn3 repeat {Human (Homo sapiens)}
vgspkgisfsditensatvswtpprsrvdsyrvsyvpitggtpnvvtvdgsktrtklvkl
vpgvdynvniisvkgfeesepisgilkt
>d1ten__ 2.1.2.1.5 Tenascin, a Fn3 repeat {Human (Homo sapiens)}
rldapsqievkdvtdttalitwfkplaeidgieltygikdvpgdrttidltedenqysig
nlkpdteyevslisrrgdmssnpaketftt
>d1cfb_1 2.1.2.1.6 (610-709) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
ivqdvpnapkltgitcqadkaeihweqqgdnrspilhytiqfntsftpaswdaayekvpn
tdssfvvqmspwanytfrviafnkigasppsahsdscttq
>d1cfb_2 2.1.2.1.6 (710-814) Neuroglian, two amino proximal Fn3 repeats {Drosophila melanogaster}
pdvpfknpdnvvgqgtepnnlviswtpmpeiehnapnfhyyvswkrdipaaawennnifd
wrqnniviadqptfvkylikvvaindrgesnvaaeevvgysgedr
>d1qg3a1 2.1.2.1.7 (1126-1217) Integin beta-4 subunit {Human (Homo sapiens)}
dlgapqnpnakaagsrkihfnwlppsgkpmgyrvkywiqgdseseahlldskvpsveltn
lypycdyemkvcaygaqgegpysslvscrthq
>d1qg3a2 2.1.2.1.7 (1218-1320) Integin beta-4 subunit {Human (Homo sapiens)}
evpsepgrlafnvvsstvtqlswaepaetngeitayevcyglvnddnrpigpmkkvlvdn
pknrmllienlresqpyrytvkarngagwgpereaiinlatqp
>d1axib1 2.1.2.1.8 (32-130) Growth hormone receptor {Human (Homo sapiens)}
epkftkcrsperetfschwtdevhhgtknegpiqlfytrrntqewtqewkecpdyvsage
nscyfnssftsiaipycikltsnggtvdekcfsvdeivq
>d1axib2 2.1.2.1.8 (131-236) Growth hormone receptor {Human (Homo sapiens)}
pdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkmmd
pilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqm
>d1eerb1 2.1.2.1.9 (8-116) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
dpkfeskaallaargpeellcfterledlvcfweeaasagvgpgqysfsyqledepwklc
rlhqaptargavrfwcslptadtssfvplelrvtaasgapryhrvihin
>d1eerb2 2.1.2.1.9 (117-220) Erythropoietin (EPO) receptor {Human (Homo sapiens)}
evvlldapvglvarladesghvvlrwlpppetpmtshiryevdvsagqgagsvqrveile
grtecvlsnlrgrtrytfavrarmaepsfggfwsewsepvsllt
>d1bp3b1 2.1.2.1.10 (202-300) Prolactin receptor {Human (Homo sapiens)}
lppgkpeifkcrspnketftcwwrpgtdgglptnysltyhregetlmhecpdyitggpns
chfgkqytsmwrtyimmvnatnqmgssfsdelyvdvtyi
>d1bp3b2 2.1.2.1.10 (301-404) Prolactin receptor {Human (Homo sapiens)}
vqpdpplelavevkqpedrkpylwikwspptlidlktgwftllyeirlkpekaaeweihf
agqqtefkilslhpgqkylvqvrckpdhgywsawspatfiqips
>d1gcf__ 2.1.2.1.11 Granulocyte colony-stimulating factor (GC-SF) receptor {Mouse (Mus musculus)}
gssleppmlqaldigpdvvshqpgclwlswkpwkpseymeqecelryqpqlkganwtlvf
hlpsskdqfelcglhqapvytlqmrcirsslpgfwspwspglqlrptmk
>d1jrhi_ 2.1.2.1.12 Interferon-gamma receptor alpha chain {Human (Homo sapiens)}
svptptnvtiesynmnpivyweyqimpqvpvftvevknygvknsewidacinishhycni
sdhvgdpsnslwvrvkarvgqkesayakseefavs
>d1bqua1 2.1.2.1.13 (5-99) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
glppekpknlscivnegkkmrcewdggrethletnftlksewathkfadckakrdtptsc
tvdystvyfvnievwveaenalgkvtsdhinfdpv
>d1bqua2 2.1.2.1.13 (100-214) Cytokyne receptor gp130 cytokine-binding domains {Human (Homo sapiens)}
ykvkpnpphnlsvinseelssilkltwtnpsiksviilkyniqyrtkdastwsqippedt
astrssftvqdlkpfteyvfrircmkedgkgywsdwseeasgityedrpskepsf
>d1nkr_1 2.1.2.1.15 (6-101) Killer cell inhibitory receptor {Human (Homo sapiens), p58-cl42 kir}
rkpsllahpgplvkseetvilqcwsdvmfehfllhregmfndtlrligehhdgvskanfs
isrmtqdlagtyrcygsvthspyqvsapsdpldivi
>d1nkr_2 2.1.2.1.15 (102-200) Killer cell inhibitory receptor {Human (Homo sapiens), p58-cl42 kir}
iglyekpslsaqpgptvlagenvtlscssrssydmyhlsregeaherrlpagpkvngtfq
adfplgpathggtyrcfgsfhdspyewskssdpllvsvt
>d2dlia1 2.1.2.1.16 (5-101) Killer cell inhibitory receptor {Human (Homo sapiens), 2dl2}
hrkpsllahpgrlvkseetvilqcwsdvrfehfllhregkfkdtlhligehhdgvskanf
sigpmmqdlagtyrcygsvthspyqlsapsdpldivi
>d2dlia2 2.1.2.1.16 (102-200) Killer cell inhibitory receptor {Human (Homo sapiens), 2dl2}
tglyekpslsaqpgptvlagesvtlscssrssydmyhlsregeahecrfsagpkvngtfq
adfplgpathggtyrcfgsfrdspyewsnssdpllvsvi
>d1bpv__ 2.1.2.1.17 Type I titin module {Human (Homo sapiens)}
spidppgkpvplnitrhtvtlkwakpeytggfkitsyivekrdlpngrwlkanfsnilen
eftvsgltedaayefrviaknaagaisppsepsdaitcrddvea
>d1b4ra_ 2.1.3.1.1 Polycystein-1, PKD-1 {Human (Homo sapiens)}
atlvgphgplasgqlaafhiaaplpvtatrwdfgdgsaevdaagpaashryvlpgryhvt
avlalgagsallgtdvqvea
>d1bgla1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgla2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bhga1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1f13a2 2.1.5.1.1 (516-627) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
snvdmdfevenavlgkdfklsitfrnnshnrytitaylsanitfytgvpkaefkketfdv
tleplsfkkeavliqageymgqlleqaslhffvtarinetrdvlakqkstvl
>d1f13a3 2.1.5.1.1 (628-728) Coagulation factor XIII, two C-terminal domains {Human (Homo sapiens), blood}
tipeiiikvrgtqvvgsdmtvtveftnplketlrnvwvhldgpgvtrpmkkmfreirpns
tvqweevcrpwvsghrkliasmssdslrhvygeldvqiqrr
>d1ncia_ 2.1.6.1.1 N-cadherin (uvomorulin), domain 1 {Mouse (Mus musculus)}
gsdwvippinlpensrgpfpqelvrirsgrdknlslrysvtgpgadqpptgifiinpisg
qlsvtkpldreliarfhlrahavdingnqvenpidivinvid
>d1ncja2 2.1.6.1.1 (102-215) N-cadherin (uvomorulin), domain 1 {Mouse (Mus musculus)}
ndnrpeflhqvwngsvpegskpgtyvmtvtaidaddpnalngmlryrivsqapstpspnm
ftinnetgdiitvaagldrekvqqytliiqatdmegnptyglsntatavitvtd
>d1edha1 2.1.6.1.2 (3-101) E-CADHERIN DOMAINS 1 AND 2 {Mouse (Mus musculus)}
vippiscpenekgefpknlvqiksnrdketkvfysitgqgadkppvgvfiieretgwlkv
tqpldreaiakyilyshavssngeavedpmeivitvtdq
>d1edha2 2.1.6.1.2 (102-213) E-CADHERIN DOMAINS 1 AND 2 {Mouse (Mus musculus)}
ndnrpeftqevfegsvaegavpgtsvmkvsatdadddvntynaaiaytivsqdpelphkn
mftvnrdtgvisvltsgldresyptytlvvqaadlqgeglsttakavitvkd
>d2mcm__ 2.1.7.1.1 Macromycin {Streptomyces macromomyceticus}
apgvtvtpatglsngqtvtvsatgltpgtvyhvgqcavvepgvigcdattstdvtadaag
kitaqlkvhssfqavvgadgtpwgtvnckvvscsaglgsdsgegaaqaitfa
>d1noa__ 2.1.7.1.2 Neocarzinostatin {Streptomyces carzinostaticis}
aaptatvtpssglsdgtvvkvagaglqagtaydvgqcawvdtgvlacnpadfssvtadan
gsastsltvrrsfegflfdgtrwgtvdcttaacqvglsdaagngpegvaisfn
>d1acx__ 2.1.7.1.3 Actinoxanthin {Actinomyces globisporus, number 1131}
apafsvspasgasdgqsvsvsvaaagetyyiaqcapvggqdacnpatatsfttdasgaas
fsftvrksyagqtpsgtpvgsvdcatdacnlgagnsglnlghvaltfg
>d1akp__ 2.1.7.1.4 Kedarcidin (apo form) {Actimomycete strain L585-6}
asaavsvspatgladgatvtvsasgfatstsatalqcailadgrgacnvaefhdfslsgg
egttsvvvrrsftgyvmpdgpevgavdcdtapggceivvggntgeygnaaisfg
>d1mfma_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavavlkgdgpvqgiinfeqkesngpvkvwgsikglteglhgfhvheeedntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhsiigrtlvvh
ekaddlgkggneqstktgnagsrlacgvigiaq
>d1srda_ 2.1.8.1.4 Cu,Zn superoxide dismutase, SOD {Spinach (Spinacia oleracea)}
atkkavavlkgtsnvegvvtltqeddgpttvnvrisglapgkhgfhlhefgdttngcmst
gphfnpdkkthgapedevrhagdlgnivantdgvaeativdnqipltgpnsvvgralvvh
eleddlgkgghelspttgnaggrlacgvvgltpv
>d1jcv__ 2.1.8.1.5 Cu,Zn superoxide dismutase, SOD {Baker's yeast (Saccharomyces cerevisiae)}
vqavavlkgdagvsgvvkfeqasesepttvsyeiagnspnaergfhihefgdatngcvsa
gphfnpfkkthgaptdevrhvgdmgnvktdengvakgsfkdslikligptsvvgrsvvih
agqddlgkgdteeslktgnagprpacgvigltn
>d1yaia_ 2.1.8.1.6 Cu,Zn superoxide dismutase, SOD {Photobacterium leiognathi}
qdltvkmtdlqtgkpvgtielsqnkygvvftpeladltpgmhgfhihqngscassekdgk
vvlggaagghydpehtnkhgfpwtddnhkgdlpalfvsanglatnpvlaprltlkelkgh
aimihaggdnhsdmpkalggggarvacgviq
>d1eso__ 2.1.8.1.7 Cu,Zn superoxide dismutase, SOD {Escherichia coli}
asekvemnlvtsqgvgqsigsvtitetdkglefspdlkalppgehgfhihakgscqpatk
dgkasaaesagghldpqntgkhegpegaghlgdlpalvvnndgkatdaviaprlksldei
kdkalmvhvggdnmsdqpkplggggeryacgvik
>d1qupa1 2.1.8.1.9 (74-222) Copper chaperone for superoxide dismutase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
gkpnssavailetfqkytidqkkdtavrglarivqvgenktlfditvngvpeagnyhasi
hekgdvskgvestgkvwhkfdepiecfnesdlgknlysgktflsaplptwqligrsfvis
kslnhpenepssvkdysflgviarsagvw
>d1qtsa1 2.1.9.1.1 (692-824) Alpa-adaptin AP2, N-terminal subdomain {Mouse (Mus musculus)}
gspgirlgssednfarfvcknngvlfenqllqiglksefrqnlgrmfifygnktstqfln
ftptlicaddlqtnlnlqtkpvdptvdggaqvqqvvniecisdfteapvlniqfryggtf
qnvsvklpitlnk
>d1qpxa1 2.1.10.1.1 (1-124) Pilus chaperone PapD, N-domain {Escherichia coli}
avsldrtravfdgseksmtldisndnkqlpylaqawienenqekiitgpviatppvqrld
pgaksmvrlsttpdisklpqdreslfyfnlreipprsekanvvqialctkiklfyrpaai
ktrp
>d1quna1 2.1.10.1.2 (1-121) Periplasmic chaperone FimC {Escherichia coli}
gvalgatrviypagqkqvqlavtnndenstyliqswvenadgvkdgrfivtpplfamkgk
kentlrildatnnqlpqdreslfwmnvkaipsmdkskltentlqlaiisriklyyrpakl
a
>d1mspa_ 2.1.10.2.1 Major sperm protein, alpha isoform (recombinant), ph 4.6 {Pig roundworm (Ascaris suum)}
svppgdintqpsqkivfnapyddkhtyhikitnaggrrigwaikttnmrrlsvdppcgvl
dpkekvlmavscdtfnaatedlnndritiewtntpdgaakqfrrewfqgdgmvrrknlpi
eynl
>d4kbpa1 2.1.11.1.1 (9-120) Purple acid phosphatase, N-terminal domain {Kidney bean (Phaseolus vulgaris)}
rdmpldsdvfrvppgynapqqvhitqgdlvgramiiswvtmdepgssavrywsekngrkr
iakgkmstyrffnyssgfihhttirklkyntkyyyevglrnttrrfsfitpp
>d1dfx_1 2.1.12.1.1 (37-125) Desulfoferrodoxin C-terminal domain {Desulfovibrio desulfuricans}
vegstdgamekhvpviekvdggylikvgsvphpmeekhwiewielladgrsytkflkpgd
apeaffaidaskvtareycnlhghwkaen
>d1inma1 2.1.13.1.1 (1-93) Intimin {Escherichia coli}
iteikadkttavangqdaitytvkvmkgdkpvsnqevtftttlgklsnstektdtngyak
vtltsttpgkslvsarvsdvavdvkapevefft
>d1inma2 2.1.13.1.1 (94-182) Intimin {Escherichia coli}
tltiddgnieivgtgvkgklptvwlqygqvnlkasggngkytwrsanpaiasvdassgqv
tlkekgtttisvissdnqtatytiatpns
>d1cwva1 2.1.13.1.2 (503-596) Invasin {(Yersinia pseudotuberculosis)}
ltltaavigdgapangktaitveftvadfegkplagqevvittnngalpnkitektdang
varialtnttdgvtvvtaevegqrqsvdthfvkg
>d1cwva2 2.1.13.1.2 (597-692) Invasin {(Yersinia pseudotuberculosis)}
tiaadkstlaavptsiiadglmastitlelkdtygdpqaganvafdttlgnmgvitdhnd
gtysapltsttlgvatvtvkvdgaafsvpsvtvnft
>d1cwva3 2.1.13.1.2 (693-795) Invasin {(Yersinia pseudotuberculosis)}
adpipdagrssftvstpdiladgtmsstlsfvpvdknghfisgmqglsftqngvpvsisp
iteqpdsytatvvgnsvgdvtitpqvdtlilstlqkkislfpv
>d1cwva4 2.1.13.1.2 (796-886) Invasin {(Yersinia pseudotuberculosis)}
ptltgilvngqnfatdkgfpktifknatfqlqmdndvanntqyewsssftpnvsvndqgq
vtityqtysevavtakskkfpsysvsyrfyp
>d1ddt_1 2.2.1.1.1 (381-535) Diphtheria toxin, C-terminal domain {Corynebacterium diphtheriae}
spghktqpflhdgyavswntvedsiirtgfqgesghdikitaentplpiagvllptipgk
ldvnkskthisvngrkirmrcraidgdvtfcrpkspvyvgngvhanlhvafhrsssekih
sneissdsigvlgyqktvdhtkvnsklslffeiks
>d1exh__ 2.2.2.1.1 Exo-1,4-beta-D-glycanase (cellulase, xylanase) {Cellulomonas fimi}
assgpagcqvlwgvnqwntgftanvtvkntssapvdgwtltfsfpsgqqvtqawsstvtq
sgsavtvrnapwngsipaggtaqfgfngshtgtnaaptafslngtpctvg
>d1xbd__ 2.2.2.1.2 Xylan binding domain {Cellulomonas fimi}
tgcsvtatraeewsdrfnvtysvsgssawtvnlalngsqtiqaswnanvtgsgstrtvtp
ngsgntfgvtvmkngssttpaatcags
>d2xbd__ 2.2.2.1.2 Xylan binding domain {Cellulomonas fimi}
tgcsvtatraeewsdrfnvtysvsgssawtvnlalngsqtiqaswnanvtgsgstrtvtp
ngsgntfgvtvmkngssttpaatcags
>d1nbca_ 2.2.2.2.1 Cellusomal scaffolding protein A, scafoldin {Clostridium thermocellum}
nlkvefynsnpsdttnsinpqfkvtntgssaidlskltlryyytvdgqkdqtfwcdhaai
igsngsyngitsnvkgtfvkmssstnnadtyleisftggtlepgahvqiqgrfakndwsn
ytqsndysfksasqfvewdqvtaylngvlvwgkep
>d1tf4a2 2.2.2.2.2 (461-605) Endo/exocellulase:cellobiose E-4, C-terminal domain {Thermomonospora fusca}
peifveaqintpgttfteikamirnqsgwparmldkgtfrywftldegvdpaditvssay
nqcatpedvhhvsgdlyyveidctgekifpggqsehrrevqfriaggpgwdpsndwsfqg
ignelapapyivlyddgvpvwgtap
>d1aoha_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
avrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgelivdpn
ptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvikfvev
ggfanndlveqktqffdggvnvg
>d1qba_2 2.2.2.3.1 (28-200) Bacterial chitobiase, n-terminal domain {Serratia marcescens}
dqqlvdqlsqlklnvkmldnragengvdcaalgadwascnrvlftlsndgqaidgkdwvi
yfhsprqtlrvdndqfkiahltgdlykleptakfsgfpagkaveipvvaeywqlfrndfl
prwyatsgdakpkmlantdtenldqfvapftgdqwkrtkddknilmtpasrfv
>d1amx__ 2.2.3.1.1 Collagen-binding domain of adhesin {Staphylococcus aureus}
tssvfyyktgdmlpedtthvrwflninneksyvskditikdqiqggqqldlstlninvtg
thsnyysgqsaitdfekafpgskitvdntkntidvtipqgygsynsfsinyktkitneqq
kefvnnsqawyqehgkeevngksfnhtvhn
>d1qunb1 2.2.3.2.1 (1-158) Mannose-specific adhesin FimH {Escherichia coli}
facktangtaipigggsanvyvnlapvvnvgqnlvvdlstqifchndypetitdyvtlqr
gsayggvlsnfsgtvkysgssypfpttsetprvvynsrtdkpwpvalyltpvssaggvai
kagsliavlilrqtnnynsddfqfvwniyanndvvvpt
>d1qunb2 2.2.3.2.1 (159-279) Mannose-specific adhesin FimH {Escherichia coli}
ggcdvsardvtvtlpdypgsvpipltvycaksqnlgyylsgttadagnsiftntasfspa
qgvgvqltrngtiipanntvslgavgtsavslgltanyartggqvtagnvqsiigvtfvy
q
>d1pdkb_ 2.2.3.2.2 PapK pilus subunit {Escherichia coli}
lldrpchvsgdslnkhvvfktrasrdfwyppgrsptesfvirlenchatavgkivtltfk
gteeaalpghlkvtgvnagrlgialldtdgssllkpgtshnkgqgekvtgnslelpfgay
vvatpealrtksvvpgdyeatatfeltyr
>d1ayoa_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1ycsa_ 2.2.5.1.1 p53 tumor supressor, DNA-binding domain {Human (Homo sapiens)}
vpsqktyqgsygfrlgflhsgtaksvtctyspalnkmfcqlaktcpvqlwvdstpppgtr
vramaiykqsqhmtevvrrcphhercsdsdglappqhlirvegnlrveylddrntfrhsv
vvpyeppevgsdcttihynymcnsscmggmnrrpiltiitledssgnllgrnsfevrvca
cpgrdrrteee
>d1a02n2 2.2.5.1.2 (399-576) Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
wplssqsgsyelrievqpkphhrahyetegsrgavkaptgghpvvqlhgymenkplglqi
figtaderilkphafyqvhritgktvtttsyekivgntkvleiplepknnmratidcagi
lklrnadielrkgetdigrkntrvrlvfrvhipessgrivslqtasnpiecsqrsahe
>d1svcp2 2.2.5.1.3 (43-250) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Human (Homo sapiens)}
pylqileqpkqrgfrfryvaegpshgglpgasseknkksypqvkicnyvgpakvivqlvt
ngknihlhahslvgkhcedgictvtagpkdmvvgfanlgilhvtkkkvfetlearmteac
irgynpgllvhpdlaylqaegggdrqlgdrekelirqaalqqtkemdlsvvrlmftaflp
dstgsftrrlepvvsdaiydskapnasn
>d1a3qa2 2.2.5.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1ikna2 2.2.5.1.5 (19-191) p65 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
pyveiieqpkqrgmrfrykcegrsagsipgerstdttkthptikingytgpgtvrislvt
kdpphrphphelvgkdcrdgyyeadlcpdrsihsfqnlgiqcvkkrdleqaisqriqtnn
npfhvpieeqrgdydlnavrlcfqvtvrdpagrpllltpvlshpifdnrapnt
>d1bvoa_ 2.2.5.1.7 Dorsal homologue Gambif1 {African malaria mosquito (Anopheles gambiae)}
pyveiteqphpkalrfryecegrsagsipgvnttaeqktfpsiqvhgyrgravvvvscvt
kegpehkphphnlvgkegckkgvctveinsttmsytfnnlgiqcvkkkdveealrlrqei
rvdpfrtgfghakepgsidlnavrlcfqvflegqqrgrftepltpvvsdiiydkk
>d1xbra_ 2.2.5.1.8 T domain from Brachyury transcription factor {African clawed frog (Xenopus laevis)}
elkvsleerdlwtrfkeltnemivtkngrrmfpvlkvsmsgldpnamytvlldfvaadnh
rwkyvngewvpggkpepqapscvyihpdspnfgahwmkdpvsfskvkltnkmngggqiml
nslhkyeprihivrvggtqrmitshsfpetqfiavtayqneeitalkikhnpfakaflda
kern
>d1bg1a2 2.2.5.1.10 (322-575) STAT3b {Mouse (Mus musculus)}
vverqpcmpmhpdrplviktgvqfttkvrllvkfpelnyqlkikvcidkdsgdvaalrgs
rkfnilgtntkvmnmeesnngslsaefkhltlreqrcgnggrancdaslivteelhlitf
etevyhqglkidlethslpvvvisnicqmpnawasilwynmltnnpknvnfftkppigtw
dqvaevlswqfssttkrglsieqlttlaekllgpgvnysgcqitwakfckenmagkgfsf
wvwldniidlvkky
>d1cmoa_ 2.2.5.1.11 Acute myeloid leukemia 1 protein (AML1), RUNT domain {Human (Homo sapiens)}
vevladhpgelvrtdspnflcsvlpthwrsnktlpiafkvvalgdvpdgtlvtvmagnde
nysaelrnataamknqvarfndlrfvgrsgrgksftltitvftnppqvatyhraikitvd
gpreprr
>d1ci3m1 2.2.6.1.3 (1-169,232-249) Cytochrome f, large domain {Phormidium laminosum}
ypfwaqqnyanpreatgrivcanchlaakpaeievpqavlpdsvfkavvkipydhsvqqv
qadgskgplnvgavlmlpegftiapedripeemkeevgpsylfqpyaddkqnivlvgplp
gdeyeeivfpvlspnpatnksvafgkysihlganrgrgqiyptgeksnnXnvggfgqkdt
eivlqspn
>d1bw8a_ 2.2.7.1.1 Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor {Rat (Rattus norvegicus)}
igwrregikyrrnelfldvlesvnllmspqgqvlsahvsgrvvmksylsgmpeckfgmnd
kiviekqgkgtadetsksgkqsiaiddctfhqcvrlskfdsersisfippdgefelmryr
ttkdiilpfrviplvrevgrtklevkvviksnfkpsllaqkievriptplntsgvqvicm
kgkakykasenaivwkikrmagmkesqisaeiellptndkkkwarppismnfevpfapsg
lkvrylkvfepklnysdhdvikwvryigrsgiyetrc
>d1cgt_2 2.3.1.1.1 (580-684) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
ltgdqvtvrfvvnnasttlgqnlyltgnvaelgnwstgstaigpafnqvihqyptwyydv
svpagkqlefkffkkngstitwesgsnhtfttpasgtatvtvnwq
>d1tcma2 2.3.1.1.1 (582-686) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus circulans}
lsgdqvsvrfvvnnattalgqnvyltgsvselgnadpakaigpmynqvvyqypnwyydvs
vpagktiefkflkkqgstvtweggsnhtftapssgtatinvnwqp
>d1cyg_2 2.3.1.1.2 (575-680) Cyclodextrin glycosyltransferase, C-terminal domain {Bacillus stearothermophilus}
ltndqvsvrfvvnnattnlgqniyivgnvyelgnwdtskaigpmfnqvvysyptwyidvs
vpegktiefkfikkdsqgnvtwesgsnhvyttptnttgkiivdwqn
>d1pama2 2.3.1.1.3 (583-686) Cyclodextrin glycosyltransferase, C-terminal domain {Alkalophilic bacillus, sp. 1011}
tgdqvtvrfvinnattalgqnvfltgnvselgnwdpnnaigpmynqvvyqyptwyydvsv
pagqtiefkflkkqgstvtwegganrtfttptsgtatvnvnwqp
>d1ciu_2 2.3.1.1.4 (579-683) Cyclodextrin glycosyltransferase, C-terminal domain {Thermoanaerobacterium thermosulfurigenes, EM1}
ltgnqicvrfvvnnastvygenvyltgnvaelgnwdtskaigpmfnqvvyqyptwyydvs
vpagttiqfkfikkngntitweggsnhtytvpssstgtvivnwqq
>d1acz__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1cqya_ 2.3.1.1.6 beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1vcbc_ 2.3.2.1.1 VHL {Human (Homo sapiens)}
lrsvnsrepsqvifcnrsprvvlpvwlnfdgepqpyptlppgtgrrihsyrghlwlfrda
gthdgllvnqtelfvpslnvdgqpifanitlpvytlkerclqvvrslvkpenyrrldivr
slyedledhpnvqkdlerltqe
>d1etb1_ 2.3.3.1.1 Transthyretin (synonym: prealbumin) {Human (Homo sapiens)}
kcplmvkvldavrgspainvavhvfrkaaddtwepfasgktsesgelhgltteeefvegi
ykveidtksywkalgispfhehaevvftandsgprrytiatllspysysttavvtnpk
>d1tfpa_ 2.3.3.1.3 Transthyretin (synonym: prealbumin) {Chicken (Gallus gallus)}
cplmvkvldavrgspaanvavkvfkkaadgtwqdfatgkttefgeiheltteeqfvegvy
rvefdtssywkglglspfheyadvvftandsghrhytiaallspfsysttavvs
>d3pcca_ 2.3.4.1.1 Protocatechuate-3,4-dioxygenase, alpha chain {Pseudomonas aeruginosa}
piellpetpsqtagpyvhiglaleaagnptrdqeiwnrlakpdapgehilllgqvydgng
hlvrdsflevwqadangeyqdaynlenafnsfgrtattfdagewtlhtvkpgvvnnaagv
pmaphinislfarginihlhtrlyfddeaqanakcpvlnlieqpqrretliakrcevdgk
tayrfdiriqgegetvffdf
>d3pccm_ 2.3.4.1.2 Protocatechuate-3,4-dioxygenase, beta chain {Pseudomonas aeruginosa}
paqdnsrfvirdrnwhpkaltpdyktsiarsprqalvsipqsisettgpnfshlgfgahd
hdlllnfnngglpigeriivagrvvdqygkpvpntlvemwqanaggryrhkndrylapld
pnfggvgrcltdsdgyysfrtikpgpypwrngpndwrpahihfgisgpsiatklitqlyf
egdplipmcpivksianpeavqqliakldmnnanpmdclayrfdivlrgqrkthfe
>d1bvnt_ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
vsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgyigs
hgharylarcl
>d1hoe__ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d2ait__ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d3ait__ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d4ait__ 2.4.1.1.1 alpha-Amylase inhibitor tendamistat {Streptomyces tendae}
dttvsepapscvtlyqswrysqadngcaetvtvkvvyeddteglcyavapgqittvgdgy
igshgharylarcl
>d1aac__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1plc__ 2.5.1.1.2 Plastocyanin {Poplar (Populus nigra), variant italica}
idvllgaddgslafvpsefsispgekivfknnagfphnivfdedsipsgvdaskismsee
dllnakgetfevalsnkgeysfycsphqgagmvgkvtvn
>d9pcy__ 2.5.1.1.3 Plastocyanin {French bean (Phaseolus vulgaris)}
levllgsgdgslvfvpsefsvpsgekivfknnagfphnvvfdedeipagvdavkismpee
ellnapgetyvvtldtkgtysfycsphqgagmvgkvtvn
>d1pla__ 2.5.1.1.4 Plastocyanin {Parsley (Petroselinum crispum)}
aevklgsddgglvfspssftvaagekitfknnagfphnivfdedevpagvnaekisqpey
lngagetyevtltekgtykfycephagagmkgevtvn
>d1ag6__ 2.5.1.1.5 Plastocyanin {Spinach (Spinacia oleracea)}
vevllggddgslaflpgdfsvasgeeivfknnagfphnvvfdedeipsgvdaakismsee
dllnapgetykvtltekgtykfycsphqgagmvgkvtvn
>d1bypa_ 2.5.1.1.6 Plastocyanin {White campion (Silene pratensis)}
aevllgssdgglafvpsdlsiasgekitfknnagfphndlfdkkevpagvdvtkismpee
dllnapgeeysvtltekgtykfycaphagagmvgkvtvn
>d1iuz__ 2.5.1.1.7 Plastocyanin {Sea lettuce (Ulva pertusa)}
aqivklggddgslafvpskisvaageaiefvnnagfphnivfdedavpagvdadaisydd
ylnskgetvvrklstpgvygvycephagagmkmtitvq
>d2plt__ 2.5.1.1.8 Plastocyanin {Green alga (Chlamydomonas reinhardtii)}
datvklgadsgalefvpktltiksgetvnfvnnagfphnivfdedaipsgvnadaisrdd
ylnapgetysvkltaageygyycephqgagmvgkiivq
>d7pcy__ 2.5.1.1.9 Plastocyanin {Green alga (Enteromorpha prolifera)}
aaivklggddgslafvpnnitvgagesiefinnagfphnivfdedavpagvdadaisaed
ylnskgqtvvrklttpgtygvycdphsgagmkmtitvq
>d1kdj__ 2.5.1.1.10 Plastocyanin {Fern (Adiantum capillus-veneris)}
akvevgdevgnfkfypdsitvsageaveftlvgetghnivfdipagapgtvaselkaasm
dendllsedepsfkakvstpgtytfyctphksanmkgtltvk
>d1nin__ 2.5.1.1.11 Plastocyanin {Anabaena variailis}
etytvklgsdkgllvfepakltikpgdtveflnnkvpphnvvfdaalnpaksadlaksls
hkqllmspgqststtfpadapageytfycephrgagmvgkitvag
>d1bawa_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1pcs__ 2.5.1.1.13 Plastocyanin {Cyanobacterium (Synechocystis), pcc 6803}
anatvkmgsdsgalvfepstvtikageevkwvnnklsphnivfdadgvpadtaaklshkg
llfaagesftstftepgtytyycephrgagmvgkvvve
>d1bxua_ 2.5.1.1.14 Plastocyanin {Cyanobacterium (Synechocystis), pcc 7942}
qtvaikmgadngmlafepstieiqagdtvqwvnnklaphnvvvegqpelshkdlafspge
tfeatfsepgtytyycephrgagmvgkivvq
>d1bxva_ 2.5.1.1.14 Plastocyanin {Cyanobacterium (Synechocystis), pcc 7942}
qtvaikmgadngmlafepstieiqagdtvqwvnnklaphnvvvegqpelshkdlafspge
tfeatfsepgtytyycephrgagmvgkivvq
>d2b3ia_ 2.5.1.1.15 Plastocyanin {Photosynthetic prokaryote (Prochlorothrix hollandica)}
asvqikmgtdkyaplyepkalsisagdtvefvmnkvgphnvifdkvpagesapalsntkl
aiapgsfysvtlgtpgtysfyctphrgagmvgtitve
>d1paz__ 2.5.1.1.16 Pseudoazurin {Alcaligenes faecalis, strain s-6}
enievhmlnkgaegamvfepayikanpgdtvtfipvdkghnvesikdmipegaekfkski
nenyvltvtqpgaylvkctphyamgmialiavgdspanldqivsakkpkivqerlekvia
>d1pmy__ 2.5.1.1.17 Pseudoazurin {Methylobacterium extorquens, strain am1}
devavkmlnsgpggmmvfdpalvrlkpgdsikflptdkghnvetikgmapdgadyvkttv
gqeavvkfdkegvygfkcaphymmgmvalvvvgdkrdnleaaksvqhnkltqkrldplfa
qiq
>d1bqk__ 2.5.1.1.18 Pseudoazurin {Achromobacter cycloclastes}
adfevhmlnkgkdgamvfepaslkvapgdtvtfiptdkghnvetikgmipdgaeafkski
nenykvtftapgvygvkctphygmgmvgvvqvgdapanleavkgaknpkkaqerldaala
algn
>d1adwa_ 2.5.1.1.19 Pseudoazurin {Thiosphaera pantotropha}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d2cbp__ 2.5.1.1.20 Cucumber basic protein {Cucumber (Cucumis sativus)}
avyvvggsggwtfnteswpkgkrfragdillfnynpsmhnvvvvnqggfstcntpagakv
ytsgrdqiklpkgqsyficnfpghcqsgmkiavnal
>d1azca_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1rkra_ 2.5.1.1.22 Azurin {Alcaligenes xylosoxidans, NCIMB (11015), different isoforms}
aecsvdiagndgmqfdkkeitvsksckqftvnlkhpgklaknvmghnwvltkqadmqgav
ndgmaagldnnyvkkddarviahtkvigggetdsvtfdvsklaagedyayfcsfpghfal
mkgvlklvd
>d1nwpa_ 2.5.1.1.25 Azurin {Pseudomonas putida}
aeckvtvdstdqmsfntkdiaidkscktftvelthsgslpknvmghnlviskeadmqpia
tdglsagidkqylkdgdarviahtkvigagekdsvtfdvsklaagekygffcsfpghism
mkgtvtlk
>d1cc3a_ 2.5.1.1.26 Azurin {Escherichia coli}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffcselcginh
almkgtltlk
>d1rcy__ 2.5.1.1.27 Rusticyanin {Thiobacillus ferrooxidans}
ttwkeatlpqvkamlekddgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknptl
eipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkfgytd
ftwhptagtyyyvcqipghaatgmfgkivvk
>d1jer__ 2.5.1.1.28 Stellacyanin {Cucumber (Cucumis sativus)}
mqstvhivgdntgwsvpsspnfysqwaagktfrvgdslqfnfpanahnvhemetkqsfda
cnfvnsdndvertspvierldelgmhyfvctvgthcsngqklsinvvaan
>d1cyx__ 2.5.1.2.1 Quinol oxidase (CYOA) {Escherichia coli}
kpitievvsmdwkwffiypeqgiatvneiafpantpvyfkvtsnsvmhsffiprlgsqiy
amagmqtrlhlianepgtydgicaeicgpghsgmkfkaiatpdraafdqwvakakqspnt
msdmaafeklaapseynqveyfsnvkpdlfadvinkfm
>d2occb1 2.5.1.2.2 (91-227) Cytochrome c oxidase {Bovine (Bos taurus)}
nnpsltvktmghqwywsyeytdyedlsfdsymiptselkpgelrllevdnrvvlpmemti
rmlvssedvlhswavpslglktdaipgrlnqttlmssrpglyygqcseicgsnhsfmpiv
lelvplkyfekwsasml
>d1ar1b1 2.5.1.2.3 (108-252) Cytochrome c oxidase {Paracoccus denitrificans}
ndpdlvikaighqwywsyeypndgvafdalmlekealadagysedeyllatdnpvvvpvg
kkvlvqvtatdvihawtipafavkqdavpgriaqlwfsvdqegvyfgqcselcginhaym
pivvkavsqekyeawlagakeefaa
>d2cuaa_ 2.5.1.2.4 Cytochrome c oxidase {Thermus thermophilus, ba3 type}
agklervdpttvrqegpwadpaqavvqtgpnqytvyvlafafgyqpnpievpqgaeivfk
itspdvihgfhvegtninvevlpgevstvrytfkrpgeyriicnqycglghqnmfgtivv
ke
>d1nif_1 2.5.1.3.1 (8-166) Nitrite reductase, NIR {Achromobacter cycloclastes}
distlprvkvdlvkppfvhahdqvaktgprvveftmtieekklvidregteihamtfngs
vpgplmvvhendyvelrlinpdtntllhnidfhaatgalgggaltqvnpgeettlrfkat
kpgvfvyhcapegmvpwhvtsgmngaimvlprdglkdek
>d1nif_2 2.5.1.3.1 (167-340) Nitrite reductase, NIR {Achromobacter cycloclastes}
gqpltydkiyyvgeqdfyvpkdeagnykkyetpgeayedavkamrtltpthivfngavga
ltgdhaltaavgervlvvhsqanrdtrphligghgdyvwatgkfrnppdldqetwlipgg
tagaafytfrqpgvyayvnhnlieafelgaaghfkvtgewnddlmtsvvkpasm
>d1aoza1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aoza2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aoza3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1a65a1 2.5.1.3.5 (1-131) Laccase {Inky cap fungus (Coprinus cinereus)}
qivnsvdtmtltnanvspdgftragilvngvhgplirggkndnfelnvvndldnptmlrp
tsihwhglfqrgtnwadgadgvnqcpispghaflykftpaghagtfwyhshfgtqycdgl
rgpmviyddnd
>d1a65a2 2.5.1.3.5 (132-303) Laccase {Inky cap fungus (Coprinus cinereus)}
phaalydeddentiitladwyhipapsiqgaaqpdatlingkgryvggpaaelsivnveq
gkkyrmrlislscdpnwqfsidgheltiievdgeltephtvdrlqiftgqrysfvldanq
pvdnywiraqpnkgrnglagtfangvnsailryagaanadpttsanpnpaql
>d1a65a3 2.5.1.3.5 (304-504) Laccase {Inky cap fungus (Coprinus cinereus)}
neadlhalidpaapgiptpgaadvnlrfqlgfsggrftingtayespsvptllqimsgaq
sandllpagsvyelprnqvvelvvpagvlggphpfhlhghafsvvrsagsstynfvnpvk
rdvvslgvtgdevtirfvtdnpgpwffhchiefhlmnglaivfaedmantvdannppvew
aqlceiyddlppeatsiqtvv
>d1kcw_1 2.5.1.3.6 (1-192) Ceruloplasmin {Human (Homo sapiens)}
kekhyyigiiettwdyasdhgekklisvdtehsniylqngpdrigrlykkalylqytdet
frttiekpvwlgflgpiikaetgdkvyvhlknlasrpytfhshgityykehegaiypdnt
tdfqraddkvypgeqytymllateeqspgegdgncvtriyhshidapkdiasgligplii
ckkdsldkekek
>d1kcw_2 2.5.1.3.6 (193-338) Ceruloplasmin {Human (Homo sapiens)}
hidrefvvmfsvvdenfswyledniktycsepekvdkdnedfqesnrmysvngytfgslp
glsmcaedrvkwylfgmgnevdvhaaffhgqaltnknyridtinlfpatlfdaymvaqnp
gewmlscqnlnhlkaglqaffqvqec
>d1kcw_3 2.5.1.3.6 (347-553) Ceruloplasmin {Human (Homo sapiens)}
irgkhvrhyyiaaeeiiwnyapsgidiftkenltapgsdsavffeqgttriggsykklvy
reytdasftnrkergpeeehlgilgpviwaevgdtirvtfhnkgayplsiepigvrfnkn
negtyyspnynpqsrsvppsashvaptetftyewtvpkevgptnadpvclakmyysavdp
tkdiftgligpmkickkgslhangrqk
>d1kcw_4 2.5.1.3.6 (554-705) Ceruloplasmin {Human (Homo sapiens)}
dvdkefylfptvfdeneslllednirmfttapdqvdkededfqesnkmhsmngfmygnqp
gltmckgdsvvwylfsagneadvhgiyfsgntylwrgerrdtanlfpqtsltlhmwpdte
gtfnveclttdhytggmkqkytvnqcrrqsed
>d1kcw_5 2.5.1.3.6 (706-884) Ceruloplasmin {Human (Homo sapiens)}
stfylgertyyiaavevewdyspqrewekelhhlqeqnvsnafldkgefyigskykkvvy
rqytdstfrvpverkaeeehlgilgpqlhadvgdkvkiifknmatrpysihahgvqtess
tvtptlpgetltyvwkipersgagtedsacipwayystvdqvkdlysgligplivcrrp
>d1kcw_6 2.5.1.3.6 (892-1040) Ceruloplasmin {Human (Homo sapiens)}
rrklefallflvfdeneswylddniktysdhpekvnkddeefiesnkmhaingrmfgnlq
gltmhvgdevnwylmgmgneidlhtvhfhghsfqykhrgvyssdvfdifpgtyqtlemfp
rtpgiwllhchvtdhihagmettytvlqn
>d1qasa2 2.6.1.1.1 (626-756) PI-specific phospholipase C isozyme D1 (PLC-D1), C-terminal domain {Rat (Rattus norvegicus)}
wrperlrvriisgqqlpkvnknknsivdpkviveihgvgrdtgsrqtavitnngfnprwd
mefefevtvpdlalvrfmvedydssskndfigqstipwnslkqgyrhvhllskngdqhps
atlfvkisiqd
>d1rlw__ 2.6.1.1.2 Domain from cytosolic phospholipase A2 {Human (Homo sapiens)}
sshkftvvvlratkvtkgafgdmldtpdpyvelfisttpdsrkrtrhfnndinpvwnetf
efildpnqenvleitlmdanyvmdetlgtatftvssmkvgekkevpfifnqvtemvlems
levass
>d1d5ra1 2.6.1.1.3 (188-351) Pten tumor suppressor (Phoshphoinositide phosphatase), N-terminal domain {Human (Homo sapiens)}
yrpvallfhkmmfetipmfsggtcnpqfvvcqlkvkiyssnsgptrredkfmyfefpqpl
pvcgdikveffhkqnkmlkkdkmfhfwvntffipgpeevdndkeylvltltkndldkank
dkanryfspnfkvklyftktv
>e1bdy.1a 2.6.1.1.5 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>d1dqva1 2.6.1.2.1 (295-424) Synaptogamin I {Rat (Rattus norvegicus)}
gapcgrisfalrylygsdqlvvrilqaldlpakdsngfsdpyvkiyllpdrkkkfqtkvh
rktlnpifnetfqfsvplaelaqrklhfsvydfdrfsrhdligqvvldnllelaeqppdr
plwrdilegg
>d1dqva2 2.6.1.2.1 (425-569) Synaptogamin I {Rat (Rattus norvegicus)}
sekadlgelnfslcylptaglltvtiikasnlkamdltgfsdpyvkaslisegrrlkkrk
tsikkntlnptynealvfdvapesvenvglsiavvdydcighnevigvcrvgpeaadphg
rehwaemlanprkpvehwhqlveek
>d1rsy__ 2.6.1.2.1 Synaptogamin I {Rat (Rattus norvegicus)}
gggildsmvekeepkeeeklgklqysldydfqnnqllvgiiqaaelpaldmggtsdpyvk
vfllpdkkkkfetkvhrktlnpvfneqftfkvpyselggktlvmavydfdrfskhdiige
fkvpmntvdfghvteewrdlqsa
>d1dsya_ 2.6.1.2.2 C2 domain from protein kinase c (alpha) {Rat (Rattus norvegicus)}
tekrgriylkaevtdeklhvtvrdaknlipmdpnglsdpyvklklipdpkneskqktkti
rstlnpqwnesftfklkpsdkdrrlsveiwdwdrttrndfmgslsfgvselmkmpasgwy
kllnqeegeyynvpipe
>d3rpba_ 2.6.1.2.4 C2b-domain of rabphilin {Rat (Rattus norvegicus)}
rgkilvslmystqqgglivgiircvhlaamdangysdpfvklwlkpdmgkkakhktqikk
ktlnpefneeffydikhsdlakksldisvwdydigksndyiggcqlgisakgerlkhwye
clknkdkkierwhqlqnenh
>d1pdka2 2.6.2.1.1 (125-215) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsvk
>d1qppa2 2.6.2.1.1 (125-214) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsv
>d1qppb2 2.6.2.1.1 (125-214) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsv
>d1qpxa2 2.6.2.1.1 (125-215) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsvk
>d1qpxb2 2.6.2.1.1 (125-215) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsvk
>d3dpa_2 2.6.2.1.1 (125-218) PapD {Escherichia coli}
nevwqdqlilnkvsggyrienptpyyvtviglggsekqaeegefetvmlsprseqtvksa
nyntpylsyindyggrpvlsficngsrcsvkkek
>d1bf8_2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgestvklpsda
gsnityrtindygaltpkmtgvme
>d1quna2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1qunc2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1qune2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1qung2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1quni2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1qunk2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1qunm2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1quno2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgesavklpsda
gsnityrtindygaltpkmtgvme
>d1who__ 2.6.3.1.1 Pollen allergen PHL P 2 {Timothy grass (Phleum pratense)}
vpkvtftvekgsnekhlavlvkyegdtmaevelrehgsdewvamtkgeggvwtfdseepl
qgpfnfrfltekgmknvfddvvpekytigatyap
>d1ca4a1 2.7.1.1.1 (350-501) TNF receptor associated factor 2 (TRAF2) {Human (Homo sapiens)}
ydgvfiwkisdfarkrqeavagripaifspafytsrygykmclriylngdgtgrgthlsl
ffvvmkgpndallrwpfnqkvtlmlldqnnrehvidafrpdvtsssfqrpvndmniasgc
plfcpvskmeaknsyvrddaifikaivdltgl
>d1npoa_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
lelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkpcgsg
grcaaagiccndescvtepec
>d1npoc_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
lrqclpcgpggagrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkpcgsggr
caaagiccndescvtepec
>d2bn2a_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
amsdlelrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkp
cgsggrcaaagiccndescvtepec
>d2bn2c_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
lrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkpcgsggr
caaagiccndescvtepec
>d2bn2e_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
lrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkpcgsggr
caaagiccndescvtepec
>d2bn2g_ 2.8.1.1.1 Neurophysin II {Bovine (Bos taurus)}
lrqclpcgpggkgrcfgpsiccgdelgcfvgtaealrcqeenylpspcqsgqkpcgsggr
caaagiccndescvtepec
>d2bpa1_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
sniqtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglai
dstvdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkip
khlfqgylniynnyfkapwmpdrteanpnelnqddarygfrcchlkniwtaplppetels
rqmttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrs
nlwasgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiq
ylnakgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvsp
ayhllegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttr
dsimts
>d2bpa2_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1gff2_ 2.9.1.1.2 Bacteriophage capsid proteins {Bacteriophage G4}
mfqkfiskhnapinstqlaatktpavaapvlsvpnlsrstilinatttavtthsglchvv
ridetnptnhhalsiagslsnvpadmiafairfevadgvvptavpalydvypietfnngk
aisfkdavtidshprtvgndvyagimlwsnawtastisgvlsvnqvnreatvlqplk
>d1stma_ 2.9.1.2.1 SPMV coat protein {Satellite panicum mosaic virus}
aaatslvydtcyvtlterattsfqrqsfptlkgmgdrafqvvaftiqgvsaaplmynarl
ynpgdtdsvhatgvqlmgtvprtvrltprvgqnnwffgnteeaetilaidglvstkgana
psntvivtgcfrlapselqss
>d1a34a_ 2.9.1.2.2 STMV coat protein {Satellite tobacco mosaic virus}
tgdnsnvvtmiragsypkvnptptwvraipfevsvqsgiafkvpvgslfsanfrtdsfts
vtvmsvrawtqltppvneysfvrlkplfktgdsteefegrasnintrasvgyriptnlrq
ntvaadnvcevrsncrqvalvisccfn
>d2stv__ 2.9.1.2.3 STNV coat protein {Satellite tobacco necrosis virus}
tmravkrminthlehkrfalinsgntnatagtvqnlsngiiqgddinqrsgdqvrivshk
lhvrgtaitvsqtfrfiwfrdnmnrgttptvlevlntanfmsqynpitlqqkrftilkdv
tlncsltgesikdriinlpgqlvnyngatavaasngpgaifmlqigdslvglwdssyeav
ytda
>d1smva_ 2.9.1.2.4 SMV coat potein {Sesbania mosaic virus}
gaitvlhceltaeigvtdsivvsselvmpytvgtwlrgvadnwskyswlsvrytyipscp
sstagsihmgfqydmadtvpvsvnklsnlrgyvsgqvwsgsaglcfinnsrcsdtstais
ttldvselgkkwypyktsadyatavgvdvniatdlvparlvialldgssstavaagriyd
tytiqmieptasalnl
>d1bmv1_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
sisqqtvwnqmatvrtplnfdsskqsfcqfsvdllgggisvdktgdwitlvqnspisnll
rvaawkkgclmvkvvmsgnaavkrsdwaslvqvfltnsnstehfdacrwtksephsweli
fpievcgpnngfemwssewanqtswhlsflvdnpkqsttfdvllgisqnfeiagntlmpa
fsvpq
>d1bmv2_ 2.9.1.2.5 BPMV coat protein {Bean pod mottle virus}
metnlfklslddvetpkgsmldlkisqskialpkntvggtilrsdllanfltegnfrasv
dlqrthrikgmikmvatvgipentgialacamnssirgrassdiyticsqdcelwnpact
kamtmsfnpnpcsdawsleflkrtgfhcdiicvtgwtatpmqdvqvtidwfissqecvpr
tycvlnpqnpfvlnrwmgkltfpqgtsrsvkrmplsigggagaksailmnmpnavlsmwr
yfvgdlvfevskmtspyikctvsffiafgnladdtinfeafphklvqfgeiqekvvlkfs
qeefltawstqvrpattlladgcpylyamvhdssvstipgdfvigvkltiienmcaygln
pgisgsrllgtipq
>d1a6ca1 2.9.1.2.6 (1-176) TRSV capsid protein {Tobacco ringspot virus}
avtvvpdptccgtlsfkvpkdakkgkhlgtfdirqaimdygglhsqewcakgivnptftv
rmhaprnafaglsiactfddykridlpalgnecppsemfelptkvfmlkdadvhewqfny
geltghglcnwanvatqptlyffvastnqvtmaadwqcivtmhvdmgpvidrfeln
>d1a6ca2 2.9.1.2.6 (177-348) TRSV capsid protein {Tobacco ringspot virus}
ptmtwpiqlgdtfaidryyeakeikldgstsmlsisynfggpvkhskkhaisysravmsr
nlgwsgtisgsvksvsslfctasfvifpweceapptlrqvlwgphqimhgdgqfeiaikt
rlhsaatteegfgrlgilplsgpiapdahvgsyefivhintwrpdsqvhppm
>d1a6ca3 2.9.1.2.6 (349-513) TRSV capsid protein {Tobacco ringspot virus}
fssselynwftltnlkpdantgvvnfdipgyihdfaskdatvtlasnplswlvaatgwhy
gevdlciswsrskqaqaqegsvsittnyrdwgaywqgqariydlrrteaeipiflgsyag
atpsgalgkqnyvrisivnakdivalrvclrpksikfwgrsatlf
>d2tbva_ 2.9.1.2.8 TBSV coat protein {Tomato bushy stunt virus}
ggvtvtshreyltqvnnssgfvvnggivgnslqlnpsngtlfswlpalasnfdqysfnsv
vldyvplcgttevgrvalyfdkdsqdpepadrvelanfgvlketapwaeamlriptdkvk
rycndsatvdqklidlgqlgiatyggagadavgelflarsvtlyfpqptntllsskrldl
tgsladatgpgylvltrtptvlthtfratgtfnlsgglrcltsltlgatgavvindilai
dnvgtasdyflnctvsslpatvtftvsgvaagillvgraranvvnll
>d1cwpa_ 2.9.1.2.9 Cowpea chlorotic mottle virus {Host: cowpea (Vigna unguiculta), (L.)}
kaikawtgysvskwtascaaaeakvtsaitislpnelssernkqlkvgrvllwlgllpsv
sgtvkscvtetqttaaasfqvalavadnskdvvaamypeafkgitleqlaadltiylyss
aaltegdvivhlevehvrptfddsftpvy
>d1auya_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
spltikqpfqsevlfagtkdaeasltianidsvstlttfyrhasleslwvtihptlqapt
fpttvgvcwvpaqspvtpaqitktyggqifciggaiqtlsplivkcplemmqprvkdsiq
yldspkllisitaqptappastciitvsgtlsmhsplitdtst
>d1qjza_ 2.9.1.2.12 PHMV coat protein {PHMV (Physalis mottle virus)}
kqasipapgsilsqpnteqspaivlpfqfeattfgtaetaaqvslqtadpitkltapyrh
aqiveckailtptdlavsnpltvylawvpanspatptqilrvyggqsfvlggaisaakti
evplnldsvnrmlkdsvtytdtpkllaysraptnpskiptasiqisgrirlskpmlian
>d2bbva_ 2.9.1.3.1 Black beetle virus (BBV, Nodamura virus) capsid protein {Nodamura virus}
ltrlsqpglaflkcafappdfntdpgkgipdrfegkvvtrkdvlnqsinftanrdtfili
aptpgvaywvadvpagtfpistttfnavnfpgfnsmfgnaaasrsdqvssfryasmnvgi
yptsnlmqfagsitvwkcpvklsnvqfpvattpatsalvhtlvgldgvlavgpdnfsesf
ikgvfsqsvcnepdfefsdilegiqtlppanvtvatsgqpfnlaagaeavsgivgwgnmd
tivirvsaptgavnsailktwacleyrpnpnamlyqfghdsppcdevalqeyrtvarslp
vaviaaqn
>d1dnv__ 2.9.1.3.2 Galleria mellonella densovirus capsid protein {Wax moth (Galleria mellonella), densovirus}
vyiiprpfsnfgkklstytkshkfmifglannvigptgtgttavnrllttclaeipwqkl
plymnqsefdllppgsrvvecnvkvifrtnriafetsstvtkqatlnqisnvqtaiglnk
lgwginraftafqsdqpmiptattapkyepvtgdtgyrgmiadyygadstndtafgnagn
yphhqvssftflqnyycmyqqtnqgtggwpclaehlqqfdsktvnnqclidvtykpkmgl
iksplnykiigqptvkgtisvgdnlvnmrgavvtnppeatqnvaesthnltrnfpadlfn
iysdieksqvlhkgpwghenpqiqpsvhigiqavpalttgallinssplnswtdsmgyid
vmssctvmeaqpthfpfsteantnpgntiyrinltpnsltsafnglygngatlgn
>d1b35a_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
vmgedqqiprneaqhgvhpisidthrisnnwspqamcigekvvsirqlikrfgifgdant
lqadgssfvvapftvtsptktltstrnytqfdyyyylyafwrgsmrikmvaetqdgtgtp
rkktnftwfvrmfnslqdsfnslistsssavtttvlpsgtinmgpstqvidptvegliev
evpyynishitpavtiddgtpsmedylkghsppclltfsprdsisatnhiitasfmralg
ddfsfmyllgvpplvnvara
>d1b35b_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
enshienedkrltseqkeivhfvsegvtpsttalpdivnlstnyldkntredrihsikdf
lsrpiiiatnlwsvsdpvekqlytanfpevlisnamyqdklkgfvglratlvvkvqvnsq
pfqqgrlmlqyipyaqympnrvtlinetlqgrsgcprtdlelsvgtevemripyvsphly
ynlitgqgsfgsiyvvvysqlhdqvsgtgsieytvwahledvdvqyptganiftgneayi
kgtsrydaaqkahaa
>d1b35c_ 2.9.1.3.3 Cricket paralysis virus (CRPV) {Host: australian black field cricket (Teleogryllus commodus)}
skptvqgkigecklrgqgrmanfdgmdmshkmalsstneietneglagtsldvmdlsrvl
sipnywdrftwktsdvintvlwdnyvspfkvkpysatitdrfrcthmgkvanaftywrgs
mvytfkfvktqyhsgrlrisfipyyynttistgtpdvsrtqkivvdlrtstavsftvpyi
gsrpwlycirpesswlskdntdgalmyncvsgivrvevlnqlvaaqnvfseidvicevng
gpdlefagptcpryvpyagdftladtrkieaertqeysnned
>d1vpsa_ 2.9.1.4.1 Murine polyomavirus coat protein vp1 {Murine polyoma virus, strain small-plaque 16}
ggmevldlvtgpdsvteieaflnprmgqpptpeslteggqyygwsrginlatsdtedspg
nntlptwsmaklqlpmlnedltcdtlqmweavsvktevvgsgslldvhgfnkptdtvntk
gistpvegsqyhvfavggepldlqglvtdartkykeegvvtiktitkkdmvnkdqvlnpi
skakldkdgmypveiwhpdpaknentryfgnytggtttppvlqftntlttvlldengvgp
lckgeglylscvdimgwrvtrnydvhhwrglpryfkitlrkrwvk
>d1qqp1_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvgallrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivapvk
>d1qqp2_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
dkkteettlledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaer
ffkthlfdwvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggc
llvamvpelcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlv
vmvvapltvntegapqikvyaniaptnvhvagefpske
>d1qqp3_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>d2cas__ 2.9.1.4.3 Parvovirus capsid {Host: canine (Canis familiaris)}
gvgistgtfnnqtefkflengwveitanssrlvhlnmpesenyrrvvvnnmdktavngnm
alddihaqivtpwslvdanawgvwfnpgdwqlivntmselhlvsfeqeifnvvlktvses
atqpptkvynndltaslmvaldsnntmpftpaamrsetlgfypwkptiptpwryyfqwdr
tlipshtgtsgtptniyhgtdpddvqfytiensvpvhllrtgdefatgtfffdckpcrlt
htwqtnralglppflnslpqsegatnfgdigvqqdkrrgvtqmgntnyiteatimrpaev
gysapyysfeastqgpfktpiaagrggaqtdenqaadgnpryafgrqhgqkttttgetpe
rftyiahqdtgrypegdwiqninfnlpvtndnvllptdpiggktginytnifntygplta
lnnvppvypngqiwdkefdtdlkprlhvnapfvcqnncpgqlfvkvapnltneydpdasa
nmsrivtysdfwwkgklvfkaklrashtwnpiqqmsinvdnqfnyvpsniggmkivyeks
qlaprkly
>d1pvc1_ 2.9.1.4.7 Poliovirus {Poliovirus type 3, sabin strain}
qdslpdtkasgpahskevpaltavetgatnplapsdtvqtrhvvqrrsrsestiesffar
gacvaiievdneqpttraqklfamwritykdtvqlrrklefftysrfdmeftfvvtanft
nannghalnqvyqimyippgaptpkswddytwqtssnpsifytygaaparisvpyvglan
ayshfydgfakvplktdandqigdslysamtvddfgvlavrvvndhnptkvtskvriymk
pkhvrvwcprppravpyygpgvdyrnnldplsekgltty
>d1aym1_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1aym2_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1aym3_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1bev1_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
qaagalvagtststhsvatdstpalqaaetgatstardesmietrtivpthgihetsves
ffgrsslvgmpllatgtsithwridfrefvqlrakmswftymrfdveftiiatsstgqnv
tteqhttyqvmyvppgapvpsnqdsfqwqsgcnpsvfadtdgppaqfsvpfmssanayst
vydgyarfmdtdpdrygilpsnflgfmyfrtledaahqvrfriyakikhtscwipraprq
apykkrynlvfsgdsdricsnrasltsy
>d2mev1_ 2.9.1.4.13 Mengo virus {Host: monkey brain; middle size plaque variant}
gvenaekgvtentdatadfvaqpvylpenqtkvaffydrsspigafavksgslesgfapf
snkacpnsviltpgpqfdpaydqlrpqrlteiwgngneetsevfplktkqdysfclfspf
vyykcdlevtlsphtsgahgllvrwcptgtptkpttqvlhevsslsegrtpqvysagpgt
snqisfvvpynsplsvlpavwynghkrfdntgdlgiapnsdfgtlffagtkpdikftvyl
ryknmrvfcprptvffpwptsgdkidmt
>d2mev2_ 2.9.1.4.13 Mengo virus {Host: monkey brain; middle size plaque variant}
enlsdrvsqdtagntvtntqstvgrlvgygtvhdgehpascadtasekilaveryytfkv
ndwtstqkpfeyiriplphvlsgedggvfgatlrrhylvktgwrvqvqcnasqfhagsll
vfmapeyptldvfamdnrwskdnlpngtrtqtnrkgpfamdhqnfwqwtlyphqflnlrt
nttvdlevpyvniaptsswtqhaswtlviavvapltystgastslditasiqpvrpvfng
lrhevlsrq
>d2mev3_ 2.9.1.4.13 Mengo virus {Host: monkey brain; middle size plaque variant}
spipvtirehagtwystlpdstvpiygktpvapanymvgeykdfleiaqiptfignkvpn
avpyieasntavktqplavyqvtlscsclantflaalsrnfaqyrgslvytfvftgtamm
kgkfliaytppgagkptsrdqamqatyaiwdlglnssysftvpfispthfrmvgtdqani
tnvdgwvtvwqltpltyppgcptsakiltmvsagkdfslkmpispapwspq
>d1amm_1 2.10.1.1.1 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gkitfyedrgfqghcyecssdcpnlqpyfsrcnsirvdsgcwmlyerpnyqghqyflrrg
dypdyqqwmgfndsirscrlipqht
>d1amm_2 2.10.1.1.1 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1dsl__ 2.10.1.1.1 gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
tfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmdfy
>d1gama_ 2.10.1.1.1 gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
tfrmriyerddfrgqmseitadcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmd
>d1gamb_ 2.10.1.1.1 gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
tfrmriyerddfrgqmseitadcpslqdrfhltevhslnvlegswvlyempsyrgrqyll
rpgeyrryldwgamnakvgslrrvmd
>d1gcs_2 2.10.1.1.1 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d4gcr_2 2.10.1.1.1 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform II (B)}
gtfrmriyerddfrgqmseitddcpslqdrfhltevhslnvlegswvlyempsyrgrqyl
lrpgeyrryldwgamnakvgslrrvmdfy
>d1elpa1 2.10.1.1.2 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpa2 2.10.1.1.2 (87-174) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1elpb1 2.10.1.1.2 (1-85) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
gkitfyedrgfqgrhyecssdhsnlqpylgrcnsvrvdsgcwmiyeqpnylgpqyflrrg
dypdyqqwmglndsirscrliphag
>d1elpb2 2.10.1.1.2 (87-174) gamma-Crystallin {Bovine (Bos taurus), isoform IIIb (D)}
shrlrlyeredyrgqmieitedcsslqdrfhfneihslnvlegswvlyelpnyrgrqyll
rpgeyrryhdwgamnakvgslrrvidiy
>d1a7ha_ 2.10.1.1.3 gamma-Crystallin {Bovine (Bos taurus), isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d1a7hb_ 2.10.1.1.3 gamma-Crystallin {Bovine (Bos taurus), isoform S}
mykiqifekgdfngqmhettedcpsimeqfhmrevhsckvlegawifyelpnyrgrqyll
dkkeyrkpvdwgaaspavqsfrrive
>d1a45_1 2.10.1.1.4 (1-84) gamma-Crystallin {Bovine (Bos taurus), isoform F}
gkitfyedrgfqgrhyecssdhsnlqpyfsrcnsirvdsgcwmlyeqpnfqgpqyflrrg
dypdyqqwmglndsirscrlipht
>d1a45_2 2.10.1.1.4 (86-174) gamma-Crystallin {Bovine (Bos taurus), isoform F}
gshrlriyeredyrgqmveitedcsslhdrfhfseihsfnvlegwwvlyemtnyrgrqyl
lrpgdyrryhdwgatnarvgslrravdfy
>d1blba1 2.10.1.1.5 (-6-85) beta-Crystallin {Bovine (Bos taurus)}
apqplnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckge
qfvfekgeyprwdswtssrrtdslsslrpikvds
>d1blbb1 2.10.1.1.5 (-2-85) beta-Crystallin {Bovine (Bos taurus)}
lnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqfvf
ekgeyprwdswtssrrtdslsslrpikvds
>d2bb2_1 2.10.1.1.5 (-2-85) beta-Crystallin {Bovine (Bos taurus)}
lnpkiiifeqenfqghshelngpcpnlketgvekagsvlvqagpwvgyeqanckgeqfvf
ekgeyprwdswtssrrtdslsslrpikvds
>d2bb2_2 2.10.1.1.5 (86-175) beta-Crystallin {Bovine (Bos taurus)}
qehkitlyenpnftgkkmevidddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqy
llekgdykdsgdfgapqpqvqsvrrirdmqw
>d1a5da1 2.10.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1a5da2 2.10.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>d1a5db1 2.10.1.1.6 (1-84) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
gkitfyedrgfqgrhyecstdhsnlqpyfsrcnsvrvdsgcwmlyeqpnftgcqyflrrg
dypdyqqwmgfsdsvrscrliphs
>d1bd7a_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1npsa_ 2.10.1.2.1 Protein S {Myxococcus xanthus}
anitvfynedfqgkqvdlppgnytraqlaalgienntissvkvppgvkailyqndgfagd
qievvanaeelgplnnnvssirvisvpv
>d1prr_1 2.10.1.2.1 (1-90) Protein S {Myxococcus xanthus}
manitvfynedfqgkqvdlppgnytraqlaalgienntissvkvppgvkailyqndgfag
dqievvanaeelgplnnnvssirvisvpvq
>d1prr_2 2.10.1.2.1 (91-173) Protein S {Myxococcus xanthus}
prarffykeqfdgkevdlppgqytqaelerygidnntissvkpqglavvlfkndnfsgdt
lpvnsdaptlgamnnntssiris
>d1prs_1 2.10.1.2.1 (1-90) Protein S {Myxococcus xanthus}
manitvfynedfqgkqvdlppgnytraqlaalgienntissvkvppgvkailyqndgfag
dqievvanaeelgplnnnvssirvisvpvq
>d1prs_2 2.10.1.2.1 (91-173) Protein S {Myxococcus xanthus}
prarffykeqfdgkevdlppgqytqaelerygidnntissvkpqglavvlfkndnfsgdt
lpvnsdaptlgamnnntssiris
>d1ag4__ 2.10.1.2.2 Spherulin 3a (S3a) {Slime mold (Physarum polycephalum)}
msvckgvsgnpakgevflykhvnfqgdswkvtgnvydfrsvsglndvvssvkvgpntkaf
ifkddrfngnfirleessqvtdlttrnlndaissiivatfesa
>d1wkt__ 2.10.1.3.1 Yeast killer toxin {Williopsis mrakii}
gdgylimckncdpntgscdwkqnwntcvgiganvhwmvtggstdgkqgcatiwegsgcvg
rsttmccpantccnintgfyirsyrrve
>d1bhu__ 2.10.1.4.1 Streptomyces metalloproteinase inhibitor, SMPI {Streptomyces nigrescens}
apscpagslctysgtglsgartvipasdmekagtdgvklpasarsfangthftlrygpar
kvtcvrfpcyqyatvgkvapgaqlrslpspgatvtvgqdlgd
>d1yge_2 2.11.1.1.1 (1-149) Plant lipoxigenase {Soybean (Glycine max), isozyme L1}
mfsaghkikgtvvlmpknelevnpdgsavdnlnaflgrsvslqlisatkadahgkgkvgk
dtflegintslptlgagesafnihfewdgsmgipgafyiknymqvefflksltleaisnq
gtirfvcnswvyntklyksvriffanhty
>d1lox_2 2.11.1.1.3 (2-112) 15-Lipoxygenase {Rabbit (Oryctolagus cuniculus)}
gvyrvcvstgasiyagsknkvelwlvgqhgevelgsclrptrnkeeefkvnvskylgsll
fvrlrkkhflkedawfcnwisvqalgaaedkywfpcyrwvvgdgvqslpvg
>d1hpla1 2.11.1.2.1 (337-449) Pancreatic lipase, C-terminal domain {Horse (Equus caballus)}
rwryrvdvtlsgkkvtghvlvslfgnkgnsrqyeifqgtlkpdntysnefdsdvevgdle
kvkfiwynnvinltlpkvgaskitverndgsvfnfcseetvredvlltltac
>d1etha1 2.11.1.2.2 (337-448) Pancreatic lipase, C-terminal domain {Pig (Sus scrofa)}
arwrykvsvtlsgkkvtghilvslfgnegnsrqyeiykgtlqpdnthsdefdsdvevgdl
qkvkfiwynvinptlprvgaskitverndgkvydfcsqetvreevlltlnpc
>d1gpl_1 2.11.1.2.4 (337-449) Pancreatic lipase, C-terminal domain {Guinea pig (Cavia porcellus)}
rwrykvsvtlsgkkvtghilvslfgnkgnskqyeifkgtlkpdsthsnefdsdvdvgdlq
mvkfiwynnvinptlprvgaskiivetnvgkqfnfcspetvreevlltltpc
>d1rp1_1 2.11.1.2.5 (337-449) Pancreatic lipase, C-terminal domain {Dog (Canis familiaris)}
rwrygvsitlsgkratgqakvalfgskgnthqfnifkgilkpgsthsnefdakldvgtie
kvkflwnnnnptfpkvgaakitvqkgeektvhsfcsestvredvlltltpc
>d1bu8a1 2.11.1.2.6 (337-449) Pancreatic lipase, C-terminal domain {Rat (Rattus norvegicus)}
rwrykvsvtlsgakklsgyilvalygnngnskqyeifkgslkpearhvrdidvdinvgei
qkvkflwnnkvinlfrptlgasqitvqsgvdgkeynfcssdtvredvlqslypc
>d1ca1_2 2.11.1.3.1 (250-370) Alpha-toxin, C-terminal domain {Clostridium perfringens}
svgknvkelvayistsgekdagtddymyfgiktkdgktqewemdnpgndfmtgskdtytf
klkdenlkiddiqnmwirkrkytafpdaykpenikviangkvvvdkdinewisgnstyni
k
>d1pgs_1 2.12.1.1.1 (4-140) Peptide:N-glycosidase F, PNGase F {Flavobacterium meningosepticum}
dntvniktfdkvknafgdglsqsaegtftfpadvttvktikmfiknecpnktcdewdrya
nvyvknkttgewyeigrfitpywvgteklprgleidvtdfksllsgntelkiytetwlak
greysvdfdivygtpdy
>d1pgs_2 2.12.1.1.1 (141-314) Peptide:N-glycosidase F, PNGase F {Flavobacterium meningosepticum}
kysavvpviqynkssidgvpygkahtlglkkniqlptntekaylrttisgwghakpydag
srgcaewcfrthtiainnantfqhqlgalgcsanpinnqspgnwtpdragwcpgmavptr
idvlnnsltgstfsyeykfqswtnngtngdafyaissfviaksntpisapvvtn
>d1phm__ 2.12.1.2.1 Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Rat (Rattus norvegicus)}
neclgtigpvtpldasdfaldirmpgvtpkesdtyfcmsmrlpvdeeafvidfkprasmd
tvhhmllfgcnmpsstgsywfcdegtctdkanilyawarnapptrlpkgvgfrvggetgs
kyfvlqvhygdisafrdnhkdcsgvsvhltrvpqpliagmylmmsvdtvippgekvvnad
iscqykmypmhvfayrvhthhlgkvvsgyrvrngqwtligrqnpqlpqafypvehpvdvt
fgdilaarcvftgegrteathiggtssdemcnlyimyymeakyalsfmtctknvapdmfr
tipaeanipi
>d1cjda_ 2.12.2.1.1 Coat protein p3 {Bacteriophage prd1}
lrnqqamaanlqarqivlqqsypviqqvetqtfdpanrsvfdvtpanvgivkgflvkvta
aitnnhateavaltdfgpanlvqrviyydpdnqrhtetsgwhlhfvntakqgapflssmv
tdspikygdvmnvidapatiaagatgeltmyywvplaysetdltgavlanvpqskqrlkl
efannntafaavganpleaiyqgagaadcefeeisytvyqsyldqlpvgqngyilplidl
stlynlensaqagltpnvdfvvqyanlyrylstiavfdnggsfnagtdinylsqrtanfs
dtrkldpktwaaqtrrriatdfpkgvyycdnrdkpiytlqygnvgfvvnpktvnqnarll
mgyeyftsr
>d1dhx__ 2.12.2.2.1 Adenovirus type 2 hexon {Host: human (Homo sapiens)}
frnptvapthdvttdrsqrltlrfipvdredtaysykarftlavgdnrvldmastyfdir
gvldrgptfkpysgtaynalapkgapnsceweqtedsgravaedeeeededeeeeeeeqn
ardqatkkthvyaqaplsgetitksglqigsdnaetqakpvyadpsyqpepqigesqwne
adanaaggrvlkkttpmkpcygsyarptnpfggqsvlvpdekgvplpkvdlqffsnttsl
ndrqgnatkpkvvlysedvnmetpdthlsykpgkgdenskamlgqqsmpnrpnyiafrdn
figlmyynstgnmgvlagqasqlnavvdlqdrntelsyqllldsigdrtryfsmwnqavd
sydpdvriienhgtedelpnycfplggigvtdtyqaikangngsgdngdttwtkdetfat
rneigvgnnfameinlnanlwrnflysnialylpdklkynptnveisdnpntydymnkrv
vapglvdcyinlgarwsldymdnvnpfnhhrnaglryrsmllgngryvpfhiqvpqkffa
iknllllpgsytyewnfrkdvnmvlqsslgndlrvdgasikfdsiclyatffpmahntas
tleamlrndtndqsfndylsaanmlypipanatnvpisipsrnwaafrgwaftrlktket
pslgsgydpyytysgsipyldgtfylnhtfkkvaitfdssvswpgndrlltpnefeikrs
vdgegynvaqcnmtkdwflvqmlanynigyqgfyipesykdrmysffrnfqpmsrqvvdd
tkykeyqqvgilhqhnnsgfvgylaptmregqaypanvpypligktavdsitqkkflcdr
tlwripfssnfmsmgaltdlgqnllyansahaldmtfevdpmdeptllyvlfevfdvvrv
hqphrgvietvylrtpfsagnatt
>d1dkva2 2.13.1.1.1 (356-514) Calpain large subunit, middle domain (domain III) {Human (Homo sapiens)}
wkltkmdgnwrrgstaggcrnypntfwmnpqylikleeededeedgesgctflvgliqkh
rrrqrkmgedmhtigfgiyevpeelsgqtnlhlsknffltnrarersdtfinlrevlnrf
klppgeyilvpstfepnkdgdfcirvfsekkadyqavdd
>d1shsa_ 2.14.1.1.1 Small heat shock protein {Methanococcus jannaschii}
tgiqisgkgfmpisiiegdqhikviawlpgvnkediilnavgdtleirakrsplmitese
riiyseipeeeeiyrtiklpatvkeenasakfengvlsvilpkaessikkginie
>d1slua_ 2.15.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
iapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktlegwgy
dyyvfdkvsspvstmmhcpdgkkekkfvtaylgdagmlrynsklpivvytpdnvdvkyrv
wkaeekidnavvr
>d1a44__ 2.16.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsg
>d1gof_2 2.17.1.1.1 (1-150) Galactose oxidase, N-terminal domain {Dactylium dendroides}
asapigsaisrnnwavtcdsaqsgnecnkaidgnkdtfwhtfygangdpkpphtytidmk
ttqnvnglsmlprqdgnqngwigrhevylssdgtnwgspvasgswfadsttkysnfetrp
aryvrlvaiteangqpwtsiaeinvfqass
>d1eut_2 2.17.1.1.2 (506-647) Sialidase, C-terminal domain {Micromonospora viridifaciens}
qarmsiadvdseetaredgrasnvidgnpstfwhtewsradapgyphrisldlggthtis
glqytrrqnsaneqvadyeiytslngttwdgpvasgrfttslapqravfpardaryirlv
alseqtghkyaavaelevegqr
>d1czsa_ 2.17.1.2.1 C2 domain of factor V {Human (Homo sapiens)}
gcstplgmengkienkqitassfkkswwgdywepfrarlnaqgrvnawqakannnkqwle
idllkikkitaiitqgckslssemyvksytihyseqgvewkpyrlkssmvdkifegntnt
kghvknffnppiisrfirvipktwnqsitlrlelfgcdiy
>d1d7pm_ 2.17.1.2.2 C2 domain of factor VIII {Human (Homo sapiens)}
lnscsmplgmeskaisdaqitassyftnmfatwspskarlhlqgrsnawrpqvnnpkewl
qvdfqktmkvtgvttqgvkslltsmyvkeflisssqdghqwtlffqngkvkvfqgnqdsf
tpvvncldpplltrylrihpqswvhqialrmevlgceaq
>d1dlc_1 2.17.1.3.1 (500-644) delta-Endotoxin, C-terminal domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
ffnmidskkitqlplvkayklqsgasvvagprftggdiiqctengsaatiyvtpdvsysq
kyrarihyastsqitftlsldgapfnqyyfdktinkgdtltynsfnlasfstpfelsgnn
lqigvtglsagdkvyidkiefipvn
>d1ciy_1 2.17.1.3.2 (462-609) delta-Endotoxin, C-terminal domain {Bacillus thuringiensis, CRYIA (A)}
nniipssqitqipltkstnlgsgtsvvkgpgftggdilrrtspgqistlrvnitaplsqr
yrvriryasttnlqfhtsidgrpinqgnfsatmssgsnlqsgsfrtvgfttpfnfsngss
vftlsahvfnsgnevyidriefvpaevt
>d1nuka_ 2.17.1.4.1 Ligand-binding domain of the ephb2 receptor tyrosine kinase {Mouse (Mus musculus)}
eetlmdsttataelgwmvhppsgweevsgydenmntirtyqvcnvfessqnnwlrtkfir
rrgahrihvemkfsvrdcssipsvpgscketfnlyyyeadfdlatktfpnwmenpwvkvd
tiaadesfsqvdlggrvmkintevrsfgpvsrngfylafqdyggcmsliavrvfyr
>d1bgla3 2.17.1.5.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bhga2 2.17.1.5.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1ulo__ 2.17.1.6.1 Cellulose-binding domain {Cellulomonas fimi}
aspigegtfddgpegwvaygtdgpldtstgalcvavpagsaqygvgvvlngvaieegtty
tlrytatastdvtvralvgqngapygtvldtspaltseprqvtetftasatypatpaadd
pegqiafqlggfsadawtlclddvaldsevel
>d1xnaa_ 2.17.1.7.1 N-terminal domain of xrcc1 {Human (Homo sapiens)}
mpeirlrhvvscssqdsthcaenllkadtyrkwraakagektisvvlqlekeeqihsvdi
gndgsafvevlvgssaggageqdyevllvtssfmspsesrsgsnpnrvrmfgpdklvraa
aekrwdrvkivcsqpyskdspfglsfvrfhs
>d1bvp12 2.18.1.1.1 (121-254) Virus coat protein vp7 (BTV-10 vp7), central (top) domain {Bluetongue virus}
parqpygffleteetfqpgrwfmraaqavtavvcgpdmiqvslnagargdvqqifqgrnd
pmmiylvwrrienfamaqgnsqqtqagvtvsvggvdmragriiawdgqaalhvhnptqqn
amvqiqvvfyismd
>d1ahsa_ 2.18.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d2viua_ 2.18.1.2.1 Hemagglutinin {Influenza A virus, different strains}
statlclghhavpngtlvktitddqievtnatelvqssstgkicnnphrildgidctlid
allgdphcdvfqnetwdlfverskafsncypydvpdyaslrslvassgtlefitegftwt
gviqnggsnackrgpgsgffsrlnwltksgstypvlnvtmpnndnfdklyiwgihhpstn
qeqtslyvqasgrvtvstrrsqqtiipnigsrpwvrglssrisiywtivkpgdvlvinsn
gnliaprgyfkmrtgkssimrsdapidtcisecitpngsipndkpfqnvnkitygacpky
vkqntlklatgmrnvpekqt
>d1flca1 2.18.1.3.1 (218-321) Hemagglutinin domain of haemagglutinin-esterase-fusion glycoprotein HEF1 {Influenza C virus}
hlvascyfiydskevynkrgcdnyfqviydsfgkvvggldnrvspytgnsgdtptmqcdm
lqlkpgrysvrssprfllmpersycfdmkekgpvtavqsiwgkg
>d1aol__ 2.19.1.1.1 F-MuLV receptor-binding domain {Friend murine leukemia virus, F-MuLV}
qvynitwevtngdretvwaisgnhplwtwwpvltpdlcmlalsgpphwgleyqapysspp
gppccsgssgssagcsrdcdepltsltprcntawnrlkldqvthkssegfyvcpgshrpr
eakscggpdsfycaswgcettgrvywkpssswdyitvdnnlttsqavqvckdnkwcnpla
iqftnagkqvtswttghywglrlyvsgrdpgltfgirlryqnlgprvp
>d1qhva_ 2.20.1.1.2 Adenovirus fiber protein head domain (knob domain) {Adenovirus serotype 2}
aitignknddkltlwttpdpspncrihsdndckftlvltkcgsqvlatvaalavsgdlss
mtgtvasvsiflrfdqngvlmensslkkhywnfrngnstnanpytnavgfmpnllaypkt
qsqtaknnivsqvylhgdktkpmiltitlngtsestetsevstysmsftwswesgkytte
tfatnsytfsyiaqe
>d1kaca_ 2.20.1.1.3 Adenovirus fiber protein head domain (knob domain) {Human adenovirus type 12}
tpydpltlwttpdpppncsliqeldakltlcltkngsivngivslvgvkgnllniqsttt
tvgvhlvfdeqgrlitstptalvpqaswgyrqgqsvstntvtnglgfmpnvsayprpnas
eaksqmvsltylqgdtskpitmkvafngitslngysltfmwsglsnyinqpfstpscsfs
yitqe
>d1aly__ 2.21.1.1.1 Extracellular domain of CD40 ligand {Human (Homo sapiens)}
gdqnpqiaahviseasskttsvlqwaekgyytmsnnlvtlengkqltvkrqglyyiyaqv
tfcsnreassqapfiaslclkspgrferillraanthssakpcgqqsihlggvfelqpga
svfvnvtdpsqvshgtgftsfgllkl
>d1c28a_ 2.21.1.1.2 30 kd adipocyte complement-related protein {Mouse (Mus musculus)}
myrsafsvgletrvtvpnvpirftkifynqqnhydgstgkfycnipglyyfsyhitvymk
dvkvslfkkdkavlftydqyqeknvdqasgsvllhlevgdqvwlqvygdgdhnglyadnv
ndstftgfllyhdt
>d1tnra_ 2.21.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
kpaahligdpskqnsllwrantdraflqdgfslsnnsllvptsgiyfvysqvvfsgkays
pkatssplylahevqlfssqypfhvpllssqkmvypglqepwlhsmyhgaafqltqgdql
sthtdgiphlvlspstvffgafal
>d2tnfa_ 2.21.1.1.4 Tumor necrosis factor (TNF) {Mouse (Mus musculus)}
sdkpvahvvanhqveeqlewlsqranallangmdlkdnqlvvpadglylvysqvlfkgqg
cpdyvllthtvsrfaisyqekvnllsavkspcpkdtpegaelkpwyepiylggvfqlekg
dqlsaevnlpkyldfaesgqvyfgvial
>d1dg6a_ 2.21.1.1.5 Apoptosis-2 ligand, apo2l/TRAIL {Human (Homo sapiens)}
qrvaahitgtrgrsntlsspnsknekalgrkinswessrsghsflsnlhlrngelvihek
gfyyiysqtyfrfqeeikentkndkqmvqyiykytsypapillmksarnscwskdaeygl
ysiyqggifelkendrifvsvtnehlidmdheasffgaflvg
>d1sfp__ 2.22.1.1.1 Acidic seminal fluid protein (ASFP) {Bovine (Bos taurus)}
lprntncggilkeesgviatyygpktncvwtiqmppeyhvrvsiqylqlncnkesleiid
glpgspvlgkicegslmdyrssgsimtvkyirepehpasfyevlyfqdpqa
>d1sppa_ 2.22.1.1.2 Major seminal plasma glycoprotein PSP-I {Pig (Sus scrofa)}
ldyhacggrltddygtiftykgpktecvwtlqvdpkykllvsiptlnltcgkeyvevleg
apgskslgkfceglsilnrgssgmtvkykrdsghpaspyeiiflrdsqg
>d1sppb_ 2.22.1.1.3 Major seminal plasma glycoprotein PSP-II {Pig (Sus scrofa)}
aringpdecgrvikdtsgsisntdrqknlctwtilmkpdqkvrmaipylnlacgkeyvev
fdgllsgpsygklcagaaivflstantmtikynrisgnssspfliyfygssp
>d1cb8a2 2.23.1.1.1 (600-700) Chondroitinase AC, C-terminal domain {Flavobacterium heparinum}
pkvlantnqlqavyhqqldmvqaifytagklsvagieietdkpcavlikhingkqviwaa
dplqkektavlsirdlktgktnrvkidfpqqefagatvelk
>d1thw__ 2.24.1.1.3 Thaumatin {Ketemfe (Thaumatococcus daniellii benth)}
atfeivnrcsytvwaaaskgdaaldaggrqlnsgeswtinvepgtkggkiwartdcyfdd
sgsgicktgdcggllrckrfgrppttlaefslnqygkdyidisnikgfnvpmdfspttrg
crgvrcaadivgqcpaklkapgggcndactvfqtseyccttgkcgpteysrffkrlcpda
fsyvldkpttvtcpgssnyrvtfcpta
>d1ygs__ 2.25.1.1.1 Smad4 tumor suppressor C-terminal domain {Human (Homo sapiens)}
apeywcsiayfemdvqvgetfkvpsscpivtvdgyvdpsggdrfclgqlsnvhrteaier
arlhigkgvqleckgegdvwvrclsdhavfvqsyyldreagrapgdavhkiypsayikvf
dlrqchrqmqqqaataqaaaaaqaaavagnipgpgsvggiapaislsaaagigvddlrrl
cilrmsfvkgwgpdyprqsiketpcwieihlhralqlldevlhtm
>d1deva_ 2.25.1.1.2 Smad2 MH2 domain {Human (Homo sapiens)}
lqpvtysepafwcsiayyelnqrvgetfhasqpsltvdgftdpsnserfclgllsnvnrn
atvemtrrhigrgvrlyyiggevfaeclsdsaifvqspncnqrygwhpatvckippgcnl
kifnnqefaallaqsvnqgfeavyqltrmctirmsfvkgwgaeyrrqtvtstpcwielhl
ngplqwldkvltqm
>d1dmza_ 2.25.1.2.1 Phosphotyrosine binding domain of Rad53 {Baker's yeast (Saccharomyces cerevisiae)}
gngrfltlkplpdsiiqesleiqqgvnpffigrsedcnckiednrlsrvhcfifkkrhav
gksmyespaqglddiwychtgtnvsylnnnrmiqgtkfllqdgdeikiiwdknnkfvigf
kveindttglfneglgmlqeqrvvlkqtaeekdlvkkl
>d1cq3a_ 2.26.1.1.1 Soluble secreted chemokine inhibitor, VCCI {Virus (Cowpox virus)}
sfssssscteeenkhhmgidviikvtkqdqtptndkicqsvtevtesedeseevvkgdpt
tyytvvgggltmdfgftkcpkissiseysdgntvnarlssvspgqgkdspaitreealsm
ikdcemsinikcseeekdsnikthpvlgsnishkkvsyediigstivdtkcvknleisvr
igdmckesselevkdgfkyvdgsasedaaddtslinsakliacv
>d1p35a_ 2.27.1.1.1 Paculovirus p35 {Nuclear polyhedrosis virus (Autographa californica), ACMNPV}
cvifpveidvsqtiirdcqvdkqtrelvyinkimntqltkpvlmmfnisgpirsvtrknn
nlrdrikskvdeqfdqlerdysdqmdgfhdsikyfkdehysvscqngsvlkskfakilks
hdytdkksieayekyclpklvderndyyvavcvlkpgfengsnqvlsfeynpignkvivp
faheindtglyeydvvayvdsvqfdgeqfeefvqslilpssfknsekvlyyneasknksm
iykalefttesswgksekynwkifcngfiydkkskvlyvklhnvtsalnknvilntika
>d1nls__ 2.28.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>e1bqp.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1bqp.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1rin.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhsels
>e1rin.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsgt
>e2ltn.1a 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
tettsflitkfspdqqnlifqgdgyttkekltltkavkntvgralysspihiwdretgnv
anfvtsftfvinapnsynvadgftffiapvdtkpqtgggylgvfnsaeydkttqtvavef
dtfynaawdpsnrdrhigidvnsiksvntkswklqngeeanvviafnaatnvltvsltyp
n
>e2ltn.1b 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsg
>e2ltn.2d 2.28.1.1.3 Lectin {Garden pea (Pisum sativum)}
vtsytlsdvvslkdvvpewvrigfsattgaeyaahevlswsfhselsg
>d1lemb_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>d1lesb_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>d1lesd_ 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaahevhswsfhsqlg
>e1len.1b 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e1len.2d 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e2lal.1b 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>e2lal.2d 2.28.1.1.4 Lectin {Common lentil (Lens culinaris)}
vtsytlnevvplkdvvpewvrigfsattgaefaaqevhswsfnsqlg
>d1led__ 2.28.1.1.5 Lectin {West-central african legume (Griffonia simplicifolia)}
xntvnftypdfwsyslkngteitflgdatripgalqltktdangnpvrssagqasysepv
flwdstgkaasfytsftfllknygaptadglafflapvdssvkdyggflglfrhetaadp
sknqvvavefdtwinkdwndppyphigidvnsivsvattrwenddaygssiatahityda
rskiltvllsyehgrdyilshvvdlakvlpqkvrigfsagvgydevtyilswhffstldg
tnk
>d1ax0__ 2.28.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>e1loa.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loa.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loa.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lob.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lob.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loc.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loc.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1lod.3f 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lod.4h 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselag
>e1loe.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1loe.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1lof.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtssn
>e1log.1b 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfhsela
>e1log.2d 2.28.1.1.8 Lectin {Lathyrus ochrus, solectin I}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfhselagtss
>e1lgb.1b 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselav
>e1lgc.1b 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsvtss
>e1lgc.2d 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
etsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>e1lgc.3f 2.28.1.1.9 Lectin {Lathyrus ochrus, isolectin II}
tsytlnevvplkefvpewvrigfsattgaefaahevlswyfnselsv
>d2pela_ 2.28.1.1.10 Lectin {Peanut (Arachis hypogaea)}
aetvsfnfnsfsegnpainfqgdvtvlsngniqltnlnkvnsvgrvlyampvriwssatg
nvasfltsfsfemkdikdydpadgiiffiapedtqipagsigggtlgvsdtkgaghfvgv
efdtysnseyndpptdhvgidvnsvdsvktvpwnsvsgavvkvtviydsstktlsvavtn
dngdittiaqvvdlkaklpervkfgfsasgslggrqihlirswsftstlitt
>e1qmo.1a 2.28.1.1.12 Lectin {Field bean (Dolichos lab lab), Fril}
aqslsfsftkfdpnqedlifqghatstnnvlqvtkldsagnpvsssagrvlysaplrlwe
dsavltsfdtiinfeistpytsriadglaffiappdsvisyhggflglfpnan
>e1qmo.1e 2.28.1.1.12 Lectin {Field bean (Dolichos lab lab), Fril}
snvvavefdtylnpdygdpnyihigidvnsirskvtakwdwqngkiatahisynsvskrl
svtsyyagskpatlsydielhtvlpewvrvglsastgqdkerntvhswsftsslwtn
>d1qnwa_ 2.28.1.1.15 Lectin {Furze (Ulex europaeus), UEA-II}
sddlsfnfdkfvpnqkniifqgdasvsttgvlqvtkvskptttsigralyaapiqiwdsi
tgkvasfatsfsfvvkadksdgvdglafflapansqipsgssagmfglfsssdskssnqi
iavefdtyfgkaynpwdpdfkhigidvnsiksiktvkwdwrngevadvvityraptkslt
vclsypsdgtsniitasvdlkailpewvsvgfsggvgnaaefethdvlswyftsnle
>d1avba_ 2.28.1.1.16 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndasfnvetfnktnlilqgdatvsseghllltnvkgneedsmgrafysapiqindrtid
nlasfstnftfrinakniensayglafalvpvgsrpklkgrylglfnttnydrdahtvav
vfdtvsnrieidvnsirpiatescnfghnngekaevritydspkndlrvsllypsseekc
hvsatvplekevedwvsvgfsatsgskkettethnvlswsfssnfi
>d1dhkb_ 2.28.1.1.16 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
atetsfiidafnktnlilqgdatvssngnlqlsynsydsmsrafysapiqirdsttgnva
sfdtnftmnirthrqansavgldfvlvpvqpeskgdtvtvefdtflsrisidvnnndiks
vpwdvhdydgqnaevritynsstkvfsvslsnpstgksnnvsttvelekevydwvsvgfs
atsgayqwsyethdvlswsfsskf
>d2ayh__ 2.28.1.2.2 Bacillus 1-3,1-4-beta-glucanase {Hybrid protein: residues 1-16 from Bacillus Amyloliquefaciens and Bacillus macerans}
qtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklklgltssaynkfd
caeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkvqf
nyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkim
mnlwngtgvddwlgsynganplyaeydwvkytsn
>d1ajka_ 2.28.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajoa_ 2.28.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtg
vddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctw
rannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssffty
tgpahgtqwdeidieflgkdttkvqfnyytng
>d1cpn__ 2.28.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsngsvfwepksyfnpstwekadgysn
ggvfnctwrannvnftndgklklgltss
>d1slta_ 2.28.1.3.1 S-lectin, different isoforms {Bovine (Bos taurus)}
cglvasnlnlkpgeclrvrgevaadaksfllnlgkddnnlclhfnprfnahgdvntivcn
skdagawgaeqresafpfqpgsvvevcisfnqtdltiklpdgyefkfpnrlnleainyls
aggdfkikcvafe
>d1bkza_ 2.28.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
snvphksslpegirpgtvlrirglvppnasrfhvnllcgeeqgsdaalhfnprldtsevv
fnskeqgswgreergpgvpfqrgqpfevliiasddgfkavvgdaqyhhfrhrlplarvrl
vevggdvqldsvrif
>d1hlca_ 2.28.1.3.2 S-lectin, different isoforms {Human (Homo sapiens)}
elevknmdmkpgstlkitgsiadgtdgfvinlgqgtdklnlhfnprfsestivcnsldgs
nwgqeqredhlcfspgsevkftvtfesdkfkvklpdgheltfpnrlghshlsylsvrggf
nmssfklke
>d1qmja_ 2.28.1.3.3 S-lectin, different isoforms {Chicken (Gallus gallus)}
qglvvtqldvqpgecvkvkgkilsdakgfsvnvgkdsstlmlhfnprfdchgdvntvvcn
skedgtwgeedrkadfpfqqgdkveicisfdaaevkvkvpevefefpnrlgmekiqylav
egdfkvkaikfs
>d1a78a_ 2.28.1.3.4 S-lectin, different isoforms {Toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqreevfpfqqgaevmvcfeyqtqkiiikfssgdqfsfpvrkvlpsipf
lsleglafksitte
>d1lcl__ 2.28.1.3.5 Charcot-Leyden crystal (CLC) protein {Human (Homo sapiens)}
sllpvpyteaaslstgstvtikgrplvcflnepylqvdfhtemkeesdivfhfqvcfgrr
vvmnsreygawkqqvesknmpfqdgqefelsisvlpdkyqvmvngqssytfdhrikpeav
kmvqvwrdisltkfnvsylkr
>d1a3k__ 2.28.1.3.6 Galectin-3 CRD {Human (Homo sapiens)}
livpynlplpggvvprmlitilgtvkpnanrialdfqrgndvafhfnprfnennrrvivc
ntkldnnwgreerqsvfpfesgkpfkiqvlvepdhfkvavndahllqynhrvkklneisk
lgisgdidltsasytmi
>d1c1la_ 2.28.1.3.7 Congerin I {Conger eel (Conger myriaster)}
gglqvknfdftvgkfltvggfinnspqrfsvnvgesmnslslhldhrfnygadqntivmn
stlkgdngweteqrstnftlsagqyfeitlsydinkfyidildgpnlefpnryskeflpf
lslagdarltlvkle
>d1qu0a_ 2.28.1.4.1 Laminin alpha2 chain {Mouse (Mus musculus)}
sgtyfdgtgfakavggfkvgldllvefefrttrptgvllgissqkmdgmgiemideklmf
hvdngagrftaiydaeipghmcngqwhkvtakkiknrlelvvdgnqvdaqspnsastsad
tndpvfvggfpgglnqfglttnirfrgcirslkltkgtgkplevnfakalelrgvqpvsc
p
>d1saca_ 2.28.1.5.1 Serum amyloid P component (SAP) {Human (Homo sapiens)}
htdlsgkvfvfpresvtdhvnlitplekplqnftlcfraysdlsrayslfsyntqgrdne
llvykervgeyslyigrhkvtskviekfpapvhicvswesssgiaefwingtplvkkglr
qgyfveaqpkivlgqeqdsyggkfdrsqsfvgeigdlymwdsvlppenilsayqgtplpa
nildwqalnyeirgyviikplvwv
>d1a8d_1 2.28.1.6.1 (1-247) Tetanus neurotoxin {Clostridium tetani}
mknldcwvdneedidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkai
hlvnnessevivhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkh
slsigsgwsvslkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlss
anlyingvlmgsaeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeiek
lytsyls
>d3btaa1 2.28.1.6.2 (872-1078) Botulinum neurotoxin serotype A {(Clostridium botulinum)}
iintsilnlryesnhlidlsryaskinigskvnfdpidknqiqlfnlesskievilknai
vynsmyenfstsfwiripkyfnsislnneytiincmennsgwkvslnygeiiwtlqdtqe
ikqrvvfkysqminisdyinrwifvtitnnrlnnskiyingrlidqkpisnlgnihasnn
imfkldgcrdthryiwikyfnlfdkel
>d1kit_1 2.28.1.8.1 (25-216) Vibrio cholerae sialidase, N-terminal and insertion domains {Vibrio cholerae}
alfdynatgdtefdspakqgwmqdntnngsgvltnadgmpawlvqgiggraqwtyslstn
qhaqassfgwrmttemkvlsggmitnyyangtqrvlpiisldssgnlvvefegqtgrtvl
atgtaateyhkfelvflpgsnpsasfyfdgklirdniqptaskqnmivwgngssntdgva
ayrdikfeiqgd
>d1kit_2 2.28.1.8.1 (347-543) Vibrio cholerae sialidase, N-terminal and insertion domains {Vibrio cholerae}
dvtdqvkersfqiagwggselyrrntslnsqqdwqsnakirivdgaanqiqvadgsrkyv
vtlsidesgglvanlngvsapiilqsehakvhsfhdyelqysalnhtttlfvdgqqittw
agevsqenniqfgnadaqidgrlhvqkivltqqghnlvefdafylaqqtpevekdleklg
wtkiktgntmslygnas
>d2sli_1 2.28.1.9.1 (81-276) Leech intramolecular trans-sialidase, N-terminal domain {North american leech (Macrobdella decora)}
ipegilmeknnvdiaegqgysldqeagakyvkamtqgtiilsykstsengiqslfsvgns
tagnqdrhfhiyitnsggigielrntdgvfnytldrpasvralykgervfntvalkadaa
nkqcrlfangellatldkdafkfisditgvdnvtlggtkrqgkiaypfggtigdikvysn
alsdeeliqatgvtty
>d6cel__ 2.28.1.10.1 Cellobiohydrolase I (cellulase) {Trichoderma reesei}
sactlqsethppltwqkcssggtctqqtgsvvidanwrwthatnsstncydgntwsstlc
pdnetcaknccldgaayastygvttsgnslsidfvtqsaqknvgarlylmasdttyqeft
llgnefsfdvdvsqlpcglngalyfvsmdadggvskyptntagakygtgycdsqcprdlk
fingqanvegwepssnnantgigghgsccsqmdiweansisealtphpcttvgqeicegd
gcggtysdnryggtcdpdgcdwnpyrlgntsfygpgssftldttkkltvvtqfetsgain
ryyvqngvtfqqpnaelgsysgnelnddyctaeeaefggssfsdkggltqfkkatsggmv
lvmslwddyyanmlwldstyptnetsstpgavrgscstssgvpaqvesqspnakvtfsni
kfgpigstgnpsg
>d1xnb__ 2.28.1.11.1 Xylanase II {Bacillus circulans}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1xyn__ 2.28.1.11.4 Xylanase II {Trichoderma reesei, xynI}
asinydqnyqtggqvsyspsntgfsvnwntqddfvvgvgwttgssapinfggsfsvnsgt
gllsvygwstnplveyyimednhnypaqgtvkgtvtsdgatytiwentrvnepsiqgtat
fnqyisvrnsprtsgtvtvqnhfnawaslglhlgqmnyqvvavegwggsgsasqsvsn
>d1enxa_ 2.28.1.11.5 Xylanase II {Trichoderma reesei, xynII}
xtiqpgtgynngyfysywndghggvtytngpggqfsvnwsnsgnfvggkgwqpgtknkvi
nfsgsynpngnsylsvygwsrnplieyyivenfgtynpstgatklgevtsdgsvydiyrt
qrvnqpsiigtatfyqywsvrrnhrssgsvntanhfnawaqqgltlgtmdyqivavegyf
ssgsasitvs
>d1bk1__ 2.28.1.11.8 Xylanase II {Aspergillus kawachii}
aginyvqnyngnlgdftydesagtfsmywedgvssdfvvglgwttgssnaitysaeysas
gsssylavygwvnypqaeyyivedygdynpcssatslgtvysdgstyqvctdtrtnepsi
tgtstftqyfsvrestrtsgtvtvanhfnfwaqhgfgnsdfnyqvmaveawsgagsasvt
is
>d2nlra_ 2.28.1.11.10 Endo-1,4-beta-glucanase (cellulase) CelB2 catalytic domain {Streptomyces lividans}
dtticepfgtttiqgryvvqnnrwgstapqcvtatdtgfrvtqadgsaptngapksypsv
fngchytncspgtdlpvrldtvsaapssisygfvdgavynasydiwldptartdgvnqte
imiwfnrvgpiqpigspvgtasvggrtwevwsggngsndvlsfvapsaisgwsfdvmdfv
ratvarglaendwyltsvqagfepwqngaglavnsfsstvet
>d1bgla4 2.29.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1oaca1 2.29.2.1.1 (301-724) Copper amine oxidase, domain 3 (catalytic) {Escherichia coli}
pavkpmqiiepegknytitgdmihwrnwdfhlsmnsrvgpmistvtyndngtkrkvmyeg
slggmivpygdpdigwyfkayldsgdygmgtltspiargkdapsnavllnetiadytgvp
meipraiavferyagpeykhqemgqpnvsterrelvvrwistvgnxdyifdwifhengti
gidagatgieavkgvkaktmhdetakddtrygtlidhnivgtthqhiynfrldldvdgen
nslvamdpvvkpntaggprtstmqvnqynigneqdaaqkfdpgtirllsnpnkenrmgnp
vsyqiipyaggthpvakgaqfapdewiyhrlsfmdkqlwvtryhpgerfpegkypnrsth
dtglgqyskdnesldntdavvwmttgtthvaraeewpimptewvhtllkpwnffdetptl
galk
>d1cb8a3 2.29.3.1.1 (336-599) Chondroitinase AC, central domain {Flavobacterium heparinum}
iepyhhqfwngdyvqhlrpaysfnvrmvskrtrrsesgnkenllgrylsdgatniqlrgp
eyynimpvwewdkipgitsrdyltdrpltklwgeqgsndfaggvsdgvygasayaldyds
lqakkawfffdkeivclgaginsnapenitttlnqswlngpvistagktgrgkittfkaq
gqfwllhdaigyyfpeganlslstqsqkgnwfhinnshskdevsgdvfklwinhgarpen
aqyayivlpginkpeeikkyngta
>d1qexa_ 2.30.1.1.1 gp9 {(Bacteriophage T4)}
mfiqepkklidtgeignastgdilfdggnkinsdfnaiynafgdqrkmavangtgadgqi
ihatgyyqkhsiteyatpvkvgtrhdidtstvgvkviiergelgdcvefinsngsisvtn
pltiqaidsikgvsgnlvvtspyskvtlrcissdnstsvwnysiesmfgqkespaegtwn
istsgsvdiplfhrteynmakllvtcqsvdgrkiktaeinilvdtvnsevisseyavmrv
gneteedeianiafsikenyvtatissstvgmraavkviatqkigvaq
>d1rie__ 2.31.1.1.1 ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1rfs__ 2.31.1.1.3 ISP subunit from chloroplast cytochrome bf complex {Spinach (Spinacia oleracea)}
tiakdalgndviaaewlkthapgdrtltqglkgdptylvvesdktlatfginavcthlgc
vvpfnaaenkficpchgsqynnqgrvvrgpaplslalahcdvddgkvvfvpwtetdfrtg
eapwwsa
>d1ndoa1 2.31.1.2.1 (1-154) Napthalene 1,2-dioxygenase alpha subunit, N-domain {Pseudomonas putida}
mnynnkilvsesglsqkhlihgdeelfqhelktifarnwlflthdslipapgdyvtakmg
idevivsrqndgsiraflnvcrhrgktlvsveagnakgfvcsyhgwgfgsngelqsvpfe
kdlygeslnkkclglkevarvesfhgfiygcfdq
>d1bia_2 2.32.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bib_2 2.32.1.1.1 (271-317) Biotin repressor/biotin holoenzyme synthetase, C-terminal domain {Escherichia coli}
finrpvkliigdkeifgisrgidkqgallleqdgiikpwmggeislr
>d1bi0_3 2.32.1.2.1 (148-226) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtirieel
>d1bi1_3 2.32.1.2.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1bi2a3 2.32.1.2.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1bi3a3 2.32.1.2.1 (148-225) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtiriee
>d1byma_ 2.32.1.2.1 Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
npipgldelgvgnsdaaapgtrvidaatsmprkvrivqineifqvetdqftqlldadirv
gseveivdrdghitlshngkdvellddlahtirieel
>d2dtr_3 2.32.1.2.1 (148-226) Diphtheria toxin repressor (DtxR) {Corynebacterium diphtheriae}
pgtrvidaatsmprkvrivqineifqvetdqftqlldadirvgseveivdrdghitlshn
gkdvellddlahtirieel
>d1b07a_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
saeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckaa_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1ckba_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
aeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyveky
>d1nloc_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1nlpc_ 2.32.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1a0nb_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1avzc_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
tlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1azgb_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efna_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1efnc_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydyeaiteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1fyna_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
gtgvtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvap
vd
>d1nyf__ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1nyg__ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1shfa_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapvd
>d1shfb_ 2.32.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapvd
>d1ark__ 2.32.2.1.3 SH3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1neb__ 2.32.2.1.3 SH3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1aboa_ 2.32.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abob_ 2.32.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abq__ 2.32.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
lfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvn
>d2abl_1 2.32.2.1.4 (75-139) Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
mgpsendpnlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsny
itpvn
>d1awo__ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
slfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvs
>d1bbza_ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbzc_ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbze_ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvas
>d1bbzg_ 2.32.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1pht__ 2.32.2.1.6 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Human (Homo sapiens)}
aegyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqearpeeigwlngynet
tgergdfpgtyveyigrkkispp
>d1pks__ 2.32.2.1.7 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Bovine (Bos taurus)}
egyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqearpeeigwlngynett
gergdfpgtyveyigr
>d1pkt__ 2.32.2.1.7 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Bovine (Bos taurus)}
egyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqearpeeigwlngynett
gergdfpgtyveyigr
>d1pnj__ 2.32.2.1.7 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Bovine (Bos taurus)}
gsmsaegyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqeakpeeigwlng
ynettgergdfpgtyveyigrkkisp
>d2pni__ 2.32.2.1.7 Phosphatidylinositol 3-kinase (p85-alpha subunit, pi3k), SH3 domain {Bovine (Bos taurus)}
gsmsaegyqyralydykkereedidlhlgdiltvnkgslvalgfsdgqeakpeeigwlng
ynettgergdfpgtyveyigrkkisp
>d1aey__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
gkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkld
>d1bk2__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
kelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevngrqgfvpaayvkkld
>d1pwt__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
mgtgkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkl
d
>d1shg__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
kelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkld
>d1tuc__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
mgprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkldsgtgkelvlalydyq
e
>d1tud__ 2.32.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
rqgfvpaayvkkldsgtgkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevn
>d1awj__ 2.32.2.1.9 IL-2 inducible T-cell (Itc) kinase {Mouse (Mus musculus)}
kkplpptpednrrsfqepeetlvialydyqtndpqelalrcdeeyylldsseihwwrvqd
knghegyapssylveks
>d1ad5a1 2.32.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5b1 2.32.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1bu1a_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1b_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1c_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1bu1d_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1bu1e_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
>d1bu1f_ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
iivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
>d1qcfa1 2.32.2.1.10 (80-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
sgiriivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarv
dslet
>d2hcka1 2.32.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d2hckb1 2.32.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d4hck__ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
sediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
s
>d5hck__ 2.32.2.1.10 Hemapoetic cell kinase Hck {Human (Homo sapiens)}
sediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvd
s
>d1fmk_1 2.32.2.1.11 (82-145) c-src tyrosine kinase {Human (Homo sapiens)}
mvttfvalydyesrtetdlsfkkgerlqivnntegdwwlahslstgqtgyipsnyvapsd
siqa
>d2src_1 2.32.2.1.11 (84-145) c-src tyrosine kinase {Human (Homo sapiens)}
ttfvalydyesrtetdlsfkkgerlqivnntegdwwlahslstgqtgyipsnyvapsdsi
qa
>d2ptk_1 2.32.2.1.12 (83-145) c-src tyrosine kinase {Chicken (Gallus gallus)}
vttfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvapsds
iqa
>d1aww__ 2.32.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awx__ 2.32.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1qlya_ 2.32.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
lkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsnyvteae
>d1gfc__ 2.32.2.1.14 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
gstyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnr
>d1gfd__ 2.32.2.1.14 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
gstyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnr
>d1gria1 2.32.2.1.14 (1-56) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemk
>d1gria2 2.32.2.1.14 (157-217) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
qptyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnrn
v
>d1grib1 2.32.2.1.14 (1-56) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemk
>d1grib2 2.32.2.1.14 (157-217) Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Human (Homo sapiens)}
qptyvqalfdfdpqedgelgfrrgdfihvmdnsdpnwwkgachgqtgmfprnyvtpvnrn
v
>d1azea_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakvdfkataddelsfkrgdilkvlneesdqnwykaelngkdgfipknyiemk
>d1gbqa_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemkp
>d1gbra_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
gsrrasvgsmeaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipkn
yiemkphpefivtd
>d2gbqa_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemkp
>d3gbqa_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemkp
>d4gbqa_ 2.32.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakydfkataddelsfkrgdilkvlneecdqnwykaelngkdgfipknyiemkp
>d1sema_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
etkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d1semb_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
tkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d2sema_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
etkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d2semb_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
tkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpynsn
>d3sema_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
etkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d3semb_ 2.32.2.1.16 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Caenorhabditis elegans, SEM-5}
etkfvqalfdfnpqesgelafkrgdvitlinkddpnwwegqlnnrrgifpsnyvcpyn
>d1hsq__ 2.32.2.1.17 Phospholipase C, SH3 domain {Human (Homo sapiens)}
gsptfkcavkalfdykaqredeltfiksaiiqnvekqeggwwrgdyggkkqlwfpsnyve
emvnpegihrd
>d2hsp__ 2.32.2.1.17 Phospholipase C, SH3 domain {Human (Homo sapiens)}
gsptfkcavkalfdykaqredeltfiksaiiqnvekqeggwwrgdyggkkqlwfpsnyve
emvnpegihrd
>d1prlc_ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1prmc_ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1rlpc_ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1rlqc_ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1srl__ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1srm__ 2.32.2.1.18 Src kinase, SH3 domain {Chicken (Gallus gallus)}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1cska_ 2.32.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskb_ 2.32.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskc_ 2.32.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1cskd_ 2.32.2.1.19 Src kinase, SH3 domain {Human (Homo sapiens)}
gteciakynfhgtaeqdlpfckgdvltivavtkdpnwykaknkvgregiipanyvqkr
>d1qwea_ 2.32.2.1.20 Src kinase, SH3 domain {Avian sarcoma virus}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1qwfa_ 2.32.2.1.20 Src kinase, SH3 domain {Avian sarcoma virus}
tfvalydyesrtetdlsfkkgerlqivnntegdwwlahslttgqtgyipsnyvaps
>d1lcka1 2.32.2.1.21 (63-116) p56-lck tyrosine kinase, SH3 domain {Human (Homo sapiens)}
dnlvialhsyepshdgdlgfekgeqlrileqsgewwkaqslttgqegfipfnfv
>d1ycsb2 2.32.2.1.22 (457-519) 53BP2 {Human (Homo sapiens)}
imnkgviyalwdyepqnddelpmkegdcmtiihrededeiewwwarlndkegyvprnllg
lyp
>d1bb9__ 2.32.2.1.23 Amphiphysin 2 {Rat (Rattus norvegicus)}
ttgrldlppgfmfkvqaqhdytatdtdelqlkagdvvlvipfqnpeeqdegwlmgvkesd
wnqhkelekcrgvfpenftervq
>d1aoja_ 2.32.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aojb_ 2.32.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1br1a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br1g1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2b1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2d1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br2f1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4a1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4c1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4e1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d1br4g1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
lvwvpsekhgfeaasikeekgdevtvelqengkkvtlskddiqkmn
>d2mysa1 2.32.3.1.1 (34-79) Myosin S1 fragment, N-terminal domain {Chicken (Gallus gallus), pectoral muscle}
axssvfvvhpkqsfvxgtiqsxeggxvtvxteggetltvkedqvfs
>d1b7ta1 2.32.3.1.2 (29-76) Myosin S1 fragment, N-terminal domain {Bay scallop (Aequipecten irradians)}
dgkkncwvpdekegfasaeiqsskgdeitvkivadsstrtvkkddiqs
>d1d0xa1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d0ya1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d0za1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1aa1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1ba1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1d1ca1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1lvk_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mma_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmd_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mmg_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mmn_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpkerdsyecgeivsetsdsftfktsdgqdrqvkkddanq
>d1mnd_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1mne_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1vom_1 2.32.3.1.3 (34-79) Myosin S1 fragment, N-terminal domain {Dictyostelium discoideum}
yiwynpdpderdsyecgeivsetsdsftfktvdgqdrqvkkddanq
>d1vie__ 2.32.4.1.1 R67 dihydrofolate reductase {Escherichia coli, plasmid PLZ1}
psnatfgmgdrvrkksgaawqgqivgwyctnltpegyaveseahpgsvqiypvaalerin
>d1vif__ 2.32.4.1.1 R67 dihydrofolate reductase {Escherichia coli, plasmid PLZ1}
psnatfgmgdrvrkksgaawqgqivgwyctnltpegyaveseahpgsvqiypvaalerin
>d1pse__ 2.32.4.2.1 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Synechococcus sp., strain PCC 7002}
aiergskvkilrkesywygdvgtvasidksgiiypvivrfnkvnyngfsgsagglntnnf
aehelevvg
>d1psf__ 2.32.4.2.1 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Synechococcus sp., strain PCC 7002}
aiergskvkilrkesywygdvgtvasidksgiiypvivrfnkvnyngfsgsagglntnnf
aehelevvg
>d1qp2a_ 2.32.4.2.2 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Nostoc sp., strain pcc8009}
mvqrgskvrilrpesywfqdvgtvasvdqsgikypvivrfekvnysgintnnfaedelve
veapkakpkk
>d1qp3a_ 2.32.4.2.2 Photosystem I accessory protein E (PsaE) {Cyanobacterium (Nostoc sp., strain pcc8009}
mvqrgskvrilrpesywfqdvgtvasvdqsgikypvivrfekvnysgintnnfaedelve
veapkakpkk
>d1dj7b_ 2.32.4.3.1 Ferredoxin thioredoxin reductase (FTR), alpha (variable) chain {Synechocystis sp.}
mnvgdrvrvtssvvvyhhpehkktafdlqgmegevaavltewqgrpisanlpvlvkfeqr
fkahfrpdevtli
>d2ahjb_ 2.32.4.4.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvnadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepa
>d1eif_1 2.32.5.1.1 (4-73) N-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
mpgtkqvnvgslkvgqyvmidgvpceivdisvskpgkhggakarvvgigifekvkkefva
ptsskvevpi
>d2eifa1 2.32.5.1.1 (1-73) N-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
viimpgtkqvnvgslkvgqyvmidgvpceivdisvskpgkhggakarvvgigifekvkke
fvaptsskvevpi
>d1bkb_1 2.32.5.1.2 (4-74) N-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
kwvxstkyveagelkegsyvvidgepcrvveieksktgkhgsakarivavgvfdggkrtl
slpvdaqvevp
>d1rl2a1 2.32.5.2.1 (126-195) C-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
gnalplenipvgtlvhnielkpgrggqlvraagtsaqvlgkegkyvivrlasgevrxilg
kcratvgevg
>d1rl2b1 2.32.5.2.1 (126-196) C-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
gnalplenipvgtlvhnielkpgrggqlvraagtsaqvlgkegkyvivrlasgevrxilg
kcratvgevgn
>d3vub__ 2.32.6.1.1 CcdB {Escherichia coli}
mqfkvytykresryrlfvdvqsdiidtpgrrmviplasarllsdkvsrelypvvhigdes
wrmmttdmasvpvsvigeevadlshrendiknainlmfwgi
>d1ihva_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihvb_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwa_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1ihwb_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrdpvwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1qmca_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrnplwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1qmcb_ 2.32.7.1.1 DNA-binding domain of HIV-1 integrase {Human immunodeficiency virus, HIV-1}
miqnfrvyyrdsrnplwkgpakllwkgegavviqdnsdikvvprrkakiird
>d1aono_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonp_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonq_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonr_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aons_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aont_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonu_ 2.33.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1lepa_ 2.33.1.1.2 Chaperonin-10 (GroES) {Mycobacterium leprae}
akvkikpledkilvqageaetmtpsglvipenakekpqegtvvavgpgrwdedgakripv
dvsegdiviyskyggteikyngeeylilsardvlavvsk
>d1g31a_ 2.33.1.1.3 GP31 co-chaperonin {Bacteriophage T4}
qqlpiravgeyvilvsepaqagdeevtesgliigkrvqgevpelcvvhsvgpdvpegfce
vgdltslpvgqirnvphpfvalglkqpkeikqkfvtchykaipclyk
>d3btoa1 2.33.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1keva1 2.33.1.2.3 (1-150,315-351) Bacterial secondary alcohol dehydrogenase {Clostridium beijerinckii}
mkgfamlginklgwiekerpvagsydaivrplavspctsdihtvfegalgdrknmilghe
avgevvevgsevkdfkpgdrvivpcttpdwrslevqagfqqhsngmlagwkfsnfkdgvf
geyfhvndadmnlailpkdmplenavmitdXdlsklvthvyhgfdhieealllmkdkpkd
likavvil
>d1qora1 2.33.1.2.5 (2-135,266-327) Quinone oxidoreductase {Escherichia coli}
atriefhkhggpevlqaveftpadpaeneiqvenkaiginfidtyirsglypppslpsgl
gteaagivskvgsgvkhikagdrvvyaqsalgayssvhniiadkaailpaaisfeqaaas
flkgltvyyllrktXlqgyittreelteasnelfsliasgvikvdvaeqqkyplkdaqra
heilesratqgssllip
>d1auua_ 2.33.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auub_ 2.33.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1pdr__ 2.34.1.1.1 Discs large protein homolog {Human (Homo sapiens)}
itreprkvvlhrgstglgfnivggedgegifisfilaggpadlsgelrkgdriisvnsvd
lraasheqaaaalknagqavtivaqyrpeeysrqha
>d1kwaa_ 2.34.1.1.2 Cask/Lin-2 {Human (Homo sapiens)}
rsrlvqfqkntdepmgitlkmnelnhcivarimhggmihrqgtlhvgdeireingisvan
qtveqlqkmlremrgsitfkivpsyref
>d1kwab_ 2.34.1.1.2 Cask/Lin-2 {Human (Homo sapiens)}
rsrlvqfqkntdepmgitlkmlnhcivarimhggmihrqgtlhvgdeireingisvanqt
veqlqkmlremrgsitfkivpsyref
>d1be9a_ 2.34.1.1.3 Synaptic protein PSD-95 {Rat (Rattus norvegicus)}
flgeedipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqil
svngvdlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1qlca_ 2.34.1.1.3 Synaptic protein PSD-95 {Rat (Rattus norvegicus)}
aekvmeiklikgpkglgfsiaggvgnqhipgdnsiyvtkiieggaahkdgrlqigdkila
vnsvgledvmhedavaalkntydvvylkvakpsna
>d1qaua_ 2.34.1.1.4 Syntrophin {Rat (Rattus norvegicus)}
nvisvrlfkrkvgglgflvkervskppviisdlirggaaeqsgliqagdiilavndrplv
dlsydsalevlrgiasethvvlilrgpegftthlettftgdgtpktirvtqp
>d1qava_ 2.34.1.1.5 Syntrophin {Mouse (Mus musculus)}
gslqrrrvtvrkadagglgisikggrenkmpiliskifkglaadqtealfvgdailsvng
edlssathdeavqalkktgkevvlevkymk
>d2pdza_ 2.34.1.1.5 Syntrophin {Mouse (Mus musculus)}
rrrvtvrkadagglgisikggrenkmpiliskifkglaadqtealfvgdailsvngedls
sathdeavqalkktgkevvlevkymk
>d1i16__ 2.34.1.2.1 Interleukin 16 {Human (Homo sapiens)}
mpdlnsstdsaasasaasdvsvestaeatvctvtlekmsaglgfsleggkgslhgdkplt
inrifkgaaseqsetvqpgdeilqlggtamqgltrfeawniikalpdgpvtivirrkslq
skettaagds
>d1fgp__ 2.35.1.1.1 N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
etvesclakphtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpig
laipenaaah
>d1g3p_1 2.35.1.1.1 (1-65) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
aetvesclakshtensftnvxkddktldryanyegclwnatgvvvctgdetqcygtwvpi
glaip
>d1g3p_2 2.35.1.1.1 (91-217) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
enegggsegggsegggsegggtkppeygdtpipgytyinpldgtyppgteqnpanpnpsl
eesqplntfmfqnnrfrnrqgaltvytgtvtqgtdpvktyyqytpvsskamydaywngkf
rdcafhsgfnedifvceyqgqssdlpqppvna
>d1tola1 2.35.1.1.1 (1-65) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
aetvesclakshtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpi
glaip
>d2g3pa1 2.35.1.1.1 (2-67) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
etvesclakphtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpig
laipen
>d2g3pb1 2.35.1.1.1 (2-67) N-terminal domains of the minor coat protein g3p {Bacteriophage fd}
etvesclakphtensftnvwkddktldryanyegclwnatgvvvctgdetqcygtwvpig
laipen
>d1b34a_ 2.36.1.1.1 D1 core SNRNP protein {Human (Homo sapiens)}
klvrflmklshetvtielkngtqvhgtitgvdvsmnthlkavkmtlknrepvqletlsir
gnniryfilpdslpldtllv
>d1b34b_ 2.36.1.1.2 D2 core SNRNP protein {Human (Homo sapiens)}
tgplsvltqsvknntqvlincrnnkkllgrvkafdrhcnmvlenvkemwtevpksgkgkk
kskpvnkdryiskmflrgdsvivvlrnpliagk
>d1d3ba_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
gvpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvyi
rgckirflilpd
>d1d3bc_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
vpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvyir
gckirflilpd
>d1d3be_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
sigvpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqv
yirgckirflilpd
>d1d3bg_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
igvpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvy
irgckirflilpd
>d1d3bi_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
igvpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvy
irgckirflilpd
>d1d3bk_ 2.36.1.1.3 D3 core SNRNP protein {Human (Homo sapiens)}
vpikvlheaeghivtcetntgevyrgklieaednmncqmsnitvtyrdgrvaqleqvyir
gckirflilpd
>d1d3bb_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
skmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaereekrv
lglvllrgenlvsmtvegppp
>d1d3bd_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
tvgksskmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaer
eekrvlglvllrgenlvsmtvegppp
>d1d3bf_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
ksskmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaereek
rvlglvllrgenlvsmtvegppp
>d1d3bh_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
vgksskmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaere
ekrvlglvllrgenlvsmtvegpppk
>d1d3bj_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
tvgksskmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaer
eekrvlglvllrgenlvsmtvegppp
>d1d3bl_ 2.36.1.1.4 B core SNRNP protein {Human (Homo sapiens)}
tvgksskmlqhidyrmrcilqdgrifigtfkafdkhmnlilcdcdefrkikpknskqaer
eekrvlglvllrgenlvsmtvegpppkdtg
>d1whi__ 2.37.1.1.1 Ribosomal protein L14 {Bacillus stearothermophilus}
miqqesrlkvadnsgarevlvikvlggsgrryanigdvvvatvkdatpggvvkkgqvvka
vvvrtkrgvrrpdgsyirfdenacviirddksprgtrifgpvarelrdkdfmkiislape
vi
>d1sty__ 2.38.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
klhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkm
venakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhl
rgkseaqakkeklniws
>d2sob__ 2.38.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
atstkklhkepatlikaidgdtvklmykgqpmtfrlllvdtpetkhpkkgvekygpeasa
ftkkmlenakkievefdkgqrtdkygrvlayiyadgkmvneal
>d1efid_ 2.38.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqtitelcseyrntqiytindkilsytesmagkremviitfksgetfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismkn
>d1tiid_ 2.38.2.1.2 Heat-labile toxin {Escherichia coli, type IIB}
gasqffkdncnrttaslvegveltkyisdinnntdgmyvvsstggvwrisrakdypdnvm
taemrkiamaavlsgmrvnmcaspasspnviwaielea
>d3chbd_ 2.38.2.1.3 Cholera toxin {Vibrio cholerae}
tpqnitdlcaeyhntqihtlndkifsyteslagkremaiitfkngatfqvevpgsqhids
qkkaiermkdtlriaylteakveklcvwnnktpraiaaisman
>d1bosa_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosb_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosc_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosd_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bose_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosf_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosg_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosh_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosi_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosj_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosk_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosl_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosm_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosn_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1boso_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosp_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosq_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bosr_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1boss_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bost_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bova_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovb_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovc_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bovd_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1bove_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d2bosa_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d2bosb_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d2bosc_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d2bosd_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d2bose_ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
adcakgkiefskynedntftvkvsgreywtnrwnlqpllqsaqltgmtvtiisntcssgs
gfaevqfn
>d4ull__ 2.38.2.1.4 Verotoxin-1/shiga-toxin, B-pentamer {Escherichia coli}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0b_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0c_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0d_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0e_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0f_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0g_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0h_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0i_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0j_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1dm0k_ 2.38.2.1.5 Verotoxin-1/shiga-toxin, B-pentamer {Shigella dysenteriae}
tpdcvtgkveytkyndddtftvkvgdkelftnrwnlqslllsaqitgmtvtiktnachng
ggfsevifr
>d1prtb1 2.38.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1prtc1 2.38.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
tiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmydal
rrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1prtd_ 2.38.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1prtf_ 2.38.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>d1esfa1 2.38.2.2.1 (1-120) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
sekseeinekdlrkkselqgtalgnlkqiyyynekaktenkeshdqflqhtilfkgfftd
hswyndllvdfdskdivdkykgkkvdlygayygyqcaggtpnktacmyggvtlhdnnrlt
>d1ste_1 2.38.2.2.2 (1-120) Staphylococcal enterotoxin C2, SEC2 {Staphylococcus aureus}
esqpdptpdelhksseftgtmgnmkylyddhyvsatkvmsvdkflahdliynisdkklkn
ydkvktellnedlakkykdevvdvygsnyyvncyfsskdnvgkvtggktcmyggitkheg
>d1aw7a1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7b1 2.38.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7c1 2.38.2.2.3 (401-493) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7d1 2.38.2.2.3 (601-693) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1qila1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1qilb1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1qilc1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts2a1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts2b1 2.38.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts2c1 2.38.2.2.3 (401-493) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts3a1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts3b1 2.38.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts3c1 2.38.2.2.3 (401-493) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts4a1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts4b1 2.38.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts5a1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1ts5b1 2.38.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2qila1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2qilb1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2qilc1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2tssa1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2tssb1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d2tssc1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d3tss_1 2.38.2.2.3 (5-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
nikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkgekvdl
ntkrikksqhtsegtwihfqisgvtntek
>d4tss_1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d5tssa1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d5tssb1 2.38.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d3seb_1 2.38.2.2.4 (1-121) Staphylococcal enterotoxin B, SEB {Staphylococcus aureus}
esqpdpkpdelhksskftglmenmkvlyddnhvsainvksidqflyfdliysikdtklgn
ydnvrvefknkdladkykdkyvdvfganyyyqcyfskktndinshqtdkrktcmyggvte
h
>d1an8_1 2.38.2.2.6 (3-95) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
kkdisnvksdllyaytitpydykdcrvnfstthtlnidtqkyrgkdyyissemsyeasqk
fkrddhvdvfglfyilnshtgeyiyggitpaqn
>d1bxta1 2.38.2.2.7 (1-119) Streptococcal superantigen SSA {Streptococcus pyogenes}
ssqpdptpeqlnkssqftgvmgnlrclydnhfvegtnvrstgqllqhdlifpikdlklkn
ydsvktefnskdlatkyknkdvdifgsnyyyncyysegnscknakktcmyggvtehhrn
>d1b1za1 2.38.2.2.8 (3-107) Streptococcal pyrogenic exotoxin A1 {Streptococcus pyogenes}
dpdpsqlhrsslvknlqniyflyegdpvthenvksvdqllshdliynvsgpnydklktel
knqematlfkdknvdiygveyyhlcylcenaersaciyggvtnhe
>d1ueab_ 2.38.3.1.1 TIMP-1 {Human (Homo sapiens)}
ctcvpphpqtafcnsdlvirakfvgtpevaqttlyqryeikmtkmykgfqalgdaadirf
vytpamesvcgyfhrsharseefliagklqdgllhittcsfvapwnslslaqrrgftkty
tvgceectvfpclsipcklqsgthclwtdqllqgsekgfqsrhlaclprepglctwqslr
s
>d1br9__ 2.38.3.1.2 TIMP-2 {Human (Homo sapiens)}
cscspvhpqqafcnadvvirakavsekevdsgndiygnpikriqyeikqikmfkgpekdi
efiytapssavcgvsldvggkkeyliagkaegdgkmhitlcdfivpwdtlsttqkkslnh
ryqmgceckitrcpmipcyisspdeclwmdwvtekninghqakffacikrsdgscawyrg
aa
>d1asza1 2.38.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1b8aa1 2.38.4.1.2 (1-103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1c0aa1 2.38.4.1.3 (1-106) Aspartyl-tRNA synthetase (AspRS) {Escherichia coli}
mrteycgqlrlshvgqqvtlcgwvnrrrdlgslifidmrdregivqvffdpdradalkla
selrnefciqvtgtvrardekninrdmatgeievlassltiinrad
>d1lyla1 2.38.4.1.6 (14-153) Lysyl-tRNA synthetase (LysRS) {Escherichia coli, gene lysU}
fndelrnrreklaalrqqgvafpndfrrdhtsdqlheefdakdnqeleslnievsvagrm
mtrrimgkasfvtlqdvggriqlyvardslpegvyndqfkkwdlgdiigargtlfktqtg
elsihctelrlltkalrplp
>d1bdxa3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxb3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxc3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxd3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1cuk_3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1hjp_3 2.38.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bvsa3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsb3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsc3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsd3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvse3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsf3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsg3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d1bvsh3 2.38.4.2.2 (1-63) DNA helicase RuvA subunit, N-terminal domain {Mycobacterium leprae}
mifsvrgevlevaldhavieaagigyrvnatpsalatlnqgsqarlvtamvvredsmtly
gfs
>d3ulla_ 2.38.4.3.1 ssDNA-binding protein {Human (Homo sapiens), mitochondria}
lerslnrvhllgrvgqdpvlrqvegknpvtifslatnemwrsgdsevyqlgdvsqkttwh
risvfrpglrdvayqyvkkgsriylegkidygeymdknnvrrqattiiadniifl
>d1kawa_ 2.38.4.3.2 ssDNA-binding protein {Escherichia coli}
rgvnkvilvgnlgqdpevrympnggavanitlatseswrdkatgemkeqtewhrvvlfgk
laevaseylrkgsqvyiegqlrtrkwtdqsgqdryttevvvnvggtmqml
>d1jmca1 2.38.4.3.3 (183-298) Replication protein A 70 KDa subunit (RPA70) fragment {Human (Homo sapiens)}
kvvpiasltpyqskwticarvtnksqirtwsnsrgegklfslelvdesgeiratafneqv
dkffplievnkvyyfskgtlkiankqftavkndyemtfnnetsvmpceddhhlptv
>d1jmca2 2.38.4.3.3 (299-420) Replication protein A 70 KDa subunit (RPA70) fragment {Human (Homo sapiens)}
qfdftgiddlenkskdslvdiigicksyedatkitvrsnnrevakrniylmdtsgkvvta
tlwgedadkfdgsrqpvlaikgarvsdfggrslsvlssstiianpdipeayklrgwfdae
gq
>d1quqa_ 2.38.4.3.4 Replication protein A 32 KDa subunit (RPA32) fragment {Human (Homo sapiens)}
hivpctisqllsatlvdevfrignveisqvtivgiirhaekaptnivykiddmtaapmdv
rqwvdtddtssentvvppetyvkvaghlrsfqnkkslvafkimpledmneftthilevin
ahmvlsk
>d1quqb_ 2.38.4.3.5 Replication protein A 14 KDa (RPA14) subunit {Human (Homo sapiens)}
dmmdlprsrinagmlaqfidkpvcfvgrlekihptgkmfilsdgegkngtielmepldee
isgivevvgrvtakatilctsyvqfkedshpfdlglyneavkiihdfpqfyplg
>d1otca1 2.38.4.3.6 (37-204) Telomere end binding protein alpha subunit {Oxytricha nova}
eyvelakasltsaqpqhfyavvidatfpyktnqeryicslkivdptlylkqqkgagdasd
yatlvlyakrfedlpiihragdiirvhratlrlyngqrqfnanvfyssswalfstdkrsv
tqeinnqdavsdttpfsfsskhatiekneisilqnlrkwanqyfssys
>d1otca2 2.38.4.3.6 (205-328) Telomere end binding protein alpha subunit {Oxytricha nova}
vissdmytalnkaqaqkgdfdvvakilqvheldeytnelklkdasgqvfytlslklkfph
vrtgevvrirsatydetstqkkvlilshysniitfiqssklakelrakiqddhsvevasl
kknv
>d1otca3 2.38.4.3.6 (329-495) Telomere end binding protein alpha subunit {Oxytricha nova}
slnavvltevdkkhaalpstslqdlfhhadsdkelqaqdtfrtqfyvtkiepsdvkewvk
gydrktkkssslkgasgkgdnifqvqflvkdastqlnnntyrvllytqdglganffnvka
dnlhknadarkkledsaelltkfnsyvdavverrngfylikdtkliy
>d1otcb_ 2.38.4.3.7 Core domain of telomere end binding protein beta subunit {Oxytricha nova}
qqsafkqlytelfnnegdfskvssnlkkplkcyvkesyphflvtdgyffvapyftkeavn
efhakfpnvnivdltdkvivinnwslelrrvnsaevftsyanlearlivhsfkpnlqerl
nptrypvnlfrddefkttiqhfrhtalqaainktvkgdnlvdiskvadaagkkgkvdagi
vkasaskgdefsdfsfkegntatlkiadifvqe
>d1pysb3 2.38.4.4.1 (39-151) Domain B2 of PheRS-beta, PheT {Thermus thermophilus (Thermus aquaticus)}
fpiprgvvfarvleahpipgtrlkrlvldagrtvevvsgaenarkgigvalalpgtelpg
lgqkvgerviqgvrsfgmalsprelgvgeygggllefpedalppgtplseawp
>d1mjc__ 2.38.4.5.1 Major cold shock protein {Escherichia coli}
sgkmtgivkwfnadkgfgfitpddgskdvfvhfsaiqndgyksldegqkvsftiesgakg
paagnvtsl
>d3mefa_ 2.38.4.5.1 Major cold shock protein {Escherichia coli}
sgkmtgivkwfnadkgfgfitpddgskdvfvhfsaiqndgyksldegqkvsftiesgakg
paagnvtsl
>d1csp__ 2.38.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1csq__ 2.38.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1nmf__ 2.38.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1nmg__ 2.38.4.5.2 Major cold shock protein {Bacillus subtilis}
mlegkvkwfnsekgfgfievegqddvfvhfsaiqgegfktleegqavsfeivegnrgpqa
anvtkea
>d1sro__ 2.38.4.5.3 S1 RNA-binding domain of polyribonucleotide phosphorylase, PNP {Escherichia coli}
aeievgrvytgkvtrivdfgafvaigggkeglvhisqiadkrvekvtdylqmgqevpvkv
levdrqgrirlsikea
>d1ah9__ 2.38.4.5.4 Translational initiation factor 1, IF1 {Escherichia coli}
akedniemqgtvletlpntmfrvelenghvvtahisgkmrknyiriltgdkvtveltpyd
lskgrivfrsr
>d1a62__ 2.38.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
nltelkntpvselitlgenxglenlarxrkqdiifailkqhaksgedifgdgvleilqdg
fgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevnf
dkpe
>d1eif_2 2.38.4.5.6 (74-133) C-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
idrrkgqvlaimgdmvqimdlqtyetlelpipegieglepggeveyieavgqykitrvig
>d2eifa2 2.38.4.5.6 (74-132) C-terminal domain of eukaryotic initiation translation factor 5a {Methanococcus jannaschii}
idrrkgqvlaimgdmvqimdlqtyetlelpipegieglepggeveyieavgqykitrvi
>d1bkb_2 2.38.4.5.7 (75-139) C-terminal domain of eukaryotic initiation translation factor 5a {Pyrobaculum aerophilum}
iiekftaqilsvsgdviqlxdxrdyktievpxkyveeeakgrlapgaevevwqildryki
irvkg
>d1rl2a2 2.38.4.5.8 (60-125) N-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
qyriidfkrdkdgipgrvatieydpnrsanialinyadgekryiiapknlkvgxeixsgp
dadiki
>d1rl2b2 2.38.4.5.8 (60-125) N-terminal domain of ribosomal protein L2 {Bacillus stearothermophilus}
qyriidfkrdkdgipgrvatieydpnrsanialinyadgekryiiapknlkvgxeixsgp
dadiki
>d1ckma1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckmb1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1ckna1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cknb1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1cko_1 2.38.4.6.1 (239-327) RNA guanylyltransferase (mRNA capping enzyme) {Chlorella virus, PBCV-1}
thhtidfiimsedgtigifdpnlrknvpvgkldgyynkgsivecgfadgtwkyiqgrsdk
nqandrltyektllnieenitidelldlf
>d1a0i_1 2.38.4.6.2 (241-349) ATP-dependent DNA ligase {Bacteriophage T7}
peneadgiiqglvwgtkglanegkvigfevllesgrlvnatnisralmdeftetvkeatl
sqwgffspygigdndactinpydgwacqisymeetpdgslrhpsfvmfr
>d1rip__ 2.38.4.7.1 Ribosomal S17 protein {Bacillus stearothermophilus}
qrkvyvgrvvsdkmdktitvlvetykkhplygkrvkyskkykahdehneakvgdivkime
trplsatkrfrlveivekavr
>d1ae2__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqrcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1ae3__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlclvpa
>d1gkh__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfhvgqfgslmidrlrlvpa
>d1gvp__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1vqa__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyadlgneypvlvkltldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqb__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqc__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyidlgneypvlvkftldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqd__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyidlgneypvlvkltldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqe__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyidlgneypvlvkmtldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqf__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyidlgneypvlvkvtldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqg__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkltldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqh__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkmtldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqi__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkvtldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1vqj__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyidlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1yhaa_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1yhab_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1yhb__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnefpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d2gn5__ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d2gvaa_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d2gvab_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d2gvba_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d2gvbb_ 2.38.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgnehpvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpak
>d1pfsa_ 2.38.4.8.2 Gene V protein {Phage pf3 (Pseudomonas)}
mniqitftdsvrqgtsakgnpytfqegflhledkphplqcqffvesvipagsyqvpyrin
vnngrpelafdfkamkra
>d1pfsb_ 2.38.4.8.2 Gene V protein {Phage pf3 (Pseudomonas)}
mniqitftdsvrqgtsakgnpytfqegflhledkphplqcqffvesvipagsyqvpyrin
vnngrpelafdfkamkra
>d1gpc__ 2.38.4.8.3 Gene 32 protein (GP32) core {Bacteriophage T4}
gfssedkgewklkldnagngqavirflpskndeqapfailvnhgfkkngkwyietcssth
gdydscpvcqyiskndlyntdnkeyslvkrktsywanilvvkdpaapenegkvfkyrfgk
kiwdkinamiavdvemgetpvdvtcpweganfvlkvkqvsgfsnydeskflnqsaipnid
desfqkelfeqmvdlsemtskdkfksfeelntkfgqvm
>d1a1d__ 2.38.4.9.1 RNA polymerase subunit RBP8 {Baker's yeast (Saccharomyces cerevisiae)}
msntlfddifqvsevdpgrynkvcrieaasttqdqckltldinvelfpvaaqdsltvtia
sslnledtpandssatrswrppqagdrsladdydyvmygtaykfeevskdliavyysfgg
llmrlegnyrnlnnlkqenayllirr
>d8prka_ 2.38.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgkpvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgklkfvrncfphhgyihnygafpqtwedpnvshpetkavgdndpid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenqfafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwffi
>d1qeza_ 2.38.5.1.2 Inorganic pyrophosphatase {Sulfolobus acidocaldarius}
klspgknapdvvnvlveipqgsnikyeyddeegvikvdrvlytsmnypfnygfipgtlee
dgdpldvlvitnyqlypgsvievrpigilymkdeegedakivavpkdktdpsfsnikdin
dlpqatknkivhffehykelepgkyvkisgwgsateaknriqlaikrvsg
>d1obwa_ 2.38.5.1.3 Inorganic pyrophosphatase {Escherichia coli}
sllnvpagkdlpediyvvieipanadpikyeidkesgalfvdrfmstamfypcnygyinh
tlsldgdpvdvlvptpyplqpgsvtrcrpvgvlkmtdeagedaklvavphsklskeydhi
kdvndlpellkaqiahffehykdlekgkwvkvegwenaeaakaeivasferaknk
>d2prd__ 2.38.5.1.4 Inorganic pyrophosphatase {Thermus thermophilus}
anlkslpvgdkapevvhmvievprgsgnkyeydpdlgaikldrvlpgaqfypgdygfips
tlaedgdpldglvlstypllpgvvvevrvvglllmedekggdakvigvvaedqrldhiqd
igdvpegvkqeiqhffetykaleakkgkwvkvtgwrdrkaaleevraciarykg
>d1b3qa2 2.38.6.1.1 (540-671) Histidine kinase CheA, C-terminal domain {Thermotoga maritima}
tlaiicallvkvnnlvyaipianidtilsiskediqrvqdrdvivirgevipvyrlwevl
qiehkeeleemeavivrvgnrkygivvddllgqddivikslgkvfsevkefsgaailgdg
sialiinvsgiv
>d6prch1 2.39.1.1.1 (37-258) Photosynthetic reaction centre {Rhodopseudomonas viridis}
rregyplveplglvklapedgqvyelpypktfvlphggtvtvprrrpetrelklaqtdgf
egaplqptgnplvdavgpasyaeraevvdatvdgkakivplrvatdfsiaegdvdprglp
vvaadgveagtvtdlwvdrsehyfrylelsvagsartaliplgfcdvkkdkivvtsilse
qfanvprlqsrdqitlreedkvsayyaggllyatperaesll
>d1qovh1 2.39.1.1.2 (36-250) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrks
>d1bfg__ 2.40.1.1.1 Basic FGF (fibroblast growth factor 2) {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpmsa
>d2afga_ 2.40.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylamdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1qqka_ 2.40.1.1.4 Keratinocyte growth factor, FGF7 {Rat (Rattus norvegicus)}
dirvrrlfcrtqwylridkrgkvkgtqemrnsynimeirtvavgivaikgveseyylamn
kegklyakkecnedcnfkelilenhyntyasakwthsggemfvalnqkglpvkgkktkke
qktahflpmait
>d1qqla_ 2.40.1.1.4 Keratinocyte growth factor, FGF7 {Rat (Rattus norvegicus)}
dirvrrlfcrtqwylridkrgkvkgtqemrnsynimeirtvavgivaikgveseyylamn
kegklyakqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqk
ailflplpvss
>d1i1b__ 2.40.1.2.1 Interleukin-1beta {Human (Homo sapiens)}
vrslnctlrdsqqkslvmsgpyelkalhlqgqdmeqqvvfsmsfvqgeesndkipvalgl
keknlylscvlkddkptlqlesvdpknypkkkmekrfvfnkieinnklefesaqfpnwyi
stsqaenmpvflggtkggqditdftmqfvss
>d1ilr1_ 2.40.1.2.3 Interleukin-1 receptor antagonist protein {Human (Homo sapiens)}
skmqafriwdvnqktfylrnnqlvagylqgpnvnleekidvvpiephalflgihggkmcl
scvksgdetrlqleavnitdlsenrkqdkrfafirsdsgpttsfesaacpgwflctamea
dqpvsltnmpdegvmvtkfyfqede
>d2ila__ 2.40.1.2.4 Interleukin-1alpha {Human (Homo sapiens)}
nvkynfmriikyefilndalnqsiiranaqyltaaalhnldeavkfdmgayksskddaki
tvilrisktqlyvtaqdedqpvllkempeipktitgsetnllffwethgtknyftsvahp
nlfiatkqdywvclaggppsitdfqile
>d2aaib1 2.40.2.1.1 (1-135) Plant cytotoxin B-chain (lectin) {Castor bean (Ricinus communis), Ricin}
advcmdpepivrivgrnglcvdvrdgrfhngnaiqlwpcksntdanqlwtlkrdntirsn
gkclttygyspgvyvmiydcntaatdatrwqiwdngtiinprsslvlaatsgnsgttltv
qtniyavsqgwlptn
>d2aaib2 2.40.2.1.1 (136-262) Plant cytotoxin B-chain (lectin) {Castor bean (Ricinus communis), Ricin}
ntqpfvttivglyglclqansgqvwiedcssekaeqqwalyadgsirpqqnrdncltsds
niretvvkilscgpassgqrwmfkndgtilnlysglvldvrasdpslkqiilyplhgdpn
qiwlplf
>d1abrb1 2.40.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ivekskicssryeptvriggrdgmcvdvydngyhngnriimwkckdrleenqlwtlksdk
tirsngkclttygyapgsyvmiydctsavaeatyweiwdngtiinpksalvlsaesssmg
gtltvqtneylmrqgwrtgn
>d1abrb2 2.40.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ntspfvtsisgysdlcmqaqgsnvwmadcdsnkkeqqwalytdgsirsvqntnncltskd
hkqgstillmgcsngwasqrwvfkndgsiyslyddmvmdvkgsdpslkqiilwpytgkpn
qiwltlf
>d1jlxa1 2.40.3.1.1 (1-153) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
aglpvimclksnnhqkylryqsdniqqygllqfsadkildplaqfevepsktydglvhik
srytnkylvrwspnhywitasanepdenksnwactlfkplyveegnmkkvrllhvqlghy
tqnytvggsfvsylfaessqidtgskdvfhvid
>d1jlxa2 2.40.3.1.1 (154-299) Agglutinin {Love-lies-bleeding (Amaranthus caudatus)}
wksifqfpkgyvtfkgnngkylgvitinqlpclqfgydnlndpkvahqmfvtsngticik
snymnkfwrlstddwilvdgndpretneaaalfrsdvhdfnvisllnmqktwfikrftsg
kpgfincmnaatqnvdetaileiiel
>d1wba__ 2.40.4.1.1 Winged bean albumin 1 {Goa bean (Psophocarpus tetragonolobus)}
ddpvydaegnklvnrgkytivsfsdgagidvvatgnenpedplsivkstrnimyatsiss
edktppqprnilenmrlkinfatdphkgdvwsvvdfqpdgqqlklagrypnqvkgaftiq
kgsntprtykllfcpvgspcknigistdpegkkrlvvsyqsdplvvkfhrh
>d1tie__ 2.40.4.1.2 Erythrina cafra trypsin inhibitor {Erythrina caffra}
vlldgngevvqnggtyyllpqvwaqgggvqlaktgeetcpltvvqspnelsdgkpiries
rlrsafipdddkvrigfayapkcapspwwtvvedeqeglsvklsedestqfdypfkfeqv
sdqlhsykllycegkhekcasiginrdqkgyrrlvvtedypltvvlkkde
>d4wbca_ 2.40.4.1.3 chymotrypsin inhibitor WCI {Winged bean (Psophocarpus tetragonolobus)}
dddlvdaegnlvenggtyyllphiwahgggietaktgnepcpltvvrspnevskgepiri
ssqflslfiprgslvalgfanppscaaspwwtvvdspqgpavklsqqklpekdilvfkfe
kvshsnihvykllycqhdeedvkcdqyigihrdrngnrrlvvteenplelvllkakseta
>d1avwb_ 2.40.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsefnnyklvfcpqdkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avac_ 2.40.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1a8d_2 2.40.4.2.1 (248-452) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d3btaa2 2.40.4.2.2 (1079-1295) Botulinum neurotoxin serotype A {(Clostridium botulinum)}
nekeikdlydnqsnsgilkdfwgdylqydkpyymlnlydpnkyvdvnnvgirgymylkgp
rgsvmttniylnsslyrgtkfiikkyasgnkdnivrnndrvyinvvvknkeyrlatnasq
agvekilsaleipdvgnlsqvvvmkskndqgitnkckmnlqdnngndigfigfhqfnnia
klvasnwynrqierssrtlgcswefipvddgwgerpl
>d1hcd__ 2.40.5.1.1 Histidine-rich actin-binding protein (hisactophilin) {Dictyostelium discoideum}
mgnrafkshhghflsaegeavkthhghhdhhthfhvenhggkvalkthcgkylsigdhkq
vylshhlhgdhslfhlehhggkvsikghhhhyisadhhghvstkehhdhdttfeeiii
>d1fnc_1 2.41.1.1.1 (19-154) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
hskkmeegitvnkfkpktpyvgrcllntkitgddapgetwhmvfshegeipyregqsvgv
ipdgedkngkphklrlysiassalgdfgdaksvslcvkrliytndagetikgvcsnflcd
lkpgaevkltgpvgke
>d1que_1 2.41.1.1.3 (1-141) Ferredoxin reductase (flavodoxin reductase) {Cyanobacterium (Anabaena), PCC 7119}
tqakakhadvpvnlyrpnapfigkvisneplvkeggigivqhikfdltggnlkyiegqsi
giippgvdkngkpeklrlysiastrhgddvddktislcvrqleykhpesgetvygvcsty
lthiepgsevkitgpvgkeml
>d1fdr_1 2.41.1.1.4 (2-100) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
adwvtgkvtkvqnwtdalfsltvhapvlpftagqftklgleidgervqraysyvnspdnp
dlefylvtvpdgklsprlaalkpgdevqvvseaagffvl
>d1a8p_1 2.41.1.1.5 (2-100) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
snlnvervlsvhhwndtlfsfkttrnpslrfengqfvmiglevdgrplmraysiaspnye
ehleffsikvqngpltsrlqhlkegdelmvsrkptgtlv
>d1qfja1 2.41.1.1.6 (1-97) NAD(P)H:flavin oxidoreductase {Escherichia coli}
ttlsckvtsveaitdtvyrvrivpdaafsfragqylmvvmderdkrpfsmastpdekgfi
elhigaseinlyakavmdrilkdhqivvdiphgeawl
>d1qfjb1 2.41.1.1.6 (1-97) NAD(P)H:flavin oxidoreductase {Escherichia coli}
ttlsckvtsveaitdtvyrvrivpdaafsfragqylmvvmderdkrpfsmastpdekgfi
elhigaseinlyakavmdrilkdhqivvdiphgeawl
>d1qfjc1 2.41.1.1.6 (1-97) NAD(P)H:flavin oxidoreductase {Escherichia coli}
ttlsckvtsveaitdtvyrvrivpdaafsfragqylmvvmderdkrpfsmastpdekgfi
elhigaseinlyakavmdrilkdhqivvdiphgeawl
>d1qfjd1 2.41.1.1.6 (1-97) NAD(P)H:flavin oxidoreductase {Escherichia coli}
ttlsckvtsveaitdtvyrvrivpdaafsfragqylmvvmderdkrpfsmastpdekgfi
elhigaseinlyakavmdrilkdhqivvdiphgeawl
>d2cnd_1 2.41.1.1.7 (11-124) Nitrate reductase core domain {Corn (Zea mays)}
grihcrlvakkelsrdvrlfrfslpspdqvlglpigkhifvcatiegklcmraytptsmv
deighfdllvkvyfknehpkfpngglmtqyldslpvgsyidvkgplghveytgr
>d1ndh_1 2.41.1.1.8 (3-125) cytochrome b5 reductase {Pig (Sus scrofa), liver}
paitlenpdikyplrlidkevvnhdtrrfrfalpspehilglpvgqhiylsaridgnlvi
rpytpvssdddkgfvdlvikvyfkdthpkfpaggkmsqylesmkigdtiefrgpngllvy
qgk
>d2pia_1 2.41.1.2.1 (1-103) Phthalate dioxygenase reductase {Pseudomonas cepacia, db01}
ttpqedgflrlkiaskekiardiwsfeltdpqgaplppfeaganltvavpngsrrtyslc
ndsqernryviavkrdsngrggsisfiddtsegdavevslprn
>d1cqxa2 2.41.1.3.1 (151-261) Flavohemoglobin, central domain {Alcaligenes eutrophus}
wkgwrtfvirekrpesdvitsfilepadggpvvnfepgqytsvaidvpalglqqirqysl
sdmpngrtyrisvkregggpqppgyvsnllhdhvnvgdqvklaapygsfhi
>d1amoa1 2.41.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1axj__ 2.41.1.5.1 FMN-binding protein {Desulfovibrio vulgaris, strain Miyazaki F}
mlpgtffevlknegvvaiatqgedgphlvntwnsylkvldgnrivvpvggmhkteanvar
dervlmtlgsrkvagrngpgtgflirgsaafrtdgpefeaiarfkwaraalvitvvsaeq
tl
>d1ci0a_ 2.41.1.5.2 Pyridoxine 5'-phoshate oxidase (PNP oxidase) {Baker's yeast (Saccharomyces cerevisiae)}
ftlnekqltddpidlftkwfneakedpretlpeaitfssaelpsgrvssrillfkeldhr
gftiysnwgtsrkahdiatnpnaaivffwkdlqrqvrvegitehvnretseryfktrprg
skigawasrqsdviknreeldeltqknterfkdaedipcpdywgglrivpleiefwqgrp
srlhdrfvyrrktendpwkvvrlap
>d1dnla_ 2.41.1.5.3 Pyridoxine 5'-phoshate oxidase (PNP oxidase) {Escherichia coli}
gglrrrdlpadpltlferwlsqaceakladptaxvvatvdehgqpyqrivllkhydekgx
vfytnlgsrkahqiennprvsllfpwhtlerqvxvigkaerlstlevxkyfhsrprdsqi
gawvskqssrisargileskflelkqkfqqgevplpsfwggfrvsleqiefwqggehrlh
drflyqrendawkidrlap
>d1fuia1 2.41.2.1.1 (356-591) L-fucose isomerase, C-terminal domain {Escherichia coli}
aqvfadvrtywspeaiervtghkldglaehgiihlinsgsaaldgsckqrdsegnptmkp
hweisqqeadaclaatewcpaiheyfrgggyssrflteggvpftmtrvniikglgpvlqi
aegwsvelpkdvhdilnkrtnstwpttwfaprltgkgpftdvysvmanwganhgvltigh
vgadfitlasmlripvcmhnveetkvyrpsawaahgmdiegqdyracqnygplykr
>d1dg1g1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1dg1h1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efca1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efcb1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efua1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1efuc1 2.41.3.1.1 (205-296) Elongation factor Tu (EF-Tu), domain 2 {Escherichia coli}
aidkpfllpiedvfsisgrgtvvtgrvergiikvgeeveivgiketqkstctgvemfrkl
ldegragenvgvllrgikreeiergqvlakpg
>d1b23p1 2.41.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus aquaticus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvglllrgvsreevergqvlakpgsitp
>d1aipa1 2.41.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1d2ea1 2.41.3.1.4 (251-348) Elongation factor Tu (EF-Tu), domain 2 {Bovine (Bos taurus), mitochondrial}
trdlekpfllpvesvysipgrgtvvtgtlergilkkgdeceflghsknirtvvtgiemfh
ksldraeagdnlgalvrglkredlrrglvmakpgsiqp
>d1dar_1 2.41.3.1.5 (283-400) Elongation factor G (EF-G), domain II {Thermus thermophilus}
pldippikgttpegevveihpdpngplaalafkimadpyvgrltfirvysgtltsgsyvy
nttkgrkervarllrmhanhreeveelkagdlgavvglketitgdtlvgedaprvile
>d1efca2 2.42.1.1.1 (297-393) Elongation factor Tu (EF-Tu), C-terminal domain {Escherichia coli}
tikphtkfesevyilskdeggrhtpffkgyrpqfyfrttdvtgtielpegvemvmpgdni
kmvvtlihpiamddglrfaireggrtvgagvvakvls
>d1b23p2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1eft_2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1ttta2 2.42.1.1.2 (314-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
tkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftve
likpvaleeglrfaireggrtvgagvvtkile
>d1tttb2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1tttc2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1tuia2 2.42.1.1.2 (314-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
tkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftve
likpvaleeglrfaireggrtvgagvvtkile
>d1tuib2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1tuic2 2.42.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipa2 2.42.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipb2 2.42.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipe2 2.42.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipf2 2.42.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1d2ea2 2.42.1.1.4 (349-451) Elongation factor Tu (EF-Tu), C-terminal domain {Bovine (Bos taurus), mitochondrial}
hqkveaqvyiltkeeggrhkpfvshfmpvmfsltwdmacriilppgkelampgedlkltl
ilrqpmilekgqrftlrdgnrtigtglvtdtpamteedknikw
>d1fmta1 2.43.1.1.1 (207-314) Methionyl-tRNAfmet formyltransferase, C-terminal domain {Escherichia coli}
lskeearidwslsaaqlercirafnpwpmswleiegqpvkvwkasvidtatnaapgtile
ankqgiqvatgdgilnllslqpagkkamsaqdllnsrrewfvpgnrlv
>d1bnka_ 2.43.1.2.1 3-methyladenine DNA glycosylase (AAG, ANPG, MPG) {Human (Homo sapiens)}
kghltrlgleffdqpavplaraflgqvlvrrlpngtelrgriveteaylgpedeaahsrg
grqtprnrgmfmkpgtlyvyiiygmyfcmnissqgdgacvllraleplegletmrhvrsq
lrkgtasrvlkdrelcsgpsklcqalainksfdqrdlaqdeavwlergplepsepavvaa
arvgvghagewarkplrfyvrgspwvsvvdrvaeqd
>d1arb__ 2.44.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1qq4a_ 2.44.1.1.2 alpha-Lytic protease {Lysobacter enzymogenes, 495}
anivggieysinnaslcsvgfsvtrgatkgfvtaghcgtvnatariggavvgtfaarvfp
gndrawvsltsaqtllprvangssfvtvrgsteaavgaavchsgrttgyqcgtitaknvt
anyaegavrgltqsnacmgrgdsggswitsagqaqgvmsggnvqsngnncgipasqrssl
ferlqpilsqyglslvtg
>d1hpga_ 2.44.1.1.4 Glutamic acid-specific protease {Streptomyces griseus}
vlgggaiygggsrcsaafnvtkggaryfvtaghctnisanwsassggsvvgvregtsfpt
ndygivrytdgsspagtvdlyngstqdissaanavvgqaikksgsttkvtsgtvtavnvt
vnygdgpvynmvrttacsaggdsggahfagsvalgihsgssgcsgtagsaihqpvteals
aygvtvy
>d1sgt__ 2.44.1.1.5 Trypsin {Streptomyces griseus, strain k1}
vvggtraaqgefpfmvrlsmgcggalyaqdivltaahcvsgsgnntsitatggvvdlqsg
aavkvrstkvlqapgyngtgkdwaliklaqpinqptlkiatttaynqgtftvagwganre
ggsqqryllkanvpfvsdaacrsaygnelvaneeicagypdtggvdtcqgdsggpmfrkd
nadewiqvgivswgygcarpgypgvytevstfasaiasaartl
>d1sgpe_ 2.44.1.1.7 Protease B {Streptomyces griseus, strain k1}
isggdaiysstgrcslgfnvrsgstyyfltaghctdgattwwansarttvlgttsgssfp
nndygivrytnttipkdgtvggqditsaanatvgmavtrrgsttgthsgsvtalnatvny
gggdvvygmirtnvcaepgdsggplysgtraigltsggsgncssggttffqpvtealvay
gvsvy
>d1agja_ 2.44.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1qtfa_ 2.44.1.1.9 Exfoliative toxin B {Staphylococcus aureus}
keysaeeirklkqkfevpptdkelythitdnarspynsvgtvfvkgstlatgvligknti
vtnyhvareaaknpsniiftpaqnrdaeknefptpygkfeaeeikespygqgldlaiikl
kpnekgesagdliqpanipdhidiakgdkysllgypynysayslyqsqiemfndsqyfgy
tevgnsgsgifnlkgeligihsgkggqhnlpigvffnrkisslysvdntfgdtlgndlkk
rakldk
>d5ptp__ 2.44.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdxggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>e1ept.1a 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyk
>e1ept.1b 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
sriqvrlgehnidvlegneqfinaakiithpnfngntldndimliklsspatlnsrvatv
slprscaaagteclisgwgntk
>e1ept.1c 2.44.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1try__ 2.44.1.2.6 Trypsin(ogen) {Mold (Fusarium oxysporum)}
ivggtsasagdfpfivsisrnggpwcggsllnantvltaahcvsgyaqsgfqiragslsr
tsggitsslssvrvhpsysgnnndlailklstsipsggnigyarlaasgsdpvagssatv
agwgatseggsstpvnllkvtvpivsratcraqygtsaitnqmfcagvssggkdscqgds
ggpivdssntligavswgngcarpnysgvyasvgalrsfidtya
>d1gcta_ 2.44.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglxxivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltryxxantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1azza_ 2.44.1.2.9 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d2hlca_ 2.44.1.2.10 HL collagenase {Common cattle grub (Hypoderma lineatum)}
iingyeaytglfpyqaglditlqdqrrvwcggslidnkwiltaahcvhdavsvvvylgsa
vqyegeavvnseriishsmfnpdtylndvalikiphveytdniqpirlpsgeelnnkfen
iwatvsgwgqsntdtvilqytynlvidndrcaqeyppgiivesticgdtsdgkspcfgds
ggpfvlsdknlligvvsfvsgagcesgkpvgfsrvtsymdwiqqntgikf
>e1a2c.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1a3b.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a3e.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a46.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1a4w.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1a5g.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a61.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1abi.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1abj.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ad8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1ae8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1afe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1aht.1h 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1aht.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1ai8.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1aix.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awh.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.2c 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1ay6.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>e1b5g.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1b7x.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1ba8.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1bb0.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bcu.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bhx.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1ca8.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1d4p.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1dm4.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyi
>e1dwb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwd.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>e1dwe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1fpc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1fph.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hah.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hai.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hao.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hap.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hbt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hgt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hlt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hlt.2j 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1hut.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1hxe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1hxf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e1ihs.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e1iht.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e1lhc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhd.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhe.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhf.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1lhg.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1nrn.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nro.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nrp.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyidgr
>e1nrq.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterelle
>e1nrr.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1nrs.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ppb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1qbv.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1qur.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1tbz.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
cglrplfekksledkterellesyi
>e1thp.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1thr.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1ths.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1tmb.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>e1tmt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1tmu.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>e1tom.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1uma.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1vit.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1vit.2m 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1vr1.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e2hgt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e2hnt.1c 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhs
>e2hnt.1e 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
ekismlekiyihprynwrenldrdialmklkkpvafsdyihpvclpdretaasllqagyk
grvtgwg
>e2hnt.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyid
>e2hpp.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e2hpq.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyid
>e2thf.1a 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>e3hat.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e3htc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
gsgeadcglrplfekksledkterellesyidgr
>e4htc.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
gsgeadcglrplfekksledkterellesyidg
>e4thn.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e5gds.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e7kme.1l 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesy
>e8kme.11 2.44.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1a0h.1a 2.44.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.2d 2.44.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1avg.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
ffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.3m 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bmm.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesy
>e1bmn.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekksledkterellesy
>e1bth.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1bth.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyidg
>e1dit.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
geadcglrplfekksledkterellesyi
>e1etr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ets.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ett.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1hdt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
sgeadcglrplfekksledkterellesyidgr
>e1hrt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1mkw.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>e1mkx.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
eadcglrplfekkqvqdqtekelfesyie
>e1tbq.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbq.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbr.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1tbr.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1toc.1a 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.2c 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.3e 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1toc.4g 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyie
>e1ucy.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ucy.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1ucy.3m 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1uvs.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekksledkterellesyi
>e1uvt.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
cglrplfekkqvqdqtekelfesyi
>e1uvu.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
cglrplfekkqvqdqtekelfesy
>e1ycp.1l 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyieg
>e1ycp.2j 2.44.1.2.12 Thrombin {Bovine (Bos taurus)}
adcglrplfekkqvqdqtekelfesyieg
>d1ppfe_ 2.44.1.2.14 Elastase {Human (Homo sapiens)}
ivggrrarphawpfmvslqlrgghfcgatliapnfvmsaahcvanvnvravrvvlgahnl
srreptrqvfavqrifengydpvnllndivilqlngsatinanvqvaqlpaqgrrlgngv
qclamgwgllgrnrgiasvlqelnvtvvtslcrrsnvctlvrgrqagvcfgdsgsplvcn
glihgiasfvrggcasglypdafapvaqfvnwidsiiq
>d1elt__ 2.44.1.2.16 Elastase {Salmon (Salmo salar)}
vvggrvaqpnswpwqislqyksgssyyhtcggslirqgwvmtaahcvdsartwrvvlgeh
nlntnegkeqimtvnsvfihsgwnsddvaggydiallrlntqaslnsavqlaalppsnqi
lpnnnpcyitgwgktstggplsdslkqawlpsvdhatcsssgwwgstvkttmvcagggan
sgcngdsggplncqvngsyyvhgvtsfvsssgcnaskkptvftrvsayiswmngim
>d1ekbb_ 2.44.1.2.17 Enteropeptidase (enterokinase light chain) {Bovine (Bos taurus)}
ivggsdsregawpwvvalyfddqqvcgaslvsrdwlvsaahcvygrnmepskwkavlglh
masnltspqietrlidqivinphynkrrknndiammhlemkvnytdyiqpiclpeenqvf
ppgricsiagwgaliyqgstadvlqeadvpllsnekcqqqmpeynitenmvcagyeaggv
dscqgdsggplmcqennrwllagvtsfgyqcalpnrpgvyarvprftewiqsflh
>d1a7s__ 2.44.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfpgvstvvlgaydlrrre
rqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveagtrcq
vagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplvcegl
ahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1a0la_ 2.44.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1cgha_ 2.44.1.2.20 Cathepsin G {Human (Homo sapiens)}
iiggresrphsrpymaylqiqspagqsrcggflvredfvltaahcwgsninvtlgahniq
rrentqqhitarrairhpqynqrtiqndimllqlsrrvrrnrnvnpvalpraqeglrpgt
lctvagwgrvsmrrgtdtlrevqlrvqrdrqclrifgsydprrqicvgdrrerkaafkgd
sggpllcnnvahgivsygkssgvppevftrvssflpwirttmrs
>d1danh_ 2.44.1.2.21 Coagulation factor VIIa {Human (Homo sapiens)}
ivggkvcpkgecpwqvlllvngaqlcggtlintiwvvsaahcfdkiknwrnliavlgehd
lsehdgdeqsrrvaqviipstyvpgttnhdiallrlhqpvvltdhvvplclpertfsert
lafvrfslvsgwgqlldrgatalelmvlnvprlmtqdclqqsrkvgdspniteymfcagy
sdgskdsckgdsggphathyrgtwyltgivswgqgcatvghfgvytrvsqyiewlqklmr
seprpgvllrapfp
>e1hia.1a 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e1hia.2x 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e2kai.1a 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e2pka.1a 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>e2pka.1b 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
adgkdyshdlmllrlqspakitdavkvlelptqepelgstceasgwgsiepgpddfefpd
eiqcvqltllqntfcadahpdkvtesmlcagylpggkdtcmgdsggplicngmwqgitsw
ghtpcgsankpsiytklifyldwiddtitenp
>e2pka.2x 2.44.1.2.24 Kallikrein A {Porcine (Sus scrofa)}
iiggreceknshpwqvaiyhyssfqcggvlvnpkwvltaahckndnyevwlgrhnlfene
ntaqffgvtadfphpgfnls
>d1ton__ 2.44.1.2.25 Tonin {Rat (Rattus rattus)}
ivggykceknsqpwqvavineylcggvlidpswvitaahcysnnyqvllgrnnlfkdepf
aqrrlvrqsfrhpdyiplivtndteqpvhdhsndlmllhlsepaditggvkvidlptkep
kvgstclasgwgstnpsemvvshdlqcvnihllsnekcietykdnvtdvmlcagemeggk
dtcagdsggplicdgvlqgitsggatpcakpktpaiyaklikftswikkvmkenp
>d1bio__ 2.44.1.2.27 Factor D {Human (Homo sapiens)}
ilggreaeaharpymasvqlngahlcggvlvaeqwvlsaahcledaadgkvqvllgahsl
sqpepskrlydvlravphpdsqpdtidhdllllqlsekatlgpavrplpwqrvdrdvapg
tlcdvagwgivnhagrrpdslqhvllpvldratcnrrthhdgaiterlmcaesnrrdsck
gdsggplvcggvlegvvtsgsrvcgnrkkpgiytrvasyaawidsvla
>e1rtf.1b 2.44.1.2.28 Two-chain tissue plasminogen activator (TC)-T-PA {Human (Homo sapiens)}
ikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaahcfqerfpphhltv
ilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdssrcaqessvvrtvc
lppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrctsqhllnrtvtdnm
lcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgcgqkdvpgvytkvt
nyldwirdnmrp
>d1bqya_ 2.44.1.2.31 Plasminogen activator from snake venom, TSV-PA {Chinese green tree viper (Trimeresurus stejnejeri)}
vfggdecninehrslvvlfnsngflcggtlinqdwvvtaahcdsnnfqllfgvhskkiln
edeqtrdpkekffcpnrkkddevdkdimlikldssvsnsehiaplslpssppsvgsvcri
mgwgktiptkeiypdvphcaninildhavcrtayswrqvanttlcagilqggrdtchfds
ggplicngifqgivswgghpcgqpgepgvytkvfdyldwiksiiagnkdatcpp
>d1faxa_ 2.44.1.2.33 Coagulation factor Xa (Chrismas factor), protease domain {Human (Homo sapiens)}
ivggqeckdgecpwqallineenegfcggtilsefyiltaahclyqakrfkvrvgdrnta
aeeggeavhevevvikhnrftketydfdiavlrlktpitfrmnvapaclperdwaestlm
tqktgivsgfgrthekgrqstrlkmlevpyvdrnscklsssfiitqnmfcagydtkqeda
cqgdsggphvtrfkdtyfvtgivswgegcarkgkygiytkvtaflkwidrsmktr
>d1autc_ 2.44.1.2.36 Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
lidgkmtrrgdspwqvvlldskkklacgavlihpswvltaahcmdeskkllvrlgeydlr
rwekweldldikevfvhpnysksttdndiallhlaqpatlsqtivpiclpdsglaereln
qagqetlvtgwgyhssrekeakrnrtfvlnfikipvvphnecsevmsnmvsenmlcagil
gdrqdacegdsggpmvasfhgtwflvglvswgegcgllhnygvytkvsryldwihghird
>d1ddja_ 2.44.1.2.41 Plasmin(ogen), catalytic domain {Human (Homo sapiens)}
sfdcgkpqvepkkcpgrvvggcvahphswpwqvslrtrfgmhfcggtlispewvltaahc
leksprpssykvilgahqevnlephvqeievsrlfleptrkdiallklsspavitdkvip
aclpspnyvvadrtecfitgwgetqgtfgagllkeaqlpvienkvcnryeflngrvqste
lcaghlaggtdscqgdaggplvcfekdkyilqgvtswglgcarpnkpgvyvrvsrfvtwi
egvmrnn
>d1svpa_ 2.44.1.3.1 Viral capsid protein {Sindbis virus}
alkleadrlfdvknedgdvighalamegkvmkplhvkgtidhpvlsklkftkssaydmef
aqlpvnmrseaftytsehpegfynwhhgavqysggrftiprgvggrgdagrpimdnsgrv
vaivlggadegtrtalsvvtwnskgktikttpegteewsa
>e1a1r.2d 2.44.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
kgsvvivgrivlsgkpaiipk
>e1jxp.1a 2.44.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
itaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgagsk
tlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgds
rgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>d1befa_ 2.44.1.3.4 NS3 protease {Dengue virus serotype 2}
wdvpspppvgkaeledgayrikqkgilgysqigagvykegtfhtmwhvtrgavlmhkgkr
iepswadvkkdlvscgggwklegewkegeevqvlalepgknpravqtkpglfktnagtig
avsldfspgtsgspiidkkgkvvgiygngvvtrsgayvsaiaqteksiednpeiedd
>d1cqqa_ 2.44.1.4.1 3C cysteine protease (picornain 3C) {Human type 2 rhinovirus}
gpeeefgmslikhnscvittengkftglgvydrfvvvpthadpgkeiqvdgittkvidsy
dlynkngikleitvlkldrnekfrdirryipnneddypncnlallanqpeptiinvgdvv
sygnillsgnqtarmlkysyptksgycggvlykigqvlgihvggngrdgfsamllrsyft
>d1hava_ 2.44.1.4.2 3C cysteine protease (picornain 3C) {Human hepatitis A virus}
stleiaglvrknlvqfgvgekngsvrwvmnalgvkddwllvpshaykfekdyemmefyfn
rggtyysisagnvviqsldvgfqdvvlmkvptipkfrditqhfikkgdvpralnrlatlv
ttvngtpmlisegplkmeekatyvhkkndgttvdltvdqawrgkgeglpgmcggalvssn
qsiqnailgihvaggnsilvaklvtqemfqnidkki
>d1bcma1 2.45.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcmb1 2.45.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bco_1 2.45.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bmfa2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfb2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1bmfc2 2.46.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1bmfd2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmfe2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1bmff2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowa2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowb2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1cowc2 2.46.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1cowd2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowe2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1cowf2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efra2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efrb2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1efrc2 2.46.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1efrd2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efre2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1efrf2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1nbma2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1nbmb2 2.46.1.1.1 (24-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
dleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgndklik
egdivkrtgai
>d1nbmc2 2.46.1.1.1 (19-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
adtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlepdnvgvvvfgn
dklikegdivkrtgai
>d1nbmd2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1nbme2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1nbmf2 2.46.1.1.1 (9-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
ttgrivavigavvdvqfdeglppilnalevqgretrlvlevaqhlgestvrtiamdgteg
lvrgqkvldsgap
>d1maba2 2.46.1.1.2 (10-94) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Rat (Rattus norvegicus)}
ssileerilgadtsvdleetgrvlsigdgiarvhglrnvqaeemvefssglkgmslnlep
dnvgvvvfgndklikegdivkrtgai
>d1mabb2 2.46.1.1.2 (1-81) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Rat (Rattus norvegicus)}
saapkagtatgqivavigavvdvqfdeglppilnalevqgresrlvlevaqhlgestvrt
iamdgteglvrgqkvldsgap
>d1skyb2 2.46.1.1.3 (21-95) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
sqiqvsdvgtviqvgdgiarahgldnvmsgeavefanavmgmalnleennvgivilgpyt
gikegdevrrtgrim
>d1skye2 2.46.1.1.3 (1-82) N-terminal domain of alpha and beta subunits of F1 ATP synthase {Bacillus ps3}
mtrgrviqvmgpvvdvkfenghlpaiynalkiqhkarnenevdidltlevalhlgddtvr
tiamastdglirgmevidtgap
>d1bd0a1 2.46.2.1.1 (2-11,245-382) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnaig
>d7odca1 2.46.2.1.2 (2-43,284-418) Eukaryotic ornithine decarboxylase {Mouse (Mus musculus)}
ssftkdefdchildegftakdildqkinevsssddkdafyvaXftlavniiakktvwkeq
pgsddedesneqtfmyyvndgvygsfncilydhahvkallqkrpkpdekyysssiwgptc
dgldrivercnlpemhvgdwmlfenmgaytvaaastfngfqrpniyyvmsrpmwqlmk
>d2toda1 2.46.2.1.3 (37-43,284-410) Eukaryotic ornithine decarboxylase {Trypanosoma brucei}
gdpffvaXftlavnviakkvtpgvqtdvgahaesnaqsfmyyvndgvygsfncilydhav
vrplpqrepipneklypssvwgptcdgldqiveryylpemqvgewllfedmgaytvvgts
sfngfqsptiyyvvs
>d1a94a_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1bdqa_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmvggiggfikvrqyd
qilieicghkaigtvlvgptpiniigrnlltqigctlnf
>d1difa_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1mtra_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtiriggqlkealldtgaddtvieemnlpgkwkpkmiggiggfikvrqyd
qipveixghkaigtvlvgptpvniigrnlltqigxtlnf
>d1qbsa_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqvtlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieixghkaigtvlvgptpvniigrnlltqigatlnf
>d2hvp__ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
wqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqydqilie
icghkaigtvlvgptpvniigrnlltqigctlnf
>d3upjb_ 2.47.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
fslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintleyknv
eievlnkkvratimtgdtpinifgrniltalgmslnl
>d4fiv__ 2.47.1.1.2 Feline immunodeficiency virus (FIV) protease {Feline (Felis catus), immunodeficiency virus}
vgttttlekrpeilifvngypikflldtgaditilnrrdfqvknsiengrqnmigvgggk
rgtnyinvhleirdenyktqcifgnvcvlednsliqpllgrdnmikfnirlvm
>d1idaa_ 2.47.1.1.3 Human immunodeficiency virus type 2 protease {Rod isolate, HIV-2}
pqfslwkrpvvtayiegqpvevlldtgaddsivagielgnnyspkivggiggfintkeyk
nveievlnkkvratimtgdtpinifgrniltalgmslnl
>d2rspa_ 2.47.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldsgaditiiseedwptdwpvmeaa
npqihgigggipmrksrdmielgvinrdgslerplllfpavamvrgsilgrdclqglglr
ltnl
>d1az5__ 2.47.1.1.6 Simian immunodeficiency virus (SIV) protease {Simian immunodeficiency virus, Mac251 isolate}
pqfhlwkrpvvtahiegqpvevlldtgaddsivtgielgphytpkivggiggfintkeyk
nvevevlgkrikgtimtgdtpinifgrnlltalgmslnf
>d1siva_ 2.47.1.1.6 Simian immunodeficiency virus (SIV) protease {Simian immunodeficiency virus, Mac251 isolate}
pqfslwrrpvvtahiegqpvevlldtgaddsivtgielgphytpkivggiggfintkeyk
nvkievlgkrikgtimtgdtpinifgrnlltalgmslnl
>d1fmb__ 2.47.1.1.7 EIAV protease {Equine infection anemia virus, EIAV}
vtynlekrpttivlindtplnvlldtgadtsvlttahynrlkyrgrkyqgtgiggvggnv
etfstpvtikkkgrhiktrmlvadipvtilgrdilqdlgaklvl
>d1bxoa_ 2.47.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d2apr__ 2.47.1.2.3 Acid protease {Bread mold (Rhizopus chinensis)}
agvgtvpmtdygndieyygqvtigtpgkkfnldfdtgssdlwiastlctncgsgqtkydp
nqsstyqadgrtwsisygdgssasgilakdnvnlggllikgqtielakreaasfasgpnd
gllglgfdtittvrgvktpmdnlisqglisrpifgvylgkaknggggeyifggydstkfk
gslttvpidnsrgwwgitvdratvgtstvassfdgildtgttllilpnniaasvarayga
sdngdgtytiscdtsafkplvfsingasfqvspdslvfeefqgqciagfgygnwgfaiig
dtflknnyvvfnqgvpevqiapvae
>d1eaga_ 2.47.1.2.5 Acid protease {Yeast (Candida albicans)}
qavpvtlhneqvtyaaditvgsnnqklnvivdtgssdlwvpdvnvdcqvtysdqtadfck
qkgtydpsgssasqdlntpfkigygdgsssqgtlykdtvgfggvsiknqvladvdstsid
qgilgvgyktneaggsydnvpvtlkkqgviaknayslylnspdaatgqiifggvdnakys
gslialpvtsdrelrislgsvevsgktintdnvdvlldsgttitylqqdladqiikafng
kltqdsngnsfyevdcnlsgdvvfnfsknakisvpasefaaslqgddgqpydkcqllfdv
ndanilgdnflrsayivydlddneislaqvkytsassisalt
>e1b5f.1b 2.47.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>e1b5f.2d 2.47.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>d2psg__ 2.47.1.2.9 Pepsin(ogen) {Pig (Sus scrofa)}
lvkvplvrkkslrqnlikdgklkdflkthkhnpaskyfpeaaaligdeplenyldteyfg
tigigtpaqdftvifdtgssnlwvpsvycsslacsdhnqfnpddsstfeats
>e1avf.1p 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekg
>e1avf.2q 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgl
>e1htr.1b 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
svtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpse
sstystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgi
mglaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqi
ywapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaq
edeygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqp
lwilgdvflrsyysvydlgnnrvgfataa
>e1htr.1p 2.47.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgllgeflrthkydpawkyrfgdl
>d1mpp__ 2.47.1.2.13 Pepsin {Mucor pusillus}
gsvdtpglydfdleeyaipvsigtpgqdfyllfdtgssdtwvphkgcdnsegcvgkrffd
psssstfketdynlnitygtggangiyfrdsitvggatvkqqtlayvdnvsgptaeqspd
selfldgifgaaypdntameaeygdtyntvhvnlykqglisspvfsvymntndgggqvvf
ggvnntllggdiqytdvlksrggyffwdapvtgvkidgsdavsfdgaqaftidtgtnffi
apssfaekvvkaalpdatesqqgytvpcskyqdskttfslvlqksgsssdtidvsvpisk
mllpvdksgetcmfivlpdggnqfivgnlflrffvnvydfgknrigfaplasgyend
>e1lyb.1a 2.47.1.2.14 Cathepsin D {Human (Homo sapiens)}
gpipevlknymdaqyygeigigtppqcftvvfdtgssnlwvpsihcklldiacwihhkyn
sdksstyvkngtsfdihygsgslsgylsqdtvsvpcq
>e1lyb.1b 2.47.1.2.14 Cathepsin D {Human (Homo sapiens)}
ggvkverqvfgeatkqpgitfiaakfdgilgmayprisvnnvlpvfdnlmqqklvdqnif
sfylsrdpdaqpggelmlggtdskyykgslsylnvtrkaywqvhldqvevasgltlckeg
ceaivdtgtslmvgpvdevrelqkaigavpliqgeymipcekvstlpaitlklggkgykl
spedytlkvsqagktlclsgfmgmdipppsgplwilgdvfigryytvfdrdnnrvgfaea
a
>d1pfza_ 2.47.1.2.18 Plasmepsin ii (a hemoglobin-degrading enzyme) {Plasmodium falciparum}
hltigfkvenahdrilktikthklknyikesvnflnsgltktnylgssndnielvdfqni
mfygdaevgdnqqpftfildtgsanlwvpsvkcttagcltkhlydssksrtyekdgtkve
mnyvsgtvsgffskdlvtvgnlslpykfievidtngfeptytastfdgilglgwkdlsig
svdpivvelknqnkienalftfylpvhdkhtgfltiggieerfyegpltyeklnhdlywq
itldahvgnimlekancivdsgtsaitvptdflnkmlqnldvikvpflpfyvtlcnnskl
ptfeftsengkytlepeyylqhiedvgpglcmlniigldfpvptfilgdpfmrkyftvfd
ydnhsvgialakknl
>d1ile_2 2.48.1.1.1 (198-386) Isoleucyl-tRNA synthetase (IleRS) editing domain {Thermus thermophilus}
keiqdpsvyvrfplkepkklglekaslliwtttpwtlpgnvaaavhpeytyaafqvgdea
lileeglgrkllgegtqvlktfpgkaleglpytppypqalekgyfvvladyvsqedgtgi
vhqapafgaedletarvyglpllktvdeegkllvepfkglyfreanrailrdlrgrgllf
keesylhsy
>d1qu2a2 2.48.1.1.2 (201-394) Isoleucyl-tRNA synthetase (IleRS) editing domain {Staphylococcus aureus}
hdkrsasiyvafnvkddkgvvdadakfiiwtttpwtipsnvaitvhpelkygqynvngek
yiiaealsdavaealdwdkasiklekeytgkelewvvaqhpfldreslvingdhvttdag
tgcvhtapghgeddyivgqqyelpvispiddkgvfteeggqfegmfydkankavtdllte
kgallkldfithsy
>d2eng__ 2.49.1.1.1 Endoglucanase V {Humicola insolens}
adgrstrywdcckpscgwakkapvnqpvfscnanfqritdfdaksgcepggvayscadqt
pwavnddfalgfaatsiagsneagwccacyeltftsgpvagkkmvvqststggdlgsnhf
dlnipgggvgifdgctpqfgglpgqryggissrnecdrfpdalkpgcywrfdwfknadnp
sfsfrqvqcpaelvartgcrrnddgnfpav
>d1bw3__ 2.49.1.2.1 Barwin {Barley (Hordeum vulgare)}
eqandvratyhyyrpaqnnwdlgapavsaycatwdaskplswrskygwtafcgpagprgq
aacgkclrvtnpatgaqitarivdqcanggldldwdtvftkidtngigyqqghlnvnyqf
vdcrd
>e1aw8.1a 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.1b 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>e1aw8.2d 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.2e 2.49.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>d1dmr_1 2.49.2.2.2 (626-781) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
erldgpgakyplhiaashpfnrlhsqlngtvlregyavqghepclmhpddaaargiadgd
vvrvhndrgqiltgvkvtdavmkgviqiyeggwydpsdvtepgtldkygdvnvlsadigt
sklaqgncgqtvlaevekytgpavtltgfvapkaae
>d1aa6_1 2.49.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1tmo_1 2.49.2.2.4 (632-798) Trimethylamine N-oxide reductase {Shewanella massilia}
ershggpgsdkhpiwlqschpdkrlhsqmcesreyretyavngrepvyispvdakargik
dgdivrvfndrgqllagavvsdnfpkgivrihegawygpvgkdgsteggaevgalcsygd
pntltldigtsklaqacsaytclvefekyqgkvpkvssfdgpievei
>d2napa1 2.49.2.2.5 (601-723) Dissimilatory nitrate reductase (NAP) {Desulfovibrio desulfuricans}
aaeepdaeyplyltsmrvidhwhtatmtgkvpelqkanpiafveineedaartgikhgds
vivetrrdamelparvsdvcrpgliavpffdpkklvnklfldatdpvsrepeykicaarv
rka
>d1qcsa1 2.49.2.3.1 (2-85) N-terminal domain of NSF-N, NSF-Nn {Hamster (Cricetulus griseus)}
agrsxqaarcptdelslsncavvsekdyqsgqhvivrtspnhkyiftlrthpsvvpgsva
fslpqrkwaglsigqeievalysf
>d1qdna1 2.49.2.3.1 (1-85) N-terminal domain of NSF-N, NSF-Nn {Hamster (Cricetulus griseus)}
magrsmqaarcptdelslsncavvsekdyqsgqhvivrtspnhkyiftlrthpsvvpgsv
afslpqrkwaglsigqeievalysf
>d1qdnb1 2.49.2.3.1 (1-85) N-terminal domain of NSF-N, NSF-Nn {Hamster (Cricetulus griseus)}
magrsmqaarcptdelslsncavvsekdyqsgqhvivrtspnhkyiftlrthpsvvpgsv
afslpqrkwaglsigqeievalysf
>d1qdnc1 2.49.2.3.1 (1-85) N-terminal domain of NSF-N, NSF-Nn {Hamster (Cricetulus griseus)}
magrsmqaarcptdelslsncavvsekdyqsgqhvivrtspnhkyiftlrthpsvvpgsv
afslpqrkwaglsigqeievalysf
>d1cr5a1 2.49.2.3.2 (26-107) N-terminal domain of NSF-N, NSF-Nn {Baker's yeast (Saccharomyces cerevisiae), sec18p}
trhlkvsncpnnsyalanvaavspndfpnniyiiidnlfvfttrhsndippgtigfngnq
rtwggwslnqdvqakafdlfky
>d1cr5b1 2.49.2.3.2 (23-107) N-terminal domain of NSF-N, NSF-Nn {Baker's yeast (Saccharomyces cerevisiae), sec18p}
dtrtrhlkvsncpnnsyalanvaavspndfpnniyiiidnlfvfttrhsndippgtigfn
gnqrtwggwslnqdvqakafdlfky
>d1cr5c1 2.49.2.3.2 (26-107) N-terminal domain of NSF-N, NSF-Nn {Baker's yeast (Saccharomyces cerevisiae), sec18p}
trhlkvsncpnnsyalanvaavspndfpnniyiiidnlfvfttrhsndippgtigfngnq
rtwggwslnqdvqakafdlfky
>d1cz4a1 2.49.2.3.3 (1-91) N-terminal domain of VAT-N, VAT-Nn {Thermoplasma acidophilum}
mesnngiilrvaeanstdpgmsrvrldessrrlldaeigdvveiekvrktvgrvyrarpe
denkgivridsvmrnncgasigdkvkvrkvr
>d1cz5a1 2.49.2.3.3 (1-91) N-terminal domain of VAT-N, VAT-Nn {Thermoplasma acidophilum}
mesnngiilrvaeanstdpgmsrvrldessrrlldaeigdvveiekvrktvgrvyrarpe
denkgivridsvmrnncgasigdkvkvrkvr
>d1b75a_ 2.50.1.1.1 Ribosomal protein L25 {Escherichia coli}
mftinaevrkeqgkgasrrlraankfpaiiyggkeaplaieldhdkvmnmqakaefysev
ltivvdgkeikvkaqdvqrhpykpklqhidfvra
>d1d6ka_ 2.50.1.1.1 Ribosomal protein L25 {Escherichia coli}
mftinaevrkeqgkgasrrlraankfpaiiyggkeaplaieldhdkvmnmqakaefysev
ltivvdgkeikvkaqdvqrhpykpklqhidfvra
>d1dfup_ 2.50.1.1.1 Ribosomal protein L25 {Escherichia coli}
mftinaevrkeqgkgasrrlraankfpaiiyggkeaplaieldhdkvmnmqakaefysev
ltivvdgkeikvkaqdvqrhpykpklqhidfvra
>d1gtra1 2.50.1.2.1 (339-547) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain {Escherichia coli}
apramavidpvklvienyqgegemvtmpnhpnkpemgsrqvpfsgeiwidradfreeank
qykrlvlgkevrlrnayvikaervekdaegnittifctydadtlskdpadgrkvkgvihw
vsaahalpveirlydrlfsvpnpgaaddflsvinpeslvikqgfaepslkdavagkafqf
eregyfcldsrhstaekpvfnrtvglrdt
>d1cl3a_ 2.51.1.1.1 Core binding factor beta {Human (Homo sapiens) |A|}
vvpdqrskfeneeffrklsreceikytgfrdrpheerqtrfqnacrdgrseiafvatgtn
lslqffpaswqgeqrqtpsreyvdlereagkvylkapmilngvcviwkgwidlhrldgmg
clefdeeraqqedalaqq
>d1mai__ 2.52.1.1.1 Phospholipase C delta-1 {Rat (Rattus norvegicus)}
glqddpdlqallkgsqllkvkssswrrerfyklqedcktiwqesrkvmrspesqlfsied
iqevrmghrteglekfardipedrcfsivfkdqrntldliapspadaqhwvqglrkiih
>d1btn__ 2.52.1.1.2 beta-spectrin {Mouse (Mus musculus), brain}
megflnrkheweahnkkassrswhnvycvinnqemgfykdaksaasgipyhsevpvslke
aicevaldykkkkhvfklrlsdgneylfqakddeemntwiqaissa
>d1dro__ 2.52.1.1.3 beta-spectrin {Fruit fly (Drosophila melanogaster)}
gsgtgageghegyvtrkhewdsttkkasnrswdkvymaakagrisfykdqkgyksnpelt
frgepsydlqnaaieiasdytkkkhvlrvklangalfllqahddtemsqwvtslkaqsds
ta
>d1dyna_ 2.52.1.1.4 Dynamin {Human (Homo sapiens)}
ilvirkgwltinnigimkggskeywfvltaenlswykddeekekkymlsvdnlklrdvek
gfmsskhifalfnteqrnvykdyrqlelacetqeevdswkasflragvyperv
>d1btka_ 2.52.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkclflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1pls__ 2.52.1.1.6 Pleckstrin, N-terminal domain {Human (Homo sapiens)}
mepkriregylvkkgsvfntwkpmwvvlledgiefykkksdnspkgmiplkgstltspcq
dfgkrmfvfkitttkqqdhffqaafleerdawvrdinkaikcieglehhhhhh
>d1dbha2 2.52.1.1.8 (418-550) Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
aikkxneiqknidgwegkdigqccnefixegtltrvgakherhiflfdglxiccksnhgq
prlpgasnaeyrlkekffxrkvqindkddtneykhafeiilkdensvifsaksaeeknnw
xaalislqyrstl
>d1bak__ 2.52.1.1.9 G-protein coupled receptor kinase 2 (beta-adrenergic receptor kinase 1) {Human (Homo sapiens)}
gshmgkdcimhgymskmgnpfltqwqrryfylfpnrlewrgegeapqslltmeeiqsvee
tqikerkclllkirggkqfilqcdsdpelvqwkkelrdayreaqqlvqrvpkmknkprs
>d1aqca_ 2.52.1.2.1 X11 {Human (Homo sapiens)}
edlidgiifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesq
pxtevdlfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenv
eashpsqdgkrqykxichvfesedaqliaqsigqafsvayqeflr
>d1qqga1 2.52.1.2.2 (12-114) Insulin receptor substrate 1, IRS-1 {Human (Homo sapiens)}
dvrkvgylrkpksmhkrffvlraaseaggparleyyenekkwrhkssapkrsiplescfn
inkradsknkhlvalytrdehfaiaadseaeqdswyqallqlh
>d1qqga2 2.52.1.2.2 (159-262) Insulin receptor substrate 1, IRS-1 {Human (Homo sapiens)}
afkevwqvilkpkglgqtknligiyrlcltsktisfvklnseaaavvlqlmnirrcghse
nfffievgrsavtgpgefwmqvddsvvaqnmhetileamramsd
>d1shca_ 2.52.1.2.3 Shc adaptor protein {Human (Homo sapiens)}
gshmgqlggeewtrhgsfvnkptrgwlhpndkvmgpgvsylvrymgcvevlqsmraldfn
trtqvtreaislvceavpgakgatrrrkpcsrplssilgrsnlkfagmpitltvstssln
lmaadckqiianhhmqsisfasggdpdtaeyvayvakdpvnqrachilecpeglaqdvis
tigqafelrfkqylr
>d2nmba_ 2.52.1.2.4 Numb {Fruit fly (Drosophila melanogaster)}
skphqwqadeeavrsatcsfsvkylgcvevfesrgmqvceealkvlrqsrrrpvrgllhv
sgdglrvvddetkglivdqtiekvsfcapdrnhergfsyicrdgttrrwmchgflackds
gerlshavgcafavclerkqrrtraaa
>d1rrpb_ 2.52.1.3.1 Ran-binding domain of nuclear pore complex protein Nup358 {Human (Homo sapiens)}
hfepvvplpdkievktgeedeeeffcnraklfrfdveskewkergignvkilrhktsgki
rllmrreqvlkicanhyispdmkltpnagsdrsfvwhaldyadelpkpeqlairfktpee
aalfkckfeeaqsi
>d1evha_ 2.52.1.4.1 Enabled {Mouse (Mus musculus)}
seqsicqaraavmvyddankkwvpaggstgfsrvhiyhhtgnntfrvvgrkiqdhqvvin
caipkglkynqatqtfhqwrdarqvyglnfgskedanvfasammhalevln
>d1qc6a_ 2.52.1.4.2 Ena/vasp-like protein {Mouse (Mus musculus)}
seqsicqarasvxvyddtskkwvpikpgqqgfsriniyhntasstfrvvgvklqdqqvvi
nysivkglkynqatptfhqwrdarqvyglnfaskeeattfsnaxlfalnixn
>d1ytfc1 2.53.1.1.1 Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
enlmlclydkvtrtkarwkcslkdgvvtinrndytfqkaqveaewv
>d1ytfd2 2.53.1.1.1 (55-119) Transcription factor IIA (TFIIA), N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
ntqskltvkgnldtygfcddvwtfivkncqvtvedshrdasqngsgdsqsvisvdklriv
acnsk
>d1wpoa_ 2.54.1.1.1 Human cytomegalovirus protease {Human cytomegalovirus, hCMV}
qavapvyvggflarydqspdeaelllprdvvehwlhaqgqgqpslsvalplninhddtav
vghvaaxqsvrdglfclgcvtsprfleivrrasekselvsrgpvsplqpdkvveflsgsy
aglslssrrcddveaatslsgsettpfkhvalcsvgrrrgtlavygrdpewvxqrfpdlt
aadrdglraqwqrcgstavdasgdpfrsdsygllgnsvdaxyirerlpklrydkqlvgvt
eresyvka
>d1at3a_ 2.54.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1a49a1 2.55.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1pkm_1 2.55.1.1.2 (116-217) Pyruvate kinase {Cat (Felis domestica)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenvlwldyknickvvevgskvyv
ddglisllvkekgadflvtevenggslgskkgvnlpgaavdl
>d1pkla1 2.55.1.1.3 (88-186) Pyruvate kinase {Leishmania mexicana}
eirtgqfvggdavmergatcyvttdpafadkgtkdkfyidyqnlskvvrpgnyiyiddgi
lilqvqshedeqtlectvtnshtisdrrgvnlpgcdvdl
>d1a3wa1 2.55.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1pkya1 2.55.1.1.5 (70-167) Pyruvate kinase {Escherichia coli}
peirtmkleggndvslkagqtftfttdksvignsemvavtyegfttdlsvgntvlvddgl
igmevtaiegnkvickvlnngdlgenkgvnlpgvsial
>d1pkyb1 2.55.1.1.5 (70-167) Pyruvate kinase {Escherichia coli}
peirtmkleggndvslkagqtftfttdksvignsemvavtyegfttdlsvgntvlvddgl
igmevtaiegnkvickvlnngdlgenkgvnlpgvsial
>d1pkyc1 2.55.1.1.5 (70-167) Pyruvate kinase {Escherichia coli}
peirtmkleggndvslkagqtftfttdksvignsemvavtyegfttdlsvgntvlvddgl
igmevtaiegnkvickvlnngdlgenkgvnlpgvsial
>d1pkyd1 2.55.1.1.5 (70-167) Pyruvate kinase {Escherichia coli}
peirtmkleggndvslkagqtftfttdksvignsemvavtyegfttdlsvgntvlvddgl
igmevtaiegnkvickvlnngdlgenkgvnlpgvsial
>d1aqb__ 2.56.1.1.2 Retinol binding protein {Pig (Sus scrofa domestica)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdydtyavqysc
rlqnldgtcadsysfvfardphgfspevqkivrqrqeelclarqyriithngycd
>d1obpa_ 2.56.1.1.5 Odorant-binding protein {Bovine (Bos taurus)}
qeeeaeqnlselsgpwrtvyigstnpekiqengpfrtyfrelvfddekgtvdfyfsvkrd
gkwknvhvkatkqddgtyvadyegqnvfkivslsrthlvahninvdkhgqtteltglfvk
lnvededlekfwkltedkgidkknvvnflenedhphpe
>d1a3ya_ 2.56.1.1.6 Odorant-binding protein {Pig (Sus scrofa)}
pfelsgkwitsyigssdlekigenapfqvfmrsiefddkeskvylnffskengiceefsl
igtkqegntydvnyagnnkfvvsyasetaliisninvdeegdktimtgllgkgtdiedqd
lekfkevtrengipeenivniierddcpa
>d1bj7__ 2.56.1.1.7 Lipocalin allergen {Bovine (Bos taurus), bos d 2}
idpskipgewriiyaaadnkdkiveggplrnyyrriecindceslsitfylkdqgtclll
tevakrqegyvyvlefygtntlevihvsenmlvtyvenydgeritkmteglakgtsftpe
elekyqqlnsergvpnenienliktdncpp
>d1beba_ 2.56.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1epba_ 2.56.1.1.9 Retinoic acid-binding protein {Rat (Rattus norvegicus), albino}
vkdfdiskflgfwyeiafaskmgtpglahkeekmgamvvelkenllaltttyysedhcvl
ekvtategdgpakfqvtrlsgkkevvveatdyltyaiiditslvagavhrtmklysrsld
dngealynfrkitsdhgfsetdlyilkhdltcvkvlqsaa
>d1mup__ 2.56.1.1.10 Major urinary protein/alpha-2u-globulin {Mouse (Mus musculus)}
eeasstgrnfnvekingewhtiilasdkrekiedngnfrlfleqihvlenslvlkfhtvr
deecselsmvadktekageysvtydgfntftipktdydnflmahlinekdgetfqlmgly
grepdlssdikerfaqlceehgilreniidlsnanrc
>d1ngla_ 2.56.1.1.12 Neutrophil gelatinase-associated lipocalin (NGAL) {Human (Homo sapiens)}
mqdstsdlipapplskvplqqnfqdnqfqgkwyvvglagnailredkdpqkmyatiyelk
edksynvtsvlfrkkkcdywirtfvpgcqpgeftlgniksypgltsylvrvvstnynqha
mvffkkvsqnreyfkitlygrtkeltselkenfirfskslglpenhivfpvpidqcidg
>d1bbpa_ 2.56.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1np4a_ 2.56.1.1.15 Nitrophorin 4 {Rhodnius prolixus}
actknaiaqtgfnkdkyfngdvwyvtdyldlepddvpkrycaalaagtasgklkealyhy
dpktqdtfydvselqveslgkytanfkkvdkngnvkvavtagnyytftvmyaddssalih
tclhkgnkdlgdlyavlnrnkdaaagdkvksavsaatlefskfistkenncaydndslks
lltk
>d1hms__ 2.56.1.2.1 Muscle fatty acid binding protein (m-fabp) {Human (Homo sapiens)}
vdaflgtwklvdsknfddymkslgvgfatrqvasmtkpttiiekngdiltlkthstfknt
eisfklgvefdettaddrkvksivtldggklvhlqkwdgqettlvrelidgkliltlthg
tavctrtyeke
>d1ifc__ 2.56.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1b56__ 2.56.1.2.5 Epidermal fatty acid binding protein {Human (Homo sapiens)}
tvqqlegrwrlvdskgfdeymkelgvgialrkmgamakpdciitcdgknltiktestlkt
tqfsctlgekfeettadgrktqtvcnftdgalvqhqewdgkestitrklkdgklvvecvm
nnvtctriyekve
>d1lid__ 2.56.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1mdc__ 2.56.1.2.7 Fatty acid-binding protein {Tobacco hornworm (Manduca sexta)}
xsylgkvyslvkqenfdgflksaglsddkiqalvsdkptqkmeangdsysntstggggak
tvsfksgvefddvigagdsvksmytvdgnvvthvvkgdagvatfkkeyngddlvvtitss
nwdgvarryyka
>d1ftpa_ 2.56.1.2.8 Fatty acid-binding protein {Desert locust (Schistocerca gregaria)}
vkefagikykldsqtnfeeymkaigvgaierkaglalspvieleildgdkfkltsktaik
nteftfklgeefdeetldgrkvkstitqdgpnklvheqkgdhptiiirefskeqcvitik
lgdlvatriykaq
>d1cbs__ 2.56.1.2.9 Cellular retinoic-acid-binding protein (CRABP) {Human (Homo sapiens), CRABP-II}
pnfsgnwkiirsenfeellkvlgvnvmlrkiavaaaskpaveikqegdtfyiktsttvrt
teinfkvgeefeeqtvdgrpckslvkwesenkmvceqkllkgegpktswtreltndgeli
ltmtaddvvctrvyvre
>d1crb__ 2.56.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
pvdfngywkmlsnenfeeylraldvnvalrkianllkpdkeivqdgdhmiirtlstfrny
imdfqvgkefeedltgiddrkcmttvswdgdklqcvqkgekegrgwtqwiegdelhlemr
aegvtckqvfkkvh
>d1opaa_ 2.56.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
tkdqngtwemesnenfegymkaldidfatrkiavrltqtkiivqdgdnfktktnstfrny
dldftvgvefdehtkgldgrnvktlvtwegntlvcvqkgekenrgwkqwvegdklylelt
cgdqvcrqvfkkk
>d1lfo__ 2.56.1.2.12 Liver fatty acid binding protein {Rat (Rattus norvegicus)}
mnfsgkyqvqsqenfepfmkamglpedliqkgkdikgvseivhegkkvkltitygskvih
neftlgeexeletmtgekvkavvkmegdnkmvttfkgiksvtefngdtitntmtlgdivy
krvskri
>d1pmpa_ 2.56.1.2.13 P2 myelin protein {Bovine (Bos taurus), caudal spinal root myelin}
snkflgtwklvssenfdeymkalgvglatrklgnlakprviiskkgdiitirtespfknt
eisfklgqefeettadnrktkstvtlargslnqvqkwngnettikrklvdgkmvveckmk
dvvctriyekv
>d1eal__ 2.56.1.2.14 Ileal lipid binding protein {Pig (Sus scrofa)}
aftgkyeieseknydefmkrlalpsdaidkarnlkiisevkqdgqnftwsqqypgghsit
ntftigkecdietiggkkfkatvqmeggkvvvnspnyhhtaeivdgklvevstvggvsye
rvskkla
>d1avgi_ 2.56.1.3.1 Thrombin inhibitor {Triatomine bug (Triatoma pallidipennis)}
aegddcsiekamgdfkpeeffngtwylahgpgvtspavcqkfttsgskgftqiveigynk
fesnvkfqcnqvdnkngeqysfkckssdntefeadftfisvsydnfalvcrsitftsqpk
edrylvfertksdtdpdakeic
>d1swga_ 2.57.1.1.1 Streptavidin {Streptomyces avidinii}
sryvltgrydsapatdgsgtalgwtvawknnyrnahsattwsgqyvggaearintqwllt
sgtteanawkstlvghdtftkvkpsaasgggsaeagitgtwynqlgstfivtagadgalt
gtyesa
>d1swua_ 2.57.1.1.1 Streptavidin {Streptomyces avidinii}
gitgtwynqlgstfivtagadgaltgtfesavgnaesryvltgrydsapatdgsgtalgw
tvawknnyrnahsattwsgqyvggaearintqwlltsgtteanawkstlvghdtftkvkp
>d2cama_ 2.57.1.1.2 Avidin {Chicken (Gallus gallus)}
recsltgewtndlgsnmtigavnsdgeftgtyitavtatsneikesplhgtentinkrtq
ptfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginift
rllt
>d1smpi_ 2.57.2.1.1 Metalloprotease inhibitor {Erwinia chrysanthemi}
sslrlpsaaelsgqwvlsgaeqhcdirlntdvldgttwklagdtaclqkllpeapvgwrp
tpdgltltqadgsavaffsrnrdryehklvdgsvrtlkkk
>d2cpl__ 2.58.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d2rmca_ 2.58.1.1.3 Cyclophilin (eukaryotic) {Mouse (Mus musculus), variant C}
krgpsvtdkvffdvrigdkdvgriviglfgnvvpktvenfvalatgekgygykgsifhrv
ikdfmiqggdftardgtggmsiygetfpdenfklkhygigwvsmanagpdtngsqffitl
tkptwldgkhvvfgkvldgmtvvhsielqatdghdrpltdctivnsgkidvktpfvvevp
dw
>d1a33__ 2.58.1.1.4 Cyclophilin (eukaryotic) {Nematode (Brugia malayi)}
kdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhykgst
fhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntngsqf
fitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1clh__ 2.58.1.1.5 Bacterial cyclophilin {Escherichia coli}
akgdphvllttsagnieleldkqkapvsvqnfvdyvnsgfynnttfhrvipgfmiqgggf
teqmqqkkpnppikneadnglrntrgtiamartadkdsatsqffinvadnafldhgqrdf
gyavfgkvvkgmdvadkisqvpthdvgpyqnvpskpvvilsakvlp
>d1lopa_ 2.58.1.1.5 Bacterial cyclophilin {Escherichia coli}
mvtfhtnhgdiviktfddkapetvknfldycregfynntifhrvingfmiqgggfepgmk
qkatkepikneannglkntrgtlamartqaphsataqffinvvdndflnfsgeslqgwgy
cvfaevvdgmdevdkikgvatgrsgmhqdvpkedviiesvtvse
>d1jsg__ 2.59.1.1.1 p14-TCL1 {Human (Homo sapiens)}
cptlgeavtdhpdrlwawekfvyldekqhawlpltieikdrlqlrvllrredvvlgrpmt
ptqigpsllpimwqlypdgryrssdssfwrlvyhikidgvedmllellpdd
>d1a1x__ 2.59.1.1.2 MTCP-1 {Human (Homo sapiens)}
agedvgappdhlwvhqegiyrdeyqrtwvavveeetsflrarvqqiqvplgdaarpshll
tsqlplmwqlypeerymdnnsrlwqiqhhlmvrgvqelllkllpdd
>d1c39a_ 2.60.1.1.1 Extracytoplasmic domain of cation-dependent mannose 6-phosphate receptor {Bovine (Bos taurus)}
ektcdlvgekgkesekelallkrltplfqksfestvgqspdmysyvfrvcreagqhssga
glvqiqksngketvvgrfnetqifqgsnwimliykggdeydnhcgreqrravvmiscnrh
tladnfnpvseergkvqdcfylfemdsslacs
>d1hxn__ 2.61.1.1.1 Hemopexin {Rabbit (Oryctolagus cuniculus)}
estrcdpdlvlsamvsdnhgatyvfsgshywrldtnrdgwhswpiahqwpqgpstvdaaf
swedklyliqdtkvyvfltkggytlvngypkrlekelgsppvisleavdaafvcpgssrl
himagrrlwwldlksgaqatwtelpwphekvdgalcmekplgpnscstsgpnlylihgpn
lycyrhvdklnaaknlpqpqrvsrllgcth
>d1qhua1 2.61.1.1.1 (24-215) Hemopexin {Rabbit (Oryctolagus cuniculus)}
ieqcsdgwsfdattlddngtmlffkdefvwkshrgireliserwknfigpvdaafrhght
svylikgdkvwvytseknekvypkslqdefpgipfpldaavechrgecqdegilffqgnr
kwfwdlttgtkkerswpavgnctsalrwlgryycfqgnqflrfnpvsgevppgypldvrd
yflscpgrghrs
>d1gen__ 2.61.1.1.2 Gelatinase A (MMP-2), C-terminal domain {Human (Homo sapiens)}
lgpvtpeickqdivfdgiaqirgeifffkdrfiwrtvtprdkpmgpllvatfwpelpeki
davyeapqeekavffagneywiysastlergypkpltslglppdvqrvdaafnwsknkkt
yifagdkfwrynevkkkmdpgfpkliadawnaipdnldavvdlqggghsyffkgayylkl
enqslksvkfgsiksdwlgc
>d1fbl_1 2.61.1.1.3 (272-466) Collagenase, C-terminal domain {Porcine (Sus scrofa)}
pqtpqvcdskltfdaittlrgelmffkdrfymrtnsfypevelnfisvfwpqvpnglqaa
yeiadrdevrffkgnkywavrgqdvlygypkdihrsfgfpstvknidaavfeedtgktyf
fvahecwrydeykqsmdtgypkmiaeefpgignkvdavfqkdgflyffhgtrqyqfdfkt
kriltlqkanswfnc
>d1pex__ 2.61.1.1.4 Collagenase-3 (MMP-13), C-terminal domain {Human (Homo sapiens)}
tpdkcdpslsldaitslrgetmifkdrffwrlhpqqvdaelfltksfwpelpnridaaye
hpshdlififrgrkfwalngydilegypkkiselglpkevkkisaavhfedtgktllfsg
nqvwryddtnhimdkdyprlieedfpgigdkvdavyekngyiyffngpiqfeysiwsnri
vrvmpansilwc
>d1tl2a_ 2.62.1.1.1 Tachylectin-2 {Japanese horseshoe crab (Tachypleus tridentatus)}
ggesmlrgvyqdkfyqgtypqnkndnwlaratligkggwsnfkflflspggelygvlndk
iykgtppthdndnwmgrakkignggwnqfqflffdpngylyavskdklykasppqsdtdn
wiaratevgsggwsgfkflffhpngylyavhgqqfykalppvsnqdnwlaratkigqggw
dtfkflffssvgtlfgvqggkfyedyppsyaydnwlaraklignggwddfrflff
>d3sil__ 2.63.1.1.1 Salmonella sialidase {Salmonella typhimurium, strain lt2}
eksvvfkaegehftdqkgntivgsgsggttkyfripamcttskgtivvfadarhntasdq
sfidtaaarstdggktwnkkiaiyndrvnsklsrvmdptcivaniqgretilvmvgkwnn
ndktwgayrdkapdtdwdlvlykstddgvtfskvetnihdivtkngtisamlggvgsglq
lndgklvfpvqmvrtknittvlntsfiystdgitwslpsgycegfgsenniiefnaslvn
nirnsglrrsfetkdfgktwtefppmdkkvdnrnhgvqgstitipsgnklvaahssaqnk
nndytrsdislyahnlysgevkliddfypkvgnasgagysclsyrknvdketlyvvyean
gsiefqdlsrhlpviksyn
>d2qwc__ 2.63.1.1.2 Influenza neuraminidase {Influenza virus A, different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctckdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>d1nsca_ 2.63.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1eur__ 2.63.1.1.4 Micromonospora sialidase, N-terminal domain {Micromonospora viridifaciens}
geplyteqdlavngregfpnyripaltvtpdgdllasydgrptgidapgpnsilqrrstd
ggrtwgeqqvvsagqttapikgfsdpsylvdretgtifnfhvysqrqgfagsrpgtdpad
pnvlhanvatstdggltwshrtitaditpdpgwrsrfaasgegiqlrygphagrliqqyt
iinaagafqavsvysddhgrtwrageavgvgmdenktvelsdgrvllnsrdsarsgyrkv
avstdgghsygpvtidrdlpdptnnasiirafpdapagsarakvllfsnaasqtsrsqgt
irmscddgqtwpvskvfqpgsmsystltalpdgtygllyepgtgiryanfnlawlggica
p
>d2sli_2 2.63.1.1.5 (277-759) Leech intramolecular trans-sialidase, C-terminal domain {North american leech (Macrobdella decora)}
genifyagdvtesnyfripslltlstgtvisaadaryggthdskskiniafakstdggnt
wseptlplkfddyiaknidwprdsvgknvqiqgsasyidpvlledkltkriflfadlmpa
gigssnasvgsgfkevngkkylklrwhkdagraydytirekgviyndatnqptefrvdge
ynlyqhdtnltckqydynfsgnnliesktdvdvnmnifyknsvfkafptnylamrysdde
gaswsdldivssfkpevskflvvgpgigkqistgenagrllvplyskssaelgfmysddh
gdnwtyveadnltggataeaqivempdgslktylrtgsnciaevtsidggetwsdrvplq
gisttsygtqlsvinysqpidgkpaiilsspnatngrkngkiwiglvndtgntgidkysv
ewkysyavdtpqmgysysclaelpdgqvgllyekydswsrnelhlkdilkfekysiselt
gqa
>d1kit_3 2.63.1.1.6 (217-346,544-781) Vibrio cholerae sialidase {Vibrio cholerae}
vifrgpdripsivassvtpgvvtafaekrvgggdpgalsntndiitrtsrdggitwdtel
nlteqinvsdefdfsdprpiydpssntvlvsyarwptdaaqngdrikpwmpngifysvyd
vasgnwqapiXvnpgpghgitltrqqnisgsqngrliypaivldrfflnvmsiysddggs
nwqtgstlpipfrwksssiletlepseadmvelqngdllltarldfnqivngvnysprqq
flskdggitwslleannanvfsnistgtvdasitrfeqsdgshfllftnpqgnpagtngr
qnlglwfsfdegvtwkgpiqlvngasaysdiyqldsenaivivetdnsnmrilrmpitll
kqkltlsqn
>d1cq1a_ 2.63.2.1.1 Soluble quinoprotein glucose dehydrogenase {Acinetobacter calcoaceticus}
dvpltpsqfakaksenfdkkvilsnlnkphallwgpdnqiwlteratgkilrvnpesgsv
ktvfqvpeivndadgqngllgfafhpdfknnpyiyisgtfknpkstdkelpnqtiirryt
ynkstdtlekpvdllaglpsskdhqsgrlvigpdqkiyytigdqgrnqlaylflpnqaqh
tptqqelngkdyhtymgkvlrlnldgsipkdnpsfngvvshiytlghrnpqglaftpngk
llqseqgpnsddeinlivkggnygwpnvagykddsgyayanysaaanksikdlaqngvkv
aagvpvtkesewtgknfvpplktlytvqdtynyndptcgemtyicwptvapssayvykgg
kkaitgwentllvpslkrgvifrikldptysttyddavpmfksnnryrdviaspdgnvly
vltdtagnvqkddgsvtntlenpgslikft
>d1qlga_ 2.63.3.1.1 3-phytase {Bacillus amyloliquefaciens}
klsdpyhftvnaaaetepvdtagdaaddpaiwldpknpqnsklittnkksglavyslegk
mlhsyhtgklnnvdirydfplngkkvdiaaasnrsegkntieiyaidgkngtlqsitdpn
rpiasaidevygfslyhsqktgkyyamvtgkegefeqyelnadkngyisgkkvrafkmns
qtegmaaddeygslyiaeedeaiwkfsaepdggsngtvidradgrhltpdiegltiyyaa
dgkgyllassqgnssyaiyerqgqnkyvadfqitdgpetdgtsdtdgidvlgfglgpeyp
fglfvaqngenidhgqkanqnfkmvpweriadkigfhpqvnkqvdprkmtdrs
>d1gof_3 2.64.1.1.1 (151-537) Galactose oxidase, central domain {Dactylium dendroides}
ytapqpglgrwgptidlpivpaaaaieptsgrvlmwssyrndafggspggitltsswdps
tgivsdrtvtvtkhdmfcpgismdgngqivvtggndakktslydsssdswipgpdmqvar
gyqssatmsdgrvftiggswsggvfekngevyspssktwtslpnakvnpmltadkqglyr
sdnhawlfgwkkgsvfqagpstamnwyytsgsgdvksagkrqsnrgvapdamcgnavmyd
avkgkiltfggspdyqdsdattnahiitlgepgtspntvfasnglyfartfhtsvvlpdg
stfitggqrrgipfedstpvftpeiyvpeqdtfykqnpnsivrvyhsislllpdgrvfng
ggglcgdcttnhfdaqiftpnylynsn
>d1mdah_ 2.64.2.1.1 Methylamine dehydrogenase, H-chain {Paracoccus denitrificans}
ekskvagsaaaasaaaasdgsscdhgpgaisrrshitlpayfagttenwvscagcgvtlg
hslgaflslavaghsgsdfalastsfarsakgkrtdyvevfdpvtflpiadielpdaprf
svgprvhiigncassacllfflfgssaaaglsvpgasddqltksascfhihpgaaathyl
gscpaslaasdlaaapaaagivgaqctgaqncssqaaqanypgmlvwavassilqgdipa
agatmkaaidgnesgrkadnfrsagfqmvaklkntdgimiltvehsrsclaaaentssvt
asvgqtsgpisnghdsdaiiaaqdgasdnyansagtevldiydaasdqdqssveldkgpe
slsvqnea
>d2bbkh_ 2.64.2.1.1 Methylamine dehydrogenase, H-chain {Paracoccus denitrificans}
deprileapapdarrvyvndpahfaavtqqfvidgeagrvigmidggflpnpvvaddgsf
iahastvfsriargertdyvevfdpvtllptadielpdaprflvgtypwmtsltpdgktl
lfyqfspapavgvvdlegkafkrmldvpdcyhifptapdtffmhcrdgslakvafgtegt
peithtevfhpedeflinhpaysqkagrlvwptytgkihqidlssgdakflpavealtea
eradgwrpggwqqvayhraldriyllvdqrdewrhktasrfvvvldaktgerlakfemgh
eidsinvsqdekpllyalstgdktlyihdaesgeelrsvnqlghgpqvittadmg
>d1gotb_ 2.64.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1a12a_ 2.64.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1c9la2 2.64.5.1.1 (3-330) Clathrin heavy-chain terminal domain {Rat (Rattus norvegicus)}
qilpirfqehlqlqnlginpanigfstltmesdkficirekvgeqaqvviidmndpsnpi
rrpisadsaimnpaskvialkagktlqifniemkskmkahtmtddvtfwkwislntvalv
tdnavyhwsmegesqpvkmfdrhsslagcqiinyrtdakqkwllltgisaqqnrvvgamq
lysvdrkvsqpieghaasfaqfkmegnaeestlfcfavrgqaggklhiievgtpptgnqp
fpkkavdvffppeaqndfpvamqisekhdvvflitkygyihlydletgtciymnrisget
ifvtapheatagiigvnrkgqvlsvcve
>d1qfma1 2.64.6.1.1 (1-430) Prolyl oligopeptidase, N-terminal domain {Porcine}
mlsfqypdvyrdetaiqdyhghkvxdpyawledpdseqtkafveaqnkitvpfleqxpir
glykermtelydypkyschfkkgkryfyfyntglqnqrvlyvqdslegearvfldpnils
ddgtvalrgyafsedgeyfayglsasgsdwvtikfmkvdgakelpdvlervkfsxmawth
dgkgmfynaypqqdgksdgtetstnlhqklyyhvlgtdqsedilcaefpdepkwmggael
sddgryvllsiregxdpvnrlwycdlqqesngitgilkwvklidnfegeydyvtnegtvf
tfktnrhspnyrlinidftdpeeskwkvlvpehekdvlewvacvrsnflvlcylhdvknt
lqlhdlatgallkifplevgsvvgysgqkkdteifyqftsflspgiiyhcdltkeelepr
vfrevtvkgi
>d1b2na_ 2.65.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1qksa2 2.65.2.1.3 (136-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Paracoccus denitrificans}
efgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvldt
gyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegwed
kyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefivn
vketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtkegk
lvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkildsf
palgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpiaew
agitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtptg
kfnvyntmtdty
>d1bli_1 2.66.1.1.1 (394-483) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsagwgefhvnggsvsiyvqr
>d1bplb1 2.66.1.1.1 (394-482) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsegwgefhvnggsvsiyvq
>d1vjs_1 2.66.1.1.1 (394-482) Bacterial alpha-Amylase (BLA) {Bacillus licheniformis}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsegwgefhvnggsvsiyvq
>d1aqm_1 2.66.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1bag_1 2.66.1.1.3 (348-425) Bacterial alpha-Amylase (BLA) {Bacillus subtilis}
qpeelsnpngnnqifmnqrgshgvvlanagsssvsintatklpdgrydnkagagsfqvnd
gkltgtinarsvavlypd
>d1cdg_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgt_3 2.66.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d1cgu_3 2.66.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d1cgv_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgw_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgx_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cgy_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxe_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxf_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxh_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxi_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1cxka3 2.66.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d1cxla3 2.66.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d1d3ca3 2.66.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d1tcma3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d1tcmb3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d2cxg_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaa
>d2dij_3 2.66.1.1.4 (407-496) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqerwinndvliyerkfgsnvavvavnrnlnapasisglvtslpqgsyndvlggllng
ntlsvgsggaasnftlaaggtavwqytaat
>d3cgt_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqyttae
>d4cgt_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqyttae
>d5cgt_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqyttae
>d6cgt_3 2.66.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d7cgt_3 2.66.1.1.4 (407-495) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqyttae
>d8cgta3 2.66.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d9cgta3 2.66.1.1.4 (407-494) Cyclodextrin glycosyltransferase {Bacillus circulans}
gstqqrwinndvyvyerkfgksvavvavnrnlstsasitglstslptgsytdvlggvlng
nnitstngsinnftlaagatavwqytta
>d1cyg_3 2.66.1.1.5 (403-491) Cyclodextrin glycosyltransferase {Bacillus stearothermophilus}
gdteqrwingdvyvyerqfgkdvvlvavnrssssnysitglftalpagtytdqlgglldg
ntiqvgsngsvnafdlgpgevgvwaysat
>d1pama3 2.66.1.1.6 (407-496) Cyclodextrin glycosyltransferase {Alkalophilic bacillus, sp. 1011}
gstherwinndviiyerkfgnnvavvainrnmntpasitglvtslprgsyndvlggilng
ntltvgaggaasnftlapggtavwqyttda
>d1pamb3 2.66.1.1.6 (407-496) Cyclodextrin glycosyltransferase {Alkalophilic bacillus, sp. 1011}
gstherwinndviiyerkfgnnvavvainrnmntpasitglvtslprgsyndvlggilng
ntltvgaggaasnftlapggtavwqyttda
>d1a47_3 2.66.1.1.7 (407-495) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
gttqqrwinndvyiyerkfgnnvalvainrnlstsynitglytalpagtytdvlggllng
nsisvasdgsvtpftlsagevavwqyvss
>d1ciu_3 2.66.1.1.7 (407-495) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
gttqqrwinndvyiyerkfgnnvalvainrnlstsynitglytalpagtytdvlggllng
nsisvasdgsvtpftlsagevavwqyvss
>d1dhka1 2.66.1.1.8 (404-496) Animal alpha-amylase {Porcine (Sus scrofa)}
qpfanwwdngsnqvafgrgnrgfivfnnddwqlsstlqtglpggtycdvisgdkvgnsct
gikvyvssdgtaqfsisnsaedpfiaihaeskl
>d1pig_1 2.66.1.1.8 (404-496) Animal alpha-amylase {Porcine (Sus scrofa)}
qpfanwwdngsnqvafgrgnrgfivfnnddwqlsstlqtglpggtycnvisgdkvgnsct
gikvyvssdgtaqfsisnsaqdpfiaihaeskl
>d1smd_1 2.66.1.1.9 (404-496) Animal alpha-amylase {Human (Homo sapiens)}
qpftnwydngsnqvafgrgnrgfivfnnddwtfsltlqtglpagtycdvisgdkingnct
gikiyvsddgkahfsisnsaedpfiaihaeskl
>d1jae_1 2.66.1.1.10 (379-471) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
gtqvenwwsnddnqiafsrgsqgfvaftnggdlnqnlntglpagtycdvisgelsggsct
gksvtvgdngsadislgsaeddgvlaihvnakl
>d1tmqa1 2.66.1.1.10 (379-471) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
gtqvenwwsnddnqiafsrgsqgfvaftnggdlnqnlntglpagtycdvisgelsggsct
gksvtvgdngsadislgsaeddgvlaihvnakl
>d1viwa1 2.66.1.1.10 (379-471) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
gtqvenwwsnddnqiafsrgsqgfvaftnggdlnqnlntglpagtycdvisgelsggsct
gksvtvgdngsadislgsaeddgvlaihvnakl
>d2aaa_1 2.66.1.1.11 (382-476) Fungal alpha-amylase {Aspergillus niger, acid amylase}
yandafytdsntiamakgtsgsqvitvlsnkgssgssytltlsgsgytsgtklieaytct
svtvdssgdipvpmasglprvllpasvvdssslcg
>d2taaa1 2.66.1.1.12 (382-478) Fungal alpha-amylase {Aspergillus oryzae, Taka-amylase}
yknpyikddttiamrkgtdgsqivtilsnkgasgdsytlslsgasytagqqltevigctt
vtvgsdgnvpvpmagglprvlypteklagskicsdss
>d6taa_1 2.66.1.1.12 (382-476) Fungal alpha-amylase {Aspergillus oryzae, Taka-amylase}
yknwpiykddttiamrkgtdgsqivtilsnkgasgdsytlslsgagytagqqltevigct
tvtvgsdgnvpvpmagglprvlypteklagskics
>d7taa_1 2.66.1.1.12 (382-476) Fungal alpha-amylase {Aspergillus oryzae, Taka-amylase}
yknwpiykddttiamrkgtdgsqivtilsnkgasgdsytlslsgagytagqqltevigct
tvtvgsdgnvpvpmagglprvlypteklagskics
>d1bvza2 2.66.1.1.13 (503-585) Alpha-amylase II (TVAII) {Thermoactinomyces vulgaris, r-47}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr
>d1bvzb2 2.66.1.1.13 (503-585) Alpha-amylase II (TVAII) {Thermoactinomyces vulgaris, r-47}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr
>d1bf2_2 2.66.1.1.14 (638-750) Isoamylase {Pseudomonas amyloderamosa}
ysgsqltwyqpsgavadsnywnntsnyaiayaingpslgdsnsiyvayngwsssvtftlp
appsgtqwyrvtdtcdwndgastfvapgsetliggagttygqcgqsllllisk
>d1jda_1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1jdc_1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1jdd_1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1qi3a1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1qi4a1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1qi5a1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1qpka1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d2amg_1 2.66.1.1.15 (358-418) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
radsaisfhsgysglvatvsgsqqtlvvalnsdlgnpgqvasgsfseavnasngqvrvwr
s
>d1amy_1 2.66.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avaa1 2.66.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avab1 2.66.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1bg9_1 2.66.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1uok_1 2.66.1.1.17 (480-558) Oligo-1,6-glucosidase {Bacillus cereus}
gsydlilennpsifayvrtygvekllvianftaeecifelpedisysevellihnydven
gpienitlrpyeamvfklk
>d1aiw__ 2.67.1.1.1 Cellulose-binding domain of endoglucanase Z {Erwinia chrysanthemi}
mgdcananvypnwvskdwaggqpthneagqsivykgnlytanwytasvpgsdsswtqvgs
cn
>d1dkga1 2.68.1.1.1 (139-197) Head domain of nucleotide exchange factor GrpE {Escherichia coli}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvakaka
>d1dkgb1 2.68.1.1.1 (139-195) Head domain of nucleotide exchange factor GrpE {Escherichia coli}
veviaetnvpldpnvhqaiamvesddvapgnvlgimqkgytlngrtiraamvtvaka
>d2cba__ 2.69.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1znca_ 2.69.1.1.3 Carbonic anhydrase {Human (Homo sapiens), isozyme IV}
wcyevqaessnypclvpvkwggncqkdrqspinivttkakvdkklgrfffsgydkkqtwt
vqnnghsvmmllenkasisggglpapyqakqlhlhwsdlpykgsehsldgehfamemhiv
hekekgtsrnvkeaqdpedeiavlaflveagtqvnegfqplvealsnipkpemsttmaes
slldllpkeeklrhyfrylgslttptcdekvvwtvfrepiqlhreqilafsqklyydkeq
tvsmkdnvrplqqlgqrtviks
>d1kopa_ 2.69.1.1.6 Carbonic anhydrase {Neisseria gonorrhoeae}
hthwgytghdspeswgnlseefrlcstgknqspvnitetvsgklpaikvnykpsmvdven
nghtiqvnypeggntltvngrtytlkqfhfhvpsenqikgrtfpmeahfvhldenkqplv
lavlyeagktngrlssiwnvmpmtagkvklnqpfdastllpkrlkyyrfagslttppcte
gvswlvlktydhidqaqaekftravgsennrpvqplnarvvie
>d4bcl__ 2.70.1.1.1 Bacteriochlorophyl A protein {Prosthecochloris aestuarii, strain 2k}
tttahsdyeiileggssswgqvkgrakvnvpaaipllptdcniridakpldaqkgvvrft
tkiesvvdsvkntlnvevdianetkdrriavgegslsvgdfshsfsfegsvvnmyyyrsd
avrrnipnpiymqgrqfhdilmkvpldnndlvdtwegfqqsisggganfgdwirefwfig
pafaaineggqrispivvnssnveggekgpvgvtrwkfshagsgvvdsisrwtelfpveq
lnkpasieggfrsdsqgievkvdgnlpgvsrdaggglrrilnhpliplvhhgmvgkfndf
tvdtqlkivlpkgykiryaapqfrsqnleeyrwsggayarwvehvckggtgqfevlyaq
>d1ospo_ 2.71.1.1.1 Outer surface protein A {Lyme disease spirochete (Borrelia burgdorferi)}
sldeknsvsvdlpgemkvlvskeknkdgkydliatvdklelkgtsdknngsgvlegvkad
kckvkltisddlgqttlevfkedgktlvskkvtskdkssteekfnekgevsekiitradg
trleytgiksdgsgkakevlkgyvlegtltaekttlvvkegtvtlsknisksgevsveln
dtdssaatkktaawnsgtstltitvnskktkdlvftkentitvqqydsngtklegsavei
tkldeiknalk
>d1vmoa_ 2.72.1.1.1 Vitelline membrane outer protein-I (VMO-I) {Hen (Gallus gallus)}
rtreytsvitvpngghwgkwgirqfchsgyangfalkvepsqfgrddtalngirlrcldg
svieslvgkwgtwtsflvcptgylvsfslrseksqgggddtaanniqfrcsdeavlvgdg
lswgrfgpwskrckicglqtkvespqglrddtalnnvrffcck
>d1dlc_2 2.72.2.1.1 (290-499) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
lypkevkteltrdvltdpivgvnnlrgygttfsnienyirkphlfdylhriqfhtrfqpg
yygndsfnywsgnyvstrpsigsndiitspfygnkssepvqnlefngekvyravantnla
vwpsavysgvtkvefsqyndqtdeastqtydskrnvgavswdsidqlppettdeplekgy
shqlnyvmcflmqgsrgtipvltwthksvd
>d1ciy_2 2.72.2.1.2 (256-461) delta-Endotoxin (insectocide), middle domain {Bacillus thuringiensis, CRYIA (A)}
pirtvsqltreiytnpvlenfdgsfrgmaqrieqnirqphlmdilnsitiytdvhrgfny
wsghqitaspvgfsgpefafplfgnagnaappvlvsltglgifrtlssplyrriilgsgp
nnqelfvldgtefsfaslttnlpstiyrqrgtvdsldvippqdnsvppragfshrlshvt
mlsqaagavytlraptfswqhrsaef
>e1jot.1a 2.72.3.1.2 Lectin MPA {Osage orange (Maclura pomifera)}
gvtfddgaytgireinfeynsetaigglrvtydlngmpfvaedhksfitgfkpvkislef
pseyivevsgyvgkvegytvirsltfktnkqtygpygvtngtpfslpienglivgfkgsi
gywldyfsiylsl
>d1c3ma_ 2.72.3.1.3 Heltuba lectin {Jerusalem artishoke (Helianthus tuberosus) |A|}
asdiavqagpwggnggkrwlqtahggkitsiiikggtcifsiqfvykdkdnieyhsgkfg
vlgdkaetitfaededitaisgtfgayyhmtvvtsltfqtnkkvygpfgtvasssfslpl
tkgkfagffgnsgdvldsiggvvvp
>d1jpc__ 2.73.1.1.1 Lectin (agglutinin) {Snowdrop (Galanthus nivalis)}
dnilysgetlstgeflnygsfvfimqedcnlvlydvdkpiwatntgglsrscflsmqtdg
nlvvynpsnkpiwasntggqngnyvcilqkdrnvviygtdrwatgtht
>d1bwua_ 2.73.1.1.2 Lectin (agglutinin) {Garlic (Allium sativum)}
rnilrndeglyggqsldvnpyhfimqedcnlvlydhstsvwasntgilgkkgcravlqsd
gnfvvydaegrslwashsvrgngnyvlvlqedgnvviyrsdiwstn
>d1b2pa_ 2.73.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1dlpa_ 2.73.1.1.5 Fetuin-binding protein Scafet precursor {Bluebell (Scilla campanulata)}
nnilfglshegshpqtlhaaqslelssfrftmqsdcnlvlfdsdvrvwasntagatgcra
vlqsdgllviltaqntirwssgtkgsignyvlvlqpdrtvtiygpglwdsgtsnkgsvvv
anngnsilystqgndnhpqtlhatqslqlspyrlsmetdcnlvlfdrddrvwstntagkg
tgcravlqpngrmdvltnqniavwtsgnsrsagryvfvlqpdrnlaiyggalwtt
>d1dlpc_ 2.73.1.1.5 Fetuin-binding protein Scafet precursor {Bluebell (Scilla campanulata)}
nnilfglshegshpqtlhaaqslelssfrftmqsdcnlvlfdsdvrvwasntagatgcra
vlqsdgllviltaqntirwssgtkgsignyvlvlqpdrtvtiygpglwdsgtsnkgsvvv
anngnsilystqgndnhpqtlhatqslqlspyrlsmetdcnlvlfdrddrvwstntagkg
tgcravlqpngrmdvltnqniavwtsgnsrsagryvfvlqpdrnlaiyggalwttg
>d1kapp1 2.74.1.1.1 (247-470) Metalloprotease, C-terminal domain {Pseudomonas aeruginosa, alkaline protease}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1air__ 2.75.1.1.1 Pectate lyase {Erwinia chrysanthemi, type C}
atdtggyaataggnvtgavsktatsmqdivniidaarldangkkvkggayplvitytgne
dslinaaaanicgqwskdprgveikeftkgitiigangssanfgiwikkssdvvvqnmri
gylpggakdgdmirvddspnvwvdhnelfaanhecdgtpdndttfesavdikgasntvtv
synyihgvkkvgldgssssdtgrnityhhnyyndvnarlplqrgglvhaynnlytnitgs
glnvrqngqaliennwfekainpvtsrydgknfgtwvlkgnnitkpadfstysitwtadt
kpyvnadswtstgtfptvaynyspvsaqcvkdklpgyagvgknlatltstac
>d1bn8a_ 2.75.1.1.3 Pectate lyase {Bacillus subtilis}
adlghqtlgsndgwgaystgttggskasssnvytvsnrnqlvsalgketnttpkiiyikg
tidmnvddnlkplglndykdpeydldkylkaydpstwgkkepsgtqeeararsqknqkar
vmvdipanttivgsgtnakvvggnfqiksdnviirniefqdaydyfpqwdptdgssgnwn
sqydnitinggthiwidhctfndgsrpdstspkyygrkyqhhdgqtdasnganyitmsyn
yyhdhdkssifgssdsktsddgklkitlhhnryknivqraprvrfgqvhvynnyyegsts
sssypfsyawgigksskiyaqnnvidvpglsaaktisvfsggtalydsgtllngtqinas
aanglsssvgwtpslhgsidasanvksnvinqagagkln
>d1qcxa_ 2.75.1.2.2 Pectin lyase {Aspergillus niger, type B}
agvvgaaegfahgvtgggsaspvyptttdelvsylgdneprviildqtfdftgtegtett
tgcapwgtasqcqvainlhswcdnyqasapkvsvtydkagilpitvnsnksivgqgtkgv
ikgkglrvvsgaknviiqniavtdinpkyvwggdaitvddsdlvwidhvttarigrqhiv
lgtsadnrvtisyslidgrsdysatcnghhywgvyldgsndmvtlkgnyfynlsgrmpkv
qgntllhavnnlfhnfdghafeigtggyvlaegnvfqdvnvvvetpisgqlfsspdantn
qqcasvfgrscqlnafgnsgsmsgsdtsiiskfagktiaaahppgaiaqwtmknagqgk
>d1tyu__ 2.75.1.3.1 P22 tailspike protein {Phage p22 (Salmonella typhimurium)}
ysieadkkfkysvklsdyptlqdaasaavdgllidrdynfyggetvdfggkvltieckak
figdgnliftklgkgsriagvfmestttpwvikpwtddnqwltdaaavvatlkqsktdgy
qptvsdyvkfpgietllppnakgqnitstleirecigvevhrasglmagflfrgchfckm
vdannpsggkdgiitfenlsgdwgkgnyviggrtsygsvssaqflrnnggferdggvigf
tsyragesgvktwqgtvgsttsrnynlqfrdsvviypvwdgfdlgadtdrpgdypitqyp
lhqlplnhlidnllvrgalgvgfgmdgkgmyvsnitvedcagsgayllthesvftniaii
dtntkdfqanqiyisgacrvnglrligirsltidapnstvsgitgmvdpsrinvanlaee
glgniransfgydsaaiklrihklsktldsgalyshinggagsgsaytqltaisgstpda
vslkvnhkdcrgaeipfvpdiasddfikdsscflpywennstslkalvkkpngelvrltl
atl
>d1rmg__ 2.75.1.4.1 Rhamnogalacturonase A {Aspergillus aculeatus}
qlsgsvgpltsastkgatktcnilsygavadnstdvgpaitsawaacksgglvyipsgny
alntwvtltggsataiqldgiiyrtgtasgnmiavtdttdfelfsstskgavqgfgyvyh
aegtygarilrltdvthfsvhdiilvdapafhftmdtcsdgevynmairggneggldgid
vwgsniwvhdvevtnkdecvtvkspannilvesiycnwsggcamgslgadtdvtdivyrn
vytwssnqmymiksnggsgtvsnvllenfighgnaysldidgywssmtavagdgvqlnni
tvknwkgteangatrppirvvcsdtapctdltlediaiwtesgsselylcrsaygsgycl
kdssshtsytttstvtaapsgysattmaadlatafgltasipiptiptsfypgltpysal
ag
>d1bhe__ 2.75.1.4.2 Polygalacturonase {Erwinia carotovora}
sdsrtvsepktpsscttlkadsstatstiqkalnncdqgkavrlsagstsvflsgplslp
sgvsllidkgvtlravnnaksfenapsscgvvdkngkgcdafitavsttnsgiygpgtid
gqggvklqdkkvswwelaadakvkklkqntprliqinksknftlynvslinspnfhvvfs
dgdgftawkttiktpstarntdgidpmssknitiaysniatgddnvaikaykgraetrni
silhndfgtghgmsigsetmgvynvtvddlkmngttnglriksdksaagvvngvrysnvv
mknvakpividtvyekkegsnvpdwsditfkdvtsetkgvvvlngenakkpievtmknvk
ltsdstwqiknvnvkk
>d1czfa_ 2.75.1.4.3 Endo-polygalacturonase II {Fungus (Aspergillus niger)}
dsctfttaaaakagkakcstitlnnievpagttldltgltsgtkvifegtttfqyeewag
plismsgehitvtgasghlincdgarwwdgkgtsgkkkpkffyahgldsssitglniknt
plmafsvqanditftdvtinnadgdtqgghntdafdvgnsvgvniikpwvhnqddclavn
sgeniwftggtcigghglsigsvgdrsnnvvknvtiehstvsnsenavriktisgatgsv
seitysnivmsgisdygvviqqdyedgkptgkptngvtiqdvklesvtgsvdsgateiyl
lcgsgscsdwtwddvkvtggkkstacknfpsvasc
>d1daba_ 2.75.1.5.1 Virulence factor P.69 pertactin {Bordetella pertussis}
dwnnqsivktgerqhgihiqgsdpggvrtasgttikvsgrqaqgillenpaaelqfrngs
vtssgqlsddgirrflgtvtvkagklvadhatlanvgdtwdddgialyvageqaqasiad
stlqgaggvqierganvtvqrsaivdgglhigalqslqpedlppsrvvlrdtnvtavpas
gapaavsvlgaseltldgghitggraagvaamqgavvhlqratirrgdalaggavpggav
pggavpggfgpggfgpvldgwygvdvsgssvelaqsiveapelgaairvgrgarvtvpgg
slsaphgnvietggarrfapqaaplsitlqagahaqgkallyrvlpepvkltltggadaq
gdivatelpsipgtsigpldvalasqarwtgatravdslsidnatwvmtdnsnvgalrla
sdgsvdfqqpaeagrfkvltvntlagsglfrmnvfadlglsdklvvmqdasgqhrlwvrn
sgsepasantlllvqtplgsaatftlankdgkvdigtyryrlaangngqwslvgakapp
>d1dbga_ 2.75.1.6.1 Chondroitinase B {Flavobacterium heparinium}
qvvasnetlyqvvkevkpgglvqiadgtykdvqlivsnsgksglpitikalnpgkvfftg
dakvelrgehlilegiwfkdgnraiqawkshgpglvaiygsynritacvfdcfdeansay
ittsltedgkvpqhcridhcsftdkitfdqvinlnntaraikdgsvggpgmyhrvdhcff
snpqkpgnagggirigyyrndigrclvdsnlfmrqdseaeiitsksqenvyygntylncq
gtmnfrhgdhqvainnfyigndqrfgyggmfvwgsrhviacnyfelsetiksrgnaalyl
npgamasehalafdmliannafinvngyaihfnplderrkeycaanrlkfetphqlmlkg
nlffkdkpyvypffkddyfiagknswtgnvalgvekgipvnisanrsaykpvkikdiqpi
egialdlnaliskgitgkplswdevrpywlkempgtyaltarlsadraakfkavikrnke
h
>d1lxa__ 2.76.1.1.1 UDP N-acetylglucosamine acyltransferase {Escherichia coli, gene lpxA}
midksafvhptaiveegasiganahigpfcivgphveigegtvlkshvvvnghtkigrdn
eiyqfasigevnqdlkyageptrveigdrnriresvtihrgtvqgggltkvgsdnllmin
ahiahdctvgnrcilannatlaghvsvddfaiiggmtavhqfciigahvmvggcsgvaqd
vppyviaqgnhatpfgvnieglkrrgfsreaitairnaykliyrsgktldevkpeiaela
etypevkaftdffarstrglir
>d3tdt__ 2.76.1.2.1 Tetrahydrodipicolinate-N-succinlytransferase, THDP-succinlytransferase, DapD {Mycobacterium bovis}
mqqlqnviesaferraditpanvdtvtreavnqviglldsgalrvaekidgqwvthqwlk
kavllsfrindnkvmdgaetryydkvpmkfadydearfqkegfrvvppatvrqgafiarn
tvlmpsyvnigayvdegtmvdtwatvgscaqigknvhlsggvgiggvleplqanptiied
ncfigarsevvegviveegsvismgvylgqstriydretgeihygrvpagsvvvsgnlps
kdgsyslycavivkkvdaktrgkvginellrtid
>d1xat__ 2.76.1.3.1 Xenobiotic acetyltransferase {Pseudomonas aeruginosa}
nyfespfrgkllseqvsnpnirvgrysyysgyyhghsfddcarylmpdrddvdklvigsf
csigsgaafimagnqghraewastfpfhfmheepafagavngyqpagdtlighevwigte
amfmpgvrvghgaiigsralvtgdvepyaivggnpartirkrfsdgdiqnllemawwdwp
ladieaampllctgdipalyqhwkqrqa
>d1qrea_ 2.76.1.4.1 Carbonic anhydrase {Arhaeon (Methanosarcina thermophila)}
tvdefsnirenpvtpwnpepsapvidptayidpqasvigevtiganvmvspmasirsdeg
mpifvgdrsnvqdgvvlhaletineegepiednivevdgkeyavyignnvslahqsqvhg
paavgddtfigmqafvfkskvgnncvleprsaaigvtipdgryipagmvvtsqaeadklp
evtddyayshtneavvyvnvhlaegykets
>d2phla1 2.77.1.1.1 (11-210) Phaseolin {French bean (Phaseolus vulgaris)}
dnpfyfnsdnswntlfknqyghirvlqrfdqqskrlqnledyrlvefrskpetlllpqqa
daelllvvrsgsailvlvkpddrreyffltsdnpifsdhqkipagtifylvnpdpkedlr
iiqlampvnnpqihefflssteaqqsylqefskhileasfnskfeeinrvlfeeegqqeg
vivnidseqikelskhakss
>d2phla2 2.77.1.1.1 (220-381) Phaseolin {French bean (Phaseolus vulgaris)}
ntignefgnltertdnslnvlissiemeegalfvphyyskaivilvvnegeahvelvgpk
gnketleyesyraelskddvfvipaaypvaikatsnvnftgfginannnnrnllagktdn
vissigraldgkdvlgltfsgsgdevmklinkqsgsyfvdah
>d1dgrm_ 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
qlrryaatlsegdiivipssfpvalkaasdlnmvgigvnaennernflaghkenvirqip
rqvsdltfpgsgeeveellenqkesyfvdgqp
>d1dgrn_ 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgle
>d1dgwa_ 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
nnpylfrsnkfltlfknqhgslrllqrfnedteklenlrdyrvleycskpntlllphhsd
sdllvlvlegqailvlvnpdgrdtykldqgdaikiqagtpfylinpdnnqnlrilkfait
frrpgtvedfflsstkrlpsylsafsknfleasydspydeieqtllqeeqegvivkmp
>d2caua2 2.77.1.1.2 (246-421) Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgleqqqqqglesmqlrryaatlsegdiivipssfpvalkaasdlnmv
gigvnaennernflaghkenvirqiprqvsdltfpgsgeeveellenqkesyfvdg
>e1dgr.1x 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgl
>e1dgr.1y 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
mqlrryaatlsegdiivipssfpvalkaasdlnmvgigvnaennernflaghkenvirqi
prqvsdltfpgsgeeveellenqkesyfvdgqp
>e1dgr.2v 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgle
>e1dgr.2w 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
mqlrryaatlsegdiivipssfpvalkaasdlnmvgigvnaennernflaghkenvirqi
prqvsdltfpgsgeeveellenqkesyfvdgqp
>e1dgw.1x 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
dkpfnlrsrdpiysnnygklyeitpeknsqlrdldillnclqmnegalfvphynsratvi
lvanegraevelvgle
>e1dgw.1y 2.77.1.1.2 Canavalin 7S vicilin {Jack bean (Canavalia ensiformis)}
qlrryaatlsegdiivipssfpvalkaasdlnmvgigvnaennernflaghkenvirqip
rqvsdltfpgsgeeveellenqkesyfvdgqp
>d1pmi__ 2.77.2.1.1 Phosphomannose isomerase {Yeast (Candida albicans)}
sseklfriqcgyqnydwgkigsssavaqfvhnsdpsitidetkpyaelwmgthpsvpska
idlnnqtlrdlvtakpqeylgesiitkfgsskelpflfkvlsiekvlsiqahpdkklgaq
lhaadpknypddnhkpemaiavtdfegfcgfkpldqlaktlatvpelneiigqelvdefi
sgiklpaevgsqddvnnrkllqkvfgklmntdddvikqqtakllertdrepqvfkdidsr
lpeliqrlnkqfpndiglfcgclllnhvglnkgeamflqakdphayisgdiiecmaasdn
vvragftpkfkdvknlvemltysyesvekqkmplqefprskgdavksvlydppiaefsvl
qtifdkskggkqvieglngpsiviatngkgtiqitgddstkqkidtgyvffvapgssiel
tadsanqdqdfttyrafvea
>d1bk0__ 2.77.3.1.1 Isopenicillin N synthase {Emericella nidulans}
svskanvpkidvsplfgddqaakmrvaqqidaasrdtgffyavnhginvqrlsqktkefh
msitpeekwdlairaynkehqdqvragyylsipgkkavesfcylnpnftpdhpriqaktp
thevnvwpdetkhpgfqdfaeqyywdvfglssallkgyalalgkeenffarhfkpddtla
svvlirypyldpypeaaiktaadgtklsfewhedvslitvlyqsnvqnlqvetaagyqdi
eaddtgylincgsymahltnnyykapihrvkwvnaerqslpffvnlgydsvidpfdprep
ngksdreplsygdylqnglvslinkngqt
>d1dcs__ 2.77.3.1.2 Deacetoxycephalosporin C synthase {Streptomyces clavuligerus}
mdttvptfslaelqqglhqdefrrclrdkglfyltdcgltdtelksakdlvidffehgse
aekravtspvptmrrgftglesestaqitntgsysdysmcysmgtadnlfpsgdferiwt
qyfdrqytasravarevlratgtepdggveafldcepllrfryfpqvpehrsaeeqplrm
aphydlsmvtliqqtpcangfvslqaevggaftdlpyrpdavlvfcgaiatlvtggqvka
prhhvaaprrdqiagssrtssvfflrpnadftfsvplarecgfdvsldgetatfqdwigg
nyvnirrtska
>d2cgpc2 2.77.4.1.1 (8-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
dptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqg
dfigelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvt
sekvgnlafl
>d1rgs_1 2.77.4.2.1 (113-242) Regulatory subunit of Protein kinase A {Bovine (Bos taurus)}
rkvipkdyktmaalakaieknvlfshlddnersdifdamfpvsfiagetviqqgdegdnf
yvidqgemdvyvnnewatsvgeggsfgelaliygtpraatvkaktnvklwgidrdsyrri
lmgstlrkrk
>d1rgs_2 2.77.4.2.1 (243-376) Regulatory subunit of Protein kinase A {Bovine (Bos taurus)}
myeeflskvsilesldkwerltvadalepvqfedgqkivvqgepgdeffiilegsaavlq
rrseneefvevgrlgpsdyfgeiallmnrpraatvvargplkcvkldrprfervlgpcsd
ilkrniqqynsfvs
>d2arca_ 2.77.5.1.1 Regulatory protein AraC {Escherichia coli}
dpllpgysfnahlvagltpieangyldffidrplgmkgyilnltirgqgvvknqgrefvc
rpgdillfppgeihhygrhpearewyhqwvyfrpraywhewlnwpsifantgffrpdeah
qphfsdlfgqiinagqgegrysellainlleqlllrrmeai
>d1c9sa_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sb_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1c9sc_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
nsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqt
rhgvieseg
>d1c9sd_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9se_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1c9sf_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sg_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
nsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqt
rhgviesegk
>d1c9sh_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9si_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sj_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1c9sk_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1c9sl_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sm_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgviesegk
>d1c9sn_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9so_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgviesegk
>d1c9sp_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sq_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sr_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9ss_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9st_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9su_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1c9sv_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
tnsdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiq
trhgvieseg
>d1wapa_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapb_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapc_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapd_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wape_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapf_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapg_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1waph_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapi_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapj_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapk_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapl_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapm_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapn_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapo_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapp_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapq_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapr_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1waps_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksekk
>d1wapt_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapu_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1wapv_ 2.77.6.1.1 Trp RNA-binding attenuation protein (TRAP) {Bacillus subtilis}
dfvvikavedgvnvigltrgtdtkfhhsekldkgeviiaqftehtsaikvrgealiqtay
gemksek
>d1qawa_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1qawb_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegkk
>d1qawc_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1qawd_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1qawe_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviesegk
>d1qawf_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1qawg_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1qawh_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1qawi_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1qawj_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgviese
>d1qawk_ 2.77.6.1.2 Trp RNA-binding attenuation protein (TRAP) {Bacillus stearothermophilus}
sdfvvikaledgvnvigltrgadtrfhhsekldkgevliaqftehtsaikvrgkayiqtr
hgvieseg
>d1qiua2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1qiub2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1qiuc2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1qiud2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1qiue2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1qiuf2 2.78.1.1.1 (319-395) Adenovirus fibre shaft {Human adenovirus}
vsikkssglnfdntaiainagkglefdtntsespdinpiktkigsgidynengamitklg
aglsfdnsgaitignkn
>d1a6x__ 2.79.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
meapaaaeisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqiea
dksgtvkailvesgqpvefdeplvvie
>d1bdo__ 2.79.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d2bdoa_ 2.79.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d3bdoa_ 2.79.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
aaeisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgt
vkailvesgqpvefdeplvvie
>d1htp__ 2.79.1.1.2 Protein H of glycine cleavage system {Pea (Pisum sativum)}
snvldglkyapshewvkhegsvatigitdhaqdhlgevvfvelpepgvsvtkgkgfgave
svkatsdvnspisgevievntgltgkpglinsspyedgwmikikptspdelesllgakey
tkfceeedaah
>d1lab__ 2.79.1.1.3 Ipoyl domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
afefklpdigegihegeivkwfvkpgdevneddvlcevqndkavveipspvkgkvleilv
pegtvatvgqtlitldapgy
>d1lac__ 2.79.1.1.3 Ipoyl domain of dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
afefklpdigegihegeivkwfvkpgdevneddvlcevqndkavveipspvkgkvleilv
pegtvatvgqtlitldapgy
>d1iyu__ 2.79.1.1.4 Ipoyl domain of dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
seiirvpdiggdgeviellvktgdlieveqglvvlesakasmevpspkagvvksvsvklg
dklkegdaiielepaagar
>d1iyv__ 2.79.1.1.4 Ipoyl domain of dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
seiirvpdiggdgeviellvktgdlieveqglvvlesakasmevpspkagvvksvsvklg
dklkegdaiielepaagar
>d1qjoa_ 2.79.1.1.5 Ipoyl domain of dihydrolipoamide acetyltransferase {Escherichia coli}
mvkevnvpdiggdevevtevmvkvgdkvaaeqslitvegdkasmevpapfagvvkelkvn
vgdkvktgslimifevegaa
>d1fyc__ 2.79.1.1.6 Ipoyl domain of dihydrolipoamide acetyltransferase {Human (Homo sapiens)}
gsnmsypphmqvllpalsptmtmgtvqrwekkvgeklsegdllaeietdkatigfevqee
gylakilvpegtrdvplgtplciivekeadisafadyrptevtdlk
>d1ghj__ 2.79.1.1.7 Lipoyl domain of the 2-oxoglutarate dehydrogenase complex {Azotobacter vinelandii}
aidikaptfpesiadgtvatwhkkpgeavkrdelivdietdkvvmevlaeadgviaeivk
negdtvlsgellgkltegg
>d1ghk__ 2.79.1.1.7 Lipoyl domain of the 2-oxoglutarate dehydrogenase complex {Azotobacter vinelandii}
aidikaptfpesiadgtvatwhkkpgeavkrdelivdietdkvvmevlaeadgviaeivk
negdtvlsgellgkltegg
>d1pmr__ 2.79.1.1.8 Lipoyl domain of the 2-oxoglutarate dehydrogenase complex {Escherichia coli}
ssvdilvpdlpesvadatvatwhkkpgdavvrdevlveietdkvvlevpasadgildavl
edegttvtsrqilgrlregn
>d1bnca1 2.79.2.1.1 (331-446) Biotin carboxylase subunit of acetyl-CoA carboxylase, C-terminal domain {Escherichia coli}
rghavecrinaedpntflpspgkitrfhapggfgvrweshiyagytvppyydsmigklic
ygenrdvaiarmknalqeliidgiktnvdlqirimndenfqhggtnihylekklgl
>d1gsoa1 2.79.2.1.2 (328-426) Glycinamide ribonucleotide synthetase (GAR-syn). {Escherichia coli}
eraslgvvmaaggypgdyrtgdvihglpleevaggkvfhagtkladdeqvvtnggrvlcv
talghtvaeaqkrayalmtdihwddcfcrkdigwraier
>d1b6ra1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1b6sa1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1b6sb1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1b6sc1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1b6sd1 2.79.2.1.3 (277-355) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
nnpsvminligsdvnydwlklplvhlhwydkevrpgrkvghlnltdsdtsrltatleali
pllppeyasgviwaqskfg
>d1ctm_2 2.79.2.2.1 (168-230) Cytochrome f, small domain {Turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1hcz_2 2.79.2.2.1 (168-230) Cytochrome f, small domain {Turnip (Brassica rapa)}
ntvynataggiiskilrkekggyeitivdasnerqvidiiprglellvsegesikldqpl
tsn
>d1cfma2 2.79.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1cfmb2 2.79.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1cfmc2 2.79.2.2.2 (169-232) Cytochrome f, small domain {Chlamydomonas reinhardtii}
tiynasaagkivaitalsekkggfevsiekangevvvdkipagpdlivkegqtvqadqpl
tnnp
>d1ci3m2 2.79.2.2.3 (170-231) Cytochrome f, small domain {Phormidium laminosum}
avynasaagvitaiakaddgsaevkirtedgttivdkipagpelivsegeevaagaaltn
np
>d1gpr__ 2.79.3.1.1 Glucose permease IIa domain, IIa-glc {Bacillus subtilis}
eplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgkilnv
fptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldavkpn
vpslmtpivftnlaegetvsikasgsvnreqedivkie
>d2gpr__ 2.79.3.1.1 Glucose permease IIa domain, IIa-glc {Bacillus subtilis}
mwffnknlkvlapcdgtiitldevedevfkermlgdgfainpksndfhapvsgklvtafp
tkhafgiqtksgveillhigldtvsldgngfesfvtqdqevnagdklvtvdlksvakkvp
sikspiiftnnggktleivkmgevkqgdvvailk
>d2f3ga_ 2.79.3.1.2 Glucose-specific factor III (glsIII) {Escherichia coli}
tieiiaplsgeivniedvpdvvfaekivgdgiaikptgnkmvapvdgtigkifetnhafs
iesdsgvelfvhfgidtvelkgegfkriaeegqrvkvgdtviefdlplleekakstltpv
visnmdeikeliklsgsvtvgetpvirikk
>d1ame__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1b7ia_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vrgyaa
>d1b7ja_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlammrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1b7ka_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnhavplgttlmpdm
vkgyaa
>d1ekla_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipakdiprlvsmqvnravplgttlmpdm
vkgyaa
>d1gzi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1jaba_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintalslvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1kde__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1kdf__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
nqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdmv
kgyaa
>d1msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
aaqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1msja_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipinvaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1ops__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
sqsvvatqlipmntaltpammegkvtnpigipfaemsqlvgkqvntpvakgqtlmpnmvk
tyaa
>d2amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipiqtaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d2jiaa_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vigyaa
>d2msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipintmltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d2msja_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvsravplgttlmpdm
vkgyaa
>d2spga_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipinsaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d3amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvantlipintaltlvmmrsevvtpvgipaediprlvsmtvnravplgttlmpdm
vkgyaa
>d3msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipinthltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d4amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintalalvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d4msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipinttltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d5msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipintcltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d6amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvamrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d6msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipintrltlvmmrsevvtpvgipaedipalvsmqvnravplgttlmpdm
vkgyaa
>d7amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipinaaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d7msi__ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
maqasvvanqlipintyltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d8amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipisthltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d8msia_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipistaltlvmmrsevvtpvgipaediprlvsmtvnravplgttlmpdm
vkgyaa
>d9amea_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvgmqvnravplgttlmpdm
vkgyaa
>d9msia_ 2.80.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintalnlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d3nla__ 2.80.1.1.2 Antifreeze protein type III {Antarctic eel pout (Lycodichthys dearborni)}
nkasvvanqlipintaltlimmkaevvtpmgipaeeipnlvgmqvnravplgttlmpdmv
knyedgttspglk
>d3rdn__ 2.80.1.1.2 Antifreeze protein type III {Antarctic eel pout (Lycodichthys dearborni)}
nkasvvanqlipintaltlimmkaevvtpmgipaeeipnlvgmqvnravplgttlmpdmv
knyedgttspglk
>d1fwab_ 2.80.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1ubpb_ 2.80.2.1.2 Urease, beta-subunit {Bacillus pasteurii}
nyivpgeyrvaegeieinagrekttirvsntgdrpiqvgshihfvevnkellfdraegig
rrlnipsgtaarfepgeemeveltelggnrevfgisdltngsvdnkelilqrakelgykg
ve
>d1dupa_ 2.80.3.1.1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Escherichia coli}
mmkkidvkildprvgkefplptyatsgsagldlraclndavelapgdttlvptglaihia
dpslaammlprsglghkhgivlgnlvglidsdyqgqlmisvwnrgqdsftiqpgeriaqm
ifvpvvqaefnlvedf
>d1duta_ 2.80.3.1.2 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Feline immunodeficiency virus, FIV}
miiegdgildkrsedagydllaakeihllpgevkviptgvklmlpkgywgliigkssigs
kgldvlggvidegyrgeigviminvsrksitlmerqkiaqliilpckhevleqgkvv
>d1dun__ 2.80.3.1.3 Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) {Equine infectious anemia virus, EIAV}
mlayqgtqikekrdedagfdlcvpydimipvsdtkiiptdvkiqvppnsfgwvtgkssma
kqgllinggiidegytgeiqvictnigksnikliegqkfaqliilqhhsnsrqpwdenki
>d1tul__ 2.80.4.1.1 ACMNPV telokin-like protein {Baculovirus (Autographa californica), nuclear polyhedrosis virus}
gtpdiivnaqinsedenvldfiiedeyylkkrgvgahiikvasspqlrllyknaystvsc
gnygvlcnlvqngeydlnaimfncaeiklnkgqmlfqtkiwr
>d1at0__ 2.81.1.1.1 Hedgehog {Fruit fly (Drosophila melanogaster)}
cftpestallesgvrkplgelsigdrvlsxtangqavysevilfxdrnleqxqnfvqlht
dggavltvtpahlvsvwqpesqkltfvfadrieeknqvlvrdvetgelrpqrvvkvgsvr
skgvvapltregtivvnsvaascya
>d1dfaa1 2.81.1.2.1 (1-180,416-454) PI-Scei intein {Baker's yeast (Saccharomyces cerevisiae)}
cfakgtnvlmadgsiecienievgnkvmgkdgrpreviklprgretmysvvqksqhrahk
sdssrevpellkftcnathelvvrtprsvrrlsrtikgveyfevitfemgqkkapdgriv
elvkevsksypisegperanelvesyrkasnkayfewtieardlsllgshvrkatyqtya
Xcrgfyfelqelkeddyygitlsddsdhqfllanqvvvhn
>d1am2__ 2.81.1.2.2 GyrA intein {Mycobacterium xenopi}
asitgdalvalpegesvriadivpgarpnsdnaidlkvldrhgnpvladrlfhsgehpvy
avrtveglrvtgtanhpllclvdvagvptllwklideikpgdyaviqrsafsvdcagfar
gkpefapttytvgvpglvrfleahhrdpdakaiadeltdgrfyyakvasvtdagvqpvys
lrvdtadhafitngfvshn
>d1umua_ 2.82.1.1.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsxidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipxnsayspitissedtldvfgvvihvvk
>d1b12a_ 2.82.1.2.1 Type 1 signal peptidase {Escherichia coli}
rsfiyepfqipsgsmmptlligdfilvekfaygikdpiyqktlietghpkrgdivvfkyp
edpkldyikravglpgdkvtydpvskeltiqpgcssgqacenalpvtysnvepsdfvqtf
srrnggeatsgffevpknetkengirlserketlgdvthriltvpiaqdqvgmyyqqpgq
qlatwivppgqyfmmgdnrdnsadsrywgfvpeanlvgrataiwmsfdkqegewptglrl
sriggih
>d3ezma_ 2.83.1.1.1 Cyanovirin-N {Cyanobacterium (Nostoc ellipsosporum)}
lgkfsqtcynsaiqgsvltstcertnggyntssidlnsvienvdgslkwqpsnfietcrn
tqlagsselaaecktraqqfvstkinlddhianidgtlkye
>d1lkta_ 2.84.1.1.1 Head-binding domain of phage p22 tailspike protein {Bacteriophage p22}
anvvvsnprpiftesrsfkavangkiyigqidtdpvnpanqipvyienedgshvqitqpl
iinaagkivyngqlvkivtvqghsmaiydangsqvdyianvlky
>d1qqha_ 2.85.1.1.1 E2 regulatory, transactivation domain {Human papillomavirus, type 18}
kskahkaielqmalqglaqsayktedwtlqdtceelwntepthcfkkggqtvqvyfdgnk
dncmtyvawdsvyymtdagtwdktatcvshrglyyvkegyntfyiefksecekygntgtw
evhfgnnvidcndsmcstsddtvs
>d1dtoa_ 2.85.1.1.2 E2 regulatory, transactivation domain {Human papillomavirus, type 16}
hmetlcqrlnvcqdkilthyendstdlrdhidywkhmrlecaiyykaremgfkhinhqvv
ptlavsknkalqaielqltletiynsqysnekwtlqdvslevyltaptgcikkhgytvev
qfdgdicntmhytnwthiyiceeasvtvvegqvdyyglyyvhegirtyfvqfkddaekys
knkvwevhaggqvilcptsvfs
>d1ubpc1 2.86.1.1.2 (1-131,435-483) alpha-Subunit of urease, composite domain {Bacillus pasteurii}
mkinrqqyaesygptvgdevrladtdlwievekdyttygdevnfgggkvlregmgengty
trtenvldllltnalildytgiykadigvkdgyivgigkggnpdimdgvtpnmivgtate
viaaegkivtaXlvlwepkffgvkadrvikggiiayaqigdpsasiptpqpvmgrrmygt
v
>d1aqt_2 2.87.1.1.1 (2-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
styhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhgheef
iylsggilevqpgnvtvladtairg
>d1bsha2 2.87.1.1.1 (1-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
amtyhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhghee
fiylsggilevqpgnvtvladtairg
>d1bsna2 2.87.1.1.1 (1-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
amtyhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhghee
fiylsggilevqpgnvtvladtairg
>d1amk__ 3.1.1.1.7 Triosephosphate isomerase {Leishmania mexicana}
sakpqpiaaanwkcngttasieklvqvfnehtishdvqcvvaptfvhiplvqaklrnpky
visaenaiaksgaftgevsmpilkdigvhwvilghserrtyygetdeivaqkvseackqg
fmviacigetlqqreanqtakvvlsqtsaiaakltkdawnqvvlayepvwaigtgkvatp
eqaqevhlllrkwvsenigtdvaaklrilyggsvnaanaatlyakpdingflvggaslkp
efrdiidatr
>d1trea_ 3.1.1.1.8 Triosephosphate isomerase {Escherichia coli}
mrhplvmgnwklngsrhmvhelvsnlrkelagvagcavaiappemyidmakreaegshim
lgaqnvnlnlsgaftgetsaamlkdigaqyiiighserrtyhkesdeliakkfavlkeqg
ltpvlcigeteaeneagkteevcarqidavlktqgaaafegaviayepvwaigtgksatp
aqaqavhkfirdhiakvdaniaeqviiqyggsvnasnaaelfaqpdidgalvggaslkad
afavivkaaeaakqa
>d2btma_ 3.1.1.1.10 Triosephosphate isomerase {Bacillus stearothermophilus}
rkpiiagnwkmngtlaeavqfvedvkghvppadevisvvcapflfldrlvqaadgtdlki
gaqtmhfadqgaytgevspvmlkdlgvtyvilghserrqmfaetdetvnkkvlaaftrgl
ipiiccgesleereagqtnavvasqvekalagltpeqvkqaviayepiwaigtgksstpe
dansvcghirsvvsrlfgpeaaeairiqyggsvkpdnirdflaqqqidgalvggaslepa
sflqlveagrh
>d1rpxa_ 3.1.2.1.1 D-ribulose-5-phosphate 3-epimerase {Potato (Solanum tuberosum)}
srvdkfsksdiivspsilsanfsklgeqvkaieqagcdwihvdvmdgrfvpnitigplvv
dslrpitdlpldvhlmivepdqrvpdfikagadivsvhceqsstihlhrtinqikslgak
agvvlnpgtpltaieyvldavdlvlimsvnpgfggqsfiesqvkkisdlrkicaerglnp
wievdggvgpknaykvieaganalvagsavfgapdyaeaikgiktskrpe
>d1pii_1 3.1.2.2.1 (1-254) N-(5'phosphoribosyl)antranilate isomerase, PRAI {Escherichia coli}
mqtvlakivadkaiwvearkqqqplasfqnevqpstrhfydalqgartafileckkasps
kgvirddfdpariaaiykhyasaisvltdekyfqgsfnflpivsqiapqpilckdfiidp
yqiylaryyqadacllmlsvldddqyrqlaavahslemgvltevsneeeqeraialgakv
vginnrdlrdlsidlnrtrelapklghnvtvisesgintyaqvrelshfangfligsalm
ahddlhaavrrvll
>d1nsj__ 3.1.2.2.2 N-(5'phosphoribosyl)antranilate isomerase, PRAI {Thermotoga maritima}
mvrvkicgitnledalfsvesgadavgfvfypkskryispedarrisvelppfvfrvgvf
vneepekildvasyvqlnavqlhgeepielcrkiaerilvikavgvsnerdmeralnyre
fpilldtktpeyggsgktfdwslilpyrdrfrylvlsgglnpenvrsaidvvrpfavdvs
sgveafpgkkdhdsikmfiknakgl
>d1pii_2 3.1.2.2.3 (255-452) Indole-3-glycerophosphate synthase, IPGS {Escherichia coli}
genkvcgltrgqdakaaydagaiygglifvatsprcvnveqaqevmaaaplqyvgvfrnh
diadvvdkakvlslaavqlhgneeqlyidtlrealpahvaiwkalsvgetlparefqhvd
kyvldngqggsgqrfdwsllngqslgnvllagglgadncveaaqtgcagldfnsavesqp
gikdarllasvfqtlray
>d1a53__ 3.1.2.2.4 Indole-3-glycerophosphate synthase, IPGS {Sulfolobus solfataricus}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d2tysa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplad
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d2tpsa_ 3.1.3.1.1 Thiamin phosphate synthase {Bacillus subtilis}
hgirmtrisremmkellsvyfimgsnntkadpvtvvqkalkggatlyqfrekggdaltge
arikfaekaqaacreagvpfivnddvelalnlkadgihigqedanakevraaigdmilgv
sahtmsevkqaeedgadyvglgpiyptetkkdtravqgvslieavrrqgisipivgiggi
tidnaapviqagadgvsmisaisqaedpesaarkfreeiqtyktgr
>d2dora_ 3.1.4.1.1 Dihydroorotate dehydrogenase A {Lactococcus lactis}
mlnttfanakfanpfmnasgvhcmtiedleelkasqagayitksstlekregnplpryvd
lelgsinsmglpnlgfdyyldyvlknqkenaqegpiffsiagmsaaeniamlkkiqesdf
sgitelnlscpnvpgkpqlaydfeatekllkevftfftkplgvklppyfdlvhfdimaei
lnqfpltyvnsvnsignglfidpeaesvvikpkdgfggiggayikptalanvrafytrlk
peiqiigtggietgqdafehllcgatmlqigtalhkegpaifdriikeleeimnqkgyqs
iadfhgklksl
>d1oyb__ 3.1.4.1.2 Old yellow enzyme (OYE) {Brewer's yeast (Saccharomyces carlsbergensis)}
sfvkdfkpqalgdtnlfkpikignnellhravippltrmralhpgnipnrdwaveyytqr
aqrpgtmiitegafispqaggydnapgvwseeqmvewtkifnaihekksfvwvqlwvlgw
aafpdnlardglrydsasdnvfmdaeqeakakkannpqhsltkdeikqyikeyvqaakns
iaagadgveihsangyllnqfldphsntrtdeyggsienrarftlevvdalveaighekv
glrlspygvfnsmsggaetgivaqyayvagelekrakagkrlafvhlveprvtnpflteg
egeyeggsndfvysiwkgpviragnfalhpevvreevkdkrtligygrffisnpdlvdrl
ekglplnkydrdtfyqmsahgyidyptyeealklgwdkk
>d1gox__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1djna1 3.1.4.1.6 (1-340) Trimethylamine dehydrogenase, N-terminal domain {Methylophilus methylotrophus w3a1}
ardpkhdilfepiqigpktlrnrfyqvphcigagsdkpgfqsahrsvkaeggwaalntey
csinpesddthrlsariwdegdvrnlkamtdevhkygalagvelwyggahapnmesratp
rgpsqyasefetlsyckemdlsdiaqvqqfyvdaakrsrdagfdivyvygahsylplqfl
npyynkrtdkyggslenrarfwletlekvkhavgsdcaiatrfgvdtvygpgqieaevdg
qkfvemadslvdmwditigdiaewgedagpsrfyqqghtipwvklvkqvskkpvlgvgry
tdpekmieivtkgyadiigcarpsiadpflpqkveqgryd
>d1bd0a2 3.1.5.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d7odca2 3.1.5.1.2 (44-283) Eukaryotic ornithine decarboxylase {Mouse (Mus musculus)}
dlgdilkkhlrwlkalprvtpfyavkcndsraivstlaaigtgfdcaskteiqlvqglgv
paerviyanpckqvsqikyaasngvqmmtfdseielmkvarahpkaklvlriatddskav
crlsvkfgatlktsrlllerakelnidvigvsfhvgsgctdpdtfvqavsdarcvfdmat
evgfsmhlldigggfpgsedtklkfeeitsvinpaldkyfpsdsgvriiaepgryyvasa
>d1ct5a_ 3.1.5.2.1 "Hypothetical" protein ybl036c {Baker's yeast (Saccharomyces cerevisiae)}
tgitydedrktqliaqyesvrevvnaeaknvhvnenaskilllvvsklkpasdiqilydh
gvrefgenyvqeliekakllpddikwhfigglqtnkckdlakvpnlysvetidslkkakk
lnesrakfqpdcnpilcnvqintshedqksglnneaeifevidfflseeckyiklnglxt
igswnvshedskenrdfatlvewkkkidakfgtslklsxgxsadfreairqgtaevrigt
difg
>d1frb__ 3.1.6.1.1 FR-1 (fibroblast growth factor-induced) protein {Mouse (Mus musculus)}
atfvelstkakmpivglgtwksppnqvkeavkaaidagyrhidcayaycnenevgeaiqe
kikekavqredlfivsklwptcfekkllkeafqktltdlkldyldlylihwpqglqpgke
lfpkddqgriltskttfleawegmeelvdqglvkalgvsnfnhfqierllnkpglkhkpv
tnqvechpyltqekliqychskgisvtaysplgspdrpsakpedpslledpkikeiaakh
ektsaqvlirfhiqrnvvvipksvtpsriqeniqvfdfqlsdeematilsfnrnwracll
petvnmeeypydaey
>d1qrqa_ 3.1.6.1.2 Voltage-dependent K+ channel beta subunit {Rat (Rattus norvegicus)}
lqfyrnlgksglrvsclglgtwvtfggqitdemaehlmtlaydnginlfdtaevyaagka
evvlgniikkkgwrrsslvittkifwggkaeterglsrkhiieglkaslerlqleyvdvv
fanrpdpntpmeetvramthvinqgmamywgtsrwssmeimeaysvarqfnlippiceqa
eyhmfqrekvevqlpelfhkigvgamtwsplacgivsgkydsgippysraslkgyqwlkd
kilseegrrqqaklkelqaiaerlgctlpqlaiawclrnegvssvllgasnaeqlmenig
aiqvlpklsssivheidsilgnkpy
>d1a80__ 3.1.6.1.8 2,5-diketo-D-gluconic acid reductase A {Corynebacterium}
tvpsivlndgnsipqlgygvfkvppadtqraveealevgyrhidtaaiygneegvgaaia
asgiarddlfittklwndrhdgdepaaaiaeslaklaldqvdlylvhwptpaadnyvhaw
ekmielraagltrsigvsnhlvphlerivaatgvvpavnqielhpayqqreitdwaaahd
vkieswgplgqgkydlfgaepvtaaaaahgktpaqavlrwhlqkgfvvfpksvrrerlee
nldvfdfdltdteiaaidamdpgdgsgrvsahpdevd
>d1ak5_1 3.1.6.2.1 (2-101,222-483) Inosine monophosphate dehydrogenase (IMPDH) {Tritrichomonas foetus}
akyynepchtfneyllipglstvdcipsnvnlstplvkfqkgqqseinlkiplvsaimqs
vsgekmaialareggisfifgsqsiesqaamvhavknfkaXhnelvdsqkrylvgagint
rdfrervpalveagadvlcidssdgfsewqkitigwirekygdkvkvgagnivdgegfry
ladagadfikigigggsicitreqkgigrgqatavidvvaernkyfeetgiyipvcsdgg
ivydyhmtlalamgadfimlgryfarfeesptrkvtingsvmkeywgegssrarnwqryd
lggkqklsfeegvdsyvpyagklkdnveaslnkvkstmcncgaltipqlqskakitlvss
vsi
>d1b3oa1 3.1.6.2.2 (10-109,232-499) Inosine monophosphate dehydrogenase (IMPDH) {Human (Homo sapiens)}
tsyvpddgltaqqlfncgdgltyndflilpgyidftadqvdltsaltkkitlktplvssp
mdtvteagmaiamaltggigfihhnctpefqanevrkvkkXdyplaskdakkqllcgaai
gtheddkyrldllaqagvdvvvldssqgnsifqinmikyikdkypnlqviggnvvtaaqa
knlidagvdalrvgmgsgsicitqevlacgrpqatavykvseyarrfgvpviadggiqnv
ghiakalalgastvmmgsllaatteapgeyffsdgirlkkyrgmgsldamdkhlssqnry
fseadkikvaqgvsgavqdkgsihkfvpyliagiqhscqdigaksltqvrammysgelkf
ekrtssaqv
>d1bli_2 3.1.7.1.1 (3-393) Bacterial alpha-amylase (BLA) {Bacillus licheniformis}
lngtlmqyfewympndgqhwkrlqndsaylaehgitavwippaykgtsqadvgygaydly
dlgefhqkgtvrtkygtkgelqsaikslhsrdinvygdvvinhkggadatedvtavevdp
adrnrvisgehlikawthfhfpgrgstysdfkwhwyhfdgtdwdesrklnriykfqgkaw
dwevsnefgnydylmyadidydhpdvaaeikrwgtwyanelqldgfrldavkhikfsflr
dwvnhvrektgkemftvaeywsydlgalenylnktnfnhsvfdvplhyqfhaastqgggy
dmrkllngtvvskhplksvtfvdnhdtqpgqslestvqtwfkplayafiltresgypqvf
ygdmygtkgdsqreipalkhkiepilkarkq
>d1bag_2 3.1.7.1.3 (1-347) Bacterial alpha-amylase (BLA) {Bacillus subtilis}
ltapsiksgtilhawnwsfntlkhnmkdihdagytaiqtspinqvkegnqgdksmsnwyw
lyqptsyqignrylgteqefkemcaaaeeygikvivdavinhttfdyaaisnevksipnw
thgntqiknwsdrwdvtqnsllglydwntqntqvqsylkrfleralndgadgfrfdaakh
ielpddgsygsqfwpnitntsaefqygqilqdsasrdaayanymdvtasnyghsirsalk
nrnlgvsnishyasdvsadklvtwveshdtyanddeestwmsdddirlgwaviasrsgst
plffsrpegggngvrfpgksqigdrgsalfedqaitavnrfhnvmag
>d1pama4 3.1.7.1.6 (1-406) Cyclodextrin glycosyltransferase {Alkalophilic bacillus, sp. 1011}
apdtsvsnkqnfstdviyqiftdrfsdgnpannptgaafdgsctnlrlycggdwqgiink
indgyltgmgitaiwisqpveniysvinysgvnntayhgywardfkktnpaygtmqdfkn
lidtahahnikviidfapnhtspassddpsfaengrlydngnllggytndtqnlfhhygg
tdfstiengiyknlydladlnhnnssvdvylkdaikmwldlgvdgirvdavkhmpfgwqk
sfmatinnykpvftfgewflgvneispeyhqfanesgmslldfrfaqkarqvfrdntdnm
yglkamlegsevdyaqvndqvtfidnhdmerfhtsngdrrkleqalaftltsrgvpaiyy
gseqymsggndpdnrarlpsfsttttayqviqklaplrksnpaiay
>d1jae_2 3.1.7.1.10 (2-378) Animal alpha-amylase {Yellow mealworm (Tenebrio molitor), larva}
kdanfasgrnsivhlfewkwndiadecerflqpqgfggvqisppneylvadgrpwweryq
pvsyiintrsgdesaftdmtrrcndagvriyvdavinhmtgmngvgtsgssadhdgmnyp
avpygsgdfhspcevnnyqdadnvrncelvglrdlnqgsdyvrgvlidymnhmidlgvag
frvdaakhmspgdlsvifsglknlntdygfadgarpfiyqevidlggeaiskneytgfgc
vlefqfgvslgnafqggnqlknlanwgpewgllegldavvfvdnhdnqrtggsqiltykn
pkpykmaiafmlahpygttrimssfdftdndqgppqdgsgnlispginddntcsngyvce
hrwrqvygmvgfrnave
>d7taa_2 3.1.7.1.12 (1-381) Fungal alpha-amylases {Aspergillus oryzae, Taka-amylase}
atpadwrsqsiyflltdrfartdgsttatcntadqkycggtwqgiidkldyiqgmgftai
witpvtaqlpqttaygdayhgywqqdiyslnenygtaddlkalssalhergmylmvdvva
nhmgydgagssvdysvfkpfssqdyfhpfcfiqnyedqtqvedcwlgdntvslpdldttk
dvvknewydwvgslvsnysidglridtvkhvqkdfwpgynkaagvycigevldgdpaytc
pyqnvmdgvlnypiyypllnafkstsgsmddlynmintvksdcpdstllgtfvenhdnpr
fasytndialaknvaafiilndgipiiyagqeqhyaggndpanreatwlsgyptdselyk
liasanairnyaiskdtgfvt
>d1bvza3 3.1.7.1.13 (121-502) Alpha-amylase II (TVAII), central domain {Thermoactinomyces vulgaris, r-47}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrldvanevdhafwrefrrlvkslnpdalivgeiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
dterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr
>d1bf2_3 3.1.7.1.14 (163-637) Isoamylase, central domain {Pseudomonas amyloderamosa}
pstqstgtkptraqkddviyevhvrgfteqdtsipaqyrgtyygaglkasylaslgvtav
eflpvqetqndandvvpnsdanqnywgymtenyfspdrryaynkaaggptaefqamvqaf
hnagikvymdvvynhtaeggtwtssdpttatiyswrgldnatyyeltsgnqyfydntgig
anfntyntvaqnlivdslaywantmgvdgfrfdlasvlgnsclngaytasapncpnggyn
fdaadsnvainrilreftvrpaaggsgldlfaepwaiggnsyqlggfpqgwsewnglfrd
slrqaqnelgsmtiyvtqdandfsgssnlfqssgrspwnsinfidvhdgmtlkdvyscng
annsqawpygpsdggtstnyswdqgmsagtgaavdqrraartgmafemlsagtplmqggd
eylrtlqcnnnaynldssanwltyswttdqsnfytfaqrliafrkahpalrpssw
>d1jdc_2 3.1.7.1.15 (1-357) G4-amylase (1,4-alpha-D-glucan maltotetrahydrolase) {Pseudomonas stutzeri}
dqagkspnavryhggdeiilqgfhwnvvreapndwynilrqqaatiaadgfsaiwmpvpw
rdfsswsdgsksgggegyfwhdfnkngrygsdaqlrqaasalggagvkvlydvvpnhmnr
gypdkeinlpagqgfwrndcadpgnypndcddgdrfiggdadlntghpqvygmfrdeftn
lrsqygaggfrfdfvrgyapervnswmtdsadnsfcvgqlwkgpseypnwdwrntaswqq
iikdwsdrakcpvfdfalkermqngsiadwkhglngnpdprwrevavtfvdnhdtgyspg
qnggqhhwalqdglirqayayiltspgtpvvywdhmydwgygdfirqliqvrraagv
>d1avaa2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1uok_2 3.1.7.1.17 (1-479) Oligo-1,6, glucosidase {Bacillus cereus}
mekqwwkesvvyqiyprsfmdsngdgigdlrgiiskldylkelgidviwlspvyespndd
ngydisdyckimnefgtmedwdellhemhernmklmmdlvvnhtsdehnwfiesrkskdn
kyrdyyiwrpgkegkepnnwgaafsgsawqydemtdeyylhlfskkqpdlnwdnekvrqd
vyemmkfwlekgidgfrmdvinfiskeeglptveteeegyvsghkhfmngpnihkylhem
neevlshydimtvgempgvtteeaklytgeerkelqmvfqfehmdldsgeggkwdvkpcs
lltlkenltkwqkalehtgwnslywnnhdqprvvsrfgndgmyriesakmlatvlhmmkg
tpyiyqgeeigmtnvrfesideyrdietlnmykekvmergediekvmqsiyikgrdnart
pmqwddqnhagfttgepwitvnpnykeinvkqaiqnkdsifyyykklielrknneivvy
>d1byb__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
snmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgp
kqydwrayrslfqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifyt
nrsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpa
gelrypsypqsqgwefprigefqcydkylkadfkaavaraghpewelpddagkyndvpes
tgffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwyk
venhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvq
qvlsggwredirvagenalprydataynqiilnakpqgvnnngppklsmfgvtylrlsdd
llqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfp
wlpetdmkvdg
>d1b9za2 3.1.7.2.3 (1-417) Bacterial beta-amylase, catalytic domain {Bacillus cereus}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaitvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakiylsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvtftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv
>d1edg__ 3.1.7.3.3 Endoglucanase CelA {Clostridium cellulolyticum}
mydaslipnlqipqknipnndgmnfvkglrlgwnlgntfdafngtnitneldyetswsgi
kttkqmidaikqkgfntvripvswhphvsgsdykisdvwmnrvqevvnycidnkmyviln
thhdvdkvkgyfpssqymasskkyitsvwaqiaarfanydehlifegmneprlvghanew
wpeltnsdvvdsincinqlnqdfvntvratggknasrylmcpgyvaspdgatndyfrmpn
disgnnnkiivsvhaycpwnfaglamadggtnawnindskdqsevtwfmdniynkytsrg
ipviigecgavdknnlktrveymsyyvaqakargilcilwdnnnfsgtgelfgffdrrsc
qfkfpeiidgmvkyafglin
>d1ceo__ 3.1.7.3.5 Endoglucanase CelC {Clostridium thermocellum}
mvsfkaginlggwisqyqvfskehfdtfitekdietiaeagfdhvrlpfdypiiesddnv
geykedglsyidrclewckkynlglvldmhhapgyrfqdfktstlfedpnqqkrfvdiwr
flakryinerehiafellnqvvepdstrwnklmlecikaireidstmwlyiggnnynspd
elknladidddyivynfhfynpfffthqkahwsesamaynrtvkypgqyegieefvknnp
kysfmmelnnlklnkellrkdlkpaiefrekkkcklycgefgviaiadlesrikwhedyi
slleeydiggavwnykkmdfeiynedrkpvsqelvnilar
>d1ecea_ 3.1.7.3.6 Endocellulase E1 {Acidothermus cellulolyticus}
agggywhtsgreildannvpvriaginwfgfetcnyvvhglwsrdyrsmldqikslgynt
irlpysddilkpgtmpnsinfyqmnqdlqgltslqvmdkivayagqiglriildrhrpdc
sgqsalwytssvseatwisdlqalaqrykgnptvvgfdlhnephdpacwgcgdpsidwrl
aaeragnavlsvnpnllifvegvqsyngdsywwggnlqgagqypvvlnvpnrlvysahdy
atsvypqtwfsdptfpnnmpgiwnknwgylfnqniapvwlgefgttlqsttdqtwlktlv
qylrptaqygadsfqwtfwswnpdsgdtggilkddwqtvdtvkdgylapikssifdpv
>d7a3ha_ 3.1.7.3.7 Endoglucanase Cel5a {Bacillus agaradherans}
svveehgqlsisngelvnergeqvqlkgmsshglqwygqfvnyesmkwlrddwginvfra
amytssggyiddpsvkekvkeaveaaidldiyviidwhilsdndpniykeeakdffdems
elygdypnviyeianepngsdvtwgnqikpyaeevipiirnndpnniiivgtgtwsqdvh
haadnqladpnvmyafhfyagthgqnlrdqvdyaldqgaaifvsewgtsaatgdggvfld
eaqvwidfmdernlswanwslthkdessaalmpganptggwteaelspsgtfvrekires
>d1bqca_ 3.1.7.3.9 Beta-mannanase {Thermomonospora fusca}
atglhvkngrlyeangqefiirgvshphnwypqhtqafadikshgantvrvvlsngvrws
kngpsdvanvislckqnrlicmlevhdttgygeqsgastldqavdywielksvlqgeedy
vlinignepygndsatvaawatdtsaaiqrlraagfehtlvvdapnwgqdwtntmrnnad
qvyasdptgntvfsihmygvysqastitsylehfvnaglpliigefghdhsdgnpdedti
maeaerlklgyigwswsgngggveyldmvynfdgdnlspwgerifygpngiastakeavi
fg
>d1cz1a_ 3.1.7.3.10 Exo-beta-(1,3)-glucanase {Candida albicans}
awdydnnvirgvnlggwfvlepymtpslfepfqngndqsgvpvdeyhwtqtlgkeaalri
lqkhwstwiteqdfkqisnlglnfvripigywafqlldndpyvqgqvqylekalgwarkn
nirvwidlhgapgsqngfdnsglrdsynfqngdntqvtlnvlntifkkyggneysdvvig
iellneplgpvlnmdklkqffldgynslrqtgsvtpviihdafqvfgywnnfltvaegqw
nvvvdhhhyqvfsggelsrnindhisvacnwgwdakkeshwnvagewsaaltdcakwlng
vnrgaryegaydnapyigscqplldisqwsdehktdtrryieaqldafeytggwvfwswk
tenapewsfqtltynglfpqpvtdrqfpnqcgfh
>d1aq0a_ 3.1.7.3.12 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1bgla5 3.1.7.3.13 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bhga3 3.1.7.3.14 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1clxa_ 3.1.7.3.17 Xylanase A, catalytic core {Pseudomonas fluorescens}
glasladfpigvavaasggnadiftssarqnivraefnqitaenimkmsymysgsnfsft
nsdrlvswaaqngqtvhghalvwhpsyqlpnwasdsnanfrqdfarhidtvaahfagqvk
swdvvnealfdsaddpdgrgsangyrqsvfyrqfggpeyideafrraraadptaelyynd
fnteengakttalvnlvqrllnngvpidgvgfqmhvmndypsianirqamqkivalsptl
kikiteldvrlnnpydgnssndytnrndcavscagldrqkarykeivqaylevvppgrrg
gitvwgiadpdswlythqnlpdwpllfndnlqpkpayqgvveals
>d1taxa_ 3.1.7.3.18 Xylanase A, catalytic core {Thermoascus aurantiacus}
asaqsvdqlikargkvyfgvatdqnrlttgknaaiiqanfgqvtpensmkwdatepsqgn
fnfagadylvnwaqqngklirghtlvwhsqlpswvtsitdkntltnvmknhittlmtryk
gkirawdvvneafnqngslrstvflnvigedyipiafqtaraadpnaklyindynldsat
ypktqaivnrvkqwraagvpidgigsqthlsagqgagvlnalpllasagtpevaiteldv
agasptdyvnvvnaclnvsscvgitvwgvadpdswrasttpllfdgnfnpkpaynaivqn
lq
>d2myr__ 3.1.7.4.1 Myrosinase {White mustard (Sinapis alba)}
eitcqennpftcgntdglnsssfeadfifgvassayqiegtigrglniwdgfthrypdks
gpdhgngdttcdsfsywqkdidvldelnatgyrfsiawsriiprgkrsrgvnqkgidyyh
glidglikkgitpfvtlfhwdlpqtlqdeyegfldpqiiddfkdyadlcfeefgdsvkyw
ltinqlysvptrgygsaldapgrcsptvdpscyagnsstepyivahhqllahakvvdlyr
knythqggkigptmitrwflpyndtdrhsiaatermkqfflgwfmgpltngtypqimidt
vgarlptfspeetnlvkgsydflglnyyftqyaqpspnpvnatnhtammdagakltyina
sghyigplfesdggdgssniyyypkgiysvmdyfknkyynpliyvtengistpgsenrke
smldytridylcshlcflnkvikekdvnvkgylawalgdnyefnngftvrfglsyinwnn
vtdrdlkksgqwyqkfisp
>d1pbga_ 3.1.7.4.3 6-phospho-beta-D-galactosidase, PGAL {Lactococcus lactis}
mtktlpkdfifggataayqaegathtdgkgpvawdkylednywytaepasdfyhkypvdl
elaeeygvngirisiawsrifptgygevnekgvefyhklfaechkrhvepfvtlhhfdtp
ealhsngdflnreniehfidyaafcfeefpevnywttfneigpigdgqylvgkfppgiky
dlakvfqshhnmmvsharavklykdkgykgeigvvhalptkypydpenpadvraaeledi
ihnkfildatylghysdktmegvnhilaenggeldlrdedfqaldaakdlndflginyym
sdwmqafdgeteiihngkgekgsskyqikgvgrrvapdyvprtdwdwiiypeglydqimr
vkndypnykkiyitenglgykdefvdntvyddgridyvkqhlevlsdaiadganvkgyfi
wslmdvfswsngyekryglfyvdfdtqerypkksahwykklaetqvie
>d1qvba_ 3.1.7.4.6 beta-Glycosidase {Thermosphaera aggregans}
mkfpkdfmigyssspfqfeagipgsedpnsdwwvwvhdpentaaglvsgdfpengpgywn
lnqndhdlaeklgvntirvgvewsrifpkptfnvkvpverdengsivhvdvddkaverld
elankeavnhyvemykdwvergrklilnlyhwplplwlhnpimvrrmgpdrapsgwlnee
svvefakyaayiawkmgelpvmwstmnepnvvyeqgymfvkggfppgylsleaadkarrn
miqaharaydnikrfskkpvgliyafqwfellegpaevfdkfkssklyyftdivskgssi
inveyrrdlanrldwlgvnyysrlvykivddkpiilhgygflctpggispaenpcsdfgw
evypeglylllkelynrygvdlivtengvsdsrdalrpaylvshvysvwkaanegipvkg
ylhwsltdnyewaqgfrqkfglvmvdfktkkrylrpsalvfreiathngipdelqhltli
q
>d1nar__ 3.1.7.5.2 Seed storage protein {Vicia narbonensis, Narbonin}
pkpifreyigvkpnsttlhdfpteiintetlefhyilgfaiesyyesgkgtgtfeeswdv
elfgpekvknlkrrhpevkvvisiggrgvntpfdpaeenvwvsnakeslkliiqkysdds
gnlidgidihyehirsdepfatlmgqlitelkkdddlninvvsiapsennsshyqklyna
kkdyinwvdyqfsnqqkpvstddafveifkslekdyhphkvlpgfstdpldtkhnkitrd
ifiggctrlvqtfslpgvffwnandsvipkrdgdkpfiveltlqqllaa
>d1cnv__ 3.1.7.5.3 Seed storage protein {Jack bean (Canavalia ensiformis), Concanavalin B}
dissteiavywgqredgllrdtcktnnykivfisfldkfgceirkpelelegvcgpsvgn
pcsflesqikecqrmgvkvflalggpkgtysacsadyakdlaeylhtyflserregplgk
valdgihfdiqkpvdelnwdnlleelyqikdvyqstfllsaapgclspdeyldnaiqtrh
fdyifvrfyndrscqystgniqrirnawlswtksvyprdknlflelpasqatapgggyip
psaligqvlpylpdlqtryagialwnrqadketgystniiryl
>d2ebn__ 3.1.7.5.4 Endo-beta-N-acetylglucosaminidase {Flavobacterium meningosepticum, endoglycosidase F1}
ttkaniklfsftevndtnplnnlnftlknsgkplvdmvvlfsaninydaandkvfvsnnp
nvqhlltnrakylkplqdkgikvilsilgnhdrsgianlstarakafaqelkntcdlynl
dgvffddeysayqtpppsgfvtpsnnaaarlayetkqampnklvtvyvysrtssfptavd
gvnagsyvdyaihdyggsydlatnypglaksgmvmssqefnqgryataqalrnivtkgyg
ghmifamdpnrsnftsgqlpalkliakelygdelvysntpyskdw
>d1edt__ 3.1.7.5.5 Endo-beta-N-acetylglucosaminidase {Streptomyces plicatus, endoglycosidase H}
kqgptsvayvevnnnsmlnvgkytladgggnafdvavifaaninydtgtktaylhfnenv
qrvldnavtqirplqqqgikvllsvlgnhqgagfanfpsqqaasafakqlsdavakygld
gvdfddeyaeygnngtaqpndssfvhlvtalranmpdkiislynigpaasrlsyggvdvs
dkfdyawnpyygtwqvpgialpkaqlspaaveigrtsrstvadlarrtvdegygvyltyn
ldggdrtadvsaftrelygseavrt
>d1edqa2 3.1.7.5.6 (133-443,517-563) Chitinase A, central domain {Serratia marcescens}
tdgshlaplkeplleknkpykqnsgkvvgsyfvewgvygrnftvdkipaqnlthllygfi
picggngindslkeiegsfqalqrscqgredfkvsihdpfaalqkaqkgvtawddpykgn
fgqlmalkqahpdlkilpsiggwtlsdpfffmgdkvkrdrfvgsvkeflqtwkffdgvdi
dwefpggkganpnlgspqdgetyvllmkelramldqlsvetgrkyeltsaisagkdkidk
vaynvaqnsmdhiflmsydfygafdlknlghqtalnapawkpdtayttvngvnallaqgv
kpgkivvgtamXdarsvqakgkyvldkqlgglfsweidadngdilnsmnaslgnsagvq
>d1qba_3 3.1.7.6.1 (338-780) Bacterial chitobiase, catalytic domain {Serratia marcescens}
fpyrgifldvarnfhkkdavlrlldqmaayklnkfhfhlsddegwrieipglpeltevgg
qrchdlsettcllpqygqgpdvyggffsrqdyidiikyaqarqievipeidmpaharaav
vsmearykklhaagkeqeanefrlvdptdtsnttsvqffnrqsylnpcldssqrfvdkvi
geiaqmhkeagqpiktwhfggdeaknirlgagytdkakpepgkgiidqgnedkpwaksqv
cqtmikegkvadmehlpsyfgqevsklvkahgidrmqawqdglkdaesskafatsrvgvn
fwdtlywggfdsvndwankgyevvvsnpdyvymdfpyevnpdergyywgtrfsderkvfs
fapdnmpqnaetsvdrdgnhfnaksdkpwpgayglsaqlwsetqrtdpqmeymifprals
vaerswhragweqdyragreykg
>d1ex1a1 3.1.7.7.1 (1-388) Beta-D-glucan exohydrolase, N-terminal domain {Barley (Hordeum vulgare)}
dyvlykdatkpvedrvadllgrmtlaekigqmtqierlvatpdvlrdnfigsllsgggsv
prkgatakewqdmvdgfqkacmstrlgipmiygidavhgqnnvygatifphnvglgatrd
pylvkrigeatalevratgiqyafapciavcrdprwgrcyesysedrrivqsmtelipgl
qgdvpkdftsgmpfvagknkvaacakhfvgdggtvdginenntiinreglmnihmpaykn
amdkgvstvmisysswngvkmhanqdlvtgylkdtlkfkgfvisdwegidrittpagsdy
sysvkasilagldmimvpnkyqqfisiltghvnggvipmsriddavtrilrvkftmglfe
npyadpamaeqlgkqehrdlareaarks
>d1a4ma_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1ubpc2 3.1.8.2.2 (132-434,484-570) alpha-subunit of urease, catalytic domain {Bacillus pasteurii}
ggidthvhfinpdqvdvalangittlfgggtgpaegskattvtpgpwniekmlksteglp
invgilgkghgssiapimeqidagaaglxihedwgatpasidrsltvadeadvqvaihsd
tlneagfledtlraingrvihsfhvegaggghapdimamaghpnvlpsstnptrpftvnt
idehldmlmvchhlkqnipedvafadsrirpetiaaedilhdlgiismmstdalamgrag
emvlrtwqtadkmkkqrgplaeekngsdnfrlkryvskytinpaiaqgiahevgsieegk
fadXgdlihdtnitfmskssiqqgvpaklglkrrigtvkncrnigkkdmkwndvttdidi
npetyevkvdgevltcepvkelpmaqryflf
>d1psca_ 3.1.8.3.1 Phosphotriesterase {Pseudomonas diminuta}
drintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr
>d1bf6a_ 3.1.8.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1nal1_ 3.1.9.1.1 N-acetylneuraminate lyase {Escherichia coli}
nlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereqvl
eivaeegkgkikliahvgcvttaesqqlaasakrygfdavsavtpfyypfsfeehcdhyr
aiidsadglpmvvynipalsgvkltldqintlvtlpgvgalkqtsgdlyqmeqirrehpd
lvlyngydeifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnkvi
dlliktgvfrglktvlhymdvvsvplcrkpfgpvdekyqpelkalaqqlmq
>d1dhpa_ 3.1.9.1.2 Dihydrodipicolinate synthase {Escherichia coli}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll
>d1fbaa_ 3.1.9.1.4 Fructose-1,6-bisphosphate aldolase {Drosophila melanogaster, strain sevelen (wild type, pupea)}
xttyfnypskelqdelreiaqkivapgkgilaadesgptmgkrlqdigventednrrayr
qllfstdpklaenisgvilfhetlyqkaddgtpfaeilkkkgiilgikvdkgvvplfgse
devttqglddlaarcaqykkdgcdfakwrcvlkigkntpsyqsilenanvlaryasicqs
qrivpivepevlpdgdhdldraqkvtetvlaavykalsdhhvylegtllkpnmvtagqsa
kkntpeeialatvqalrrtvpaavtgvtflsggqseeeatvnlsainnvplirpwaltfs
ygralqasvlrawagkkeniaagqnellkrakangdaaqgkyvagsagagsgslfvanha
y
>d1onra_ 3.1.9.1.7 Transaldolase {Escherichia coli}
tdkltslrqyttvvadtgdiaamklyqpqdattnpslilnaaqipeyrkliddavawakq
qsndraqqivdatdklavnigleilklvpgristevdarlsydteasiakakrliklynd
agisndriliklastwqgiraaeqlekegincnltllfsfaqaracaeagvflispfvgr
ildwykantdkkeyapaedpgvvsvseiyqyykehgyetvvmgasfrnigeilelagcdr
ltiapallkelaesegaierklsytgevkarpariteseflwqhnqdpmavdklaegirk
faidqeklekmigdll
>d1dosa_ 3.1.9.2.1 Fructose-bisphosphate aldolase {Escherichia coli}
skifdfvkpgvitgddvqkvfqvakennfalpavncvgtdsinavletaakvkapvivqf
snggasfiagkgvksdvpqgaailgaisgahhvhqmaehygvpvilhtdhcakkllpwid
glldagekhfaatgkplfsshmidlseeslqenieicskylermskigmtleielgctgg
eedgvdnshmdasalytqpedvdyaytelskisprftiaasfgnvhgvykagnvvltpti
lrdsqeyvskkhnlphnslnfvfhggsgstaqeikdsvsygvvkmnidtdtqwatwegvl
nyykaneaylqgqlgnpkgedqpnkkyydprvwlragqtsmiarlekafqelnaidvl
>d1ylva_ 3.1.9.3.1 5-aminolevulinate dehydratase, ALAD (porphobilinogen synthase) {Baker's yeast (Saccharomyces cerevisiae)}
mhtaefletepteissvlaggynhpllrqwqserqltknmlifplfisdnpddfteidsl
pninrigvnrlkdylkplvakglrsvilfgvplipgtkdpvgtaaddpagpviqgikfir
ekfpelyiicdvclceytshghcgvlyddgtinrersvsrlaavavnyakagahcvapsd
midgrirdikrglinanlahktfvlsyaakfsgnlygpfrdaacsapsngdrkcyqlppa
grglarralerdmsegadgiivkpstfyldimrdaseickdlpicayhvsgeyamlhaaa
ekgvvdlktiafeshtgflragarliitylapefldwldee
>d1b4ka_ 3.1.9.3.2 5-aminolevulinate dehydratase, ALAD (porphobilinogen synthase) {Pseudomonas aeruginosa}
ypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsidqll
ieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgiitdva
ldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigaireal
esaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhevaad
laegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesviles
ltafkragadgiltyfakqaaeqlrr
>d1qr7a_ 3.1.9.4.1 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase {Escherichia coli}
lrikeikellppvallekfpatenaantvaharkaihkilkgnddrllvvigpcsihdpv
aakeyatrllalreelkdeleivmrvyfekprttvgwkglindphmdnsfqindglriar
kllldindsglpaagefldmitpqyladlmswgaigarttesqvhrelasglscpvgfkn
gtdgtikvaidainaagaphcflsvtkwghsaivntsgngdchiilrggkepnysakhva
evkeglnkaglpaqvmidfshansskqfkkqmdvcadvcqqiaggekaiigvmveshlve
gnqslesgeplaygksitdacigwedtdallrqlanavkarrg
>d1onea1 3.1.10.1.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl
>d1bqg_1 3.1.10.2.1 (144-422) D-glucarate dehydratase {Pseudomonas putida}
egqqrdavemlgylfyvgdrnktdlgyrseheadnewfrlrnkealtpesvvalaeaayd
rygfkdfklkggvlrgedeiaavtalserfpdaritldpngawslkeavalcrdqhhvla
yaedpcgaengysgrevmaefrrstglrtatnmiatdwrqmghaiqlqsvdipladphfw
tmqgsvrvaqmcnewgltwgshsnnhfdislamfthvaaaapgnitaidthwiwqdgqrl
tkeplqikgglvevpkkpglgveldwdalmkahevyksm
>d1muca1 3.1.10.2.2 (131-372) Muconate-lactonizing enzyme {Pseudomonas putida}
rvrdslevawtlasgdtardiaearhmleirrhrvfklkiganpveqdlkhvvtikrelg
dsasvrvdvnqywdesqairacqvlgdngidlieqpisrinrggqvrlnqrtpapimade
siesvedafslaadgaasifalkiaknggpravlrtaqiaeaagiglyggtmlegsigtl
asahafltlrqltwgtelfgplllteeivneppqyrdfqlhiprtpglgltldeqrlarf
ar
>d2mnr_1 3.1.10.2.3 (133-359) Mandelate racemase {Pseudomonas putida}
pvqaydshsldgvklateravtaaelgfravktkigypaldqdlavvrsirqavgddfgi
mvdynqsldvpaaikrsqalqqegvtwieeptlqhdyeghqriqsklnvpvqmgenwlgp
eemfkalsigacrlampdamkiggvtgwirasalaqqfgipmsshlfqeisahllaatpt
ahwlerldlagsvieptltfeggnavipdlpgvgiiwrekeigkylv
>d1a49a2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1dik_1 3.1.11.2.1 (510-874) Pyruvate phosphate dikinase, C-terminal domain {Escherichia coli}
ietqeasvsgsferimvwadkfrtlkvrtnadtpedtlnavklgaegiglcrtehmffea
drimkirkmilsdsveareealnelipfqkgdfkamykalegrpmtvryldpplhefvph
teeeqaelaknmgltlaevkakvdelhefnpmmghrgcrlavtypeiakmqtravmeaai
evkeetgidivpeimiplvgekkelkfvkdvvvevaeqvkkekgsdmqyhigtmieipra
altadaiaeeaeffsfgtndltqmtfgfsrddagkfldsyykakiyesdpfarldqtgvg
qlvemavkkgrqtrpglkcgicgehggdpssvefchkvglnyvscspfrvpiarlaaaqa
alnnk
>d1fiy__ 3.1.11.3.1 Phosphoenolpyruvate carboxylase {Escherichia coli}
qysalrsnvsmlgkvlgetikdalgehilervetirklskssragndanrqellttlqnl
sndellpvarafsqflnlantaeqyhsispkgeaasnpeviartlrklknqpelsedtik
kaveslslelvltahpteitrrtlihkmvevnaclkqldnkdiadyehnqlmrrlrqlia
qswhtdeirklrpspvdeakwgfavvenslwqgvpnylrelneqleenlgyklpvefvpv
rftswmggdrdgnpnvtaditrhvlllsrwkatdlflkdiqvlvselsmveatpellalv
geegaaepyrylmknlrsrlmatqawlearlkgeelpkpeglltqneelweplyacyqsl
qacgmgiiangdlldtlrrvkcfgvplvridirqestrhtealgeltrylgigdyeswse
adkqaflirelnskrpllprnwqpsaetrevldtcqviaeapqgsiaayvismaktpsdv
lavhlllkeagigfampvaplfetlddlnnandvmtqllnidwyrgliqgkqmvmigysd
sakdagvmaaswaqyqaqdaliktcekagieltlfhgrggsigrggapahaallsqppgs
lkgglrvteqgemirfkyglpeitvsslslytgaileanllpppepkeswrrimdelsvi
scdvyrgyvrenkdfvpyfrsatpeqelgklplgsrpakrrptggveslraipwifawtq
nrlmlpawlgagtalqkvvedgkqseleamcrdwpffstrlgmlemvfakadlwlaeyyd
qrlvdkalwplgkelrnlqeedikvvlaiandshlmadlpwiaesiqlrniytdplnvlq
aellhrsrqaekegqepdprveqalmvtiagiaagmrntg
>d1d8ca_ 3.1.12.1.1 Malate synthase G {Escherichia coli}
qtitqsrlridanfkrfvdeevlpgtgldaaafwrnfdeivhdlapenrqllaerdriqa
aldewhrsnpgpvkdkaayksflrelgylvpqpervtvettgidseitsqagpqlvvpax
naryalnaanarwgslydalygsdiipqegaxvsgydpqrgeqviawvrrfldeslplen
gsyqdvvafkvvdkqlriqlkngkettlrtpaqfvgyrgdaaaptcillknnglhielqi
dangrigkddpahindviveaaistildcedsvaavdaedkillyrnllglxqgtlqekx
ekngrqivrklnddrhytaadgseislhgrsllfirnvghlxtipviwdsegneipegil
dgvxtgaialydlkvqknsrtgsvyivkpkxhgpqevafanklftrietxlgxapntlkx
gixdeerrtslnlrsciaqarnrvafintgfldrtgdexhsvxeagpxlrknqxkstpwi
kayernnvlsglfcglrgkaqigkgxwaxpdlxadxysqkgdqlragantawvpsptaat
lhalhyhqtnvqsvqaniaqtefnaefepllddlltipvaenanwsaqeiqqeldnnvqg
ilgyvvrwveqgigcskvpdihnvalxedratlrissqhianwlrhgiltkeqvqaslen
xakvvdqqnagdpayrpxagnfanscafkaasdliflgvkqpngytepllhawrlrekes
>d1bura1 3.1.13.1.2 (148-475) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwkeikfefpamdtv
>d5ruba1 3.1.13.1.6 (138-457) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Rhodospirillum rubrum}
gpsvnisalwkvlgrpevdgglvvgtiikpklglrpkpfaeachafwlggdfikndepqg
nqpfaplrdtialvadamrraqdetgeaklfsanitaddpfeiiargeyvletfgenash
vallvdgyvagaaaittarrrfpdnflhyhraghgavtspqskrgytafvhckmarlqga
sgihtgtmgfgkmegessdraiaymltqdeaqgpfyrqswggmkactpiisggmnalrmp
gffenlgnanviltagggafghidgpvagarslrqawqawrdgvpvldyarehkelaraf
esfpgdadqiypgwrkalgv
>d1qtwa_ 3.1.14.1.1 Endonuclease IV {Escherichia coli}
mkyigahvsaagglanaairaaeidatafalftknqrqwraaplttqtidefkaacekyh
ytsaqilphdsylinlghpvtealeksrdafidemqrceqlglsllnfhpgshlmqisee
dclariaesinialdktqgvtavientagqgsnlgfkfehlaaiidgvedksrvgvcidt
chafaagydlrtpaecektfadfartvgfkylrgmhlndakstfgsrvdrhhslgegnig
hdafrwimqddrfdgipliletinpdiwaeeiawlkaqqtekava
>d1xis__ 3.1.14.2.4 D-xylose isomerase {Streptomyces rubiginosus}
nyqptpedrftfglwtvgwqgrdpfgdatrraldpvesvrrlaelgahgvtfhdddlipf
gssdsereehvkrfrqalddtgmkvpmattnlfthpvfkdggftandrdvrryalrktir
nidlavelgaetyvawggregaesggakdvrdaldrmkeafdllgeyvtsqgydirfaie
pkpneprgdillptvghalafierlerpelygvnpevgheqmaglnfphgiaqalwagkl
fhidlngqngikydqdlrfgagdlraafwlvdllesagysgprhfdfkpprtedfdgvwa
saagcmrnylilkeraaafradpevqealrasrldelarptaadglqallddrsafeefd
vdaaaargmaferldqlamdhllgarg
>d1a0ca_ 3.1.14.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1luca_ 3.1.15.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfgnflltyqppelsqtevmkrlvnlgkasegcgfdtvwllehhftefgllgnpyvaaa
hllgatetlnvgtaaivlptahpvrqaedvnlldqmskgrfrfgicrglydkdfrvfgtd
mdnsralmdcwydlmkegfnegyiaadnehikfpkiqlnpsaytqggapvyvvaesastt
ewaaerglpmilswiinthekkaqldlynevatehgydvtkidhclsyitsvdhdsnrak
dicrnflghwydsyvnatkifddsdqtkgydfnkgqwrdfvlkghkdtnrridysyeinp
vgtpeeciaiiqqdidatgidniccgfeangseeeiiasmklfqsdvmpylkekq
>d1lucb_ 3.1.15.1.1 Bacterial luciferase (alkanal monooxygenase) {Vibrio harveyi}
mkfglfflnfmnskrssdqvieemldtahyvdqlkfdtlavyenhfsnngvvgapltvag
fllgmtknakvaslnhvitthhpvrvaeeaclldqmsegrfafgfsdceksadmrffnrp
tdsqfqlfsechkiindafttgychpnndfysfpkisvnphafteggpaqfvnatskevv
ewaaklglplvfrwddsnaqrkeyaglyhevaqahgvdvsqvrhkltllvnqnvdgeaar
aearvyleefvresysntdfeqkmgellsenaigtyeestqaarvaieccgaadllmsfe
smedkaqqravidvvnaniv
>d1nfp__ 3.1.15.2.1 Non-fluorescent flavoprotein (luxF, FP390) {Photobacterium leiognathi}
mtkwnygvfflnfyhvgqqepsltmsnaletlriidedtsiydvvafsehhidksyndet
klapfvslgkqihvlatspetvvkaakygmpllfkwddsqqkriellnhyqaaaakfnvd
ianvrhrlmlfvnvndnptqakaelsiyledylsytqaetsideiinsnaagnfdtclhh
vaemaqglnnkvdflfcfesmkdqenkkslminfdkrvinyrkehnln
>d1qapa1 3.1.16.1.1 (130-296) Quinolinic acid phosphoribosyltransferase, C-terminal domain {Salmonella typhimurium}
vasevrryvgllagtqtqlldtrktlpglrtalkyavlcggganhrlgltdaflikenhi
iasgsvrqavekafwlhpdvpvevevenldelddalkagadiimldnfntdqmreavkrv
ngqarlevsgnvtaetlrefaetgvdfisvgaltkhvraldlsmrfc
>d1qpoa1 3.1.16.1.2 (117-285) Quinolinic acid phosphoribosyltransferase, C-terminal domain {Mycobacterium tuberculosis}
iatataawvdavrgtkakirdtrktlpglralqkyavrtgggvnhrlglgdaalikdnhv
aaagsvvdalravrnaapdlpcevevdsleqldavlpekpelilldnfavwqtqtavqrr
dsraptvmlessgglslqtaatyaetgvdylavgalthsvrvldigldm
>d1qasa3 3.1.17.1.1 (299-625) Phospholipase C isozyme D1 (PLC-D1) {Rat (Rattus norvegicus)}
dqplshylvssshntylledqltgpssteayiralckgcrcleldcwdgpnqepiiyhgy
tftskilfcdvlrairdyafkaspypvilslenhcsleqqrvmarhlrailgpilldqpl
dgvttslpspeqlkgkillkgkklggllpaggengseatdvsdeveaaemedeavrsqvq
hkpkedklklvpelsdmiiycksvhfggfsspgtsgqafyemasfsesralrllqesgng
fvrhnvsclsriypagwrtdssnyspvemwnggcqivalnfqtpgpemdvylgcfqdngg
cgyvlkpaflrdpnttfnsraltqgpw
>d2ptd__ 3.1.17.2.1 Phosphatidylinositol-specific phospholipase C {Bacillus cereus}
assvnelenwskwmqpipdsiplarisipgthdsgtfklqnpikqvwgmtqeydfryqmd
hgarifdirgrltddntivlhhgplylyvtlhefineakqflkdnpsetiimslkkeyed
mkgaedsfsstfekkyfvdpiflktegniklgdargkivllkrysgsnepggynnfywpd
netftttvnqnanvtvqekykvsydekvksikdtmdetmnnsedlnhlyinftslssggt
awnspyyyasyinpeianyikqknparvgwviqdyinekwspllyqeviranksli
>d2plc__ 3.1.17.2.2 Phosphatidylinositol-specific phospholipase C {Listeria monocytogenes}
vttkqwmsalpdttnlaalsipgthdtmsyngditwtltkplaqtqtmslyqqleagiry
idirakdnlniyhgpiflnaslsgvletitqflkknpketiimrlkdeqnsndsfdyriq
pliniykdyfyttprtdtsnkiptlkdvrgkilllsenhtkkplvinsrkfgmqfgapnq
viqddyngpsvktkfkeivqtayqaskadnklflnhisatsltftprqyaaalnnkveqf
vlnltsekvrglgilimdfpekqtikniiknnkf
>d7reqa1 3.1.18.1.1 (4-560) Methylmalonyl-CoA mutase, alpha and beta subunits {Propionibacterium freudenreichii, shermani}
lprfdsvdlgnapvpadaarrfeelaakagtgeawetaeqipvgtlfnedvykdmdwldt
yagippfvhgpyatmyafrpwtirqyagfstakesnafyrrnlaagqkglsvafdlpthr
gydsdnprvagdvgmagvaidsiydmrelfagipldqmsvsmtmngavlpilalyvvtae
eqgvkpeqlagtiqndilkefmvrntyiyppqpsmriiseifaytsanmpkwnsisisgy
hmqeagatadiemaytladgvdyiragesvglnvdqfaprlsffwgigmnffmevaklra
armlwaklvhqfgpknpksmslrthsqtsgwsltaqdvynnvvrtcieamaatqghtqsl
htnsldeaialptdfsariarntqlflqqesgttrvidpwsgsayveeltwdlarkawgh
iqevekvggmakaiekgipkmrieeaaartqaridsgrqpligvnkyrleheppldvlkv
dnstvlaeqkaklvklraerdpekvkaaldkitwaagnpddkdpdrnllklcidagrama
tvgemsdalekvfgryt
>d7reqb1 3.1.18.1.1 (16-475) Methylmalonyl-CoA mutase, alpha and beta subunits {Propionibacterium freudenreichii, shermani}
ltpttlslagdfpkateeqwerevekvlnrgrppekqltfaeclkrltvhtvdgidivpm
yrpkdapkklgypgvapftrgttvrngdmdawdvralhedpdekftrkaileglergvts
lllrvdpdaiapehldevlsdvllemtkvevfsrydqgaaaealvsvyersdkpakdlal
nlgldpigfaalqgtepdltvlgdwvrrlakfspdsravtidaniyhnagagdvaelawa
latgaeyvralveqgftateafdtinfrvtathdqfltiarlralreawarigevfgvde
dkrgarqnaitswreltredpyvnilrgsiatfsasvggaesittlpftqalglpeddfp
lriarntgivlaeevnigrvndpaggsyyvesltrsladaawkefqeveklggmskavmt
ehvtkvldacnaerakrlanrkqpitavsefpmigarsie
>d1dioa_ 3.1.18.2.1 Diol dehydratase, alpha subunit {Klebsiella oxytoca}
mrskrfealakrpvnqdgfvkewieegfiamespndpkpsikivngavteldgkpvsdfd
lidhfiaryginlnraeevmamdsvklanmlcdpnvkrseivplttamtpakivevvshm
nvvemmmamqkmrarrtpsqqahvtnvkdnpvqiaadaaegawrgfdeqettvavaryap
fnaiallvgsqvgrpgvltqcsleeatelklgmlghtcyaetisvygtepvftdgddtpw
skgflassyasrglkmrftsgsgsevqmgyaegksmlylearciyitkaagvqglqngsv
scigvpsavpsgiravlaenlicssldlecassndqtfthsdmrrtarllmqflpgtdfi
ssgysavpnydnmfagsnedaedfddynviqrdlkvdgglrpvreedviairnkaaralq
avfagmglppitdeeveaatyahgskdmpernivedikfaqeiinknrnglevvkalaqg
gftdvaqdmlniqkakltgdylhtsaiivgdgqvlsavndvndyagpatgyrlqgerwee
iknipgaldpn
>d1pud__ 3.1.19.1.1 tRNA-guanine transglycosylase {Zymomonas mobilis}
rprfsfsiaaregkartgtiemkrgvirtpafmpvgtaatvkalkpetvratgadiilgn
tyhlmlrpgaeriaklgglhsfmgwdrpiltdsggyqvmslssltkqseegvtfkshldg
srhmlspersieiqhllgsdivmafdectpypatpsraassmersmrwakrsrdafdsrk
eqaenaalfgiqqgsvfenlrqqsadalaeigfdgyavgglavgegqdemfrvldfsvpm
lpddkphylmgvgkpddivgavergidmfdcvlptrsgrngqaftwdgpinirnarfsed
lkpldsechcavcqkwsrayihhlirageilgamlmtehniafyqqlmqkirdsisegrf
sqfaqdfraryf
>d1aj2__ 3.1.20.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1ad1a_ 3.1.20.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhn
>d1uroa_ 3.1.21.1.1 Uroporphyrinogen decarboxylase, UROD {Human (Homo sapiens)}
gfpelkndtflraawgeetdytpvwcmrqagrylpefretraaqdffstcrspeaccelt
lqplrrfpldaaiifsdilvvpqalgmevtmvpgkgpsfpeplreeqdlerlrdpevvas
elgyvfqaitltrqrlagrvpligfagapwtlmtymvegggsstmaqakrwlyqrpqash
qllriltdalvpylvgqvvagaqalqlfeshaghlgpqlfnkfalpyirdvakqvkarlr
eaglapvpmiifakdghfaleelaqagyevvgldwtvapkkarecvgktvtlqgnldpca
lyaseeeigqlvkqmlddfgphryianlghglypdmdpehvgafvdavhkhsrllrq
>d1b5ta_ 3.1.22.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
gqinvsfeffpprtsemeqtlwnsidrlsslkpkfvsvtygansgerdrthsiikgikdr
tgleaaphltcidatpdelrtiardywnngirhivalrgdlppgsgkpemyasdlvtllk
evadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvs
agidveiipgilpvsnfkqakkfadmtnvripawmaqmfdgldddaetrklvganiamdm
vkilsregvkdfhfytlnraemsyaichtlgvrpa
>d1pyma_ 3.1.23.1.1 Phosphoenolpyruvate mutase {Blue mussel (Mytilus edulis)}
vkkttqlkqxlnskdlefixeahnglsarivqeagfkgiwgsglsvsaqlgvrdsneasw
tqvvevlefxsdasdvpilldadtgygnfnnarrlvrkledrgvagacledklfpktnsl
hdgraqpladieefalkikackdsqtdpdfcivarveafiagwgldealkraeayrnaga
dailxhskkadpsdieafxkawnnqgpvvivptkyyktptdhfrdxgvsxviwanhnlra
svsaiqqttkqiyddqslvnvedkivsvkeifrlqrddelvqaedkylpkn
>d1cdoa2 3.2.1.1.1 (176-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gvstgfgaavntakvepgstcavfglgavglaavmgchsagakriiavdlnpdkfekakv
fgatdfvnpndhsepisqvlskmtnggvdfslecvgnvgvmrnalesclkgwgvsvlvgw
tdlhdvatrpiqliagrtwkgsmfggfkg
>d3btoa2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1keva2 3.2.1.1.3 (151-314) Bacterial secondary alcohol dehydrogenase {Clostridium beijerinckii}
mmttgfhgaeladiqmgssvvvigigavglmgiagaklrgagriigvgsrpicveaakfy
gatdilnyknghivdqvmkltngkgvdrvimagggsetlsqavsmvkpggiisninyhgs
gdalliprvewgcgmahktikgglcpggrlraemlrdmvvynrv
>d1qora2 3.2.1.1.5 (136-265) Quinone oxidoreductase {Escherichia coli}
yeikpdeqflfhaaaggvgliacqwakalgakligtvgtaqkaqsalkagawqvinyree
dlverlkeitggkkvrvvydsvgrdtwersldclqrrglmvsfgnssgavtgvnlgilnq
kgslyvtrps
>d1udc__ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fsssatvygdqpkipyvesfptgtpqspygksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1bxka_ 3.2.1.2.2 dTDP-glucose 4,6-dehydratase {Escherichia coli}
mrkilitggagfigsalvryiinetsdavvvvdkltyagnlmslapvaqserfafekvdi
cdraelarvftehqpdcvmhlaaeshvdrsidgpaafietnivgtytlleaaraywnalt
edkksafrfhhistdevygdlhstddfftettpyapsspysaskassdhlvrawlrtygl
ptlitncsnnygpyhfpekliplmilnalagkslpvygngqqirdwlyvedharalycva
ttgkvgetynigghnerknldvveticelleelapnkphgvahyrdlitfvadrpghdlr
yaidaskiarelgcvpqetfesgmrktvqwylaneswwkqvqdgsyqgerlg
>d1bsva_ 3.2.1.2.3 GDP-4-keto-6-deoxy-d-mannose epimerase/reductase (GDP-fucose synthetase) {Escherichia coli}
kqrvfiaghrgmvgsairrqleqrgdvelvlrtrdelnlldsravhdffaseridqvyla
aakvggivanntypadfiyqnmmiesniihaahqndvnkllflgssciypklakqpmaes
ellqgtleptnepyaiakiagiklcesynrqygrdyrsvmptnlygphdnfhpsnshvip
allrrfheataqnapdvvvwgsgtpmreflhvddmaaasihvmelahevwlentqpmlsh
invgtgvdctirelaqtiakvvgykgrvvfdaskpdgtprklldvtrlhqlgwyheisle
aglastyqwflenqdrf
>d1db3a_ 3.2.1.2.4 GDP-mannose 4,6-dehydratase {Escherichia coli}
skvalitgvtgqdgsylaefllekgyevhgikrrassfntervdhiyqdphtcnpkfhlh
ygdlsdtsnltrilrevqpdevynlgamshvavsfespeytadvdamgtlrlleairflg
lekktrfyqastselyglvqeipqkettpfyprspyavaklyaywitvnyresygmyacn
gilfnhesprrgetfvtrkitraianiaqglesclylgnmdslrdwghakdyvkmqwmml
qqeqpedfviatgvqysvrqfvemaaaqlgiklrfegtgveekgivvsvtghdapgvkpg
dviiavdpryfrpaevetllgdptkaheklgwkpeitlremvsemvandleaakkhs
>d1qrra_ 3.2.1.2.5 Sulfolipid biosynthesis protein SQD1 {Thale cress (Arabidopsis thaliana)}
krvmviggdgycgwatalhlskknyevcivdnlvrrlfdhqlglesltpiasihdrisrw
kaltgksielyvgdicdfeflaesfksfepdsvvhfgeqrsapysmidrsravytqhnnv
igtlnvlfaikefgeechlvklgtmgeygtpnidieegyitithngrtdtlpypkqassf
yhlskvhdshniaftckawgiratdlnqgvvygvktdetemheelrnrldydavfgtaln
rfcvqaavghpltvygkggqtrgyldirdtvqcveiaianpakagefrvfnqfteqfsvn
elaslvtkagsklgldvkkmtvpnprveaeehyynakhtklmelglephylsdslldsll
nfavqfkdrvdtkqimpsvswkkigvktks
>d1cyda_ 3.2.1.2.6 Carbonyl reductase {Mouse (Mus musculus)}
lnfsglralvtgagkgigrdtvkalhasgakvvavtrtnsdlvslakecpgiepvcvdlg
dwdatekalggigpvdllvnnaalvimqpflevtkeafdrsfsvnlrsvfqvsqmvardm
inrgvpgsivnvssmvahvtfpnlitysstkgamtmltkamamelgphkirvnsvnptvv
ltdmgkkvsadpefarklkerhplrkfaevedvvnsilfllsdrsastsgggilvdagyl
as
>d1oaa__ 3.2.1.2.7 Sepiapterin reductase {Mouse (Mus musculus)}
adglgcavcvltgasrgfgralapqlarllspgsvmlvsarsesmlrqlkeelgaqqpdl
kvvlaaadlgteagvqrllsavrelprpeglqrlllinnaatlgdvskgflnvndlaevn
nywalnltsmlcltsgtlnafqdspglsktvvnisslcalqpykgwglycagkaardmly
qvlaaeepsvrvlsyapgpldndmqqlaretskdpelrsklqklksdgalvdcgtsaqkl
lgllqkdtfqsgahvdfyd
>d1hdr__ 3.2.1.2.9 Dihydropteridin reductase {Human (Homo sapiens)}
earrvlvyggrgalgsrcvqafrarnwwvasvdvveneeasasiivkmtdsfteqadqvt
aevgkllgeekvdailcvaggwaggnakskslfkncdlmwkqsiwtstisshlatkhlke
gglltlagakaaldgtpgmigygmakgavhqlcqslagknsgmppgaaaiavlpvtldtp
mnrksmpeadfsswtpleflvetfhdwitgknrpssgsliqvvttegrteltpayf
>d1fds__ 3.2.1.2.10 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfgdv
>d1fmca_ 3.2.1.2.11 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1hdca_ 3.2.1.2.12 3-alpha,20-beta-hydroxysteroid dehydrogenase {Streptomyces hydrogenans}
ndlsgktviitggarglgaeaarqavaagarvvladvldeegaatarelgdaaryqhldv
tieedwqrvvayareefgsvdglvnnagistgmfletesverfrkvveinltgvfigmkt
vipamkdagggsivnissaaglmglaltssygaskwgvrglsklaavelgtdrirvnsvh
pgmtytpmtaetgirqgegnypntpmgrvgepgeiagavvkllsdtssyvtgaelavdgg
wttgptvkyvmgq
>d1bdb__ 3.2.1.2.13 Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase {Pseudomonas lb400}
mklkgeavlitggasglgralvdrfvaegakvavldksaerlaeletdhgdnvlgivgdv
rsledqkqaasrcvarfgkidtlipnagiwdystalvdlpeesldaafdevfhinvkgyi
havkaclpalvasrgnviftisnagfypngggplytaakhaivglvrelafelapyvrvn
gvgsgginsdlrgpsslgmgskaistvpladmlksvlpigrmpeveeytgayvffatrgd
aapatgallnydgglgvrgffsgaggndlleqlnih
>d1b16a_ 3.2.1.2.14 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1eno__ 3.2.1.2.15 Enoyl-ACP reductase {Oil seed rape (Brassica napus)}
lpidlrgkrafiagiaddngygwavakslaaagaeilvgtwvpalnifetslrrgkfdqs
rvlpdgslmeikkvypldavfdnpedvpedvkankryagssnwtvqeaaecvrqdfgsid
ilvhslangpevskplletsrkgylaaisassysfvsllshflpimnpggasisltyias
eriipgygggmssakaalesdtrvlafeagrkqnirvntisagplgsraakaigfidtmi
eysynnapiqktltadevgnaaaflvsplasaitgatiyvdnglnsmgvaldspvfk
>d1eny__ 3.2.1.2.16 Enoyl-ACP reductase {Mycobacterium tuberculosis, TB, gene InhA}
aglldgkrilvsgiitdssiafhiarvaqeqgaqlvltgfdrlrliqritdrlpakapll
eldvqneehlaslagrvteaigagnkldgvvhsigfmpqtgmginpffdapyadvskgih
isaysyasmakallpimnpggsivgmdfdpsrampaynwmtvaksalesvnrfvareagk
ygvrsnlvaagpirtlamsaivggalgeeagaqiqlleegwdqrapigwnmkdatpvakt
vcallsdwlpattgdiiyadggahtqll
>d1qg6a_ 3.2.1.2.17 Enoyl-ACP reductase {Escherichia coli}
gflsgkrilvtgvasklsiaygiaqamhregaelaftyqndklkgrveefaaqlgsdivl
qcdvaedasidtmfaelgkvwpkfdgfvhsigfapgdqldgdyvnavtregfkiahdiss
ysfvamakacrsmlnpgsalltlsylgaeraipnynvmglakasleanvrymanamgpeg
vrvnaisagpirtlaasgikdfrkmlahceavtpirrtvtiedvgnsaaflcsdlsagis
gevvhvdggfsiaamne
>d2ae2a_ 3.2.1.2.19 Tropinone reductase {Jimsonweed (Datura stramonium), II}
agrwnlegctalvtggsrgigygiveelaslgasvytcsrnqkelndcltqwrskgfkve
asvcdlssrserqelmntvanhfhgklnilvnnagiviykeakdytvedyslimsinfea
ayhlsvlahpflkasergnvvfissvsgalavpyeavygatkgamdqltrclafewakdn
irvngvgpgviatslvemtiqdpeqkenlnklidrcalrrmgepkelaamvaflcfpaas
yvtgqiiyvdgglmancgf
>d1ybva_ 3.2.1.2.20 1,3,8-trihydroxynaphtalene reductase (THNR, naphtol reductase) {Rice blast fungus (Magnaporthe grisea)}
daipgplgpqsaslegkvalvtgagrgigremamelgrrgckvivnyanstesaeevvaa
ikkngsdaacvkanvgvvedivrmfeeavkifgkldivcsnsgvvsfghvkdvtpeefdr
vftintrgqffvareaykhleiggrlilmgsitgqakavpkhavysgskgaietfarcma
idmadkkitvnvvapggiktdmyhavcreyipngenlsneevdeyaavqwsplrrvglpi
diarvvcflasndggwvtgkvigidggacm
>d1gado1 3.2.1.3.1 (0-148,313-330) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Escherichia coli}
tikvgingfgrigrivfraaqkrsdieivaindlldadymaymlkydsthgrfdgtvevk
dghlivngkkirvtaerdpanlkwdevgvdvvaeatglfltdetarkhitagakkvvmtg
pskdntpmfvkganfdkyagqdivsnasXnetgysnkvldliahisk
>d1gd1o1 3.2.1.3.2 (0-148,313-333) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
avkvgingfgrigrnvfraalknpdievvavndltdantlahllkydsvhgrldaevsvn
gnnlvvngkeiivkaerdpenlawgeigvdivvestgrftkredaakhleagakkviisa
pakneditivmgvnqdkydpkahhvisnasXnetgyshrvvdlaayiaskgl
>d1hdgo1 3.2.1.3.4 (1-148,313-331) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Thermotoga maritima}
arvaingfgrigrlvyriiyerknpdievvaindltdtktlahllkydsvhkkfpgkvey
tenslivdgkeikvfaepdpsklpwkdlgvdfviestgvfrnrekaelhlqagakkviit
apakgeditvvigcnedqlkpehtiiscasXneygysnrvvdtlelllkm
>d1b7go1 3.2.1.3.5 (1-138,301-340) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
mvnvavngygtigkrvadaiikqpdmklvgvaktspnyeafiahrrgiriyvpqqsikkf
eesgipvagtvedliktsdivvdttpngvgaqykpiylqlqrnaifqggekaevadisfs
alcnynealgkkyirvvsXesivvpenidairasmklmsaedsmritneslgilkgyli
>d1gypa1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1dssg1 3.2.1.3.9 (1-148,313-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
skigingfgrigrlvlraalemgaqvvavndpfialeymvymfkydsthgmfkgevkaed
galvvdgkkitvfnemkpenipwskagaeyivestgvfttiekasahfkggakkviisap
sadapmfvcgvnlekyskdmkvvsnasXnefgysqrvidlikhmqkvdsa
>d1brma1 3.2.1.3.11 (1-133,355-367) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
mknvgfigwrgmvgsvlmqrmveerdfdairpvffstsqlgqaapsfggttgtlqdafdl
ealkaldiivtcqggdytneiypklresgwqgywidaasslrmkddaiiildpvnqdvit
dglnngirtfvggXaaeplrrmlrqla
>d2dap_1 3.2.1.3.12 (1-118,269-320) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
mtnirvaivgygnlgrsvekliakqpdmdlvgifsrratldtktpvfdvadvdkhaddvd
vlflcmgsatdipeqapkfaqfactvdtydnhrdiprhrqvmneaataagnvalvstgXr
npdftassqiafgraahrmkqqgqsgaftvlevapyllspenlddliardv
>d1dih_1 3.2.1.3.13 (2-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
hdanirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvt
vqssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadi
aivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1ofga1 3.2.1.3.14 (1-160,323-381) Glucose-fructose oxidoreductase, N-terminal domain {Zymomonas mobilis}
atlpagasqvpttpagrpmpyairpmpedrrfgyaivglgkyalnqilpgfagcqhsrie
alvsgnaekakivaaeygvdprkiydysnfdkiakdpkidavyiilpnslhaefairafk
agkhvmcekpmatsvadcqrmidaakaankklmigyrchyXnqfsaqldhlaeavinnkp
vrspgeegmqdvrliqaiyeaartgrpvntdwgyvrqggy
>d1dpga1 3.2.1.3.15 (1-181,413-426) Glucose 6-phosphate dehydrogenase, N-terminal domain {Leuconostoc mesenteroides}
vseiktlvtffggtgdlakrklypsvfnlykkgylqkhfaivgtarqalnddefkqlvrd
cikdftddqaqaeafiehfsyrahdvtdaasyavlkeaieeaadkfdidgnrifymsvap
rffgtiakylkseglladtgynrlmiekpfgtsydtaaelqndlenafddnqlfridhyl
gXepyermihdtmngd
>d2naca1 3.2.1.4.1 (148-335) Formate dehydrogenase {Pseudomonas sp. 101}
isvaehvvmmilslvrnylpshewarkggwniadcvshaydleamhvgtvaagriglavl
rrlapfdvhlhytdrhrlpesvekelnltwhatredmypvcdvvtlncplhpetehmind
etlklfkrgayivntargklcdrdavaralesgrlagyagdvwfpqpapkdhpwrtmpyn
gmtphisg
>d1qp8a1 3.2.1.4.2 (83-263) Putative formate dehydrogenase {Pyrobaculum aerophilum}
adavaefalalllapykriiqygekxkrgdygrdveipliqgekvavlglgeigtrvgki
laalgaqvrgfsrtpkegpwrftnsleealrearaavcalplnkhtrglvkyqhlalxae
davfvnvgraevldrdgvlrilkerpqfifasdvwwgrndfakdaeffslpnvvatpwva
g
>d1dxy_1 3.2.1.4.3 (101-330) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
spaaiaefaltdtlyllrnmgkvqaqlqagdyekagtfigkelgqqtvgvmgtghigqva
iklfkgfgakviaydpypmkgdhpdfdyvsledlfkqsdvidlhvpgieqnthiineaaf
nlmkpgaivintarpnlidtqamlsnlksgklagvgidtyeyetedllnlakhgsfkdpl
wdellgmpnvvlsphiayytetavhnmvyfslqhlvdfltkgetstevtg
>d1gdha1 3.2.1.4.4 (101-291) D-glycerate dehydrogenase {Hyphomicrobium methylovorum}
vtvataeiamllllgsarragegekmirtrswpgweplelvgekldnktlgiygfgsigq
alakraqgfdmdidyfdthrasssdeasyqatfhdsldsllsvsqffslnapstpetryf
fnkatikslpqgaivvntargdlvdnelvvaaleagrlayagfdvfagepninegyydlp
ntflfphigsa
>d1psda1 3.2.1.4.5 (108-295) Phosphoglycerate dehydrogenase {Escherichia coli}
ntrsvaelvigelllllrgvpeanakahrgvwnklaagsfeargkklgiigyghigtqlg
ilaeslgmyvyfydienklplgnatqvqhlsdllnmsdvvslhvpenpstknmmgakeis
lmkpgsllinasrgtvvdipalcdalaskhlagaaidvfptepatnsdpftsplcefdnv
lltphigg
>d2dlda1 3.2.1.4.6 (104-300) D-lactate dehydrogenase {Lactobacillus helveticus}
pnaiaehaaiqaarvlrqdkrmdekmakrdlrwaptigrevrdqvvgvvgtghigqvfmr
imegfgakviaydifknpelekkgyyvdslddlykqadvislhvpdvpanvhmindksia
emkdgvvivncsrgrlvdtdavirgldsgkifgfvmdtyedevgvfnkdwegkefpdkrl
adlidrpnvlvtphtaf
>d1pjca1 3.2.1.4.7 (136-303) L-alanine dehydrogenase {Phormidium lapideum}
agrlsvqfgarflerqqggrgvllggvpgvkpgkvvilgggvvgteaakmavglgaqvqi
fdinverlsyletlfgsrvellysnsaeietavaeadlligavlvpgrrapilvpaslve
qmrtgsvivdvavdqggcvetlhptshtqptyevfgvvhygvpnmpga
>d1b3ra1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1mlda1 3.2.1.5.1 (1-144) Malate dehydrogenase {Porcine (Sus scrofa)}
akvavlgasggigqplslllknsplvsrltlydiahtpgvaadlshietratvkgylgpe
qlpdclkgcdvvvipagvprkpgmtrddlfntnativatltaacaqhcpdamiciisnpv
nstipitaevfkkhgvynpnkifg
>d5mdha1 3.2.1.5.1 (1-154) Malate dehydrogenase {Porcine (Sus scrofa)}
sepirvlvtgaagqiaysllysigngsvfgkdqpiilvllditpmmgvldgvlmelqdca
lpllkdviatdkeeiafkdldvailvgsmprrdgmerkdllkanvkifkcqgaaldkyak
ksvkvivvgnpantncltasksapsipkenfscl
>d7mdha1 3.2.1.5.2 (23-197) Malate dehydrogenase {Sorghum (Sorghum vulgare), chloroplast}
dcfgvfcttydlkaedktkswkklvniavsgaagmisnhllfklasgevfgqdqpialkl
lgsersfqalegvameledslypllrevsigidpyevfedvdwalligakprgpgmeraa
lldingqifadqgkalnavasknvkvlvvgnpcntnaliclknapdipaknfhal
>d2cmd_1 3.2.1.5.3 (1-145) Malate dehydrogenase {Escherichia coli}
mkvavlgaaggigqalalllktqlpsgselslydiapvtpgvavdlshiptavkikgfsg
edatpalegadvvlisagvrrkpgmdrsdlfnvnagivknlvqqvaktcpkacigiitnp
vnttvaiaaevlkkagvydknklfg
>d2hlpa1 3.2.1.5.5 (22-162) Malate dehydrogenase {Haloarcula marismortui}
tkvsvvgaagtvgaaagynialrdiadevvfvdipdkeddtvgqaadtnhgiaydsntrv
rqggyedtagsdvvvitagiprqpgqtridlagdnapimediqssldehnddyislttsn
pvdllnrhlyeagdrsreqvig
>d1b8pa1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1hyha1 3.2.1.5.7 (21-166) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {Lactobacillus confusus}
arkigiiglgnvgaavahgliaqgvaddyvfidaneakvkadqidfqdamanleahgniv
indwaaladadvvistlgniklqqdnptgdrfaelkftssmvqsvgtnlkesgfhgvlvv
isnpvdvitalfqhvtgfpahkvigt
>d1ldm_1 3.2.1.5.10 (1-160) Lactate dehydrogenase {Dogfish (Squalus acanthias)}
atlkdklighlatsqeprsynkitvvgvgavgmacaisilmkdladevalvdvmedklkg
emmdlqhgslflhtakivsgkdysvsagsklvvitagarqqegesrlnlvqrnvnifkfi
ipnivkhspdciilvvsnpvdvltyvawklsglpmhriig
>d1ceqa1 3.2.1.5.11 (19-163) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
pkakivlvgsgmiggvmatlivqknlgdvvlfdivknmphgkaldtshtnvmaysnckvs
gsntyddlagsdvvivtagftkapgksdkewnrddllplnnkimieigghikkncpnafi
ivvtnpvdvmvqllhqhsgvpknkiigl
>d1ldna1 3.2.1.5.12 (15-162) Lactate dehydrogenase {Bacillus stearothermophilus}
mknnggarvvvigagfvgasyvfalmnqgiadeivlidaneskaigdamdfnhgkvfapk
pvdiwhgdyddcrdadlvvicaganqkpgetrldlvdkniaifrsivesvmasgfqglfl
vatnpvdiltyatwkfsglphervigsg
>d1llc_1 3.2.1.5.13 (13-164) Lactate dehydrogenase {Lactobacillus casei}
asitdkdhqkvilvgdgavgssyafamvlqgiaqeigivdifkdktkgdaidlsnalpft
spkkiysaeysdakdadlvvitagapkqpgetrldlvnknlkilksivdpivdsgfnlif
lvaanpvdiltyatwklsgfpknrvvgsg
>d1llda1 3.2.1.5.14 (7-149) Lactate dehydrogenase {Bifidobacterium longum, strain am101-2}
ptklavigagavgstlafaaaqrgiareivlediakerveaevldmqhgssfyptvsidg
sddpeicrdadmvvitagprqkpgqsrlelvgatvnilkaimpnlvkvapnaiymlitnp
vdiathvaqkltglpenqifgsg
>d1a5z_1 3.2.1.5.15 (22-163) Lactate dehydrogenase {Thermotoga maritima}
mkigivglgrvgsstafallmkgfaremvlidvdkkraegdaldlihgtpftrraniyag
dyadlkgsdvvivaagvpqkpgetrlqllgrnarvmkeiarnvskyapdsivivvtnpvd
vltyfflkesgmdprkvfgs
>d1yvei2 3.2.1.6.1 (83-307) Acetohydroxy acid isomeroreductase, ketoacid reductoisomerase (KARI) {Spinach (Spinacia oleracea)}
attfdfdssvfkkekvtlsghdeyivrggrnlfpllpdafkgikqigvigwgsqapaqaq
nlkdslteaksdvvvkiglrkgsnsfaearaagfseengtlgdmwetisgsdlvlllisd
saqadnyekvfshmkpnsilglshgfllghlqslgqdfpknisviavcpkgmgpsvrrly
vqgkevngaginssfavhqdvdgratdvalgwsialgspftfatt
>d2pgd_2 3.2.1.6.2 (1-176) 6-phosphogluconate dehydrogenase {Sheep (Ovis orientalis aries)}
aqadialiglavmgqnlilnmndhgfvvcafnrtvskvddflaneakgtkvlgahsleem
vsklkkprriillvkagqavdnfieklvplldigdiiidggnseyrdtmrrcrdlkdkgi
lfvgsgvsggedgarygpslmpggnkeawphikaifqgiaakvgtgepccdwvgdd
>d1pgja2 3.2.1.6.3 (1-178) 6-phosphogluconate dehydrogenase {Trypanosoma brucei}
smdvgvvglgvmganlalniaekgfkvavfnrtyskseefmkanasapfagnlkafetme
afaaslkkprkalilvqagaatdstieqlkkvfekgdilvdtgnahfkdqgrraqqleaa
glrflgmgisggeegarkgpaffpggtlsvweeirpiveaaaakaddgrpcvtmngsg
>d2hdha2 3.2.1.6.4 (12-203) Short chain L-3-hydroxyacyl CoA dehydrogenase {Human (Homo sapiens)}
kiivkhvtviggglxgagiaqvaaatghtvvlvdqtedilakskkgieeslrkvakkkfa
enpkagdefvaktlstiatstdaasvvhstdlvveaivenlkvknelfkrldkraaehti
fasntsslqitsianattrqdrfaglhffnpvpvxklveviktpxtsqktfeslvdfska
lgkhpvsckdtp
>d1bg6_2 3.2.1.6.6 (4-187) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
sktyavlglgngghafaaylalkgqsvlawdidaqrikeiqdrgaiiaegpglagtahpd
lltsdiglavkdadvilivvpaihhasiaaniasyisegqliilnpgatggalefrkilr
engapevtigetssmlftcrserpgqvtvnaikgamdfaclpaakagwaleqigsvlpqy
vave
>d1bgva1 3.2.1.7.1 (195-449) Glutamate dehydrogenase {Clostridium symbiosum}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1gtma1 3.2.1.7.2 (181-419) Glutamate dehydrogenase {Pyrococcus furiosus}
ggslgrieatargasytireaakvlgwdtlkgktiaiqgygnagyylakimsedfgmkvv
avsdskggiynpdglnadevlkwknehgsvkdfpgatnitneellelevdvlapaaieev
itkknadnikakivaevangpvtpeadeilfekgilqipdflcnaggvtvsyfewvqnit
gyywtieevrerldkkmtkafydvyniakeknihmrdaayvvavqrvyqamldrgwvkh
>d1ch6a1 3.2.1.7.5 (209-501) Glutamate dehydrogenase {Bovine (Bos taurus)}
hgrisatgrgvfhgienfienasymsilgmtpgfgdktfavqgfgnvglhsmrylhrfga
kcvavgesdgsiwnpdgidpkeledfklqhgtilgfpkakiyegsilevdcdilipaase
kqltksnaprvkakiiaegangpttpqadkiflernimvipdlylnaggvtvsyfqilkn
lnhvsygrltfkyerdsnyhllmsvqeslerkfgkhggtipivptaefqdrisgasekdi
vhsglaytmersarqimrtamkynlgldlrtaayvnaiekvfrvyneagvtft
>d1leha1 3.2.1.7.6 (135-364) Leucine dehydrogenase {Bacillus sphaericus}
gispafgssgnpspvtaygvyrgmkaaakeafgsdsleglavsvqglgnvakalckklnt
egaklvvtdvnkaavsaavaeegadavapnaiygvtcdifapcalgavlndftipqlkak
viagsadnqlkdprhgkylhelgivyapdyvinaggvinvadelygynrtramkrvdgiy
dsiekifaiskrdgvpsyvaadrmaeeriakvakarsqflqdqrnilngr
>d1bw9a1 3.2.1.7.7 (149-350) Phenylalanine dehydrogenase {Rhodococcus M4}
safttavgvfeamkatvahrglgsldgltvlvqglgavggslaslaaeagaqllvadtdt
ervahavalghtavaledvlstpcdvfapcamggvittevartldcsvvagaannviade
aasdilhargilyapdfvanaggaihlvgrevlgwsesvvheravaigdtlnqvfeisdn
dgvtpdeaartlagrrareast
>d1a4ia1 3.2.1.7.8 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1b0aa1 3.2.1.7.9 (123-288) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
fhpynvgrlcqraprlrpctprgivtllerynidtfglnavvigasnivgrpmsmellla
gctttvthrftknlrhhvenadllivavgkpgfipgdwikegaividvginrlengkvvg
dvvfedaakrasyitpvpggvgpmtvatlientlqacveyhdpqde
>d1qr6a1 3.2.1.7.10 (280-573) Mitochondrial NAD(P)-dependenent malic enzyme {Human (Homo sapiens)}
iqgtaavalagllaaqkviskpisehkilflgageaalgianlivxsxvenglseqeaqk
kiwxfdkygllvkgrkakidsyqepfthsapesipdtfedavnilkpstiigvagagrlf
tpdviraxasinerpvifalsnptaqaectaeeaytltegrclfasgspfgpvkltdgrv
ftpgqgnnvyifpgvalavilcntrhisdsvfleaakaltsqltdeelaqgrlypplani
qevsiniaikvteylyankxafrypepedkakyvkertwrseydsllpdvyewp
>d2scua1 3.2.1.8.1 (1-121) Succinyl-CoA synthetase, alpha-chain, N-terminal (CoA-binding) domain {Escherichia coli}
silidkntkvicqgftgsqgtfhseqaiaygtkmvggvtpgkggtthlglpvfntvreav
aatgatasviyvpapfckdsileaidagikliititegiptldmltvkvkldeagvrmig
p
>d1djna2 3.3.1.1.2 (490-645) Trimethylamine dehydrogenase, C-terminal domain {Methylophilus methylotrophus w3a1}
rwntdgtnclthdpipgadaslpdqltpeqvmdgkkkigkrvvilnadtyfmapslaekl
ataghevtivsgvhlanymhftleypnmmrrlhelhveelgdhfcsriepgrmeiyniwg
dgskrtyrgpgvsprdantshrwiefdslvlvtgrh
>d1cjca1 3.3.1.1.3 (107-331) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
hqaldipgeelpgvfsarafvgwynglpenrelapdlscdtavilgqgnvaldvarillt
ppdhlektditeaalgalrqsrvktvwivgrrgplqvaftikelremiqlpgtrpmldpa
dflglqdrikeaarprkrlmelllrtatekpgveeaarrasasrawglrffrspqqvlps
pdgrraagirlavtrlegigeatravptgdvedlpcglvlssigy
>d1b4va1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1pbe_1 3.3.1.2.3 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas fluorescens}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareacgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1b3ma1 3.3.1.2.5 (1-217,322-385) Sarcosine oxidase {Bacillus sp.}
sthfdvivvgagsmgmaagyqlakqgvktllvdafdpphtngshhgdtriirhaygegre
yvplalrsqelwyelekethhkiftktgvlvfgpkgesafvaetmeaakehsltvdlleg
deinkrwpgitvpenynaifepnsgvlfsencirayrelaeargakvlthtrvedfdisp
dsvkietangsytadklivsmgawnskllsklnldipXdehfiidlhpehsnvviaagfs
ghgfkfssgvgevlsqlaltgktehdisifsinrpalkeslq
>d1foha1 3.3.1.2.6 (1-240) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
tkysesycdvlivgagpaglmaarvlseyvrqkpdlkvriidkrstkvyngqadglqcrt
leslknlgladkilseandmstialynpdenghirrtdripdtlpgisryhqvvlhqgri
erhildsiaeisdtrikverplipekmeidsskaedpeaypvtmtlrymsdhestplqfg
hktenslfhsnlqtqeeedanyrlpegkeageietvhckyvigcdgghswvrrtlgfemi
>d1foha2 3.3.1.2.6 (342-461) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
vtekfskdervfiagdachthspkagqgmntsmmdtynlgwklglvltgrakrdilktye
eerhafaqalidfdhqfsrlfsgrpakdvademgvsmdvfkeafvkgnefasgtainyde
>d1gpea1 3.3.1.2.8 (1-328,525-587) Glucose oxidase {Penicillium amagasakiense}
ylpaqqidvqssllsdpskvagktydyiiagggltgltvaakltenpkikvlviekgfye
sndgaiiedpnaygqifgttvdqnyltvplinnrtnnikagkglggstlingdswtrpdk
vqidswekvfgmegwnwdnmfeymkkaeaartptaaqlaaghsfnatchgtngtvqsgar
dngqpwspimkalmntvsalgvpvqqdflcghprgvsmimnnldenqvrvdaarawllpn
yqrsnleiltgqmvgkvlfkqtasgpqavgvnfgtnkavnfdvfakhevllaagsaispl
ileysgiglksvldqanvtqlldlpvgiXcsmmsrelggvvdatakvygtqglrvidgsi
pptqvsshvmtifygmalkvadailddyaksa
>d1b37a1 3.3.1.2.9 (5-293,406-463) Polyamine oxidase {Maize (Zea mays)}
prvivvgagmsgisaakrlseagitdllileatdhiggrmhktnfaginvelganwvegv
nggkmnpiwpivnstlklrnfrsdfdylaqnvykedggvydedyvqkrieladsveemge
klsatlhasgrddmsilamqrlnehqpngpatpvdmvvdyykfdyefaepprvtslqntv
platfsdfgddvyfvadqrgyeavvyylagqylktddksgkivdprlqlnkvvreikysp
ggvtvktednsvysadyvmvsaslgvlqsdliqfkpklptwkvraiyqfXwpvgvnryey
dqlrapvgrvyftgehtsehyngyvhgaylsgidsaeilincaqkkmc
>d1gnd_1 3.3.1.3.1 (1-291,389-430) Guanine nucleotide dissosiation inhibitor, GDI {Bovine (Bos taurus)}
mdeeydvivlgtgltecilsgimsvngkkvlhmdrnpyyggesssitpleelykrfqlle
gppetmgrgrdwnvdlipkflmangqlvkmllytevtryldfkvvegsfvykggkiykvp
stetealasnlmgmfekrrfrkflvfvanfdendpktfegvdpqntsmrdvyrkfdlgqd
vidftghalalyrtddyldqpcletinriklyseslarygkspylyplyglgelpqgfar
lsaiyggtymlnkpvddiimengkvvgvksegevarckqlicdpsyvpdrvXpiddgses
qvfcscsydatthfettcndikdiykrmagsafd
>d1chua2 3.3.1.4.1 (2-237,354-422) L-aspartate oxidase {Escherichia coli}
ntlpehscdvliigsgaaglslalrladqhqvivlskgpvtegstfyaqggiaavfdetd
sidshvedtliagagicdrhavefvasnarscvqwlidqgvlfdthiqpngeesyhltre
gghshrrilhaadatgrevettlvskalnhpnirvlertnavdlivsdkiglpgtrrvvg
awvwnrnketvetchakavvlatggaskvyqyttnpdissgdgiamawragcrvanXcgg
vmvddhgrtdveglyaigevsytglhganrmasnslleclvygwsaaeditrrmpyahdi
stlppw
>d1fuma2 3.3.1.4.2 (1-225,358-442) Fumarate reductase flavoprotein subunit {Escherichia coli}
qtfqadlaivgaggaglraaiaaaqanpnakialiskvypmrshtvaaeggsaavaqdhd
sfeyhfhdtvaggdwlceqdvvdyfvhhcptemtqlelwgcpwsrrpdgsvnvrrfggmk
iertwfaadktgfhmlhtlfqtslqfpqiqrfdehfvldilvddghvrglvamnmmegtl
vqiranavvmatggagrvyryntnggivtgdgmgmalshgvplrdXmggietdqncetri
kglfavgecssvglhganrlgsnslaelvvfgrlageqateraatagngneaaieaqaag
veqrlkdlvnq
>d1qlaa2 3.3.1.4.3 (1-250,372-457) Fumarate reductase flavoprotein subunit {Wolinella succinogenes}
mkvqycdslviggglaglraavatqqkglstivlslipvkrshsaaaqggmqaslgnskm
sdgdnedlhfmdtvkgsdwgcdqkvarmfvntapkairelaawgvpwtrihkgdrmaiin
aqkttiteedfrhglihsrdfggtkkwrtcytadatghtmlfavaneclklgvsiqdrke
aialihqdgkcygavvrdlvtgdiiayvakgtliatggygriyknttnavvcegtgtaia
letgiaqlgnXmggirtdyrgeaklkglfsageaacwdmhgfnrlggnsvseavvagmiv
geyfaehcantqvdletktlekfvkgqeaymkslves
>d1qjda2 3.3.1.4.4 (103-359,506-568) Flavocytochrome c3 (respiratory fumarate reductase) {Shewanella frigidimarina}
ptiaelakdkserqaalasaphdtvdvvvvgsggagfsaaisatdsgakviliekepvig
gnaklaaggmnaawtdqqkakkitdspelmfedtmkggqnindpalvkvlsshskdsvdw
mtamgadltdvgmmggasvnrahrptggagvgahvvqvlydnavkrnidlrmntrgievl
kddkgtvkgilvkgmykgyywvkadavilatggfaknnervakldpslkgfistnqpgav
gdgldvaenaggalkdmXtmggvmidtkaevmnakkqvipglygagevtggvhganrlgg
naisdiitfgrlageeaakys
>d3grs_1 3.3.1.5.1 (18-165,291-363) Glutathione reductase {Human (Homo sapiens)}
vasydylvigggsgglasarraaelgaraavveshklggtcvnvgcvpkkvmwntavhse
fmhdhadygfpscegkfnwrvikekrdayvsrlnaiyqnnltkshieiirghaaftsdpk
ptievsgkkytaphiliatggmpstpheXrvpntkdlslnklgiqtddkghiivdefqnt
nvkgiyavgdvcgkalltpvaiaagrklahrlfeykedskld
>d3grs_2 3.3.1.5.1 (166-290) Glutathione reductase {Human (Homo sapiens)}
sqipgaslgitsdgffqleelpgrsvivgagyiavemagilsalgsktslmirhdkvlrs
fdsmistncteelenagvevlkfsqvkevkktlsglevsmvtavpgrlpvmtmipdvdcl
lwaig
>d1gesa2 3.3.1.5.2 (147-262) Glutathione reductase {Escherichia coli}
dipgveygidsdgffalpalpervavvgagyigvelggvinglgakthlfemfdaplpsf
dpmisetlvevmnaegpqlhtnaipkavvkntdgsltleledgrsetvdcliwaig
>d1feca1 3.3.1.5.3 (1-169,287-357) Trypanothione reductase {Crithidia fasciculata}
sraydlvvigagsggleagwnaaslhkkrvavidlqkhhgpphyaalggtcvnvgcvpkk
lmvtganymdtiresagfgweldresvrpnwkaliaaknkavsgindsyegmfadteglt
fhqgfgalqdnhtvlvresadpnsavletldteyillatgswpqhlgieXvprsqtlqle
kagvevakngaikvdaysktnvdniyaigdvtdrvmltpvainegaafvdtvfankprat
d
>d1feca2 3.3.1.5.3 (170-286) Trypanothione reductase {Crithidia fasciculata}
gddlcitsneafyldeapkralcvgggyisiefagifnaykarggqvdlayrgdmilrgf
dselrkqlteqlranginvrthenpakvtknadgtrhvvfesgaeadydvvmlaigr
>d1aoga2 3.3.1.5.4 (170-286) Trypanothione reductase {Trypanosoma cruzi}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1trb_1 3.3.1.5.5 (1-118,245-316) Thioredoxin reductase {Escherichia coli}
gttkhskllilgsgpagytaavyaaranlqpvlitgmekggqlttttevenwpgdpndlt
gpllmermhehatkfeteiifdhinkvdlqnrpfrlngdngeytcdaliiatgasaryXh
spntaifegqlelengyikvqsgihgnatqtsipgvfaagdvmdhiyrqaitsagtgcma
aldaeryldgl
>d1trb_2 3.3.1.5.5 (119-244) Thioredoxin reductase {Escherichia coli}
lglpseeafkgrgvsacatsdgffyrnqkvavigggntaveealylsniasevhlihrrd
gfraekilikrlmdkvengniilhtnrtleevtgdqmgvtgvrlrdtqnsdniesldvag
lfvaig
>d1vdc_1 3.3.1.5.6 (1-117,244-316) Thioredoxin reductase {Mouse-ear cress (Arabidopsis thaliana)}
lethntrlcivgsgpaahtaaiyaaraelkpllfegwmandiapggqlttttdvenfpgf
pegilgveltdkfrkqserfgttiftetvtkvdfsskpfklftdskailadavilaigav
akXghepatkfldggveldsdgyvvtkpgttqtsvpgvfaagdvqdkkyrqaitaagtgc
maaldaehylqei
>d1vdc_2 3.3.1.5.6 (118-243) Thioredoxin reductase {Mouse-ear cress (Arabidopsis thaliana)}
rlsfvgsgevlggfwnrgisacavcdgaapifrnkplavigggdsameeanfltkygskv
yiihrrdafraskimqqralsnpkidviwnssvveaygdgerdvlgglkvknvvtgdvsd
lkvsglffai
>d1nhp_1 3.3.1.5.7 (1-119,243-321) NADH peroxidase {Streptococcus enterococcus faecalis}
mkvivlgsshggyeaveellnlhpdaeiqwyekgdfisflsagmqlylegkvkdvnsvry
mtgekmesrgvnvfsnteitaiqpkehqvtvkdlvsgeervenydkliispgavpfeldX
gvrpntawlkgtlelhpngliktdeymrtsepdvfavgdatlikynpadtevnialatna
rkqgrfavknleepvkpfp
>d1nhp_2 3.3.1.5.7 (120-242) NADH peroxidase {Streptococcus enterococcus faecalis}
ipgkdldniylmrgrqwaiklkqktvdpevnnvvvigsgyigieaaeafakagkkvtvid
ildrplgvyldkeftdvlteemeannitiatgetveryegdgrvqkvvtdknaydadlvv
vav
>d1lpfa2 3.3.1.5.8 (159-277) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
paplsddiivdstgalefqavpkklgvigagviglelgsvwarlgaevtvlealdkflpa
adeqiakealkvltkqglnirlgarvtasevkkkqvtvtftdangeqketfdklivavg
>d1lvl_1 3.3.1.5.8 (1-150,266-335) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
qqtiqttlliigggpggyvaairagqlgiptvlvegqalggtclnigcipskalihvaeq
fhqasrftepsplgisvasprldigqsvawkdgivdrlttgvaallkkhgvkvvhgwakv
ldgkqvevdgqriqcehlllatgsssvelpXrrprtkgfnlecldlkmngaaiaidercq
tsmhnvwaigdvagepmlahramaqgemvaeiiagkarrfe
>d1lvl_2 3.3.1.5.8 (151-265) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
mlplggpvisstealapkalpqhlvvvgggyiglelgiayrklgaqvsvvearerilpty
dseltapvaeslkklgialhlghsvegyengcllandgkggqlrleadrvlvavg
>d3lada1 3.3.1.5.8 (1-158,278-348) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
sqkfdvivigagpggyvaaiksaqlglktaliekykgkegktalggtclnvgcipskall
dssykfheahesfklhgistgevaidvptmiarkdqivrnltggvaslikangvtlfegh
gkllagkkvevtaadgssqvldtenvilasgskpveipXrrpvttdllaadsgvtlderg
fiyvddycatsvpgvyaigdvvrgamlahkaseegvvvaeriaghkaqmn
>d3lada2 3.3.1.5.8 (159-277) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
papvdqdvivdstgaldfqnvpgklgvigagviglelgsvwarlgaevtvleamdkflpa
vdeqvakeaqkiltkqglkillgarvtgtevknkqvtvkfvdaegeksqafdklivavg
>d1ebda1 3.3.1.5.9 (7-154,272-346) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aietetlvvgagpggyvaairaaqlgqkvtivekgnlggvclnvgcipskalisashrye
qakhseemgikaenvtidfakvqewkasvvkkltggvegllkgnkveivkgeayfvdant
vrvvngdsaqtytfknaiiatgsrpielXvgrrpntdelgleqigikmtnrglievdqqc
rtsvpnifaigdivpgpalahkasyegkvaaeaiaghpsavdyv
>d1ebda2 3.3.1.5.9 (155-271) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
pnfkfsnrildstgalnlgevpkslvvigggyigielgtayanfgtkvtilegageilsg
fekqmaaiikkrlkkkgvevvtnalakgaeeredgvtvtyeangetktidadyvlvt
>d1ojt_1 3.3.1.5.10 (117-275,401-470) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
gsadaeydvvvlgggpggysaafaaadeglkvaiveryktlggvclnvgcipskallhna
avidevrhlaangikypepeldidmlraykdgvvsrltgglagmaksrkvdviqgdgqfl
dphhlevsltagdayeqaaptgekkivafknciiaagsrXapngklisaekagvavtdrg
fievdkqmrtnvphiyaigdivgqpmlahkavheghvaaencaghkayfd
>d1ojt_2 3.3.1.5.10 (276-400) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
vtklpfipedpriidssgalalkevpgklliigggiiglemgtvystlgsrldvvemmdg
lmqgadrdlvkvwqkqneyrfdnimvntktvavepkedgvyvtfeganapkepqrydavl
vaagr
>d1fcda1 3.3.1.5.11 (1-114,256-327) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
agrkvvvvgggtggataakyikladpsievtliepntdyytcylsneviggdrklesikh
gydglrahgiqvvhdsatgidpdkklvktaggaefgydrcvvapgieliydkieXqragk
iaqiagltndagwcpvdiktfessihkgihvigdasianpmpksgysansqgkvaaaavv
vllkgee
>d1fcda2 3.3.1.5.11 (115-255) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
gyseeaaaklphawkageqtailrkqledmadggtvviappaapfrcppgpyerasqvay
ylkahkpmskviildssqtfskqsqfskgwerlygfgtenamiewhpgpdsavvkvdgge
mmvetafgdefkadvinlipp
>d1djna3 3.4.1.1.2 (341-489,646-729) Trimethylamine dehydrogenase, middle domain {Methylophilus methylotrophus w3a1}
dirvcigcnvcisrweiggppmictqnatageeyrrgwhpekfrqtknkdsvlivgagps
gseaarvlmesgytvhltdtaekigghlnqvaalpglgewsyhrdyretqitkllkknke
sqlalgqkpmtaddvlqygadkviiatgaXsectlwnelkaresewaendikgiyligda
eaprliadatftghrvareieeanpqiaipykretiawgtphmpggnfkieykv
>d1cjca2 3.4.1.1.3 (6-106,332-460) Adrenodoxin reductase of mitochondrial p450 systems {Bovine (Bos taurus)}
tpqicvvgsgpagfytaqhllkhhsrahvdiyekqlvpfglvrfgvapdhpevknvintf
tqtarsdrcafygnvevgrdvtvqelqdayhavvlsygaedXksrpidpsvpfdpklgvv
pnmegrvvdvpglycsgwvkrgptgvitttmtdsfltgqillqdlkaghlpsgprpgsaf
ikalldsrgvwpvsfsdwekldaeevsrgqasgkpreklldpqemlrllgh
>d1an9a1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1tml__ 3.5.1.1.1 Cellulase E2 {Thermomonospora fusca, strain yx}
ndspfyvnpnmssaewvrnnpndprtpvirdriasvpqgtwfahhnpgqitgqvdalmsa
aqaagkipilvvynapgrdcgnhssggapshsayrswidefaaglknrpayiivepdlis
lmsscmqhvqqevletmayagkalkagssqariyfdaghsawhspaqmaswlqqadisns
ahgiatntsnyrwtadevayakavlsaignpslravidtsrngngpagnewcdpsgraig
tpsttntgdpmidaflwiklpgeadgciagagqfvpqaayemaiaa
>d1bvwa_ 3.5.1.1.3 Cellobiohydrolase II (Cel6a) {Humicola insolens}
gnpfegvqlwannyyrsevhtlaipqitdpalraaasavaevpsfqwldrnvtvdtllvq
tlseireanqaganpqyaaqivvydlpdrdcaaaasngewaianngvnnykayinrirei
lisfsdvrtilviepdslanmvtnmnvpkcsgaastyreltiyalkqldlphvamymdag
hagwlgwpaniqpaaelfakiyedagkpravrglatnvanynawsvsspppytspnpnyd
ekhyieafrplleargfpaqfivdqgrsgkqptgqkewghwcnaigtgfgmrptantghq
yvdafvwvkpggecdgtsdttaarydyhcgledalkpapeagqwfneyfiqllrnanppf
>d1cm5a_ 3.6.1.1.1 Pyruvate formate-lyase, PFL {Escherichia coli}
selneklatawegftkgdwqnevnvrdfiqknytpyegdesflagateatttlwdkvmeg
vklenrthapvdfdtavastitshdagyinkqlekivglqteaplkralipfggikmieg
sckaynreldpmikkifteyrkthnqgvfdvytpdilrcrksgvltglpdaygrgriigd
yrrvalygidylmkdklaqftslqadlengvnleqtirlreeiaeqhralgqmkemaaky
gydisgpatnaqeaiqwtyfgylaavksqngaamsfgrtstfldvyierdlkagkiteqe
aqemvdhlvmklrmvrflrtpeydelfsgdpiwatesiggmgldgrtlvtknsfrflntl
ytmgpspepnmtilwseklplnfkkfaakvsidtsslqyenddlmrpdfnnddyaiaaav
spmivgkqmqffgaranlaktmlyainggvdeklkmqvgpksepikgdvlnydevmermd
hfmdwlakqyitalniihymhdkysyeaslmalhdrdvirtmacgiaglsvaadslsaik
yakvkpirdedglaidfeiegeypqfgnndprvddlavdlverfmkkiqklhtyrdaipt
qsvltitsnvvygkktgntpdgrragapfgpganpmhgrdqkgavasltsvaklpfayak
dgisytfsivpnalgkddevrktnlaglmdgyfhheasieggqhlnvnvmnremlldame
npekypqltirvsgyavrfnsltkeqqqdvitrtftqsm
>d1rlr_2 3.6.1.2.1 (222-748) R1 subunit of ribonucleotide reductase, C-terminal domain {Escherichia coli}
fsscvliecgdsldsinatssaivkyvsqragiginagriralgspirggeafhtgcipf
ykhfqtavkscsqggvrggaatlfypmwhlevesllvlknnrgvegnrvrhmdygvqink
lmytrllkgeditlfspsdvpglydaffadqeeferlytkyekddsirkqrvkavelfsl
mmqerastgriyiqnvdhcnthspfdpaiapvrqsnlcleialptkplndvndengeial
ctlsafnlgainnldeldelailavraldalldyqdypipaakrgamgrrtlgigvinfa
yylakhgkrysdgsannlthktfeaiqyyllkasnelakeqgacpwfnettyakgilpid
tykkdldtianeplhydwealresikthglrnstlsalmpsetssqisnatngiepprgy
vsikaskdgilrqvvpdyehlhdayellwempgndgylqlvgimqkfidqsisantnydp
srfpsgkvpmqqllkdlltaykfgvktlyyqntrddiddlsnfql
>d1b8ba_ 3.6.1.3.1 Class III anaerobic ribonucleotide triphosphate reductase NRDD subunit {Bacteriophage T4}
srvfptqrdlmagivskhiaknmvpsfimkahesgiihvhdidyspalpftncclvdlkg
mlengfklgnaqietpksigvataimaqitaqvashqyggttfanvdkvlspyvkrtyak
hiedaekwqiadalnyaqsktekdvydafqayeyevntlfssngqtpfvtltfgtgtdwt
ermiqkailknrikglgrdgitpifpklvmfveegvnlykddpnydikqlalecaskrmy
pdiisaknnkaitgssvpvspmgcrsflsvwkdstgneildgrnnlgvvtlnlprialds
yigtqfneqkfvelfnermdlcfealmcrisslkgvkatvapilyqegafgvrlkpdddi
ielfkngrssvslgyigihelnilvgrdigreiltkmnahlkqwtertgfafslystpae
nlcyrfckldtekygsvkdvtdkgwytnsfhvsveenitpfekisreapyhfiatgghis
yvelpdmknnlkgleavwdyaaqhldyfgvnmpvdkcftcgsthemtptengfvcsicge
tdpkkmntirrtcgylgnpnerg
>d1dik_2 3.7.1.1.1 (377-505) Pyruvate phosphate dikinase, central domain {Escherichia coli}
lhptfnpaalkagevigsalpaspgaaagkvyftadeakaahekgervilvrletspedi
egmhaaegiltvrggmtshaavvargmgtccvsgcgeikineeaktfelgghtfaegdyi
sldgstgki
>d1zyma2 3.7.1.2.1 (3-21,145-249) N-terminal domain of enzyme I of the PEP:sugar phosphotransferase system {Escherichia coli}
sgilaspgiafgkalllkeXkiidlsaiqdevilvaadltpsetaqlnlkkvlgfitdag
grtshtsimarslelpaivgtgsvtsqvknddylildavnnqvyvnptnevidkmravqe
qvase
>d1aco_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1a9xb1 3.7.3.1.1 (1502-1652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1de4c2 3.7.4.1.1 (190-382) Transferrin receptor ectodomain, apical domain {Human (Homo sapiens)}
iqvkdsaqnsviivdkngrlvylvenpggyvayskaatvtgklvhanfgtkkdfedlytp
vngsivivragkitfaekvanaeslnaigvliymdqtkfpivnaelsffghahlgtgdpy
tpgfpsfnhtqfppsrssglpnipvqtisraaaeklfgnmegdcpsdwktdstcrmvtse
sknvkltvsnvlk
>d1kid__ 3.7.5.1.1 GroEL {Escherichia coli}
glvprgsegmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavaka
gkplliiaedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtvise
eigmelekatledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydre
klqervaklaggv
>d1ass__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1a19a_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1a19b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1ab7__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1ay7b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b27d_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegaditiils
>d1b27e_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1b27f_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1b2sd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2se_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2sf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdclagwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b2ud_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b2ue_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b2uf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenlaalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b3sd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
mkkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqs
kqltengaesvlqvfreakaegcditiils
>d1b3se_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1b3sf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpefygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1bgse_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bgsg_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brsd_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1brse_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqskq
ltengaesvlqvfreakaegaditiils
>d1brsf_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1bta__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1btb__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1a4ya_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1d0ba_ 3.9.2.1.1 Internalin B LRR domain {Listeria monocytogenes}
etitvstpikqifpddafaetikdnlkkksvtdavtqnelnsidqiiannsdiksvqgiq
ylpnvtklflngnkltdikpltnlknlgwlfldenkikdlsslkdlkklkslslehngis
dinglvhlpqleslylgnnkitditvlsrltkldtlslednqisdivplagltklqnlyl
sknhisdlralaglknldvlelfsqec
>d1a9na_ 3.9.3.1.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfk
>d1igra1 3.9.3.2.1 (1-149) L1 and L2 domains of the type 1 insulin-like growth factor receptor {Human (Homo sapiens)}
eicgpgidirndyqqlkrlenctviegylhilliskaedyrsyrfpkltviteylllfrv
agleslgdlfpnltvirgwklfynyalvifemtnlkdiglynlrnitrgairieknadlc
ylstvdwslildavsnnyivgnkppkecg
>d1igra2 3.9.3.2.1 (300-478) L1 and L2 domains of the type 1 insulin-like growth factor receptor {Human (Homo sapiens)}
kvceeekktktidsvtsaqmlqgctifkgnllinirrgnniaselenfmglievvtgyvk
irhshalvslsflknlrlilgeeqlegnysfyvldnqnlqqlwdwdhrnltikagkmyfa
fnpklcvseiyrmeevtgtkgrqskgdintrnngerascesdvddddkeqkliseedln
>d1aua_2 3.10.1.1.1 (97-299) C-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
ydekpliakfypqyyhktdkdgrpvyfeelgavnlhemnkvtseermlknlvweyesvvq
yrlpacsraaghlvetsctimdlkgisissaysvmsyvreasyisqnyypermgkfyiin
apfgfstafrlfkpfldpvtvskifilgssyqkellkqipaenlpvkfggksevdeskgg
lylsdigpwrdpkyigpegeape
>d1auz__ 3.10.2.1.1 SpoIIaa {Bacillus subtilis}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1tyfa_ 3.11.1.1.1 Clp protease, ClpP subunit {Escherichia coli}
srgersfdiysrllkervifltgqvedhmanlivaqmlfleaenpekdiylyinspggvi
tagmsiydtmqfikpdvsticmgqaasmgaflltagakgkrfclpnsrvmihqplggyqg
qatdieihareilkvkgrmnelmalhtgqsleqierdterdrflsapeaveyglvdsilt
hrn
>d1nzya_ 3.11.1.2.1 4-Chlorobenzoyl-CoA dehalogenase {Pseudomonas strain CBS-3}
myeaighrvedgvaeitiklprhrnalsvkamqevtdalnraeeddsvgavmitgaedaf
cagfylreipldkgvagvrdhfriaalwwhqmihkiirvkrpvlaaingvaaggglgisl
asdmaicadsakfvcawhtigigndtatsyslarivgmrramelmltnrtlypeeakdwg
lvsrvypkdefrevawkvarelaaapthlqvmakerfhagwmqpveectefeiqnviasv
thphfmpcltrfldghradrpqvelpagv
>d2duba_ 3.11.1.2.2 Enoyl-CoA hydratase {Rat (Rattus norvegicus)}
nfqyiitekkgknssvgliqlnrpkalnalcnglieelnqaletfeedpavgaivltgge
kafaagadikemqnrtfqdcysgkflshwdhitrikkpviaavngyalgggcelammcdi
iyagekaqfgqpeillgtipgaggtqrltravgkslamemvltgdrisaqdakqaglvsk
ifpvetlveeaiqcaekiannskiivamakesvnaafemtltegnklekklfystfatdd
rregmsafvekrkanfkdh
>d1dcia_ 3.11.1.2.3 Dienoyl-CoA isomerase {Rat (Rattus norvegicus)}
ayesiqvtsaqkhvlhvqlnrpekrnamnrafwrelvecfqkiskdsdcravvvsgagkm
ftsgidlmdmasdilqppgddvariawylrdlisryqktftviekcpkpviaaihggcig
ggvdlisacdiryctqdaffqvkevdvglaadvgtlqrlpkvignrslvneltftarkmm
adealdsglvsrvfpdkdvmlnaafalaadisskspvavqgskinliysrdhsvdesldy
matwnmsmlqtqdiiksvqaamekkdsksitfskl
>d1rvv1_ 3.12.1.1.1 beta-subunit (capsid) of the lumazine synthase/riboflavin synthase complex {Bacillus subtilis}
mniiqgnlvgtglkigivvgrfndfitskllsgaedallrhgvdtndidvawvpgafeip
faakkmaetkkydaiitlgtvirgatthydyvcneaakgiaqaanttgvpvifgivtten
ieqaieragtkagnkgvdcavsaiemanlnrsfe
>d1cp3a_ 3.13.1.1.1 Apopain {Human (Homo sapiens)}
nsykmdypemglciiinnknfhkstgmtsrsgtdvdaanlretfrnlkyevrnkndltre
eivelmrdvskedhskrssfvcvllshgeegiifgtngpvdlkkitnffrgdrcrsltgk
pklfiiqacrgteldcgietdsgvdddmachkipvdadflyaystapgyyswrnskdgsw
fiqslcamlkqyadklefmhiltrvnrkvatefesfsfdatfhakkqipcivsmltkely
fyh
>e1pau.1b 3.13.1.1.1 Apopain {Human (Homo sapiens)}
kipveadflyaystapgyyswrnskdgswfiqslcamlkqyadklefmhiltrvnrkvat
efesfsfdatfhakkqipcivsmltkelyfy
>e1bmq.1b 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpdgraqmpttervtltrcfylfpgh
>e1ibc.1a 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
gnvklcsleeaqriwkqksaeiypimdkssrtrlaliicneefdsiprrtgaevditgmt
mllqnlgysvdvkknltasdmtteleafahrpehktsdstflvfmshgiregicgkkhse
qvpdilqlnaifnmlntkncpslkdkpkviiiqacrgdspgvvwfkd
>e1ibc.1b 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpagraqmpttervtltrcfylfpgh
>e1ice.1b 3.13.1.1.2 Interleukin-1beta converting enzyme (a cysteine protease) {Human (Homo sapiens)}
aikkahiekdfiafcsstpdnvswrhptmgsvfigrliehmqeyacscdveeifrkvrfs
feqpdgraqmpttervtltrcfylfpgh
>d1laue_ 3.14.1.1.2 Uracil-DNA glycosylase {Herpes simplex virus, type 1, HSV1}
ldwttfrrvfliddawrplmepelanpltahllaeynrrcqteevlppredvfswtryct
pdevrvviigqdpyhhpgqahglafsvranvppppslrnvlaavkncypearmsghgcle
kwardgvlllnttltvkrgaaashsrigwdrfvggvirrlaarrpglvfmlwgthaqnai
rpdprvhcvlkfshpsplskvpfgtcqhflvanryletrsispidwsv
>d3euga_ 3.14.1.1.3 Uracil-DNA glycosylase {Escherichia coli}
ltwhdvlaeekqqphflntlqtvaserqsgvtiyppqkdvfnafrftelgdvkvvilgqd
pyhgpgqahglafsvrpgiaippsllnmykelentipgftrpnhgyleswarqgvlllnt
vltvragqahshaslgwetftdkvislinqhregvvfllwgshaqkkgaiidkqrhhvlk
aphpsplsahrgffgcnhfvlanqwleqhgetpidwmpvlpaese
>d1muga_ 3.14.1.2.1 G:T/U mismatch-specific DNA glycosylase {Escherichia coli}
mvedilapglrvvfcginpglssagtgfpfahpanrfwkviyqagftdrqlkpqeaqhll
dyrcgvtklvdrptvqanevskqelhaggrkliekiedyqpqalailgkqayeqgfsqrg
aqwgkqtltigstqiwvlpnpsglsrvsleklveayreldqalvv
>d1mla_1 3.15.1.1.1 (3-127,198-307) Catalytic domain of malonyl-CoA ACP transacylase {Escherichia coli}
qfafvfpgqgsqtvgmladmaasypiveetfaeasaalgydlwaltqqgpaeelnktwqt
qpalltasvalyrvwqqqggkapammaghslgeysalvcagvidfadavrlvemrgkfmq
eavpeXvpshcalmkpaadklavelakitfnaptvpvvnnvdvkcetngdairdalvrql
ynpvqwtksveymaaqgvehlyevgpgkvltgltkrivdtltasalnepsamaaal
>d1cf9a1 3.16.1.1.1 (598-753) Catalase, C-terminal domain {Escherichia coli, HPII}
vkgrvvaillndevrsadllailkalkakgvhakllysrmgevtaddgtvlpiaatfaga
psltvdavivpcgniadiadngdanyylmeaykhlkpialagdarkfkatikiadqgeeg
iveadsadgsfmdelltlmaahrvwsripkidkipa
>d3chy__ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1tmy__ 3.16.2.1.3 CheY protein {Thermotoga maritima}
gkrvlivddaafmrmmlkdiitkagyevageatngreavekykelkpdivtmditmpemn
gidaikeimkidpnakiivcsamgqqamvieaikagakdfivkpfqpsrvvealnkvs
>d1a04a2 3.16.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1ntr__ 3.16.2.1.5 NTRC receiver domain {Salmonella typhimurium}
mqrgivwvvdddssirwvleralagagltcttfengnevlaalasktpdvllsdirmpgm
dglallkqikqrhpmlpviimtahsdldaavsayqqgafdylpkpfdideavalverais
hyqe
>d1dbwa_ 3.16.2.1.6 Transcriptional regulatory protein FixJ, receiver domain {Rhizobium meliloti}
mqdytvhivddeepvrkslafmltmngfavkmhqsaeaflafapdvrngvlvtdlrmpdm
sgvellrnlgdlkinipsivitghgdvpmaveamkagavdfiekpfedtviieaierase
hlv
>d1qmpa_ 3.16.2.1.7 Sporulation response regulator Spo0A {Bacillus stearothermophilus}
sikvciaddnrelvslldeyissqpdmevigtayngqdclqmleekrpdilllxiimphl
dglavleriragfehqpnvimltafgqedvtkkavelgasyfilkpfdmenlahhirqvy
gkttpvv
>d1srra_ 3.16.2.1.8 Sporulation response regulator Spo0F {Bacillus subtilis}
nekilivddqsgirillnevfnkegyqtfqaanglqaldivtkerpdlvlldmkipgmdg
ieilkrmkvidenirviimtaygeldmiqeskelgalthfakpfdideirdavkkylpl
>d1a2oa1 3.16.2.1.9 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1b00a_ 3.16.2.1.10 PhoB receiver domain {Escherichia coli}
arrilvvedeapiremvcfvleqngfqpveaedydsavnqlnepwpdlilldwmlpggsg
iqfikhlkresmtrdipvvmltargeeedrvrgletgaddyitkpfspkelvarikavmr
ri
>d1dcfa_ 3.16.2.2.1 Receiver domain of the ethylene receptor {Thale cress (Arabidopsis thaliana)}
hmsnftglkvlvmdengvsrmvtkgllvhlgcevttvssneeclrvvshehkvvfmdvcm
pgvenyqialrihekftkqrhqrpllvalsgntdkstkekcmsfgldgvllkpvsldnir
dvlsdlleprvlye
>d1qo0d_ 3.16.2.3.1 Negative regulator of the amidase operon AmiR {Pseudomonas aeruginosa}
sansllgslrelqvlvlnppgevsdalvlqlirigcsvrqcwpppeafdvpvdvvftsif
qnrhhdeiaallaagtprttlvalveyespavlsqiielechgvitqpldahrvlpvlvs
arriseemaklkqkteqlqdriagqarinqakvllmqrhgwdereahqhlsreamkrrep
ilkiaqell
>d2scua2 3.16.3.1.1 (122-286) Succinyl-CoA synthetase, alpha-chain, C-terminal domain {Escherichia coli}
ncpgvitpgeckigiqpghihkpgkvgivsrsgtltyeavkqttdygfgqstcvgiggdp
ipgsnfidilemfekdpqteaivmigeiggsaeeeaaayikehvtkpvvgyiagvtapkg
krmgxagaiiaggkgtadekfaaleaagvktvrsladigealktv
>d2scub1 3.16.3.1.2 (245-385) Succinyl-CoA synthetase, beta-chain, C-terminal domain {Escherichia coli}
aaqwelnyvaldgnigcmvngaglamgtmdivklhggepanfldvgggatkervteafki
ilsddkvkavlvnifggivrcdliadgiigavaevgvnvpvvvrlegnnaelgakklads
glniiaakgltdaaqqvvaav
>d2fcr__ 3.16.4.1.1 Flavodoxin {Chondrus crispus}
kigiffststgnttevadfigktlgakadapidvddvtdpqalkdydllflgaptwntga
dtersgtswdeflydklpevdmkdlpvaifglgdaegypdnfcdaieeihdcfakqgakp
vgfsnpddydyeesksvrdgkflglpldmvndqipmekrvagwveavvsetgv
>d1akr__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwa
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1rcf__ 3.16.4.1.3 Flavodoxin {Anabaena PCC 7119 and 7120}
skkiglfygtqtgktesvaeiirdefgndvvtlhdvsqaevtdlndyqyliigcptwnig
elqsdweglyselddvdfngklvayfgtgdqigyadnfqdaigileekisqrggktvgyw
stdgydfndskalrngkfvglaldednqsdltddrikswvaqlksefgl
>d1ag9a_ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d5nul__ 3.16.4.1.6 Flavodoxin {Clostridium beijerinckii}
mkivywsgtgntekmaeliakgiiesgkdvntinvsdvnidellnedililgcsamtdev
leesefepfieeistkisgkkvalfgsygwgdgkwmrdfeermngygcvvvetplivqne
pdeaeqdciefgkkiani
>d1bvyf_ 3.16.4.1.7 FMN-binding domain of the cytochrome P450bm-3 {Bacillus megaterium}
ntpllvlygsnmgtaegtardladiamskgfapqvatldshagnlpregavlivtasyng
hppdnakqfvdwldqasadevkgvrysvfgcgdknwattyqkvpafidetlaakgaenia
drgeadasddfegtyeewrehmwsdvaayfnl
>d1b1ca_ 3.16.4.2.2 NADPH-cytochrome p450 reductase, N-terminal domain {Human (Homo sapiens)}
ssfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladlsslp
eidnalvvfcmatygegdptdnaqdfydwlqetdvdlsgvkfavfglgnktyehfnamgk
yvdkrleqlgaqrifelglgdddgnleedfitwreqfwpavcehfg
>d1d4aa_ 3.16.4.3.3 NAD(P)H:quinone reductase {Human (Homo sapiens)}
vgrralivlahsertsfnyamkeaaaaalkkkgwevvesdlyamnfnpiisrkditgklk
dpanfqypaesvlaykeghlspdivaeqkkleaadlvifqfplqwfgvpailkgwfervf
igefaytyaamydkgpfrskkavlsittggsgsmyslqgihgdmnvilwpiqsgilhfcg
fqvlepqltysightpadariqilegwkkrleniwdetplyfapsslfdlnfqagflmkk
evqdeeknkkfglsvghhlgksiptdnqikark
>d1bmta2 3.16.5.1.1 (741-896) Methionine synthase, C-terminal domain {Escherichia coli}
eqgktngkmviatvkgdvhdigknivgvvlqcnnyeivdlgvmvpaekilrtakevnadl
iglsglitpsldemvnvakemerqgftiplliggattskahtavkieqnysgptvyvqna
srtvgvvaallsdtqrddfvartrkeyetvriqhgr
>d1b1a__ 3.16.5.1.3 Glutamate mutase, small subunit {Clostridium cochlearium}
mekktivlgvigsdchavgnkildhaftnagfnvvnigvlspqevfikaaietkadaill
sslygqgeidckglrqkcdeaglegillyvggnivvgkqhwpdvekrfkdmgydrvyapg
tppevgiadlkkdlnie
>d7reqa2 3.16.5.1.4 (561-728) Methylmalonyl-CoA mutase C-terminal domains of alpha and beta subunits {Propionibacterium freudenreichii, shermani}
aqirtisgvyskevkntpeveearelveefeqaegrrprillakmgqdghdrgqkviata
yadlgfdvdvgplfqtpeetarqaveadvhvvgvsslagghltlvpalrkeldklgrpdi
litvggvipeqdfdelrkdgaveiytpgtvipesaislvkklraslda
>d7reqb2 3.16.5.1.4 (476-638) Methylmalonyl-CoA mutase C-terminal domains of alpha and beta subunits {Propionibacterium freudenreichii, shermani}
tkpfpaaparkglawhrdsevfeqlmdrstsvserpkvflaclgtrrdfggregfsspvw
hiagidtpqveggttaeiveafkksgaqvadlcssakvyaqqglevakalkaagakalyl
sgafkefgddaaeaeklidgrlfmgmdvvdtlsstldilgvak
>d1orda1 3.16.6.1.1 (1-107) Ornithine decarboxylase N-terminal "wing" domain {Lactobacillus strain 30a}
ssslkiastqearqyfdtdrvvvdavgsdftdvgaviamdyetdvidaadatkfgipvfa
vtkdaqaisadelkkifhiidlenkfdatvnareietavnnyedsil
>d1qcza_ 3.16.7.1.1 N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) mutase PurE {Escherichia coli}
parvaivxgsksdwatxqfaaeifeilnvphhvevvsahrtpdklfsfaesaeengyqvi
iagaggaahlpgxiaaktlvpvlgvpvqsaalsgvdslysivqxprgipvgtlaigkaga
anaallaaqilathdkelhqrlndwrkaqtdevlenpdprgaa
>d1cex__ 3.16.8.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascadvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1bs9__ 3.16.8.1.2 Acetylxylan esterase {Penicillium purpurogenum}
scpaihvfgarettaspgygssstvvngvlsaypgstaeainypacggqsscggasysss
vaqgiaavasavnsfnsqcpstkivlvgysqggeimdvalcgggdpnqgytntavqlsss
avnmvkaaifmgdpmfraglsyevgtcaaggfdqrpagfscpsaakiksycdasdpyccn
gsnaathqgygseygsqalafvksklg
>d1esc__ 3.16.9.1.1 Esterase {Streptomyces scabies}
dpvptvffgdsytanfgiapvtnqdsergwcfqakenypavatrsladkgitldvqadvs
cggalihhfwekqelpfgagelppqqdalkqdtqltvgslggntlgfnrilkqcsdelrk
psllpgdpvdgdepaakcgeffgtgdgkqwlddqfervgaeleelldrigyfapdakrvl
vgyprlvpedttkcltaapgqtqlpfadipqdalpvldqiqkrlndamkkaaadggadfv
dlyagtgantacdgadrgigglledsqlellgtkipwyahpndkgrdiqakqvadkieei
ln
>d1flca2 3.16.9.2.1 (1-217,322-427) Esterase domain of haemagglutinin-esterase-fusion glycoprotein HEF1 {Influenza C virus}
ekikiclqkqvnssfslhngfggnlyateekrmfelvkpkagasvlnqstwigfgdsrtd
ksnsafprsadvsaktadkfrflsggslmlsmfgppgkvdylyqgcgkhkvfyegvnwsp
haaincyrknwtdiklnfqkniyelasqshcmslvnaldktiplqvtagtagncnnsflk
npalytqevkpsenkcgkenlafftlptqfgtyecklXresdyavdqaclstpgcmliqk
qkpyigeaddhhgdqemrellsgldyearcisqsgwvnetspftekyllppkfgrcplaa
keesipkipdglliptsgtdttvt
>d1wab__ 3.16.9.3.1 Platelet-activating factor acetylhydrolase {Bovine (Bos taurus)}
enpaskptpvqdvqgdgrwmslhhrfvadskdkepevvfigdslvqlmhqceiwrelfsp
lhalnfgiggdstqhvlwrlengelehirpkivvvwvgtnnhghtaeqvtggikaivqlv
nerqpqarvvvlgllprgqhpnplreknrrvnelvraalaghprahfldadpgfvhsdgt
ishhdmydylhlsrlgytpvcralhslllrll
>d1ex1a2 3.16.10.1.1 (389-602) Beta-D-glucan exohydrolase, C-terminal domain {Barley (Hordeum vulgare)}
lvllkngktstdapllplpkkapkilvagshadnlgyqcggwtiewqgdtgrttvgttil
eavkaavdpstvvvfaenpdaefvksggfsyaivavgehpytetkgdnlnltipepglst
vqavcggvrcatvlisgrpvvvqpllaasdalvaawlpgsegqgvtdalfgdfgftgrlp
rtwfksvdqlpmnvgdahydplfrlgyglttnat
>d2naca2 3.16.11.1.1 (1-147,336-374) Formate dehydrogenase {Pseudomonas sp. 101}
akvlcvlyddpvdgypktyarddlpkidhypggqtlptpkaidftpgqllgsvsgelglr
kylesnghtlvvtsdkdgpdsvferelvdadvvisqpfwpayltperiakaknlklalta
gigsdhvdlqsaidrnvtvaevtycnsXttltaqaryaagtreilecffegrpirdeyli
vqggala
>d1qp8a2 3.16.11.1.2 (2-82,264-302) Putative formate dehydrogenase {Pyrobaculum aerophilum}
elyvnfelppeaeeelrkyfkivrggdlgnveaalvsritaeelakxprlkfiqvvtagl
dhlpwesipphvtvagnagsnXgygnervwrqxvxeavrnlityatggrprniakredyi
g
>d1dxy_2 3.16.11.1.3 (1-100) D-2-hydroxyisocaproate dehydrogenase {Lactobacillus casei}
mkiiaygarvdeiqyfkqwakdtgntleyhtefldentvewakgfdginslqttpyaagv
fekmhaygikfltirnvgtdnidmtamkqygirlsnvpay
>d1gdha2 3.16.11.1.4 (2-100,292-321) D-glycerate dehydrogenase {Hyphomicrobium methylovorum}
kkkilitwplpeaamararesydviahgddpkitidemietaksvdallitlnekcrkev
idripenikcistysigfdhidldackargikvgnaphgXatqaredmahqandlidalf
ggadmsyala
>d1psda2 3.16.11.1.5 (7-107,296-326) Phosphoglycerate dehydrogenase {Escherichia coli}
ekdkikfllvegvhqkaleslraagytniefhkgalddeqlkesirdahfiglrsrthlt
edvinaaeklvaigcfcigtnqvdldaaakrgipvfnapfsXstqeaqeniglevagkli
kysdngstlsavn
>d2dlda2 3.16.11.1.6 (1-103,301-337) D-lactate dehydrogenase {Lactobacillus helveticus}
mtkvfayairkdeepflnewkeahkdidvdytdklltpetaklakgadgvvvyqqldyta
dtlqaladagvtkmslrnvgvdnidmdkakelgfqitnvpvysXytthavrnmvvkafnn
nlklingekpdspvalnknkf
>d1pjca2 3.16.11.2.1 (1-135,304-361) L-alanine dehydrogenase {Phormidium lapideum}
meigvpkeiknqefrvglspssvrtlveaghtvfietqagigagfadqdyvqagaqvvps
akdawsremvvkvkeplpaeydlmqkdqllftylhlaaarelteqlmrvgltaiayetve
lpnrslplltpmsiiXvpwtatqalnnstlpyvvklanqglkaletddalakglnvqahr
lvhpavqqvfpdla
>d1b3ra2 3.16.11.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d2dhqa_ 3.16.12.1.1 Type II 3-dehydroquinate dehydratase {Mycobacterium tuberculosis}
livnvingpnlgrlgrrepavyggtthdelvaliereaaelglkavvrqsdseaqlldwi
hqaadaaepvilnagglthtsvalrdacaelsaplievhisnvhareefrrhsylspiat
gvivglgiqgyllalrylaeh
>d1a9xa2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1b93a_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryla
>d1fnc_2 3.18.1.1.1 (155-314) Ferredoxin reductase (flavodoxin reductase) {Spinach (Spinacia oleracea)}
mlmpkdpnatiimlgtgtgiapfrsflwkmffekhddykfnglawlflgvptsssllyke
efekmkekapdnfrldfavsreqtnekgekmyiqtrmaqyavelwemlkkdntyvymcgl
kgmekgiddimvslaaaegidwieykrqlkkaeqwnvevy
>d1que_2 3.18.1.1.3 (142-303) Ferredoxin reductase (flavodoxin reductase) {Cyanobacterium (Anabaena), PCC 7119}
lpddpeanvimlatgtgiapmrtylwrmfkdaeraanpeyqfkgfswlvfgvpttpnily
keeleeiqqkypdnfrltyaisreqknpqggrmyiqdrvaehadqlwqliknqkthtyic
glrgmeegidaalsaaaakegvtwsdyqkdlkkagrwhvety
>d1fdr_2 3.18.1.1.4 (101-248) Ferredoxin reductase (flavodoxin reductase) {Escherichia coli}
devphcetlwmlatgtaigpylsilrlgkdldrfknlvlvhaaryaadlsylplmqelek
ryegklriqtvvsretaagsltgripaliesgelestiglpmnketshvmlcgnpqmvrd
tqqllketrqmtkhlrrrpghmtaehyw
>d1a8p_2 3.18.1.1.5 (101-258) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
tsdllpgkhlymlstgtglapfmsliqdpevyerfekvvlihgvrqvnelayqqfitehl
pqseyfgeavkekliyyptvtresfhnqgrltdlmrsgklfediglppinpqddramicg
spsmldescevldgfglkisprmgepgdylierafvek
>d1qfja2 3.18.1.1.6 (98-232) NAD(P)H:flavin oxidoreductase {Escherichia coli}
rddeerpmiliaggtgfsyarsilltalarnpnrditiywggreeqhlydlcelealslk
hpglqvvpvveqpeagwrgrtgtvltavlqdhgtlaehdiyiagrfemakiardlfcser
naredrlfgdafafi
>d2cnd_2 3.18.1.1.7 (125-270) Nitrate reductase {Corn (Zea mays)}
gsfvingkqrnarrlamicggsgitpmyqiiqavlrdqpedhtemhlvyanrteddillr
deldrwaaeypdrlkvwyvidqvkrpeegwkysvgfvteavlrehvpeggddtlalacgp
ppmiqfaispnlekmkydmansfvvf
>d1ndh_2 3.18.1.1.8 (126-272) cytochrome b5 reductase {Pig (Sus scrofa), liver}
gkfairpdkksspviktvksvgmiaggtgitpmlqviraimkdpddhtvchllfanqtek
dillrpeleelrnehsarfklwytvdrapeawdysqgfvneemirdhlpppeeeplvlmc
gpppmiqyaclpnlervghpkercfaf
>d2pia_2 3.18.1.2.1 (104-223) Phthalate dioxygenase reductase {Pseudomonas cepacia, db01}
efpldkraksfilvaggigitpmlsmarqlraeglrsfrlyyltrdpegtaffdeltsde
wrsdvkihhdhgdptkafdfwsvfekskpaqhvyccgpqalmdtvrdmtghwpsgtvhfe
>d1amoa3 3.18.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1cqxa3 3.18.1.4.1 (262-403) Flavohemoglobin, C-terminal domain {Alcaligenes eutrophus}
dvdaktpivlisggvgltpmvsmlkvalqapprqvvfvhgarnsavhamrdrlreaakty
enldlfvfydqplpedvqgrdydypglvdvkqieksillpdadyyicgpipfmrmqhdal
knlgihearihyevfgpdlfae
>d2ts1_2 3.19.1.1.1 (1-227) Tyrosyl-tRNA synthetase (TyrRS) {Bacillus stearothermophilus, nca 1503}
mdllaelqwrglvnqttdedglrkllneervtlycgfdptadslhighlatiltmrrfqq
aghrpialvggatgligdpsgkksertlnaketveawsarikeqlgrfldfeadgnpaki
knnydwigpldvitflrdvgkhfsvnymmakesvqsrietgisftefsymmlqaydflrl
yetegcrlqiggsdqwgnitaglelirktkgearafgltiplvtkad
>d1gtra2 3.19.1.1.2 (8-338) Glutaminyl-tRNA synthetase (GlnRS) {Escherichia coli}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen
>d1gln_2 3.19.1.1.3 (1-305) Glutamyl-tRNA synthetase (GluRS) {Thermus thermophilus}
mvvtriapsptgdphvgtayialfnyawarrnggrfivriedtdraryvpgaeerilaal
kwlglsydegpdvaaptgpyrqserlplyqkyaeellkrgwayrafetpeeleqirkekg
gydgrarnippeeaeerarrgephvirlkvprpgttevkdelrgvvvydnqeipdvvllk
sdgyptyhlanvvddhlmgvtdviraeewlvstpihvllyrafgweaprfyhmpllrnpd
ktkiskrkshtsldwykaegflpealrnylclmgfsmpdgreiftleefiqaftwervsl
ggpvf
>d1a8h_2 3.19.1.1.5 (1-348) Methionyl-tRNA synthetase (MetR) {Thermus thermophilus}
mekvfyvttpiyyvnaephlghayttvvadflarwhrldgyrtffltgtdehgetvyraa
qaagedpkafvdrvsgrfkrawdllgiayddfirtteerhkkvvqlvlkkvyeagdiyyg
eyeglycvscerfytekelveglcpihgrpverrkegnyffrmekyrpwlqeyiqenpdl
irpegyrnevlamlaepigdlsisrpksrvpwgiplpwdenhvtyvwfdallnyvsaldy
pegeayrtfwphawhligkdilkphavfwptmlkaagipmyrhlnvggfllgpdgrkmsk
tlgnvvdpfallekygrdalryyllreipygqdtpvseealrtryead
>d1qqta2 3.19.1.1.6 (3-140,176-388) Methionyl-tRNA synthetase (MetR) {Escherichia coli}
vakkilvtcalpyangsihlghmlehiqadvwvryqrmrghevnficaddahgtpimlka
qqlgitpeqmigemsqehqtdfagfnisydnyhsthseenrqlseliysrlkengfiknr
tisqlydpekgmflpdrfXvvsgatpvmrdsehfffdlpsfsemlqawtrsgalqeqvan
kmqewfesglqqwdisrdapyfgfeipnapgkyfyvwldapigymgsfknlcdkrgdsvs
fdeywkkdstaelyhfigkdivyfhslfwpamlegsnfrkpsnlfvhgyvtvngakmsks
rgtfikastwlnhfdadslryyytaklssriddidlnledfvqrvnadivnk
>d1qu2a3 3.19.1.1.8 (1-200,395-644) Isoleucyl-tRNA synthetase (IleRS) {Staphylococcus aureus}
mdyektllmpktdfpmrgglpnkepqiqekwdaedqyhkaleknkgnetfilhdgppyan
gnlhmghalnkilkdfivryktmqgfyapyvpgwdthglpieqaltkkgvdrkkmstaef
rekckefaleqielqkkdfrrlgvrgdfndpyitlkpeyeaaqirifgemadkgliykgk
kpvywspssesslaeaeieyXphdwrtkkpvifratpqwfasiskvrqdildaientnfk
vnwgktriynmvrdrgewvisrqrvwgvplpvfyaengeiimtketvnhvadlfaehgsn
iwfereakdllpegfthpgspngtftketdimdvwfdsgsshrgvletrpelsfpadmyl
egsdqyrgwfnssittsvatrgvspykfllshgfvmdgegkkmskslgnvivpdqvvkqk
gadiarlwvsstdyladvrisdeilkqtsdd
>d1bs2a2 3.19.1.1.9 (136-483) Arginyl-tRNA synthetase (ArgRS) {Baker's yeast (Saccharomyces cerevisiae)}
scklvenkkviiefsspniakpfhaghlrstiiggflanlyeklgwevirmnylgdwgkq
fgllavgferygneealvkdpihhlfdvyvrinkdieeegdsipleqstngkareyfkrm
edgdeealkiwkrfrefsiekyidtyarlnikydvysgesqvskesmlkaidlfkekglt
hedkgavlidltkfnkklgkaivqksdgttlyltrdvgaamdryekyhfdkmiyviasqq
dlhaaqffeilkqmgfewakdlqhvnfgmvqgmstrkgtvvfldnileetkekmhevmkk
nenkyaqiehpeevadlvgisavmiqdmqgkrinnyefkwermlsfeg
>d1coza_ 3.19.1.2.1 CTP:glycerol-3-phosphate cytidylyltransferase {(Bacillus subtilis)}
mkkvitygtfdllhwghikllerakqlgdylvvaistdefnlqkqkkayhsyehrklile
tiryvdevipeknweqkkqdiidhnidvfvmgddwegkfdflkdqcevvylprtegistt
kikeei
>d1gpma1 3.19.2.1.1 (208-404) GMP synthetase, central domain {Escherichia coli}
wtpakiiddavarireqvgddkvilglsggvdssvtamllhraigknltcvfvdngllrl
neaeqvldmfgdhfglnivhvpaedrflsalagendpeakrkiigrvfvevfdeealkle
dvkwlaqgtiypdviesaasatgkahvikshhnvgglpkemkmglveplkelfkdevrki
glelglpydmlyrhpfp
>d2nsya_ 3.19.2.1.2 NH3-dependent NAD+-synthetase {Bacillus subtilis}
smqekimrelhvkpsidpkqeiedrvnflkqyvkktgakgfvlgisggqdstlagrlaql
avesireeggdaqfiavrlphgtqqdeddaqlalkfikpdkswkfdikstvsafsdqyqq
etgdqltdfnkgnvkartrmiaqyaiggqegllvlgtdhaaeavtgfftkygdggadllp
ltgltkrqgrtllkelgaperlylkeptadlldekpqqsdetelgisydeiddylegkev
sakvsealekrysmtehkrqvpasmfddwwk
>d1ct9a1 3.19.2.1.3 (193-516) Asparagine synthetase B, C-terminal domain {Escherichia coli}
rdwfdydavkdnvtdknelrqaledsvkshlmsdvpygvllsggldssiisaitkkyaar
rvedqerseawwpqlhsfavglpgspdlkaaqevanhlgtvhheihftvqegldairdvi
yhietydvttirastpmylmsrkikamgikmvlsgegsdevfggylyfhkapnakelhee
tvrkllalhmydcarankamsawgvearvpfldkkfldvamrinpqdkmcgngkmekhil
recfeaylpasvawrqkeqfsdgvgyswidtlkevaaqqvsdqqletarfrfpyntptsk
eaylyreifeelfplpsaaecvpg
>d1sur__ 3.19.2.2.1 Phosphoadenylyl sulphate (PAPS) reductase {Escherichia coli}
skldlnalnelpkvdrilalaetnaelekldaegrvawaldnlpgeyvlsssfgiqaavs
lhlvnqirpdipviltdtgylfpetyrfideltdklklnlkvyratesaawqearygklw
eqgvegiekyndinkvepmnralkelnaqtwfaglrreqsgsranlpvlaiqrgvfkvlp
iidwdnrtiyqylqkhglkyhplwdegylsvgdth
>d1brwa2 3.20.1.1.2 (71-330) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
lssirgvkvdkhstggvgdtttlvlgplvasvgvpvakmsgrglghtggtidklesvpgf
hveiskdefirlvnengiaiigqtgdltpadkklyalrdvtatvnsipliassimskkia
agadaivldvktgagafmkkldearrlarvmvdigkrvgrrtmavisdmsqplgyavgna
levkeaietlkgngphdltelcltlgshmvylaekapsldearrlleeairsgaaiaafk
tflaaqggdasvvddldklp
>d1dnpa2 3.21.1.1.1 (1-200) N-terminal domain of DNA photolyase {Escherichia coli}
tthlvwfrqdlrlhdnlalaaacrnssarvlalyiatprqwathnmsprqaelinaqlng
lqialaekgipllfrevddfvasveivkqvcaensvthlfynyqyevnerardveveral
rnvvcegfddsvilppgavmtgnhemykvftpfknawlkrlregmpecvaapkvrssgsi
epspsitlnyprqsfdtahf
>d1qnf_2 3.21.1.1.2 (1-204) N-terminal domain of DNA photolyase {Anacystis nidulans}
maapilfwhrrdlrlsdniglaaaraqsaqliglfcldpqilqsadmaparvaylqgclq
elqqryqqagsrllllqgdpqhlipqlaqqlqaeavywnqdiepygrdrdgqvaaalkta
giravqlwdqllhspdqilsgsgnpysvygpfwknwqaqpkptpvatptelvdlspeqlt
aiaplllselptlkqlgfdwdggf
>d1uag_1 3.22.1.1.1 (1-93) N-terminal domain of MurD (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase) {Escherichia coli}
adyqgknvviiglgltglscvdfflargvtprvmdtrmtppgldklpeaverhtgslnde
wlmaadlivaspgialahpslsaaadagieivg
>d1efva1 3.23.1.1.1 (20-207) Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
qstlviaehandslapitlntitaatrlggevsclvagtkcdkvaqdlckvagiakvlva
qhdvykgllpeeltplilatqkqfnythicagasafgknllprvaaklevapisdiiaik
spdtfvrtiyagnalctvkcdekvkvfsvrgtsfdaaatsggsassekasstspveisew
ldqkltks
>d1efvb1 3.23.1.1.1 Electron transfer flavoprotein, ETFP {Human (Homo sapiens)}
lrvlvavkrvidyavkirvkpdrtgvvtdgvkhsmnpfceiaveeavrlkekklvkevia
vscgpaqcqetirtalamgadrgihvevppaeaerlgplqvarvlaklaekekvdlvllg
kqaidddcnqtgqmtagfldwpqgtfasqvtlegdklkvereidggletlrlklpavvta
dlrlnepryatlpnimkakkkkievikpgdlgvdltsklsvisvedppqrtagvkvette
dlvaklkeigri
>d1efpa1 3.23.1.1.2 (2-184) Electron transfer flavoprotein, ETFP {Paracoccus denitrificans}
avlllgevtngalnrdatakavaavkalgdvtvlcagasakaaaeeaakiagvakvlvae
dalyghrlaeptaalivglagdyshiaapattdaknvmprvaalldvmvlsdvsaildad
tferpiyagnaiqvvkskdakkvftirtasfdaageggtapvtetaaaadpglsswvade
vae
>d1mjha_ 3.23.1.2.1 "Hypothetical" protein MJ0577 {Methanococcus jannaschii}
vmykkilyptdfsetaeialkhvkafktlkaeevillhvidereikkrdifslllgvagl
nksveefenelknklteeaknkmenikkeledvgfkvkdiivvgipheeivkiaedegvd
iiimgshgktnlkeillgsvtenvikksnkpvlvvkrkns
>d1cr6a1 3.24.1.1.1 (4-225) Epoxide hydrolase, N-terminal domain {Mouse (Mus musculus)}
rvaafdldgvlalpsiagafrrseealalprdfllgayqtefpegpteqlmkgkitfsqw
vplmdesyrksskacganlpenfsisqifsqamaarsinrpmlqaaialkkkgfttcivt
nnwlddgdkrdslaqmmcelsqhfdfliescqvgmikpepqiynflldtlkakpnevvfl
ddfgsnlkpardmgmvtilvhntasalrelekvtgtqfpeap
>d1bnca2 3.25.1.1.1 (1-114) Biotin carboxylase (BC) subunit of acetyl-CoA carboxylase {Escherichia coli}
mldkivianrgeialrilrackelgiktvavhssadrdlkhvlladetvcigpapsvksy
lnipaiisaaeitgavaihpgygflsenanfaeqversgfifigpkaetirlmg
>d1gsoa2 3.25.1.1.2 (-2-103) Glycinamide ribonucleotide synthetase (GAR-syn). {Escherichia coli}
efmkvlvignggrehalawkaaqsplvetvfvapgnagtalepalqnvaigvtdipalld
faqnekidltivgpeaplvkgvvdtfraaglkifgptagaaqleg
>d1b6ra2 3.25.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
qlarhpafvnrdvfpiia
>d1b6sa2 3.25.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
elarhpafvnrdvfpiia
>d1b6sb2 3.25.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
elarhpafvnrdvfpiia
>d1b6sc2 3.25.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
elarhpafvnrdvfpiia
>d1b6sd2 3.25.1.1.3 (1-78) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
mkqvcvlgngqlgrmlrqageplgiavwpvgldaepaavpfqqsvitaeierwpetaltr
elarhpafvnrdvfpiia
>d1a9xa3 3.25.1.1.4 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xa4 3.25.1.1.4 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1iov_1 3.25.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain {Escherichia coli, gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d1iow_1 3.25.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain {Escherichia coli, gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d2dln_1 3.25.1.2.1 (1-96) D-Ala-D-Ala ligase, N-terminal domain {Escherichia coli, gene ddlB}
mtdkiavllggtsaerevslnsgaavlaglreggidaypvdpkevdvtqlksmgfqkvfi
alhgrggedgtlqgmlelmglpytgsgvmasalsmd
>d1gsa_1 3.25.1.3.1 (1-122) Prokaryotic glutathione synthetase, N-terminal domain {Escherichia coli}
miklgivmdpianinikkdssfamlleaqrrgyelhymemgdlylingearahtrtlnvk
qnyeewfsfvgeqdlpladldvilmrkdppfdtefiyatyileraeekgtlivnkpqslr
dc
>d2hgsa1 3.25.1.4.1 (202-303) Eukaryotic glutathione synthetase {Human (Homo sapiens)}
pnalvlliaqekernifdqraienellarnihvirrtfedisekgsldqdrrlfvdgqei
avvyfrdgymprqyslqnwearlllershaakcpdiatqlag
>d1auva1 3.25.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1dhs__ 3.26.1.1.1 Deoxyhypusine synthase, DHS {Human (Homo sapiens)}
apagalaavlkhsstlppestqvrgydfnrgvnyralleafgttgfqatnfgravqqvna
miekklepltsctiflgytsnlissgiretirylvqhnmvdvlvttaggveedlikclap
tylgefslrgkelrenginrignllvpnenyckfedwlmpildqmvmeqntegvkwtpsk
miarlgkeinnpesvyywaqknhipvfspaltdgslgdmiffhsyknpglvldivedlrl
intqaifakctgmiilgggvvkhhiananlmrngadyavyintaqefdgsdsgarpdeav
swgkirvdaqpvkvyadaslvfpllvaetfaqkmdafmhekned
>d1efva2 3.26.1.2.1 (208-331) C-terminal domain of the electron transfer flavoprotein alpha subunit {Human (Homo sapiens)}
drpeltgakvvvsggrglksgenfkllydladqlhaavgasraavdagfvpndmqvgqtg
kivapelyiavgisgaiqhlagmkdsktivainkdpeapifqvadygivadlfkvvpemt
eilk
>d1efpa2 3.26.1.2.2 (185-308) C-terminal domain of the electron transfer flavoprotein alpha subunit {Paracoccus denitrificans}
sdrpeltsarrvvsggrglgskesfaiieeladklgaavgasraavdsgyapndwqvgqt
gkvvapelyvavgisgaiqhlagmkdskvivainkdeeapifqiadyglvgdlfsvvpel
tgkl
>d1poxa1 3.26.1.3.1 (183-365) Pyruvate oxidase {Lactobacillus plantarum}
yasannyqtpllpepdvqavtrltqtllaaerpliyygigarkagkeleqlsktlkiplm
stypakgivadrypaylgsanrvaqkpanealaqadvvlfvgnnypfaevskafkntryf
lqididpaklgkrhktdiavladaqktlaailaqvserestpwwqanlanvknwraylas
led
>d1pvda1 3.26.1.3.3 (182-360) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
qtpidmslkpndaesekevidtilalvkdaknpviladaccsrhdvkaetkklidltqfp
afvtpmgkgsiseqhpryggvyvgtlskpevkeavesadlilsvgallsdktknivefhs
dhmkirnatfpgvqmkfvlqklltniadaakgykpvavpartpanaavp
>d1zpda1 3.26.1.3.4 (188-362) Pyruvate decarboxylase {Zymomonas mobilis}
easdeaslnaavdetlkfianrdkvavlvgsklraagaeeaavkftdalggavatmaaak
sffpeenalyigtswgevsypgvektmkeadavialapvfndysttgwtdipdpkklvla
eprsvvvngirfpsvhlkdyltrlaqkvskktgsldffkslnagelkkaapadps
>d1bfd_1 3.26.1.3.5 (182-341) Benzoylformate decarboxylase {Pseudomonas putida}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap
>d1d4oa_ 3.26.1.4.1 Transhydrogenase domain III {Bovine (Bos taurus)}
gthteinldnaidmireansiiitpgyglcaakaqypiadlvkmlseqgkkvrfgihpva
grmpgqlnvllaeagvpydivlemdeinhdfpdtdlvlvigandtvnsaaqedpnsiiag
mpvlevwkskqvivmkrslgvgyaavdnpifykpntamllgdakktcdalqakvres
>d1fsz_1 3.27.1.1.1 (23-231) Cell-division protein FtsZ {Methanococcus jannaschii}
spedkelleylqqtkakitvvgcggagnntitrlkmegiegaktvaintdaqqlirtkad
kkiligkkltrglgaggnpkigeeaakesaeeikaaiqdsdmvfitcglgggtgtgsapv
vaeiskkigaltvavvtlpfvmegkvrmknameglerlkqhtdtlvvipneklfeivpnm
plklafkvadevlinavkglvelitkdgl
>d1tuba1 3.27.1.1.2 (1-245) Tubulin alpha-subunit {Bovine (Bos taurus)}
mrecisihvgqagvqignacwelyclehgiqpdgqmpsdktigggddsfntffsetgagk
hvpravfvdleptvidevrtgtyrqlfhpeqlitgkedaannyarghytigkeiidlvld
rirkladqctglqgfsvfhsfgggtgsgftsllmerlsvdygkksklefsiypapqvsta
vvepynsiltthttlehsdcafmvdneaiydicrrnldierptytnlnrligqivssita
slrfd
>d1nbaa_ 3.28.1.1.1 N-carbamoylsarcosine amidohydrolase {Arthrobacter}
tfndiearlaavleeafeagtsiynergfkrrigygnrpavihidlanawtqpghpfscp
gmetiipnvqrineaarakgvpvfyttnvyrnrdassgtndmglwyskiptetlpadsyw
aqiddriapadgevvieknrasafpgtnlelfltsnridtlivtgataagcvrhtvedai
akgfrpiipretigdrvpgvvqwnlydidnkfgdvestdsvvqyldalpqfedtvpktls
dpqpeveapadpv
>d1yaca_ 3.28.1.2.1 YcaC {Escherichia coli}
tkpyvrldkndaavllvdhqagllslvrdiepdkfknnvlalgdlakyfnlptilttsae
tgpngplvpelkaqfpdapyiarpgninawdnedfvkavkatgkkqliiagvvtevcvaf
palsaieegfdvfvvtdasgtfneitrhsawdrmsqagaqlmtwfgvacelhrdwrndia
glatlfsnhipdyrnlmtsydtlt
>d1deaa_ 3.29.1.1.1 Glucosamine 6-phosphate deaminase {Escherichia coli}
mrliplttaeqvgkwaarhivnrinafkptadrpfvlglptggtpmttykalvemhkagq
vsfkhvvtfnmdeyvglpkehpesyysfmhrnffdhvdipaeninllngnapdidaecrq
yeekirsygkihlfmggvgndghiafnepasslasrtriktlthdtrvansrffdndvnq
vpkyaltvgvgtlldaeevmilvlgsqkalalqaavegcvnhmwtisclqlhpkaimvcd
epstmelkvktlryfneleaenikgl
>d1pvda2 3.30.1.1.2 (2-181) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
seitlgkylferlkqvnvntvfglpgdfnlslldkiyevegmrwagnanelnaayaadgy
arikgmsciittfgvgelsalngiagsyaehvgvlhvvgvpsishhtlgngdftvfhrms
anisettamitdiatapaeidrcirttyvtqrpvylglpanlvdlnvpakll
>d1pvda3 3.30.1.1.2 (361-556) Pyruvate decarboxylase {Baker's yeast (Saccharomyces cerevisiae)}
astplkqewmwnqlgnflqegdvviaetgtsafginqttfpnntygisqvlwgsigfttg
atlgaafaaeeidpkkrvilfigdgslqltvqeistmirwglkpylfvlnndgytiekli
hgpkaqyneiqgwdhlsllptfgakdyethrvattgewdkltqdksfndnskirmieiml
pvfdapqnlvkqaklt
>d1zpda2 3.30.1.1.3 (2-187) Pyruvate decarboxylase {Zymomonas mobilis}
sytvgtylaerlvqiglkhhfavagdynlvlldnlllnknmeqvyccnelncgfsaegya
rakgaaaavvtysvgalsafdaiggayaenlpvilisgapnnndhaaghvlhhalgktdy
hyqlemaknitaaaeaiytpeeapakidhviktalrekkpvyleiacniasmpcaapgpa
salfnd
>d1zpda3 3.30.1.1.3 (363-566) Pyruvate decarboxylase {Zymomonas mobilis}
aplvnaeiarqvealltpnttviaetgdswfnaqrmklpngarveyemqwghigwsvpaa
fgyavgaperrnilmvgdgsfqltaqevaqmvrlklpviiflinnygytievmihdgpyn
niknwdyaglmevfngnggydsgaakglkaktggelaeaikvalantdgptliecfigre
dcteelvkwgkrvaaansrkpvnk
>d1poxa2 3.30.1.1.4 (9-182) Pyruvate oxidase {Lactobacillus plantarum}
tnilagaavikvleawgvdhlygipggsinsimdalsaerdrihyiqvrheevgamaaaa
dakltgkigvcfgsagpggthlmnglydaredhvpvlaligqfgttgmnmdtfqemnenp
iyadvadynvtavnaatlphvideairrayahqgvavvqipvdlpwqqisaedw
>d1poxa3 3.30.1.1.4 (366-593) Pyruvate oxidase {Lactobacillus plantarum}
kqegplqayqvlravnkiaepdaiysidvgdinlnanrhlkltpsnrhitsnlfatmgvg
ipgaiaaklnyperqvfnlagdggasmtmqdlvtqvqyhlpvinvvftncqygfikdeqe
dtnqndfigvefndidfskiadgvhmqafrvnkieqlpdvfeqakaiaqhepvlidavit
gdrplpaeklrldsamssaadieafkqryeaqdlqplstylkqfgldd
>d1bfd_2 3.30.1.1.5 (2-181) Benzoylformate decarboxylase {Pseudomonas putida}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
>d1bfd_3 3.30.1.1.5 (342-524) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv
>d1trka1 3.30.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvhgaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1trka2 3.30.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1qs0a1 3.30.1.3.1 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase) {Pseudomonas putida}
neyaplrlhvpeptgrpgcqtdfsylrlndagqarkppvdvdaadtadlsyslvrvldeq
gdaqgpwaedidpqilrqgxraxlktrifdsrxvvaqrqkkxsfyxqslgeeaigsgqal
alnrtdxcfptyrqqsilxardvslvexicqllsnerdplkgrqlpixysvreagfftis
gnlatqfvqavgwaxasaikgdtkiasawigdgataesdfhtaltfahvyrapvilnvvn
nqwaistfqaiaggesttfagrgvgcgiaslrvdgndfvavyaasrwaaerarrglgpsl
iewvtyragphstsddpskyrpaddwshfplgdpiarlkqhlikighwseeehqattaef
eaaviaaqkeaeqygtlanghipsaasxfedvykexpdhlrrqrqel
>d1qs0b1 3.30.1.3.1 (2-205) 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase) {Pseudomonas putida}
atttxtxiqalrsaxdvxlerddnvvvygqdvgyfggvfrcteglqtkygksrvfdapis
esgivgtavgxgayglrpvveiqfadyfypasdqivsexarlryrsagefiapltlrxpc
gggiyggqthsqspeaxftqvcglrtvxpsnpydakglliasiecddpviflepkrlyng
pfdghhdrpvtpwskhphsavpdg
>d1b0pa1 3.30.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pa2 3.30.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1gky__ 3.31.1.1.1 Guanylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
xsrpivisgpsgtgkstllkklfaeypdsfgfsvssttrtpragevngkdynfvsvdefk
smiknnefiewaqfsgnyygstvasvkqvsksgktcildidmqgvksvkaipelnarflf
iappsvedlkkrlegrgteteesinkrlsaaqaelayaetgahdkvivnddldkaykelk
dfifaek
>d1deka_ 3.31.1.1.3 Deoxynucleoside monophosphate kinase {Bacteriophage T4}
mkliflsgvkrsgkdttadfimsnysavkyqlagpikdalayawgvfaantdypxltrke
fegidydretnlnltklevitimeqafcylngkspikgvfvfddegkesvnfvafnkitd
vinniedqwsvrrlmqalgtdlivnnfdrmywvklfaldyldkfnsgydyyivpdtrqdh
emdaaramgatvihvvrpgqksndthiteaglpirdgdlvitndgsleelfskikntlkv
l
>d1ckea_ 3.31.1.1.4 CMP kinase {Escherichia coli}
aiapvitidgpsgagkgtlckamaealqwhlldsgaiyrvlalaalhhhvdvasedalvp
lashldvrfvstngnlevilegedvsgeirtqevanaasqvaafprvreallrrqrafre
lpgliadgrdmgtvvfpdapvkifldasseerahrrmlqlqvkgfsvnferllaeikerd
drdrnravaplvpaadalvldsttlsieqviekalqyarqklala
>d1qf9a_ 3.31.1.1.5 UMP/CMP kinase {Dictyostelium discodeum}
mekskpnvvfvlggpgsgkgtqcanivrdfgwvhlsagdllrqeqqsgskdgemiatmik
ngeivpsivtvkllknaidanqgknflvdgfprneennnsweenmkdfvdtkfvlffdcp
eevmtqrllkrgessgrsddniesikkrfntfnvqtklvidhynkfdkvkiipanrdvne
vyndvenlfksmgf
>d1qhia_ 3.31.1.1.6 Thymidine kinase {Herpes simplex virus, type 1, HSV1}
mptllrvyidgphgmgkttttqllvalgsrddivyvpepmtywrvlgasetianiyttqh
rldqgeisagdaavvmtsaqitmgmpyavtdavlaphiggeagsshapppaltlifdrhp
iaallcypaarylmgsmtpqavlafvalipptlpgtnivlgalpedrhidrlakrqrpge
rldlamlaairrvygllantvrylqcggswredwgqlsgtavppqgaepqsnagprphig
dtlftlfrapellapngdlynvfawaldvlakrlrsmhvfildydqspagcrdallqlts
gmvqthvttpgsipticdlartfaremgea
>d3adk__ 3.31.1.1.7 Adenylate kinase {Porcine (Sus scrofa)}
xmeeklkkskiifvvggpgsgkgtqcekivqkygythlstgdllraevssgsargkmlse
imekgqlvpletvldmlrdamvakvdtskgflidgyprevkqgeeferkigqptlllyvd
agpetmtkrllkrgetsgrvddneetikkrletyykatepviafyekrgivrkvnaegsv
ddvfsqvcthldtlk
>d1nksa_ 3.31.1.1.8 Adenylate kinase {Sulfolobus acidocaldarius}
mkigivtgipgvgkstvlakvkeildnqginnkiinygdfmlatalklgyakdrdemrkl
svekqkklqidaakgiaeearaggegylfidthavirtpsgylpglpsyviteinpsvif
lleadpkiilsrqkrdttrnrndysdesviletinfaryaatasavlagstvkvivnveg
dpsiaaneiirsmk
>d2ak3a1 3.31.1.1.9 (0-124,162-225) Adenylate kinase {Bovine (Bos taurus), mitochondrial izozyme-3}
gasarllraaimgapgsgkgtvssritkhfelkhlssgdllrdnmlrgteigvlaktfid
qgklipddvmtrlvlhelknltqynwlldgfprtlpqaealdrayqidtvinlnvpfevi
kqrltXdrpetvvkrlkayeaqtepvleyyrkkgvletfsgtetnkiwphvyaflqtklp
qrsqetsvtp
>d1ak2_1 3.31.1.1.10 (14-146,177-233) Adenylate kinase {Bovine (Bos taurus), mitochondrial izozyme-2}
pkgvravllgppgagkgtqapklaknfcvchlatgdmlramvasgselgkklkatmdagk
lvsdemvlelieknletppckngflldgfprtvrqaemlddlmekrkekldsviefsipd
sllirritgrlihXsddnkkalkirleayhtqttplveyyskrgihsaidasqtpdvvfa
silaafskats
>d1aky_1 3.31.1.1.11 (3-130,169-220) Adenylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
esirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqggl
vsddimvnmikdeltnnpackngfildgfprtipqaekldqmlkeqgtplekaielkvdd
ellvaritXnadalkkrlaayhaqtepivdfykktgiwagvdasqppatvwadilnklgk
n
>d1akea1 3.31.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1zaka1 3.31.1.1.13 (3-127,159-222) Adenylate kinase {Maize (Zea mays)}
adplkvmisgapasgkgtqceliktkyqlahisagdllraeiaagsengkrakefmekgq
lvpdeivvnmvkerlrqpdaqengwlldgyprsysqamaletleirpdtfilldvpdell
vervvXfddteekvklrletyyqniesllstyeniivkvqgdatvdavfakidellgsil
ekknemvsst
>d1zin_1 3.31.1.1.14 (1-125,161-217) Adenylate kinase {Bacillus stearothermophilus}
mnlvlmglpgagkgtqaekivaaygiphistgdmfraamkegtplglqakqymdrgdlvp
devtigivrerlskddcqngflldgfprtvaqaealetmladigrkldyvihidvrqdvl
merltXaddneatvanrlevnmkqmkplvdfyeqkgylrningeqdmekvfadirellgg
lar
>d1tmka_ 3.31.1.1.15 Thymidylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
grgkliliegldrtgkttqcnilykklqpnckllkfperstrigglineyltddsfqlsd
qaihllfsanrweivdkikkdllegknivmdryvysgvaysaakgtngmdldwclqpdvg
llkpdltlflstqdvdnnaeksgfgderyetvkfqekvkqtfmklldkeirkgdesitiv
dvtnkgiqevealiwqivepvlsthidhdkfsff
>d4tmka_ 3.31.1.1.16 Thymidylate kinase {Escherichia coli}
rskyivieglegagkttarnvvvetleqlgirdmvftrepggtqlaeklrsllldiksvg
devitdkaevlmfyaarvqlvetvikpalangtwvigdrhdlstqayqgggrgidqhmla
tlrdavlgdfrpdltlyldvtpevglkrarargeldrieqesfdffnrtrarylelaaqd
ksihtidatqpleavmdairttvthwvkel
>d1shka_ 3.31.1.2.1 Shikimate kinase {Erwinia chrysanthemi}
mtepifmvgargcgkttvgrelaralgyefvdtdifmqhtsgmtvadvvaaegwpgfrrr
esealqavatpnrvvatgggmvlleqnrqfmrahgtvvylfapaeelalrlqaspqahqr
ptltgrpiaeemeavlrerealyqdvahyvvdatqppaaivcelmqtmrlpaa
>d1d6ja_ 3.31.1.3.1 Adenosine-5'phosphosulfate kinase (APS kinase) {Penicillium chrysogenum}
hasaltrsertelrnqrgltiwltglsasgkstlavelehqlvrdrrvhayrldgdnirf
glnkdlgfseadrnenirriaevaklfadsnsiaitsfispyrkdrdtarqlhevatpge
etglpfvevyvdvpvevaeqrdpkglykkaregvikeftgisapyeapanpevhvknyel
pvqdavkqiidyldtkgylpakk
>d1aqua_ 3.31.1.4.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1nsta_ 3.31.1.4.3 Heparan sulfate N-deacetylase/N-sulfotransferase domain {Human (Homo sapiens) |A|}
dplwqdpcedkrhkdiwskektcdrfpklliigpqktgttalylflgmhpdlssnypsse
tfeeiqffnghnyhkgidwymeffpipsnttsdfyfeksanyfdsevaprraaallpkak
vltilinpadrayswyqhqrahddpvalkytfhevitagsdassklralqnrclvpgwya
thierwlsayhanqilvldgkllrtepakvmdmvqkflgvtntidyhktlafdpkkgfwc
qlleggktkclgkskgrkypemdldsraflkdyyrdhnielskllykmgqtlptwlredl
q
>d1a7j__ 3.31.1.5.1 Phosphoribulokinase {Rhodobacter sphaeroides}
skkhpiisvtgssgagtstvkhtfdqifrregvkavsiegdafhrfnradmkaeldrrya
agdatfshfsyeanelkelervfreygetgqgrtrtyvhddaeaartgvapgnftdwrdf
dsdshllfyeglhgavvnsevniagladlkigvvpvinlewiqkihrdratrgytteavt
dvilrrmhayvhcivpqfsqtdinfqrvpvvdtsnpfiarwiptadesvvvirfrnprgi
dfpyltsmihgswmsransivvpgnkldlamqliltplidrvvreskv
>d1bif_1 3.31.1.6.1 (37-249) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, kinase domain {Rat (Rattus norvegicus)}
cptlivmvglpargktyiskkltrylnfigvptrefnvgqyrrdmvktyksfefflpdne
eglkirkqcalaalndvrkflseegghvavfdatnttrerramifnfgeqngyktffves
icvdpeviaanivqvklgspdyvnrdsdeatedfmrriecyensyesldeeqdrdlsyik
imdvgqsyvvnrvadhiqsrivyylmnihvtpr
>d1ctqa_ 3.31.1.7.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1mh1__ 3.31.1.7.2 Rac1 {Human (Homo sapiens)}
gspqaikcvvvgdgavgktcllisyttnafpgeyiptvfdnysanvmvdgkpvnlglwdt
agqedydrlrplsypqtdvslicfslvspasfenvrakwypevrhhcpntpiilvgtkld
lrddkdtieklkekkltpitypqglamakeigavkylecsaltqrglktvfdeairavlc
ppp
>d1kao__ 3.31.1.7.4 Rap2a {Human (Homo sapiens)}
mreykvvvlgsggvgksaltvqfvtgtfiekydptiedfyrkeievdsspsvleildtag
teqfasmrdlyikngqgfilvyslvnqqsfqdikpmrdqiirvkryekvpvilvgnkvdl
eserevsssegralaeewgcpfmetsaksktmvdelfaeivrqmnya
>d3raba_ 3.31.1.7.5 Rab3a {Rat (Rattus norvegicus)}
nfdymfkiliignssvgktsflfryaddsftpafvstvgidfkvktiyrndkriklqiwd
tagqeryrtittayyrgamgfilmyditneesfnavqdwstqiktyswdnaqvllvgnkc
dmedervvssergrqladhlgfeffeasakdninvkqtferlvdvicek
>d1byua_ 3.31.1.7.6 Ran {Dog (Canis familiaris)}
epqvqfklvlvgdggtgkttfvkrhltgefekkyvptlgvevhplvfhtnrgpikfnvwd
tagqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvd
ikdrkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalapp
evvmdpalaaqyehdlevaqtt
>d1hura_ 3.31.1.7.9 ADP-ribosylation factor 1 (ARF1) {Human (Homo sapiens)}
gnifanlfkglfgkkemrilmvgldaagkttilyklklgeivttiptigfnvetveykni
sftvwdvggqdkirplwrhyfqntqglifvvdsndrervneareelmrmlaedelrdavl
lvfankqdlpnamnaaeitdklglhslrhrnwyiqatcatsgdglyegldwlsnqlrnqk
>d1azsc2 3.31.1.7.12 (36-66,202-393) Transducin (alpha subunit) {Bovine (Bos taurus)}
vyrathrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqyel
>d1cipa2 3.31.1.7.13 (32-60,182-347) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviiknn
>d1d2ea3 3.31.1.7.17 (55-250) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Bovine (Bos taurus), mitochondrial}
kphvnvgtighvdhgkttltaaitkilaegggakfkkyeeidnapeerargitinaahve
ystaarhyahtdcpghadyvknmitgtapldgcilvvaandgpmpqtrehlllarqigve
hvvvyvnkadavqdsemvelveleirelltefgykgeetpiivgsalcaleqrdpelglk
svqklldavdtyipvp
>d1dar_2 3.31.1.7.18 (1-282) Elongation factor G (EF-G), N-terminal (G) domain {Thermus thermophilus}
mavkveydlkrlrnigiaahidagktttterilyytgrihkigevhegaatmdfmeqere
rgititaavttcfwkdhriniidtpghvdftieversmrvldgaivvfdssqgvepqset
vwrqaekykvpriafankmdktgadlwlvirtmqerlgarpvvmqlpigredtfsgiidv
lrmkaytygndlgtdireipipeeyldqareyheklvevaadfdenimlkylegeeptee
elvaairkgtidlkitpvflgsalknkgvqllldavvdylps
>d1egaa1 3.31.1.7.19 (4-182) GTPase Era, N-terminal domain {Escherichia coli}
dksycgfiaivgrpnvgkstllnkllgqkisitsrkaqttrhrivgihtegayqaiyvdt
pglhmeekrainrlmnkaasssigdvelvifvvegtrwtpddemvlnklregkapvilav
nkvdnvqekadllphlqflasqmnfldivpisaetglnvdtiaaivrkhlpeathhfpe
>d1dg3a2 3.31.1.7.20 (6-283) Interferon-induced guanylate-binding protein 1 (GBP1), N-terminal domain {Human (Homo sapiens)}
hmtgpmclientngrlmanpealkilsaitqpmvvvaivglyrtgksylmnklagkkkgf
slgstvqshtkgiwmwcvphpkkpghilvlldteglgdvekgdnqndswifalavllsst
fvynsigtinqqamdqlyyvtelthrirsksspdenenevedsadfvsffpdfvwtlrdf
sldleadgqpltpdeyltyslklkkgtsqkdetfnlprlcirkffpkkkcfvfdrpvhrr
klaqleklqdeeldpefvqqvadfcsyifsnsktktls
>d1b7ta2 3.31.1.8.2 (5-28) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
fsdpdfqylavdrkklmkeqtaaf
>d1lvk_2 3.31.1.8.3 (2-33,80-759) Myosin S1, motor domain {Slime mold (Dictyostelium discoideum)}
npihdrtsdyhkylkvkqgdsdlfkltvsdkrXrnpikfdgvedmselsylnepavfhnl
rvrynqdliytysglflvavnpfkripiytqemvdifkgrrrnevaphifaisdvayrsm
lddrqnqsllitgesgagktentkkviqylasvagrnqangsgvleqqilqanpileafg
nakttrnnnssrfgkfieiqfnnagfisgasiqsylleksrvvfqstsernyhifyqlla
gataeekkalhlagpesfnylnqsgcvdikgvsdedefkitrqamdivgfsqeeqmsifk
iiagilhlgnikfekgagegavlkdktalnaastvfgvnpsvlekalmeprilagrdlva
qhlnvekssssrdalvkalygrlflwlvkkinnvlcserkayfigvldisgfeifkvnsf
eqlcinytneklqqffnhhmfkveqekylkekinwtfidfgldsqatidlidgrqppgil
alldeqsvfpnatdntlitklhshfskknakyeeprfsktefgvthyagqvmyeiqdwle
knkdplqqdlelcfkdssdnvvtklfndpniasrakkganfltvaaqykeqlaslmatle
ttnphfvrciipnnkqlpakledkvvldqlrcngvlegiritrkgfpnriiyadfvkryy
dlapnvprdaedsqkatdavlkhlnidpeqfrfgitkiffragqlarieeare
>d1bg2__ 3.31.1.8.4 Kinesin {Human (Homo sapiens)}
dlaecnikvmcrfrplnesevnrgdkyiakfqgedtvviaskpyafdrvfqsstsqeqvy
ndcakkivkdvlegyngtifaygqtssgkthtmegklhdpegmgiiprivqdifnyiysm
denlefhikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgcterfvcspdevmdt
idegksnrhvavtnmnehssrshsiflinvkqentqteqklsgklylvdlagsekvsktg
aegavldeakninkslsalgnvisalaegstyvpyrdskmtrilqdslggncrttivicc
spssynesetkstllfgqrakti
>e2kin.1b 3.31.1.8.5 Kinesin {Rat (Rattus norvegicus)}
akninkslsalgnvisalaegtkthvpyrdskmtrilqdsldgncrttiviccspsvfne
aetkstlmfgqraktikntvsvnleltaeewkkkyekeke
>e3kin.1b 3.31.1.8.5 Kinesin {Rat (Rattus norvegicus)}
nkslsalgnvisalaegtkthvpyrdskmtrilqdslggncrttiviccspsvfneaetk
stlmfgqraktikntvsvnleltaeewkkkyekekeknkalksviqhlevelnrwrn
>d3kar__ 3.31.1.8.7 Kinesin motor Ncd (non-claret disjunctional) {Baker's yeast (Saccharomyces cerevisiae), Kar}
gnirvycrirpalknlensdtslinvnefddnsgvqsmevtkiqntaqvhefkfdkifdq
qdtnvdvfkevgqlvqssldgynvcifaygqtgsgktftmlnpgdgiipstishifnwin
klktkgwdykvncefieiynenivdllrsdnnnkedtsiglkheirhdqetktttitnvt
sckleseemveiilkkanklrstastasnehssrshsifiihlsgsnaktgahsygtlnl
vdlagserinvsqvvgdrlretqninkslsclgdvihalgqpdstkrhipfrnskltyll
qysltgdsktlmfvnispssshinetlnslrfaskvns
>d1byi__ 3.31.1.9.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1qf5a_ 3.31.1.9.2 Adenylosuccinate synthetase, PurA {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1cp2a_ 3.31.1.9.4 Nitrogenase iron protein {Clostridium pasteurianum}
mrqvaiygkggigkstttqnltsglhamgktimvvgcdpkadstrlllgglaqksvldtl
reegedveldsilkegyggircvesggpepgvgcagrgiitsinmleqlgaytddldyvf
ydvlgdvvcggfampiregkaqeiyivasgemmalyaanniskgiqkyaksggvrlggii
cnsrkvaneyelldafakelgsqlihfvprspmvtkaeinkqtvieydptceqaeeyrel
arkvdanelfvipkpmtqerleeilmqyg
>d1ffh_2 3.31.1.9.5 (89-295) GTPase domain of the signal sequence recognition protein Ffh {Thermus aquaticus}
earlpvlkdrnlwflvglqgsgktttaaklalyykgkgrrpllvaadtqrpaareqlrll
gekvgvpvlevmdgespesirrrveekarleardlilvdtagrlqideplmgelarlkev
lgpdevllvldamtgqealsvarafdekvgvtglvltkldgdarggaalsarhvtgkpiy
fagvsekpeglepfyperlagrilgmg
>d1fts_2 3.31.1.9.6 (285-495) GTPase domain of the signal recognition particle receptor FtsY {Escherichia coli}
plnvegkapfvilmvgvngvgktttigklarqfeqqgksvmlaagdtfraaaveqlqvwg
qrnnipviaqhtgadsasvifdaiqaakarnidvliadtagrlqnkshlmeelkkivrvm
kkldveaphevmltidastgqnavsqaklfheavgltgitltkldgtakggvifsvadqf
gipiryigvgeriedlrpfkaddfiealfar
>d2reb_1 3.31.1.10.1 (3-268) RecA protein, ATPase-domain {Escherichia coli}
denkqkalaaalgqiekqfgkgsimrlgedrsmdvetistgslsldialgagglpmgriv
eiygpessgkttltlqviaaaqregktcafidaehaldpiyarklgvdidnllcsqpdtg
eqaleicdalarsgavdvivvdsvaaltpkaeiegeigdshmglaarmmsqamrklagnl
kqsntllifinqirmkigvmfgnpetttggnalkfyasvrldirrigavkegenvvgset
rvkvvknkiaapfkqaefqilygegi
>d1cr1a_ 3.31.1.10.2 Gene 4 protein (DNA primase), helicase domain {Bacteriophage T7}
mrerirehlsseesvgllfsgctgindktlgarggevimvtsgsgmgkstfvrqqalqwg
tamgkkvglamleesveetaedliglhnrvrlrqsdslkreiiengkfdqwfdelfgndt
fhlydsfaeaetdrllaklaymrsglgcdviildhisivvsasgesderkmidnlmtklk
gfakstgvvlvvichlknpdkgkaheegrpvsitdlrgsgalrqlsdtiialernqqgdm
pnlvlvrilkcrftgdtgiagymeynketgwlepssy
>d1bmfa3 3.31.1.10.3 (95-379) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
vdvpvgeellgrvvdalgnaidgkgpigskarrrvglkapgiiprisvrepmqtgikavd
slvpigrgqreliigdrqtgktsiaidtiinqkrfndgtdekkklyciyvaigqkrstva
qlvkrltdadamkytivvsatasdaaplqylapysgcsmgeyfrdngkhaliiyddlskq
avayrqmslllrrppgreaypgdvfylhsrlleraakmndafgggsltalpvietqagdv
sayiptnvisitdgqifletelfykgirpainvglsvsrvgsaaq
>d1bmfd3 3.31.1.10.3 (82-357) Central domain of alpha and beta subunits of F1 ATP synthase {Bovine (Bos taurus)}
iripvgpetlgrimnvigepidergpiktkqfaaihaeapefvemsveqeilvtgikvvd
llapyakggkiglfggagvgktvlimelinnvakahggysvfagvgertregndlyhemi
esgvinlkdatskvalvygqmneppgararvaltgltvaeyfrdqegqdvllfidnifrf
tqagsevsallgripsavgyqptlatdmgtmqeritttkkgsitsvqaiyvpaddltdpa
pattfahldattvlsraiaelgiypavdpldstsri
>d1cbua_ 3.31.1.10.6 Adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase CobU {Salmonella typhimurium}
milvtggarsgksrhaealigdapqvlyiatsqilddemaariqhhkdgrpahwrtaecw
rhldtlitadlapddaillecittmvtnllfalggendpeqwdyaameraiddeiqilia
acqrcpakvvlvtnevgmgivpenrlarhfrdiagrvnqrlaaaadevwlvvsgigvkik
>d1b0ua_ 3.31.1.11.1 ATP-binding subunit of the histidine permease {Salmonella typhimurium}
nklhvidlhkrygghevlkgvslqaragdvisiigssgsgkstflrcinflekpsegaii
vngqninlvrdkdgqlkvadknqlrllrtrltmvfqhfnlwshmtvlenvmeapiqvlgl
skhdareralkylakvgideraqgkypvhlsggqqqrvsiaralamepdvllfdeptsal
dpelvgevlrimqqlaeegktmvvvthemgfarhvsshviflhqgkieeegdpeqvfgnp
qsprlqqflkgslkkleh
>d1pjr_1 3.31.1.12.1 (1-318) DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
mnflseqllahlnkeqqeavrttegpllimagagsgktrvlthriaylmaekhvapwnil
aitftnkaaremrervqsllggaaedvwistfhsmcvrilrrdidriginrnfsildptd
qlsvmktilkeknidpkkfeprtilgtisaaknellppeqfakrastyyekvvsdvyqey
qqrllrnhsldfddlimttiqlfdrvpdvlhyyqykfqyihideyqdtnraqytlvkkla
erfqnicavgdadqsiyrwrgadiqnilsferdypnakvilleqnyrstkrilqaanevi
ehnvnrkpkriwtenpeg
>d1pjr_2 3.31.1.12.1 (319-651) DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
kpilyyeamneadeaqfvagrireavergerryrdfavlyrtnaqsrvmeemllkanipy
qivgglkfydrkeikdilaylrvianpdddlsllriinvpkrgigastidklvryaadhe
lslfealgelemiglgakaagalaafrsqleqwtqlqeyvsvtelveevldksgyremlk
aertieaqsrlenldeflsvtkhfenvsddksliafltdlalisdldeldgteqaaegda
vmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeelvlt
saqmrtlfgniqmdppsrflneipahlletasr
>e1qhg.1c 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
lfealgelemiglgakaagalaafrsqleqwtqlqeyvsvtelveevldksgyremlkae
rtieaqsrlenldeflsvtkhfenvsddksliafltdlalis
>e1qhg.1d 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
gdavmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeel
vltsaqmrtlfgniqmdppsrflneipahlletasr
>e1qhh.1c 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
lfealgelemiglgakaagalaafrsqleqwtqlqeyvsvtelveevldksgyremlkae
rtieaqsrlenldeflsvtkhfenvsddksliafltdlalis
>e1qhh.1d 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
gdavmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeel
vltsaqmrtlfgniqmdppsrflneipahlletasr
>e2pjr.1b 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
gdavmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeel
vltsaqmrtlfgniqmdppsrflneipahlletas
>e2pjr.2g 3.31.1.12.1 DEXX box DNA helicase {Bacillus stearothermophilus, PcrA}
gdavmlmtlhaakglefpvvfligmeegifphnrsledddemeeerrlayvgitraeeel
vltsaqmrtlfgniqmdppsrflneipahlletas
>d1a5t_2 3.31.1.12.3 (1-166) delta prime subunit of DNA polymerase III, N-terminal domain {Escherichia coli}
mrwypwlrpdfeklvasyqagrghhalliqalpgmgddaliyalsryllcqqpqghkscg
hcrgcqlmqagthpdyytlapekgkntlgvdavrevteklneharlggakvvwvtdaall
tdaaanallktleeppaetwfflatreperllatlrsrcrlhylap
>d1d2na_ 3.31.1.12.4 Hexamerization domain of N-ethylmalemide-sensitive fusion (NSF) protein {Chinese hamster (Cricetulus griseus)}
edyasyimngiikwgdpvtrvlddgellvqqtknsdrtplvsvllegpphsgktalaaki
aeesnfpfikicspdkmigfsetakcqamkkifddayksqlscvvvddierlldyvpigp
rfsnlvlqallvllkkappqgrklliigttsrkdvlqememlnafsttihvpniatgeql
lealellgnfkdkerttiaqqvkgkkvwigikkllmliemslqmdpeyrvrkflallree
gaspld
>d1dooe_ 3.31.1.12.5 HslU {Bacteria (Escherichia coli)}
semtpreivseldkhiigqdnakrsvaialrnrwrrmqlneelrhevtpknilmigptgv
gkteiarrlaklanapfikveatkftevgyvgkevdsiirdltdaavkmvrvqaieknry
raeelaeerildvlippaknnwgqteqqqepsaarqafrkklregqlddkeieidlaaap
mgveimappgmeemtsqlqsmfqnlggqkqkarklkikdamkllieeeaaklvnpeelkq
daidaveqhgivfideidkickrgessgpdvsregvqrdllplvegctvstkhgmvktdh
ilfiasgafqiakpsdlipelqgrlpirvelqalttsdferiltepnasitvqykalmat
egvnieftdsgikriaeaawqvnestenigarrlhtvlerlmeeisydasdlsgqnitid
adyvskhldalvadedlsrfil
>d1a1va1 3.31.1.13.1 (190-325) HCV helicase domain {Hepatitis C virus, HCV}
ppavpqsfqvahlhaptgsgkstkvpaayaaqgykvlvlnpsvaatlgfgaymskahgvd
pnirtgvrtittgspitystygkfladggxsggaydiiicdechstdatsilgigtvldq
aetagarlvvlatatp
>d1a1va2 3.31.1.13.1 (326-624) HCV helicase domain {Hepatitis C virus, HCV}
pgsvtvphpnieevalsttgeipfygkaiplevikggrhlifchskkkcdelaaklvalg
inavayyrgldvsviptsgdvvvvatdalmtgftgdfdsvidcntxvtqtvdfsldptft
ietttlpqdavsrtqrrgrtgrgkpgiyrfvapgerpsgmfdssvlcecydagxawyelt
paettvrlraymntpglpvcqdhlefwegvftglthidahflsqtkqsgenfpylvayqa
tvcaraqapppswdqmwkclirlkptlhgptpllyrlgavqnevtlthpitkyimtcms
>d1ble__ 3.32.1.1.1 Fructose permease, subunit IIb {Bacillus subtilis}
mnivlariddrfihgqiltrwikvhaadriivvsddiaqdemrktlilsvapsnvkasav
svskmakafhspryegvtamllfenpsdivslieagvpiktvnvggmrfenhrrqitksv
svteqdikafetlsdkgvklelrqlpsdasedfvqilrnvt
>d1d0va_ 3.33.1.1.1 Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) {Salmonella typhimurium}
lhallrdipapdaeamartqqhidgllkppgslgrletlavqlagmpglngtpqvgekav
lvmcadhgvwdegvavspkivtaiqaanmtrgttgvcvlaaqagakvhvidvgidaepip
gvvnmrvargcgniavgpamsrlqaealllevsryacdlaqrgvtlfgvgelgmanttpa
aamvsvftgsdakevvgiganlppsridnkvdvvrraiainqpnprdgidvlskvggfdl
vgmtgvmlgaarcglpvlldgflsysaalaacqiapavrpylipshfsaekgarialahl
smepylhmamrlgegsgaalampiveaacamfhnmgelaasnivlp
>d1chd__ 3.34.1.1.1 Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
llssekliaigastggteairhvlqplplsspaviitqhmppgftrsfaerlnklcqisv
keaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsvdvlfhsvakha
grnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreainmggvsevvdls
qvsqqmlakisagqairi
>d1gci__ 3.35.1.1.6 Subtilisin BL {Bacillus lentus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapsaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d2prk__ 3.35.1.1.13 Proteinase K {Fungus (Tritirachium album), strain limber}
aaqtnapwglarisstspgtstyyydesagqgscvyvidtgieashpefegraqmvktyy
yssrdgnghgthcagtvgsrtygvakktqlfgvkvlddngsgqystiiagmdfvasdknn
rncpkgvvaslslgggysssvnsaaarlqssgvmvavaagnnnadarnyspasepsvctv
gasdrydrrssfsnygsvldifgpgtsilstwiggstrsisgtsmatphvaglaaylmtl
gkttaasacryiadtankgdlsnipfgtvnllaynnyqa
>d1d3va_ 3.36.1.1.1 Arginase {Rat (Rattus norvegicus)}
kpieiigapfskgqprggvekgpaalrkaglveklketeynvrdhgdlafvdvpndspfq
ivknprsvgkaneqlaavvaetqkngtisvvlggdhsmaigsisgharvhpdlcviwvda
htdintplttssgnlhgqpvafllkelkgkfpdvpgfswvtpcisakdivyiglrdvdpg
ehyiiktlgikyfsmtevdklgigkvmeetfsyllgrkkrpihlsfdvdgldpvftpatg
tpvvgglsyreglyiteeiyktgllsgldimevnptlgktpeevtrtvntavaltlscfg
tkregnhk
>d1c3pa_ 3.36.1.2.1 HDAC homologue {Aquifex aeolicus |A|}
kkvkligtldygkyrypknhplkiprvslllrfkdamnlidekeliksrpatkeelllfh
tedyintlmeaercqcvpkgarekyniggyenpvsyamftgsslatgstvqaieeflkgn
vafnpaggmhhafksrangfcyinnpavgieylrkkgfkrilyidldahhcdgvqeafyd
tdqvfvlslhqspeyafpfekgfleeigegkgkgynlniplpkglndneflfalekslei
vkevfepevyllqlgtdplledylskfnlsnvaflkafnivrevfgegvylggggyhpya
larawtliwcelsgrevpeklnnkakellksidfeefddevdrsymletlkdpwrggevr
kevkdtlekaka
>d1qvaa_ 3.37.1.1.1 Initiation factor 4a N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
qiqtnyqkvvykfddmeldeqllrgvfgygfeepsaiqqraimpiieghdvlaqaqsgtg
ktgtfsiaalqridtsvkapqalmlaptrelalqiqkvvmalafhmdikvhaciggtsfv
edaeglrdaqivvgtpgrvfdniqrrrfrtdkikmfildeademlssgfkeqiyqiftll
ppttqvvllsatmpndvlevttkfmrnpvrilv
>d3cla__ 3.38.1.1.1 Chloramphenicol acetyltransferase {Escherichia coli}
mnytkfdvknwvrrehfefyrhrlpcgfsltskidittlkkslddsaykfypvmiyliaq
avnqfdelrmaikddelivwdsvdpqftvfhqetetfsalscpyssdidqfmvnylsvme
ryksdtklfpqgvtpenhlnisalpwvnfdsfnlnvanftdyfapiitmakyqqegdrll
lplsvqvhhavcdgfhvarfinrlqelcnsklk
>d1eaf__ 3.38.1.1.3 Dihydrolipoamide acetyltransferase {Azotobacter vinelandii}
ippippvdfakygeieevpmtrlmqigatnlhrswlnvphvtqfesaditeleafrvaqk
avakkagvkltvlplllkacayllkelpdfnsslapsgqalirkkyvhigfavdtpdgll
vpvirnvdqksllqlaaeaaelaekarskklgadamqgacftisslghiggtaftpivna
pevailgvskasmqpvwdgkafqprlmlplslsydhrvingaaaarftkrlgdlladira
ill
>d1b5sa_ 3.38.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1e2o__ 3.38.1.1.5 Dihydrolipoamide succinyltransferase {Escherichia coli}
arsekrvpmtrlrkrvaerlleaknstamlttfnevnmkpimdlrkqygeafekrhgirl
gfmsfyvkavvealkrypevnasidgddvvyhnyfdvsmavstprglvtpvlrdvdtlgm
adiekkikelavkgrdgkltvedltggnftitnggvfgslmstpiinppqsailgmhaik
drpmavngqveilpmmylalsydhrlidgresvgflvtikelledptrllldv
>d1phr__ 3.39.1.1.1 Tyrosine phosphatase {Bovine (Bos taurus)}
vtksvlfvclgnicrspiaeavfrklvtdqnisdnwvidsgavsdwnvgrspdpravscl
rnhgintahkarqvtkedfvtfdyilcmdesnlrdlnrksnqvkncrakiellgsydpqk
qliiedpyygndadfetvyqqcvrccraflekvr
>d1iiba_ 3.39.2.1.1 Enzyme IIB-cellobiose {Escherichia coli}
kkhiylfssagmstsllvskmraqaekyevpviieafpetlagekgqnadvvllgpqiay
mlpeiqrllpnkpvevidsllygkvdglgvlkaavaaikkaaa
>d1vhra_ 3.40.1.1.1 VH1-related dual-specificity phosphatase, VHR {Human (Homo sapiens)}
svqdlndllsdgsgcyslpsqpcnevtpriyvgnasvaqdipklqklgithvlnaaegrs
fmhvntnanfykdsgitylgikandtqefnlsayferaadfidqalaqkngrvlvhcreg
ysrsptlviaylmmrqkmdvksalsivrqnreigpndgflaqlcqlndrlakegklkp
>d1mkp__ 3.40.1.1.2 Mapk phosphotase Pyst1 (mkp3) {Human (Homo sapiens)}
asfpveilpflylgcakdstnldvleefgikyilnvtpnlpnlfenagefkykqipisdh
wsqnlsqffpeaisfideargkncgvlvhslagisrsvtvtvaylmqklnlsmndaydiv
kmkksnispnfnfmgqlldfertl
>d1pty__ 3.40.1.2.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhssagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshedl
>d2shpa1 3.40.1.2.4 (219-525) Tyrosine phosphatase {Human (Homo sapiens), shp-2}
trinaaeiesrvrelsklaettdkvkqgfweefetlqqqeckllysrkegqrqenknknr
yknilpfdhtrvvlhdgdpnepvsdyinaniimpefetkcnnskpkksyiatqgclqntv
ndfwrmvfqensrvivmttkevergkskcvkywpdeyalkeygvmrvrnvkesaahdytl
relklskvgqgntertvwqyhfrtwpdhgvpsdpggvldfleevhhkqesimdagpvvvh
csagigrtgtfividilidiirekgvdcdidvpktiqmvrsqrsgmvqteaqyrsiymav
qhyietl
>d1ypta_ 3.40.1.2.6 Tyrosine phosphatase {Yersinia enterocolitica}
pearaelssrlttlrntlapatndprylqacggeklnrfrdiqcrrqtavradlnanyiq
vgntrtiacqyplqsqleshfrmlaenrtpvlavlassseianqrfgmpdyfrqsgtygs
itveskmtqqvglgdgimadmytltireagqktisvpvvhvgnwpdqtavssevtkalas
lvdqtaetkrnmyeskgssavaddsklrpvihcragvgrtaqligamcmndsrnsqlsve
dmvsqmrvqrngimvqkdeqldvliklaegqgrpllns
>d1d5ra2 3.40.1.3.1 (14-187) Phoshphoinositide phosphatase Pten (Pten tumor suppressor), N-terminal domain {Human (Homo sapiens)}
rryqedgfdldltyiypniiamgfpaerlegvyrnniddvvrfldskhknhykiynlcae
rhydtakfncrvaqypfedhnppqlelikpfcedldqwlseddnhvaaihckagkgrtgv
micayllhrgkflkaqealdfygevrtrdkkgvtipsqrryvyyysyllknhld
>d1c25__ 3.41.1.1.1 CDC25a {Human (Homo sapiens)}
mligdfskgylfhtvagkhqdlkyispeimasvlngkfanlikefviidcrypyeyeggh
ikgavnlhmeeevedfllkkpivptdgkrvivvfhcefssergprmcryvrerdrlgney
pklhypelyvlkggykeffmkcqsyceppsyrpmhhedfke
>d1rhs__ 3.41.1.2.1 Rhodanese {Bovine (Bos taurus)}
vhqvlyralvstkwlaesvragkvgpglrvldaswyspgtrearkeylerhvpgasffdi
eecrdkaspyevmlpseagfadyvgslgisndthvvvydgddlgsfyaprvwwmfrvfgh
rtvsvlnggfrnwlkeghpvtsepsrpepaifkatlnrsllktyeqvlenleskrfqlvd
sraqgrylgtqpepdavgldsghirgsvnmpfmnfltedgfekspeelramfeakkvdlt
kpliatxrkgvtachialaaylcgkpdvaiydgswfewfhrappetwvsqgkg
>d2trxa_ 3.42.1.1.1 Thioredoxin {Escherichia coli}
sdkiihltddsfdtdvlkadgailvdfwaewcgpckmiapildeiadeyqgkltvaklni
dqnpgtapkygirgiptlllfkngevaatkvgalskgqlkefldanla
>d1thx__ 3.42.1.1.2 Thioredoxin {Anabaena}
skgvititdaefesevlkaeqpvlvyfwaswcgpcqlmsplinlaantysdrlkvvklei
dpnpttvkkykvegvpalrlvkgeqildstegviskdkllsfldthln
>d1dbya_ 3.42.1.1.3 Thioredoxin {Chlamydomonas reinhardtii}
meagavnddtfknvvlessvpvlvdfwapwcgpcriiapvvdeiageykdklkcvklntd
espnvaseygirsiptimvfkggkkcetiigavpkativqtvekyln
>d1tof__ 3.42.1.1.3 Thioredoxin {Chlamydomonas reinhardtii}
ggsvividskaawdaqlakgkeehkpivvdftatwcgpckmiaplfetlsndyagkvifl
kvdvdavaavaeaagitamptfhvykdgvkaddlvgasqdklkalvakhaaa
>d1quwa_ 3.42.1.1.4 Thioredoxin {Bacillus acidocaldarius}
atmtltdanfqqaiqgdkpvlvdfwaawcgpcrmmapvleefaeahadkvtvaklnvden
pettsqfgimsiptlilfkggrpvkqligyqpkeqleaqladvlq
>d1erv__ 3.42.1.1.5 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevksmptfqffkkgqkvgefsgankekleatinelv
>d1jhb__ 3.42.1.1.6 Glutaredoxin {Human (Homo sapiens)}
aqefvnckiqpgkvvvfikptcpycrraqeilsqlpikqgllefvditatnhtneiqdyl
qqltgartvprvfigkdciggcsdlvslqqsgelltrlkqigalq
>d1aaza_ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1aazb_ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1aba__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcgpcdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1de1a_ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1de2a_ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1ego__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1egr__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpycvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1grx__ 3.42.1.1.7 Glutaredoxin {Bacteriophage T4}
mqtvifgrsgcpysvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d1qfna_ 3.42.1.1.8 Glutaredoxin {Escherichia coli}
mqtvifgrsgcpysvrakdlaeklsnerddfqyqyvdiraegitkedlqqkagkpvetvp
qifvdqqhiggytdfaawvkenlda
>d3grx__ 3.42.1.1.8 Glutaredoxin {Escherichia coli}
anveiytketcpyshrakallsskgvsfqelpidgnaakreemikrsgrttvpqifidaq
higgyddlyaldarggldpllk
>d1kte__ 3.42.1.1.9 Thioltransferase {Pig (Sus scrofa)}
aqafvnskiqpgkvvvfikptcpfcrktqellsqlpfkegllefvditatsdtneiqdyl
qqltgartvprvfigkeciggctdlesmhkrgelltrlqqvgavk
>d1bjx__ 3.42.1.2.1 Protein disulfide isomerase {Human (Homo sapiens)}
aattlpdgaaaeslvessevavigffkdvesdsakqflqaaeaiddipfgitsnsdvfsk
yqldkdgvvlfkkfdegrnnfegevtkenlldfikhnqlplviefteqta
>d1mek__ 3.42.1.2.1 Protein disulfide isomerase {Human (Homo sapiens)}
dapeeedhvlvlrksnfaealaahkyllvefyapwcghckalapeyakaagklkaegsei
rlakvdateesdlaqqygvrgyptikffrngdtaspkeytagreaddivnwlkkrtgpaa
>d1a8l_1 3.42.1.2.2 (1-119) Protein disulfide isomerase {Pyrococcus furiosus}
mglisdadkkvikeeffskmvnpvklivfvrkdhcqycdqlkqlvqelseltdklsyeiv
dfdtpegkelakryridrapattitqdgkdfgvryfglpaghefaafledivdvsreet
>d1a8l_2 3.42.1.2.2 (120-226) Protein disulfide isomerase {Pyrococcus furiosus}
nlmdetkqairnidqdvrilvfvtptcpycplavrmahkfaientkagkgkilgdmveai
eypewadqynvmavpkiviqvngedrvefegaypekmflekllsals
>d1a8y_1 3.42.1.3.1 (3-126) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
gldfpeydgvdrvinvnaknyknvfkkyevlallyheppeddkasqrqfemeelilelaa
qvledkgvgfglvdsekdaavakklglteedsiyvfkedevieydgefsadtlveflldv
ledp
>d1a8y_2 3.42.1.3.1 (127-228) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
veliegerelqafeniedeikligyfknkdsehykafkeaaeefhpyipffatfdskvak
kltlklneidfyeafmeepvtipdkpnseeeivnfveehrrs
>d1a8y_3 3.42.1.3.1 (229-347) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
tlrklkpesmyetweddmdgihivafaeeadpdgyefleilksvaqdntdnpdlsiiwid
pddfpllvpywektfdidlsapqigvvnvtdadsvwmemddeedlpsaeeledwledvl
>d1fvka2 3.42.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1bed_2 3.42.1.4.2 (1-62,127-181) Disulphide-bond formation facilitator (DSBA) {Vibrio cholerae}
aqfkegehyqvlktpassspvvseffsfycphcntfepiiaqlkqqlpegakfqknhvsf
mgXfavdsmvrrfdkqfqdsgltgvpavvvnnrylvqgqsvksldeyfdlvnylltlk
>d1gsba2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbc2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsbd2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsca2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscc2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gscd2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d2gsta2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d2gstb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d3gsta2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d3gstb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d4gsta2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d4gstb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d5gsta2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d5gstb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsta2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gstb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsua2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglahpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsub2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglahpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsva2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglshpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsvb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglshpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gswa2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglvhpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gswb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgywnvrglvhpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsxa2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgfwnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsxb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgfwnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsya2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgfwnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d6gsyb2 3.42.1.5.1 (1-84) Glutathione S-transferase {Rat (Rattus rattus)}
pmilgfwnvrglthpirllleytdssyeekryamgdapdydrsqwlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1baya2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1bayb2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1glpa2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glpb2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glqa2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1glqb2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d2glra2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d2glrb2 3.42.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d2gsra2 3.42.1.5.3 (1-76) Glutathione S-transferase {Pig (Sus scrofa), class pi}
ppytityfpvrgrceamrmlladqdqswkeevvtmetwpplkpsclfrqlpkfqdgdltl
yqsnailrhlgrsfgl
>d2gsrb2 3.42.1.5.3 (1-76) Glutathione S-transferase {Pig (Sus scrofa), class pi}
ppytityfpvrgrceamrmlladqdqswkeevvtmetwpplkpsclfrqlpkfqdgdltl
yqsnailrhlgrsfgl
>d10gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d10gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d11gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d11gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d12gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d12gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d13gsa2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d13gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d14gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d14gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d17gsa2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgd
ltlyqsntilrhlgrtl
>d17gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgdlt
lyqsntilrhlgrtl
>d18gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d18gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d19gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d19gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqva2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqvb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwa2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwc2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwd2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqxa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxc2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxd2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1gssa2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtlgl
>d1gssb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtlgl
>d1pgta2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d1pgtb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d20gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d20gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d21gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d21gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d22gsa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclfgqlpkfqdgdlt
lyqsntilrhlgrtl
>d22gsb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclfgqlpkfqdgdlt
lyqsntilrhlgrtl
>d2gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d2gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d2pgta2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d2pgtb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d3gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d3gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d3pgta2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d3pgtb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d4gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d4gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d4pgta2 3.42.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d4pgtb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d5gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d5gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d6gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d6gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d7gssa2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d7gssb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d8gssa2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d8gssb2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d8gssc2 3.42.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d9gssa2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d9gssb2 3.42.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1gsya2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gsyb2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptclygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtia2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtib2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtic2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtid2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtie2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtif2 3.42.1.5.5 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqgllkptxlygqlpkfedgdl
tlyqsnailrhlgrslgl
>d1gtua2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmilgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d1gtub2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmilgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d1gtuc2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmilgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d1gtud2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmilgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d1hna_2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnba2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnbb2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hnca2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncb2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncc2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d1hncd2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d2gtua2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d2gtub2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d3gtua2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d3gtub2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
scessmvlgywdirglahairllleftdtsyeekrytcgeapdydrsqwldvkfkldldf
pnlpylldgknkitqsnailryia
>d3gtuc2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
pmtlgywnirglahsirllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgthkitqsnailryiarkhn
>d3gtud2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
scessmvlgywdirglahairllleftdtsyeekrytcgeapdydrsqwldvkfkldldf
pnlpylldgknkitqsnailryia
>d4gtua2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtub2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtuc2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtud2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtue2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtuf2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtug2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d4gtuh2 3.42.1.5.6 (1-84) Glutathione S-transferase {Human (Homo sapiens), class mu}
smtlgywdirglahairllleytdssyeekkytmgdapdydrsqwlnekfklgldfpnlp
ylidgahkitqsnailcyiarkhn
>d3fyga2 3.42.1.5.7 (1-84) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
pmilgxwnvrglthpirlllextdssxeekrxamgdapdxdrsqwlnekfklgldfpnlp
xlidgsrkitqsnaimrxlarkhh
>d3fygb2 3.42.1.5.7 (1-84) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
pmilgxwnvrglthpirlllextdssxeekrxamgdapdxdrsqwlnekfklgldfpnlp
xlidgsrkitqsnaimrxlarkhh
>d5fwga2 3.42.1.5.7 (1-84) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
pmilgyxnvrglthpirllleytdssyeekryamgdapdydrsqxlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d5fwgb2 3.42.1.5.7 (1-84) Glutathione S-transferase {Rat (Rattus norvegicus), class mu}
pmilgyxnvrglthpirllleytdssyeekryamgdapdydrsqxlnekfklgldfpnlp
ylidgsrkitqsnaimrylarkhh
>d1gsua2 3.42.1.5.8 (1-84) Glutathione S-transferase {Chicken (Gallus gallus), class mu}
vvtlgywdirglahairllleytetpyqerrykagpapdfdpsdwtnekeklgldfpnlp
ylidgdvkltqsnailryiarkhn
>d1gsub2 3.42.1.5.8 (1-84) Glutathione S-transferase {Chicken (Gallus gallus), class mu}
vvtlgywdirglahairllleytetpyqerrykagpapdfdpsdwtnekeklgldfpnlp
ylidgdvkltqsnailryiarkhn
>d1agsa2 3.42.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agsb2 3.42.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsda2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsdb2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsea2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargkmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gseb2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargkmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsfa2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gsfb2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1guha2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1guhb2 3.42.1.5.9 (2-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1gula2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gulb2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gulc2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1guld2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gule2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gulf2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gulg2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gulh2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1guma2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumb2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumc2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumd2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gume2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumf2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumg2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1gumh2 3.42.1.5.9 (4-80) Glutathione S-transferase {Human (Homo sapiens), class alpha}
rpklhypngrgrmesvrwvlaaagvefdeefletkeqlyklqdgnhllfqqvpmveidgm
klvqtrsilhyiadkhn
>d1b48a2 3.42.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1b48b2 3.42.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1guka2 3.42.1.5.10 (5-79) Glutathione S-transferase {Mouse (Mus musculus)}
pklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveidgmm
ltqtrailsylaaky
>d1gukb2 3.42.1.5.10 (5-79) Glutathione S-transferase {Mouse (Mus musculus)}
pklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveidgmm
ltqtrailsylaaky
>d1ljra2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d1ljrb2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d2ljra2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d2ljrb2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d3ljra2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d3ljrb2 3.42.1.5.11 (1-79) Glutathione S-transferase {Human (Homo sapiens), class theta}
mglelfldlvsqpsravyifakkngiplelrtvdlvkgqhkskeflqinslgklptlkdg
dfiltessailiylsckyq
>d1pd212 3.42.1.5.12 (1-75) Glutathione S-transferase {Rat (Rattus norvegicus), class sigma}
mpnykllyfnmrgraeiiryifayldikyedhrieqadwpkikptlpfgkipvleveglt
lhqslaiaryltknt
>d1pd222 3.42.1.5.12 (1-75) Glutathione S-transferase {Rat (Rattus norvegicus), class sigma}
mpnykllyfnmrgraeiiryifayldikyedhrieqadwpkikptlpfgkipvleveglt
lhqslaiaryltknt
>d1gsq_2 3.42.1.5.13 (1-75) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus), class sigma}
pkytlhyfplmgraelcrfvlaahgeeftdrvvemadwpnlkatmysnampvldidgtkm
sqsmciarhlarefg
>d2gsq_2 3.42.1.5.13 (1-75) Glutathione S-transferase {Squid (Ommastrephes sloani pacificus), class sigma}
pkytlhyfplmgraelcrfvlaahgeeftdrvvemadwpnlkatmysnampvldidgtkm
sqsmciarhlarefg
>d1bg5_2 3.42.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1duga2 3.42.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1dugb2 3.42.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1gne_2 3.42.1.5.14 (1-79) Glutathione S-transferase {Schistosoma japonicum}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhn
>d1gta_2 3.42.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1gtb_2 3.42.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1fhe_2 3.42.1.5.15 (1-80) Glutathione S-transferase {Fasciola hepatica}
paklgywklrglaqpvrlfleylgeeyeehlygrddrekwmsekfnmgldlpnlpyyidd
kckltqsvaimryiadkhgm
>d2fhea2 3.42.1.5.15 (1-80) Glutathione S-transferase {Fasciola hepatica}
paklgywkirglqqpvrllleylgekyeeqiyerddgekwfskkfelgldlpnlpyyidd
kckltqslailryiadkhgm
>d2fheb2 3.42.1.5.15 (1-80) Glutathione S-transferase {Fasciola hepatica}
paklgywkirglqqpvrllleylgekyeeqiyerddgekwfskkfelgldlpnlpyyidd
kckltqslailryiadkhgm
>d1bx9a2 3.42.1.5.16 (1-85) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnll
>d1gnwa2 3.42.1.5.16 (2-85) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnl
>d1gnwb2 3.42.1.5.16 (2-85) Glutathione S-transferase {Mouse-ear cress (Arabidopsis thaliana)}
gikvfghpasiatrrvlialheknldfelvhvelkdgehkkepflsrnpfgqvpafedgd
lklfesraitqyiahryenqgtnl
>d1axda2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1axdb2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byea2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byeb2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byec2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1byed2 3.42.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1aw9_2 3.42.1.5.18 (2-82) Glutathione S-transferase {Maize (Zea mays), type III}
aplklygmplspnvvrvatvlnekgldfeivpvdlttgahkqpdflalnpfgqipalvdg
devlfesrainryiaskyase
>d1a0fa2 3.42.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1a0fb2 3.42.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1b8xa2 3.42.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1pmt_2 3.42.1.5.20 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d2pmta2 3.42.1.5.20 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d2pmtb2 3.42.1.5.20 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d2pmtc2 3.42.1.5.20 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d2pmtd2 3.42.1.5.20 (1-80) Glutathione S-transferase {Proteus mirabilis}
mklyytpgscslsphivlretgldfsieridlrtkktesgkdflainpkgqvpvlqldng
diltegvaivqyladlkpdr
>d2trcp_ 3.42.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskerxsrkxs
iqeyelihqdkedegclrkyrrqcxqdxhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypxvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1qgva_ 3.42.1.7.1 spliceosomal protein U5-15Kd {Human (Homo sapiens)}
symlphlhngwqvdqailseedrvvvirfghdwdptcmkmdevlysiaekvknfaviylv
ditevpdfnkmyelydpctvmfffrnkhimidlgtgnnnkinwamedkqemvdiietvyr
garkgrglvvspkdyst
>d1gp1a_ 3.42.1.8.1 Glutathione peroxidase {Bovine (Bos taurus)}
rtvyafsarplaggepfnlsslrgkvllienvaslxgttvrdytqmndlqrrlgprglvv
lgfpcnqfghqenakneeilnclkyvrpgggfepnfmlfekcevngekahplfaflrevl
ptpsddatalmtdpkfitwspvcrndvswnfekflvgpdgvpvrrysrrfltidiepdie
tllsq
>d1qq2a_ 3.42.1.8.2 Thioredoxin peroxidase 2 (2-cys peroxiredoxin) {Norvey rat (Rattus norvegicus)}
sgnakighpapsfkatavmpdgqfkdislsdykgkyvvfffypldftfvcpteiiafsdr
aeefkklncqvigasvdshfshlawintpkkqgglgpmniplvsdpkrtiaqdygvlkad
egisfrglfiiddkgilrqitindlpvgrsvdeilrlvqafqftdkhgevcpa
>d1prxa_ 3.42.1.8.3 HorF6 peroxidase {Human (Homo sapiens)}
lllgdvapnfeanttvgrirfhdflgdswgilfshprdftpvxttelgraaklapefakr
nvklialsidsvedhlawskdinaynseepteklpfpiiddrnrelaillgmldpaekde
kgmpvtarvvfvfgpdkklklsilypattgrnfdeilrvvislqltaekrvatpvdwkdg
dsvmvlptipeeeakklfpkgvftkelpsgkkylrytpqp
>d1foha3 3.42.1.8.4 (462-662) Phenol hydroxylase, C-terminal domain {Soil-living yeast (Trichosporon cutaneum)}
nlvtdkksskqelakncvvgtrfksqpvvrhseglwmhfgdrlvtdgrfriivfagkatd
atqmsrikkfsayldsensvislytpkvsdrnsridvitihschrddiemhdfpapalhp
kwqydfiyadcdswhhphpksyqawgvdetkgavvvvrpdgytslvtdlegtaeidryfs
gilvepkeksgaqteadwtks
>d1trka3 3.43.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1qs0b2 3.43.1.2.1 (206-339) 2-oxoisovalerate dehydrogenase beta-subunit, C-domain {Pseudomonas putida}
yytvpldkaaitrpgndvsvltygttvyvaqvaaeesgvdaevidlrslwpldldtives
vkktgrcvvvheatrtcgfgaelvslvqehcfhhleapiervtgwdtpyphaqewayfpg
psrvgaalkkvxev
>d1b0pa3 3.43.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1a49a3 3.44.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1pkla3 3.44.1.1.3 (358-498) Pyruvate kinase, C-terminal domain {Leishmania mexicana}
neyvffnsikklqhipmsadeavcssavnsvyetkakamvvlsntgrsarlvakyrpncp
ivcvttrlqtcrqlnitqgvesvffdadklghdegkehrvaagvefakskgyvqtgdycv
vihadhkvkgyanqtrillve
>d1a3wa3 3.44.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1pkya3 3.44.1.1.5 (351-470) Pyruvate kinase, C-terminal domain {Escherichia coli}
klriteavcrgavetaekldaplivvatqggksaravrkyfpdatilalttnektahqlv
lskgvvpqlvkeitstddfyrlgkelalqsglahkgdvvvmvsgalvpsgttntasvhvl
>d1lam_1 3.45.1.1.1 (1-159) Leucine aminopeptidase, N-terminal domain {Bovine (Bos taurus)}
tkglvlgiyskekeedepqftsagenfnklvsgklreilnisgpplkagktrtfyglhed
fpsvvvvglgkktagideqenwhegkeniraavaagcrqiqdleipsvevdpcgdaqaaa
egavlglyeyddlkqkrkvvvsaklhgsedqeawqrgvl
>d1htta1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httb1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httc1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1httd1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmma1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmb1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmc1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmmd1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmna1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnb1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnc1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1kmnd1 3.46.1.1.1 (326-424) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Escherichia coli}
dpvvdiylvasgadtqsaamalaerlrdelpgvklmtnhgggnfkkqfaradkwgarvav
vlgesevangtavvkdlrsgeqtavaqdsvaahlrtllg
>d1adja1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjb1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjc1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjd1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adya1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyb1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyc1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyd1 3.46.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1atia1 3.46.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1qf6a1 3.46.1.1.4 (533-642) Threonyl-tRNA synthetase (ThrRS), C-terminal domain {Escherichia coli}
fptwlapvqvvimnitdsqseyvneltqklsnagirvkadlrnekigfkirehtlrrvpy
mlvcgdkevesgkvavrtrrgkdlgsmdvnevieklqqeirsrslkqlee
>d1diob_ 3.46.2.1.1 Diol dehydratase, beta subunit {Klebsiella oxytoca}
gfltevgearqgtqqdeviiavgpafglaqtvnivgiphksilreviagieeegikarvi
rcfkssdvafvavegnrlsgsgisigiqskgttvihqqglpplsnlelfpqaplltlety
rqigknaaryakrespqpvptlndqmarpkyqaksailhiketkyvvtgknpqelrval
>d1b78a_ 3.46.3.1.1 XTP pyrophosphatase {(Methanococcus jannaschii)}
kiyfatgnpnkikeaniilkdlkdveieqikisypeiqgtleevaefgakwvynilkkpv
ivedsgffvealngfpgtyskfvqetignegilkllegkdnrnayfktvigycdengvrl
fkgivkgrvseeirskgygfaydsifipeeeertfaemtteeksqishrkkafeefkkfl
ldri
>d1ckqa_ 3.47.1.1.1 Restriction endonuclease EcoRI {Escherichia coli}
sqgvigifgdyakahdlavgevsklvkkalsneypqlsfryrdsikkteinealkkidpd
lggtlfvsnssikpdggivevkddygewrvvlvaeakhqgkdiinirngllvgkrgdqdl
maagnaiershkniseianfmlseshfpyvlflegsnfltenisitrpdgrvvnleynsg
ilnrldrltaanygmpinsnlcinkfvnhkdksimlqaasiytqgdgrewdskimfeimf
disttslrvlgrdlfeqltsk
>d1rvaa_ 3.47.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bam__ 3.47.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkdkvenk
>d1dmua_ 3.47.1.4.1 Restriction endonuclease BglI {Bacillus subtilis (synonym: Bacillus globigii)}
mynlhrekifmsynqnkqylednpeiqekielyglnllnevisdneeeiradyneanflh
pfwmnyppldrgkmpkgdqipwievgekavgskltrlvsqreditvreiglptgpderyl
ltsptiysltngftdsimmfvdiksvgprdsdydlvlspnqvsgngdwaqleggiqnnqq
tiqgprssqiflptipplyilsdgtiapvvhlfikpiyamrsltkgdtgqslykiklasv
pnglglfcnpgyafdsaykflfrpgkddrtksllqkrvrvdlrvldkigprvmtidmdk
>d1dfma_ 3.47.1.5.1 Restriction endonuclease BglII {Bacillus subtilis (synonym: Bacillus globigii)}
kiditdynhadeilnpqlwkeieetllkxplhvkasdqaskvgslifdpvgtnqyikdel
vpkhwknnipipkrfdflgtdidfgkrdtlvevqfsnypfllnntvrselfhksnxdide
egxkvaiiitkghxfpasnsslyyeqaqnqlnslaeynvfdvpirlvgliedfetdidiv
sttyadkrysrtitkrdtvkgkvidtntpntrrrkrgtivty
>d3pvia_ 3.47.1.6.1 Restriction endonuclease PvuII {Proteus vulgaris}
shpdlnkllelwphiqeyqdlalkhgindifqgnggkllqvllitgltvlpgregndavd
nagqeyelksinidltkgfsthhhmnpviiakyrqvpwifaiyrgiaieaiyrlepkdle
fyydkwerkwysdghkdinnpkipvkyvmehgtkiy
>d1cfr__ 3.47.1.7.1 Restriction endonuclease Cfr10I {Citrobacter freundii}
mdiisksgegnkytinsaiafvayashidinttefskvlsglrdfindeairlggkisdg
sfnkcngdwyewligiraiefflesetnfivvkmpnatsfdvmsiyksclsefiydlrsk
lslnnvnlitsnpdfsiidirgrreelksmlkdisfsnislstiseidnlyknfidyael
ehiksflsvkttfrpdrrlqlahegslmkalythlqtrtwtinptgiryyaaatsignad
viglktvathsitdvkslpqsavdeifkinsvldvdsclshil
>d2foka4 3.47.1.8.1 (387-579) Restriction endonuclease FokI, C-terminal (catalytic) domain {Flavobacterium okeanokoites}
kseleekkselrhklkyvpheyielieiarnstqdrilemkvmeffmkvygyrgkhlggs
rkpdgaiytvgspidygvivdtkaysggynlpigqademqryveenqtrnkhinpnewwk
vypssvtefkflfvsghfkgnykaqltrlnhitncngavlsveelliggemikagtltle
evrrkfnngeinf
>d1avqa_ 3.47.1.9.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1azo__ 3.47.1.10.1 DNA mismatch repair protein MutH from {Escherichia coli}
prpllsppeteeqllaqaqqlsgytlgelaalvglvtpenlkrdkgwigvlleiwlgasa
gskpeqdfaalgvelktipvdslgrplettfvcvapltgnsgvtwetshvrhklkrvlwi
pvegeasiplaqrrvgspllwspneeedrqlredweelxdxivlgqveritarhgeylqi
rpkaanakalteaigargeriltlprgfylkknftsallarhfliq
>d1vsra_ 3.47.1.11.1 Very short patch repair (VSR) endonuclease {(Escherichia coli)}
aiekrlaslltgqglafrvqdaslpgrpdfvvdeyrcvifthgcfwhhhhcylfkvpatr
tefwlekigknverdrrdisrlqelgwrvlivwecalrgrekltdealterleewicgeg
asaqidtqgihlla
>d1a79a1 3.47.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d2rsla_ 3.48.1.1.1 gamma,delta resolvase, large fragment {Escherichia coli}
mrlfgyarvstsqqsldiqvralkdagvkanriftdkasgsssdrkgldllrmkveegdv
ilvkkldrlgrdtadmiqlikefdaqgvsirfiddgistdgemgkmvvtilsavaqaerq
ri
>d1tfr_2 3.48.1.2.1 (12-180) T4 RNase H {Bacteriophage T4}
kegiclidfsqialstalvnfpdkekinlsmvrhlilnsikfnvkkaktlgytkivlcid
naksgywrrdfayyykknrgkareestwdwegyfesshkvidelkaympyivmdidkyea
ddhiavlvkkfsleghkiliissdgdftqlhkypnvkqwspmhkkwvki
>d1bgxt2 3.48.1.2.2 (1-173) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
mrgmlplfepkgrvllvdghhlayrtfhalkglttsrgepvqavygfaksllkalkedgd
avivvfdakapsfrheayggykagraptpedfprqlalikelvdllglarlevpgyeadd
vlaslakkaekegyevriltadkdlyqllsdrihvlhpegylitpawlwekyg
>d1xo1a2 3.48.1.2.3 (19-185) T5 5'-exonuclease {Bacteriophage T5}
rrnlmivdgtnlgfrfkhnnskkpfassyvstiqslaksysarttivlgdkgksvfrleh
lpeykgnrdekyaqrteeekaldeqffeylkdafelckttfptftirgveaddmaayivk
lighlydhvwlistdgdwdtlltdkvsrfsfttrreyhlrdmyehhn
>d1a77_2 3.48.1.2.4 (2-208) Flap endonuclease-1 {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1pdo__ 3.49.1.1.1 IIA domain of mannose transporter, IIA-Man {Escherichia coli}
tiaivigthgwaaeqllktaemllgeqenvgwidfvpgenaetliekynaqlakldttkg
vlflvdtwggspfnaasrivvdkehyeviagvnipmlvetlmardddpsfdelvalavet
gregvkalk
>d1bupa1 3.50.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgstyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1bupa2 3.50.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1dkgd_ 3.50.1.1.3 Heat shock protein 70kDa, ATPase fragment {Escherichia coli, gene dnaK}
kiigidlgttnscvaimdgttprvlenaegdrttpsiiaytqdgetlvgqpakrqavtnp
qntlfaikrligrrfqdeevqrdvsimpfkiiaadngdawvevkgqkmappqisaevlkk
mkktaedylgepvteavitvpayfndaqrqatkdagriaglevkriineptaaalaygld
kgtgnrtiavydlgggtfdisiieidevdgektfevlatngdthlggedfdsrlinylve
efkkdqgidlrndplamqrlkeaaekakielssaqqtdvnlpyitadatgpkhmnikvtr
akleslvedlvnrsiellkvalqdaglsvsdiddvilvggqtrmpmvqkkvaeffgkepr
kdvnpdeavaigaavqggvlt
>d1yaga1 3.50.1.1.7 (4-146) Actin {Baker's yeast (Saccharomyces cerevisiae)}
evaalvidngsgmckagfagddapravfpsivgrprhqgimvgmgqkdsyvgdeaqskrg
iltlrypiehgivtnwddmekiwhhtfynelrvapeehpvllteapmnpksnrekmtqim
fetfnvpafyvsiqavlslyssg
>d1yaga2 3.50.1.1.7 (147-375) Actin {Baker's yeast (Saccharomyces cerevisiae)}
rttgivldsgdgvthvvpiyagfslphailridlagrdltdylmkilsergysfsttaer
eivrdikeklcyvaldfeqemqtaaqsssieksyelpdgqvitignerfrapealfhpsv
lglesagidqttynsimkcdvdvrkelygnivmsggttmfpgiaermqkeitalapssmk
vkiiapperkysvwiggsilaslttfqqmwiskqeydesgpsivhhkcf
>d1bdg_1 3.50.1.2.1 (13-222) Hexokinase {Blood fluke (Schistosoma mansoni)}
fsdqqlfekvveilkpfdlsvvdyeeicdrmgesmrlglqkstnekssikmfpsyvtktp
ngtetgnflaldlggtnyrvlsvtlegkgkspriqertycipaekmsgsgtelfkyiaet
ladflenngmkdkkfdlgftfsfpcvqkglthatlvrwtkgfsadgveghnvaellqtel
dkrelnvkcvavvndtvgtlascaledp
>d1bdg_2 3.50.1.2.1 (223-460) Hexokinase {Blood fluke (Schistosoma mansoni)}
kcavglivgtgtnvayiedsskvelmdgvkepevvintewgafgekgeldcwrtqfdksm
didslhpgkqlyekmvsgmylgelvrhiivylveqkilfrgdlperlkvrnslltryltd
verdpahllynthymltddlhvpvvepidnrivryacemvvkraaylagagiacilrrin
rsevtvgvdgslykfhpkfcermtdmvdklkpkntrfclrlsedgsgkgaaaiaasc
>d1qhaa1 3.50.1.2.2 (12-222) Mammalian type I hexokinase {Human (Homo sapiens)}
telkddqvkkidkylyamrlsdetlidimtrfrkemknglsrdfnptatvkmlptfvrsi
pdgsekgdfialdlggssfrilrvqvnheknqnvhmesevydtpenivhgsgsqlfdhva
eclgdfmekrkikdkklpvgftfsfpcqqskideailitwtkrfkasgvegadvvkllnk
aikkrgdydanivavvndtvgtmmtcgyddq
>d1qhaa2 3.50.1.2.2 (223-465) Mammalian type I hexokinase {Human (Homo sapiens)}
hcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreid
rgslnpgkqlfekmvsgmylgelvrlilvkmakegllfegritpelltrgkfntsdvsai
eknkeglhnakeiltrlgvepsdddcvsvqhvctivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykthpqysrrfhktlrrlvpdsdvrfllsesgsgkgaamvtavayr
lae
>d1bu6o1 3.50.1.3.1 (3-253) Glycerol kinase {Escherichia coli}
kkyivaldqgttssravvmdhdaniisvsqrefeqiypkpgwvehdpmeiwatqsstlve
vltkadissdqiaaigitnqrettivweketgkpiynaivwqcrrtaeicehlkrdgled
yirsntglvidpyfsgtkvkwildhvegsrerarrgellfgtvdtwliwkmtqgrvhvtd
ytnasrtmlfnihtldwddkmlevldipremlpevrrssevygqtniggkggtripisgi
agdqqaalfgq
>d1bu6o2 3.50.1.3.1 (254-499) Glycerol kinase {Escherichia coli}
lcvkegmakntygtgcfmlmntgekavksengllttiacgptgevnyalegavfmagasi
qwlrdemklindaydseyfatkvqntngvyvvpaftglgapywdpyargaifgltrgvna
nhiiratlesiayqtrdvleamqadsgirlhalrvdggavannflmqfqsdilgtrverp
evrevtalgaaylaglavgfwqnldelqekavierefrpgietternyryagwkkavkra
maweeh
>d1chma1 3.50.2.1.1 (2-156) Creatinase, N-terminal domain {Pseudomonas putida}
qmpktlrirngdkvrstfsaqeyanrqarlrahlaaenidaaiftsyhninyysdflycs
fgrpyalvvteddvisisanidggqpwrrtvgtdnivytdwqrdnyfaaiqqalpkarri
giehdhlnlqnrdklaarypdaelvdvaaacmrmr
>d2rn2__ 3.50.3.1.1 RNase H {Escherichia coli}
mlkqveiftdgsclgnpgpggygailryrgrektfsagytrttnnrmelmaaivalealk
ehcevilstdsqyvrqgitqwihnwkkrgwktadkkpvknvdlwqrldaalgqhqikwew
vkghaghpenercdelaraaamnptledtgyqvev
>d1ril__ 3.50.3.1.3 RNase H {Thermus thermophilus}
rkrvalftdgaclgnpgpggwaallrfhahekllsggeacttnnrmelkaaieglkalke
pcevdlytdshylkkaftegwlegwrkrgwrtaegkpvknrdlwealllamaphrvrfhf
vkghtghpenervdrearrqaqsqakt
>d1vrta1 3.50.3.1.4 (430-539) HIV RNase H (Domain of reverse transcriptase) {Human immunodeficiency virus, type 1}
ekepivgaetfyvdgaanretklgkagyvtnrgrqkvvtltdttnqktelqaiylalqds
glevnivtdsqyalgiiqaqpdqseselvnqiieqlikkekvylawvpah
>d1cxqa_ 3.50.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
grglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiav
lgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvla
egdgfmkriptskqgellakamyalnh
>d1b9da_ 3.50.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnkkrkggiggysagerivdiiatdiqt
>d1bco_2 3.50.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1b7ea_ 3.50.3.4.1 Transposase inhibitor (Tn5 transposase) {Escherichia coli}
saeairkagamqtvklaqefpellaiedttslsyrhqvaeelgklgsiqdksrgwwvhsv
llleattfrtvgllhqewwmrpddpadadekesgkwlaaaatsrlrmgsmmsnviavcdr
eadihaylqdklahnerfvvrskhprkdvesglylydhlknqpelggyqisipqkgvvdk
rgkrknrparkaslslrsgritlkqgnitlnavlaeeinppkgetplkwllltsepvesl
aqalrvidiythrwrieefhkawktgagaerqrmeepdnlermvsilsfvavrllqlres
ftlpqalraqgllkeaehvesqsaetvltpdecqllgyldkgkrkrkekgslqwaymaia
rlggfmdskrtgiaswgalwegwealqskldgflaakdlmaq
>d1kfsa1 3.50.3.5.1 (324-518) Exonuclease domain of DNA polymerase {Escherichia coli}
misydnyvtildeetlkawiaklekapvfafdtetdsldnisanlvglsfaiepgvaayi
pvahdyldapdqisreralellkplledekalkvgqnlkydrgilanygielrgiafdtm
lesyilnsvagrhdmdslaerwlkhktitfeeiagkgknqltfnqialeeagryaaedad
vtlqlhlkmwpdlqk
>d1qtma1 3.50.3.5.2 (293-450) Exonuclease domain of DNA polymerase {Thermus aquaticus}
aleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkeargll
akdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraalserl
fanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1xwl_1 3.50.3.5.3 (297-492) Exonuclease domain of DNA polymerase {Bacillus stearothermophilus, newly identified strain as yet unnamed}
akmaftladrvteemladkaalvvevveenyhdapivgiavvnehgrfflrpetaladpq
fvawlgdetkkksmfdskraavalkwkgielcgvsfdlllaaylldpaqgvddvaaaakm
kqyeavrpdeavygkgakravpdepvlaehlvrkaaaiwelerpfldelrrneqdrllve
leqplssilaemefag
>d1t7pa1 3.50.3.6.1 (1-210) T7-like DNA polymerase {Bacteriophage T7}
mivsdieanallesvtkfhcgviydystaeyvsyrpsdfgayldaleaevargglivfhn
ghkydvpaltklaklqlnrefhlprencidtlvlsrlihsnlkdtdmgllrsgklpgale
awgyrlgemkgeykddfkrmleeqgeeyvdgmewwnfneemmdynvqdvvvtkallekll
sdkhyfppeidftdvgyttfwses
>d1noya_ 3.50.3.6.2 T4-like DNA polymerase {Bacteriophage T4}
defyisietvgnniveryidengkertreveylptmfrhckeeskykdiygkncapqkfp
smkdardwmkrmediglealgmndfklayisdtygseivydrkfvrvancdievtgdkfp
dpmkaeyeidaithydsiddrfyvfdllnsmygsvskwdaklaakldceggdevpqeild
rviympfdnerdmlmeyinlweqkrpaiftgwniegfdvpyimnrvkmilgersmkrfsp
igrvkskllqnmygskeiysidgvsildyldlykkfaftnlpsfslesvaqhetkkgklp
ydgpinklretnhqryisyniidvesvqaidkirgfidlvlsmsyyakmpfsgvmspikt
wdaiifnslkge
>d1tgoa1 3.50.3.6.4 (1-347) T4-like DNA polymerase {Thermococcus gorgonarius}
mildtdyitedgkpvirifkkengefkidydrnfepyiyallkddsaiedvkkitaerhg
ttvrvvraekvkkkflgrpievwklyfthpqdvpairdkikehpavvdiyeydipfakry
lidkglipmegdeelkmlafdietlyhegeefaegpilmisyadeegarvitwknidlpy
vdvvstekemikrflkvvkekdpdvlityngdnfdfaylkkrseklgvkfilgregsepk
iqrmgdrfavevkgrihfdlypvirrtinlptytleavyeaifgqpkekvyaeeiaqawe
tgeglervarysmedakvtyelgkeffpmeaqlsrlvgqslwdvsrs
>d1hjra_ 3.50.3.7.1 RuvC resolvase {Escherichia coli}
aiilgidpgsrvtgygvirqvgrqlsylgsgcirtkvddlpsrlkliyagvteiitqfqp
dyfaieqvfmaknadsalklgqargvaivaavnqelpvfeyaarqvkqtvvgigsaeksq
vqhmvrtllklpanpqadaadalaiaithchvsqnamq
>d1sfe_2 3.50.4.1.1 (12-92) Ada DNA repair protein {Escherichia coli}
lavryaladcelgrclvaesergicaillgdddatliselqqmfpaadnapadlmfqqhv
reviaslnqrdtpltlpldir
>d1qnta2 3.50.4.1.2 (6-91) O6-alkylguanine-DNA alkyltransferase {Human (Homo sapiens) |A|}
emkrttldsplgklelsgceqglheikllgkgtsaadavevpapaavlggpeplmqctaw
lnayfhqpeaieefpvpalhhpvfqq
>d1mgta2 3.50.4.1.3 (1-88) O6-alkylguanine-DNA alkyltransferase {Pyrococcus kodakaraensis}
mlsvekfrvgervvwigvifsgrvqgiafafdrgtlmkrihdlaehlgkrgvsisldvqp
sdypekvfkvligeldnasflrelsfeg
>d1b8oa_ 3.51.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
ngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestvp
ghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaagglnp
nfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqmg
eqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfslit
nkvimdyesqgkanheevleagkqaaqkleqfvsllmasi
>d1ecpa_ 3.51.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1qe5a_ 3.51.1.1.4 Purine nucleoside phosphorylase, PNP {Cellulomonas sp.}
pplddpatdpflvaraaadhiaqatgveghdmalvlgsgwggaaellgevvaevptheip
gfssvtrsirveradgsvrhalvlgsrthlyegkgvravvhgvrtaaatgaetliltngc
gglnqewgagtpvllsdhinltarsplegptfvdltdvysprlrelahrvdptlpegvya
qfpgphyetpaevrmagilgadlvgmsttleaiaarhcglevlgvslvtnlaagisptpl
shaevieagqaagprisalladiakr
>d1cb0a_ 3.51.1.1.5 5'-deoxy-5'-methylthioadenosine phosphorylase {Human (Homo sapiens)}
avkigiiggtglddpeilegrtekyvdtpfgkpsdalilgkiknvdcvllarhgrqhtim
pskvnyqaniwalkeegcthvivttacgslreeiqpgdiviidqfidrttmrpqsfydgs
hscargvchipmaepfcpktrevlietakklglrchskgtmvtiegprfssraesfmfrt
wgadvinmttvpevvlakeagicyasiamatdydcwkeheeavsvdrvlktlkenankak
slllttipqigstewsetlhnlknmaqfsvllp
>d2pth__ 3.51.2.1.1 Peptidyl-tRNA hydrolase {Escherichia coli}
tiklivglanpgaeyaatrhnagawfvdllaerlraplreeakffgytsrvtlggedvrl
lvpttfmnlsgkavaamasffrinpdeilvahdeldlppgvakfklggghgghnglkdii
sklgnnpnfhrlrigighpgdknkvvgfvlgkppvseqklideaideaarctemwftdgl
tkatnrlhafkaq
>d1a2za_ 3.51.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1auga_ 3.51.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d2ctc__ 3.51.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavealkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtlnn
>d1obr__ 3.51.4.2.1 Carboxypeptidase T {Thermoactinomyces vulgaris}
dfpsydsgyhnynemvnkintvasnypnivkkfsigksyegrelwavkisdnvgtdenep
evlytalhharehltvemalytldlftqnynldsritnlvnnreiyivfninpdggeydi
ssgsykswrknrqpnsgssyvgtdlnrnygykwgccggssgspssetyrgrsafsapeta
amrdfinsrvvggkqqiktlitfhtyselilypygytytdvpsdmtqddfnvfktmantm
aqtngytpqqasdlyitdgdmtdwaygqhkifaftfemyptsynpgfyppdevigretsr
nkeavlyvaekadcpysvigksc
>d1lam_2 3.51.4.3.1 (160-484) Leucine aminopeptidase, C-terminal domain {Bovine (Bos taurus)}
fasgqnlarrlmetpanemtptkfaeiveenlksasiktdvfirpkswieeqemgsflsv
akgseeppvfleihykgspnasepplvfvgkgitfdsggisikaaanmdlmradmggaat
icsaivsaakldlpinivglaplcenmpsgkankpgdvvrarngktiqvdntdaegrlil
adalcyahtfnpkviinaatltgamdialgsgatgvftnsswlwnklfeasietgdrvwr
mplfehytrqvidcqladvnnigkyrsagactaaaflkefvthpkwahldiagvmtnkde
vpylrkgmagrptrtlieflfrfsq
>d1amp__ 3.51.4.4.1 Aminopeptidase {Aeromonas proteolytica}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1xjo__ 3.51.4.4.2 Aminopeptidase {Streptomyces griseus}
apdiplanvkahltqlstiaannggnrahgrpgykasvdyvkakldaagytttlqqftsg
gatgynlianwpggdpnkvlmagahldsvssgagindngsgsaavletalavsragyqpd
khlrfawwgaeelgligskfyvnnlpsadrsklagylnfdxigspnpgyfvydddpviek
tfknyfaglnvpteietegdgrsdhapfknvgvpvgglftgagytksaaqaqkwggtagq
afdrcyhsscdslsnindtaldrnsdaaahaiwtlss
>d1cg2a1 3.51.4.4.3 (26-213,327-414) Carboxypeptidase G2, catalytic domain {Pseudomonas strain rs-16}
qkrdnvlfqaatdeqpaviktleklvnietgtgdaegiaaagnfleaelknlgftvtrsk
saglvvgdnivgkikgrggknlllmshmdtvylkgilakapfrvegdkaygpgiaddkgg
navilhtlkllkeygvrdygtitvlfntdeekgsfgsrdliqeeakladyvlsfeptsag
deklslgtXfnageggkklvdkavayykeaggtlgveertgggtdaayaalsgkpviesl
glpgfgyhsdkaeyvdisaiprrlymaarlimdlgag
>d1de4c3 3.51.4.5.1 (122-189,383-608) Transferrin receptor ectodomain, protease-like domain {Human (Homo sapiens)}
lywddlkrklsekldstdftstikllnensyvpreagsqkdenlalyvenqfrefklskv
wrdqhfvkXeikilnifgvikgfvepdhyvvvgaqrdawgpgaaksgvgtalllklaqmf
sdmvlkdgfqpsrsiifaswsagdfgsvgatewlegylsslhlkaftyinldkavlgtsn
fkvsaspllytliektmqnvkhpvtgqflyqdsnwaskvekltldnaafpflaysgipav
sfcfcedtdypylgttmdtykelieripelnkvaraaaevagqfviklthdveln
>d1boub_ 3.51.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1di6a_ 3.52.1.1.1 Molybdenumm cofactor biosynthesis protein MogA {Escherichia coli}
atlriglvsisdrassgvyqdkgipaleewltsalttpfeletrlipdeqaiieqtlcel
vdemschlvlttggtgparrdvtpdatlavadrempgfgeqmrqislhfvptailsrqvg
virkqalilnlpgqpksiketlegvkdaegnvvvhgifasvpyciqllegpyvetapevv
aafrpksarr
>d1bgva2 3.53.1.1.1 (1-194) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1gtma2 3.53.1.1.2 (3-180) Glutamate dehydrogenase {Pyrococcus furiosus}
adpyeivikqleraaqymeiseealeflkrpqrivevtipvemddgsvkvftgfrvqhnw
argptkggirwhpeetlstvkalaawmtwktavmdlpygggkggiivdpkklsdrekerl
argyiraiydvispyedipapdvytnpqimawmmdeyetisrrktpafgiitgkplsi
>d1ch6a2 3.53.1.1.5 (6-208) Glutamate dehydrogenase {Bovine (Bos taurus)}
dpnffkmvegffdrgasivedklvedlktrqtqeqkrnrvrgilriikpcnhvlslsfpi
rrddgsweviegyraqhshqrtpckggirystdvsvdevkalaslmtykcavvdvpfgga
kagvkinpknytdedlekitrrftmelakkgfigpgvdvpapnmstgeremswiadtyas
tighydinahacvtgkpisqggi
>d1leha2 3.53.1.1.6 (1-134) Leucine dehydrogenase {Bacillus sphaericus}
meifkymekydyeqlvfcqdeasglkaviaihdttlgpalggarmwtynaeeeaiedalr
largmtyknaaaglnlgggktviigdpfadknedmfralgrfiqglngryitaedvgttv
ddmdlihqetdyvt
>d1bw9a2 3.53.1.1.7 (1-148) Phenylalanine dehydrogenase {Rhodococcus M4}
sidsalnwdgemtvtrfdsmtgahfvirldstqlgpaaggtraaqysnladaltdagkla
gamtlkmavsnlpmgggksvialpaprhsidpstwarilrihaenidklsgnywtgpdvn
tnsadmdtlndttefvfgrslerggags
>d1a4ia2 3.53.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1b0aa2 3.53.1.2.2 (2-122) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
aakiidgktiaqqvrsevaqkvqariaaglrapglavvlvgsnpasqiyvaskrkaceev
gfvsrsydlpettseaellelidtlnadntidgilvqlplpagidnvkvlerihpdkdvd
g
>d1qr6a2 3.53.1.3.1 (23-279) Mitochondrial NAD(P)-dependenent malic enzyme {Human (Homo sapiens)}
ekgkplxlnprtnkgxaftlqerqxlglqgllppkietqdiqalrfhrnlkkxtspleky
iyixgiqerneklfyrilqddieslxpivytptvglacsqyghifrrpkglfisisdrgh
vrsivdnwpenhvkavvvtdgerilglgdlgvygxgipvgklclytacagirpdrclpvc
idvgtdniallkdpfyxglyqkrdrtqqyddlidefxkaitdrygrntliqfedfgnhna
frflrkyrekyctfndd
>d1uag_2 3.54.1.1.1 (298-437) C-terminal domain of MurD (UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase) {Escherichia coli}
glphrfevvlehngvrwindskatnvgsteaalnglhvdgtlhlllggdgksadfsplar
ylngdnvrlycfgrdgaqlaalrpevaeqtetmeqamrllaprvqpgdmvllspacasld
qfknfeqrgnefarlakelg
>d1fgs_1 3.54.1.2.1 (297-425) Folylpolyglutamate synthetase, C-terminal domain {Lactobacillus casei}
wparlekisdtplividgahnpdginglitalkqlfsqpitviagiladkdyaamadrlt
aafstvylvpvpgtpralpeagyealhegrlkdswqealaaslndvpdqpivitgslyla
savrqtllg
>d1qhfa_ 3.55.1.1.1 Phosphoglycerate mutase {Baker's yeast (Saccharomyces cerevisiae)}
pklvlvrhgqsewneknlftgwvdvklsakgqqeaaragellkekkvypdvlytsklsra
iqtanialekadrlwipvnrswrlnerhygdlqgkdkaetlkkfgeekfntyrrsfdvpp
ppidasspfsqkgderykyvdpnvlpeteslalvidrllpywqdviakdllsgktvmiaa
hgnslrglvkhlegisdadiaklniptgiplvfeldenlkpskpsyyldpeaaaagaaav
>d2hpaa_ 3.55.1.2.2 Acid phosphatase {Human (Homo sapiens)}
kelkfvtlvfrhgdrspidtfptdpikesswpqgfgqltqlgmeqhyelgeyirkryrkf
lnesykheqvyirstdvdrtlmsamtnlaalfppegvsiwnpillwqpipvhtvplsedq
llylpfrncprfqelesetlkseefqkrlhpykdfiatlgklsglhgqdlfgiwskvydp
lycesvhnftlpswatedtmtklrelselsllslygihkqkeksrlqggvlvneilnhmk
ratqipsykklimysahdttvsglqmaldvyngllppyaschltelyfekgeyfvemyyr
netqhepyplmlpgcspscplerfaelvgpvipqdwstecmt
>d1ihp__ 3.55.1.3.1 Phytase (myo-inositol-hexakisphosphate-3-phosphohydrolase) {Aspergillus ficuum}
scdtvdqgyqcfsetshlwgqyapffslanesvispevpagcrvtfaqvlsrhgaryptd
skgkkysalieeiqqnattfdgkyaflktynyslgaddltpfgeqelvnsgikfyqryes
ltrnivpfirssgssrviasgkkfiegfqstklkdpraqpgqsspkidvviseasssnnt
ldpgtctvfedseladtveanftatfvpsirqrlendlsgvtltdtevtylmdmcsfdti
ststvdtklspfcdlfthdewinydylqslkkyyghgagnplgptqgvgyaneliarlth
spvhddtssnhtldsspatfplnstlyadfshdngiisilfalglyngtkplstttveni
tqtdgfssawtvpfasrlyvemmqcqaeqeplvrvlvndrvvplhgcpvdalgrctrdsf
vrglsfarsggdwaecfa
>d1bif_2 3.55.1.4.1 (250-468) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain {Rat (Rattus norvegicus)}
siylcrhgeselnlkgriggdpglsprgrefskhlaqfisdqnikdlkvftsqmkrtiqt
aealsvpyeqfkvlneidagvceemtyeeiqdhyplefalrdqdkyryrypkgesyedlv
qrlepvimelerqenvlvichqavmrcllayfldkaaeelpylkcplhtvlkltpvaygc
kvesiflnvaavnthrdrpqnvdisrpseealvtvpahq
>d1nula_ 3.56.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1hgxa_ 3.56.1.1.2 Hypoxantine-guanine-xanthine PRTase {Tritrichomonas foetus}
mddlervlynqddiqkrirelaaeltefyedknpvmicvltgavffytdllkhldfqlep
dyiicssysgtkstgnltiskdlktniegrhvlvvediidtgltmyqllnnlqmrkpasl
kvctlcdkdigkkaydvpidycgfvvenryiigygfdfhnkyrnlpvigilke
>d1qk3a_ 3.56.1.1.3 Hypoxantine-guanine-xanthine PRTase {Toxoplasma gondii}
maskpiedygkgkgriepmyipdntfynaddflvpphckpyidkillpgglvkdrvekla
ydihrtyfgeelhiicilkgsrgffnllidylatiqkysgressvppffehyvrlksyqn
dnstgqltvlsddlsifrdkhvlivedivdtgftltefgerlkavgpksmriatlvekrt
drsnslkgdfvgfsiedvwivgccydfnemfrdfdhvavlsdaarkkf
>d1gph11 3.56.1.1.4 (235-465) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsvdeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvkeavltk
>d1ecfa1 3.56.1.1.5 (250-492) Glutamine PRPP amidotransferase, C-terminal domain {Escherichia coli}
npclfeyvyfarpdsfidkisvysarvnmgtklgekiarewedldidvvipipetscdia
leiarilgkpyrqgfvknryvgrtfimpgqqlrrksvrrklnanraefrdknvllvddsi
vrgttseqiiemareagakkvylasaapeirfpnvygidmpsateliahgrevdeirqii
gadglifqdlndlidavraenpdiqqfecsvfngvyvtkdvdqgyldfldtlrnddakav
qrq
>d1bzya_ 3.56.1.1.6 Hypoxantine-guanine PRTase (HGPRTase) {Human (Homo sapiens)}
spgvvisddepgydldlfcipnhyaedlervfiphglimdrterlardvmkemgghhiva
lcvlkggykffadlldyikalnrnsdrsipmtvdfirlksycndqstgdikviggddlst
ltgknvlivediidtgktmqtllslvrqynpkmvkvasllvkrtprsvgykpdfvgfeip
dkfvvgyaldyneyfrdlnhvcvisetgkakyka
>d1tc1a_ 3.56.1.1.8 Hypoxanthine PRTase {(Trypanosoma cruzi)}
yefaekilfteeeirtrikevakriaddykgkglrpyvnplvlisvlkgsfmftadlcra
lcdfnvpvrmeficvssygegltssgqvrmlldtrhsieghhvlivedivdtaltlnyly
hmyftrrpaslktvvlldkregrrvpfsadyvvanipnafvigygldyddtyrelrdivv
lrpe
>d1qb7a_ 3.56.1.1.9 Adenine PRTase {Leishmania donovani}
pfkevspnsfllddshalsqllkksyrwyspvfsprnvprfadvssitespetlkairdf
lvqryramspapthilgfdargflfgpmiaveleipfvlmrkadknagllirsepyekey
keaapevmtirygsigkgsrvvliddvlatggtalsglqlveasdavvvemvsilsipfl
kaaekihstansrykdikfisllsddalteencgdsknytgprvlscgdvlaehph
>d1oroa_ 3.56.1.1.11 Orotate PRTase {Escherichia coli}
mkpyqrqfiefalskqvlkfgeftlksgrkspyffnaglfntgrdlallgrfyaealvds
giefdllfgpaykgipiatttavalaehhdldlpycfnrkeakdhgeggnlvgsalqgrv
mlvddvitagtairesmeiiqangatlagvlisldrqergrgeisaiqeverdynckvis
iitlkdliayleekpemaehlaavkayreefgv
>d1a3c__ 3.56.1.1.12 Uracil PRTase {Bacillus subtilis}
qkavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpv
tvgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalv
dvgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1bd3a_ 3.56.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1lfaa_ 3.57.1.1.1 Integrin CD11a/CD18 (Leukocyte function associated antigen-1, LFA-1) {Human (Homo sapiens)}
gnvdlvflfdgsmslqpdefqkildfmkdvmkklsntsyqfaavqfstsyktefdfsdyv
krkdpdallkhvkhmllltntfgainyvatevfreelgarpdatkvliiitdgeatdsgn
idaakdiiryiigigkhfqtkesqetlhkfaskpasefvkildtfeklkdlftelqkkiy
vie
>d1atza_ 3.57.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
qpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpwnv
vpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsvds
vdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgnsf
lhkl
>d1auq__ 3.57.1.1.3 von Willebrand factor A1 domain {Human (Homo sapiens)}
disepplhdfycsrlldlvflldgssrlseaefevlkafvvdmmerlrisqkwvrvavve
yhdgshayiglkdrkrpselrriasqvkyagsqvastsevlkytlfqifskidrpeasri
alllmasqepqrmsrnfvryvqglkkkkvivipvgigphanlkqirliekqapenkafvl
ssvdeleqqrdeivsylcdlapeapppt
>d1ido__ 3.57.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
dsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrek
>d1aoxa_ 3.57.1.1.5 Integrin alpha2-beta1 {Human (Homo sapiens)}
scpslidvvvvcdesnsiypwdavknflekfvqgldigptktqvgliqyannprvvfnln
tyktkeemivatsqtsqyggdltntfgaiqyarkyaysaasggrrsatkvmvvvtdgesh
dgsmlkavidqcnhdnilrfgiavlgylnrnaldtknlikeikaiasipteryffnvsde
aallekagtlgeqifsieggt
>d1poia_ 3.58.1.1.1 Glutaconate-CoA transferase alpha {Acidaminococcus fermentans}
skvmtlkdaiakyvhsgdhialggfttdrkpyaavfeilrqgitdltglggaaggdwdml
igngrvkayincytansgvtnvsrrfrkwfeagkltmedysqdviymmwhaaalglpflp
vtlmqgsgltdewgiskevrktldkvpddkfkyidnpfkpgekvvavpvpqvdvaiihaq
qaspdgtvriwggkfqdvdiaeaakytivtceeiisdeeirrdptkndipgmcvdavvla
pygahpsqcyglydydnpflkvydkvsktqedfdafckewvfdlkdhdeylnklgatrli
nlkvvpglgyhidmtke
>d1poib_ 3.58.1.1.2 Glutaconate-CoA transferase beta {Acidaminococcus fermentans}
dytnytnkemqavtiakqikngqvvtvgtglpligasvakrvyapdchiivesglmdcsp
vevprsvgdlrfmahcgciwpnvrfvgfeineylhkanrliafiggaqidpygnvnstsi
gdyhhpktrftgsggangiatysntiimmqhekrrfmnkidyvtspgwidgpggrerlgl
pgdvgpqlvvtdkgilkfdektkrmylaayyptsspedvlentgfdldvskaveleapdp
aviklireeidpgqafiqvp
>d1b0pa4 3.59.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d2gar__ 3.60.1.1.1 Glycinamide ribonucleotide transformylase, GART {Escherichia coli, k12 strain tx635, with plasmid pjs167}
mnivvlisgngsnlqaiidacktnkikgtvravfsnkadafglerarqagiathtliasa
fdsreaydraliheidmyapdvvvlagfmrilspafvshyagrllnihpsllpkypglht
hrqalengdeehgtsvhfvtdeldggpvilqakvpvfagdsedditarvqtqehaiyplv
iswfadgrlkmhenaawldgqrlppqgya
>d1fmta2 3.60.1.1.2 (1-206) Methionyl-tRNAfmet formyltransferase {Escherichia coli}
seslriifagtpdfaarhldallssghnvvgvftqpdrpagrgkklmpspvkvlaeekgl
pvfqpvslrpqenqqlvaelqadvmvvvayglilpkavlemprlgcinvhgsllprwrga
apiqrslwagdaetgvtimqmdvgldtgdmlyklscpitaedtsgtlydklaelgpqgli
ttlkqladgtakpevqdetlvtyaek
>d1vid__ 3.61.1.1.1 Catechol O-methyltransferase, COMT {Rat (Rattus norvegicus)}
tkeqrilryvqqnakpgdpqsvleaidtyctqkewamnvgdakgqimdavireyspslvl
elgaycgysavrmarllqpgarlltmemnpdyaaitqqmlnfaglqdkvtilngasqdli
pqlkkkydvdtldmvfldhwkdrylpdtlllekcgllrkgtvlladnvivpgtpdflayv
rgsssfecthyssyleymkvvdglekaiyqgps
>d1xvaa_ 3.61.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1af7_2 3.61.1.3.1 (92-284) Chemotaxis receptor methyltransferase CheR, C-terminal domain {Salmonella typhimurium}
nltaffreahhfpilaeharrrhgeyrvwsaaastgeepysiaitladalgmapgrwkvf
asdidtevlekarsgiyrlselktlspqqlqryfmrgtgpheglvrvrqelanyvefssv
nllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvpllkpdgllfaghsenfsnlvr
efslrgqtvyals
>d3mag__ 3.61.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrspkrggnestadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d2erca_ 3.61.1.4.3 rRNA methyltransferase {Bacillus subtilis, Ermc'}
qnfitskhnidkimtnirlnehdnifeigsgkghftlelvqrcnfvtaieidhklcktte
nklvdhdnfqvlnkdilqfkfpknqsykifgnipynistdiirkivfdsiadeiylivey
gfakrllntkrslalflmaevdisilsmvpreyfhpkpkvnsslirlnrkksrishkdkq
kynyfvmkwvnkeykkiftknqfnnslkhagiddlnnisfeqflslfnsyklfnk
>d6mhta_ 3.61.1.5.1 DNA methylase HhaI, coenzyme-binding domain {Haemophilus haemolyticus}
mieikdkqltglrfidlfaglggfrlalescgaecvysnewdkyaqevyemnfgekpegd
itqvnektipdhdilcagfpcqafsisgkqkgfedsrgtlffdiarivrekkpkvvfmen
vknfashdngntlevvkntmneldysfhakvlnaldygipqkreriymicfrndlniqnf
qfpkpfelntfvkdlllpdsevehlvidrkdlvmtnqeieqttpktvrlgivgkggqger
iystrgiaitlsaygggifaktggylvngktrklhprecarvmgypdsykvhpstsqayk
qfgnsvvinvlqyiaynigsslnfkpy
>d2adma_ 3.61.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1dcta_ 3.61.1.5.3 DNA methylase HaeIII, coenzyme-binding domain {Haemophilus aegyptius}
mnlislfsgaggldlgfqkagfriicaneydksiwktyesnhsaklikgdiskissdefp
kcdgiiggppcqswseggslrgiddprgklfyeyirilkqkkpifflaenvkgmmaqrhn
kavqefiqefdnagydvhiillnandygvaqdrkrvfyigfrkelninylppiphlikpt
fkdviwdlkdnpipaldknktngnkciypnheyfigsystifmsrnrvrqwnepaftvqa
sgrqcqlhpqapvmlkvsknlnkfvegkehlyrrltvrecarvqgfpddfifhyeslndg
ykmignavpvnlayeiaktiksal
>d2dpma_ 3.61.1.5.4 DpnM DNA adenine methyltransferase {Streptococcus pneumoniae}
tlqpftkwtggkrqllpvirelipktynryfepfvgggalffdlapkdavindfnaelin
cyqqikdnpqelieilkvhqeynskeyyldlrsadrderidmmsevqraarilymlrvnf
nglyrvnsknqfnvpygryknpkivdeelisaisvyinnnqleikvgdfekaivdvrtgd
fvyfdppyiplsetsaftsythegfsfadqvrlrdafkrlsdtgayvmlsnsssalveel
ykdfnihyveatrtngaksssrgkiseiivtnyek
>d1booa_ 3.61.1.6.1 PvuII DNA methyltransferase {Proteus vulgaris}
nfgkkpayttsngsmyigdslellesfpeesislvmtsppfalqrkkeygnleqheyvdw
flsfakvvnkklkpdgsfvvdfggaymkgvparsiynfrvlirmidevgfflaedfywfn
psklpspiewvnkrkirvkdavntvwwfsktewpksditkvlapysdrmkkliedpdkfy
tpktrpsghdigksfskdnggsippnllqisnsesngqylancklmgikahparfpaklp
effirmltepddlvvdifggsnttglvaeresrkwisfemkpeyvaasafrfldnnisee
kitdiynrilngesldlnsi
>d1ajsa_ 3.62.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsknfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1bjwa_ 3.62.1.1.6 Aspartate aminotransferase, AAT {Thermus thermophilus}
mrglsrrvqamkpsatvavnakalelrrqgvdlvaltagepdfdtpehvkeaarralaqg
ktkyappagipelrealaekfrrenglsvtpeetivtvggkqalfnlfqaildpgdeviv
lspywvsypemvrfaggvvvevetlpeegfvpdpervrraitprtkalvvnspnnptgav
ypkevlealarlavehdfylvsdeiyehllyegehfspgrvapehtltvngaaxafamtg
wrigyacgpkevikamasvssqsttspdtiaqwatlealtnqeasrafvemareayrrrr
dlllegltalglkavrpsgafyvlmdtspiapdevraaerlleagvavvpgtdfaafghv
rlsyatseenlrkalerfarvl
>d1bw0a_ 3.62.1.1.9 Tyrosine aminotransferase (TAT) {Trypanosoma cruzi}
wdvsmsnhaglvfnpirtvsdnakpspspkpiiklsvgdptldknlltsaaqikklkeai
dsqecngyfptvgspeareavatwwrnsfvhkeelkstivkdnvvlcsggshgilmaita
icdagdyalvpqpgfphyetvckaygigmhfyncrpendweadldeirrlkddktklliv
tnpsnpcgsnfsrkhvedivrlaeelrlplfsdeiyagmvfkgkdpnatftsvadfettv
prvilggtaxnlvvpgwrlgwllyvdphgngpsfleglkrvgmlvcgpctvvqaalgeal
lntpqehldqivakieesamylynhigeciglaptmprgamylmsridlekyrdiktdve
ffeklleeenvqvlpgtifhapgftrltttrpvevyreaverikafcqrhaa
>d1ax4a_ 3.62.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1cl1a_ 3.62.1.3.1 Cystathionine beta-lyase, CBL {Escherichia coli}
kldtqlvnagrskkytlgavnsviqrasslvfdsveakkhatrnrangelfygrrgtlth
fslqqamceleggagcvlfpcgaaavansilafieqgdhvlmtntayepsqdfcskilsk
lgvttswfdpligadivkhlqpntkivflespgsitmevhdvpaivaavrsvvpdaiimi
dntwaagvlfkaldfgidvsiqaatxylvghsdamigtavcnarcweqlrenaylmgqmv
dadtayitsrglrtlgvrlrqhhesslkvaewlaehpqvarvnhpalpgskghefwkrdf
tgssglfsfvlkkklnneelanyldnfslfsmayswggyeslilanqpehiaairpqgei
dfsgtlirlhigledvddliadldagfariv
>d1cs1a_ 3.62.1.3.2 Cystathionine gamma-synthase {Escherichia coli}
rkqatiavrsglnddeqygcvvppihlsstynftgfneprahdysrrgnptrdvvqrala
eleggagavltntgmsaihlvttvflkpgdllvaphdcyggsyrlfdslakrgcyrvlfv
dqgdeqalraalaekpklvlvespsnpllrvvdiakichlarevgavsvvdntflspalq
nplalgadlvlhsctxylnghsdvvagvviakdpdvvtelawwannigvtggafdsylll
rglrtlvprmelaqrnaqaivkylqtqplvkklyhpslpenqgheiaarqqkgfgamlsf
eldgdeqtlrrflgglslftlaeslggveslishaatmthagmapearaaagisetllri
stgiedgedliadlengfraankg
>d1d2fa_ 3.62.1.3.3 Modulator in mal gene expression, MalY {Escherichia coli}
llpftisdmdfatapciiealnqrlmhgvfgysrwkndeflaaiahwfstqhytaidsqt
vvygpsviymvselirqwsetgegvvihtpaydafykaiegnqrtvmpvalekqadgwfc
dmgkleavlakpeckimllcspqnptgkvwtcdeleimadlcerhgvrvisdeihmdmvw
geqphipwsnvargdwalltsgsksfnipaltgaygiiensssrdaylsalkgrdglssp
svlaltahiaayqqgapwldalriylkdnltyiadkmnaafpelnwqipqstylawldlr
plniddnalqkalieqekvaimpgytygeegrgfvrlnagcprsklekgvaglinairav
r
>d2dkb__ 3.62.1.4.1 Dialkylglycine decarboxylase {Pseudomonas cepacia}
lnddatfwrnarhhlvryggtfepmiierakgsfvydadgraildftsgqmsavlghchp
eivsvigeyagkldhlfsemlsrpvvdlatrlanitppgldralllstgaesneaairma
klvtgkyeivgfaqswhgmtgaaasatysagrkgvgpaavgsfaipapftyrprfernga
ydylaeldyafdlidrqssgnlaafiaepilssggiielpdgymaalkrkceargmllil
deaqtgvgrtgtmfacqrdgvtpdiltlsktlgaglplaaivtsaaieerahelgylfyt
thvsdplpaavglrvldvvqrdglvaranvmgdrlrrglldlmerfdcigdvrgrglllg
veivkdrrtkepadglgakitrecmnlglsmnivqlpgmggvfriappltvsedeidlgl
sllgqaieral
>d2gsaa_ 3.62.1.4.2 Glutamate-1-semialdehyde aminomutase (aminotransferase) {Synechococcus strain GR6}
fktiksdeifaaaqklmpggvsspvrafksvggqpivfdrvkdayawdvdgnryidyvgt
wgpaicghahpeviealkvamekgtsfgapcalenvlaemvndavpsiemvrfvnsgtea
cmavlrlmraytgrdkiikfegcyhghadmflvkagsgvatlglpsspgvpkkttantlt
tpyndleavkalfaenpgeiagvilepivgnsgfivpdagfleglreitlehdallvfde
vmtgfriayggvqekfgvtpdlttlgkiiggglpvgayggkreimqlvapagpmyqagtl
sgnplamtagiktlellrqpgtyeyldqitkrlsdgllaiaqetghaacggqvsgmfgff
ftegpvhnyedakksdlqkfsrfhrgmleqgiylapsqfeagftslahteedidatlaaa
rtvmsal
>d2oata_ 3.62.1.4.3 Ornithine aminotransferase {Human (Homo sapiens)}
gpptsddifereykygahnyhplpvalergkgiylwdvegrkyfdflssysavnqghchp
kivnalksqvdkltltsrafynnvlgeyeeyitklfnyhkvlpmntgveagetacklark
wgytvkgiqkykakivfaagnfwgrtlsaissstdptsydgfgpfmpgfdiipyndlpal
eralqdpnvaafmvepiqgeagvvvpdpgylmgvrelctrhqvlfiadeiqtglartgrw
lavdyenvrpdivllgkalsgglypvsavlcdddimltikpgehgstyggnplgcrvaia
alevleeenlaenadklgiilrnelmklpsdvvtavrgkgllnaiviketkdwdawkvcl
rlrdngllakpthgdiirfapplvikedelresieiinktilsf
>d1gtxa_ 3.62.1.4.4 4-aminobutyrate aminotransferase, GABA-aminotransferase {Pig (Sus scrofa)}
fdydgplmktevpgprsrelmkqlniiqnaeavhffcnyeesrgnylvdvdgnrmldlys
qissipigyshpalvklvqqpqnvstfinrpalgilppenfveklresllsvapkgmsql
itmacgscsnenafktifmwyrskergqsafskeeletcminqapgcpdysilsfmgafh
grtmgclatthskaihkidipsfdwpiapfprlkypleefvkenqqeearcleevedliv
kyrkkkktvagiivepiqseggdnhasddffrklrdisrkhgcaflvdevqtgggstgkf
wahehwglddaadvmtfskkmmtggffhkeefrpnapyrifntwlgdpsknlllaevini
ikredllsnaahagkvlltglldlqarypqfisrvrgrgtfcsfdtpdesirnklisiar
nkgvmlggcgdksirfrptlvfrdhhahlflnifsdiladfk
>d1bjna_ 3.62.1.4.6 Phosphoserine aminotransferase, PSAT {Escherichia coli}
qifnfssgpamlpaevlkqaqqelrdwnglgtsvmevshrgkefiqvaeeaekdfrdlln
vpsnykvlfchgggrgqfaavplnilgdkttadyvdagywaasaikeakkyctpnvfdak
vtvdglravkpmrewqlsdnaaymhycpnetidgiaidetpdfgadvvvaadfsstilsr
pidvsrygviyagaqxnigpagltivivredllgkaniacpsildysilndngsmfntpp
tfawylsglvfkwlkanggvaemdkinqqkaellygvidnsdfyrndvakrnrsrmnvpf
qladsaldklfleesfaaglhalkghrvvggmrasiynamplegvkaltdfmveferrhg
>d1dfoa_ 3.62.1.4.9 Serine hydroxymethyltransferase {Escherichia coli}
lkremniadydaelwqameqekvrqeehieliasenytsprvmqaqgsqltnkyaegypg
kryyggceyvdiveqlaidrakelfgadyanvqphsgsqanfavytallepgdtvlgmnl
ahgghlthgspvnfsgklynivpygidatghidyadlekqakehkpkmiiggfsaysgvv
dwakmreiadsigaylfvdmahvaglvaagvypnpvphahvvtttthktlagprgglila
kggseelykklnsavfpggqggplmhviagkavalkeamepefktyqqqvaknakamvev
flergykvvsggtdnhlflvdlvdknltgkeadaalgranitvnknsvpndpkspfvtsg
irvgtpaitrrgfkeaeakelagwmcdvldsindeavierikgkvldicarypvya
>d1b9ha_ 3.62.1.4.10 3-amino-5-hydroxybenzoic acid synthase (AHBA synthase) {Amycolatopsis mediterranei}
kapefpawpqyddaernglvraleqgqwwrmggdevnsferefaahhgaahalavtngth
alelalqvmgvgpgtevivpaftfisssqaaqrlgavtvpvdvdaatynldpeavaaavt
prtkvimpvhmaglmadmdalakisadtgvpllqdaahahgarwqgkrvgeldsiatfsf
qngklmtageggavvfpdgetekyetaflrhscgrprddrryfhkiagsnmrlnefsasv
lraqlarldeqiavrderwtllsrllgaidgvvpqggdvradrnshymamfripglteer
rnalvdrlveaglpafaafraiyrtdafwelgapdesvdaiarrcpntdaissdcvwlhh
rvllagepelhataeiiadavara
>d1bs0a_ 3.62.1.4.11 PLP-dependent acyl-CoA synthase (8-amino-7-oxonanoate synthase, AONS) {Escherichia coli}
swqekinaaldarraadalrrrypvaqgagrwlvaddrqylnfssndylglshhpqiira
wqqgaeqfgigsggsghvsgysvvhqaleeelaewlgysrallfisgfaanqaviaamma
kedriaadrlshaslleaaslspsqlrrfahndvthlarllaspcpgqqmvvtegvfsmd
gdsaplaeiqqvtqqhngwlmvddahgtgvigeqgrgscwlqkvkpellvvtfgkgfgvs
gaavlcsstvadyllqfarhliystsmppaqaqalraslavirsdegdarreklaalitr
fragvqdlpftladscsaiqplivgdnsralqlaeklrqqgcwvtairpptvpagtarlr
ltltaahemqdidrllevlhgng
>d1dtya_ 3.62.1.4.12 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {Escherichia coli}
mttddlafderhiwhpytsmtsplpvypvvsaegcelilsdgrrlvdgmsswwaaihgyn
hpqlnaamksqidamshvmfgeithapaielcrklvamtpqplecvfladsgsvavevam
kmalqywdakgeardrfltfrngyhgdtfgamsvcdpdnsmhslwkgylpenlfapapqs
rmdgewderdmvgfarlmaahrheiaaviiepivqgaggmrmyhpewlkrirkicdregi
lliadeiatgfgrtgklfacehaeiapdilclgkaltggtmtlsatlttrevaetisdge
agcfmhgptfmgnplacaaanaslailesgdwqqqvadievqlreqlapardaemvadvr
vlgaigvvetthpvnmaalqkffveqgvwirpfgkliylmppyiilpqqlqrltaavnra
vqdetffcq
>d1b8ga_ 3.62.1.4.13 1-aminocyclopropane-1-carboxylate synthase (ACC synthase) {Apple (Malus domestica)}
mlsrnatfnshgqdssyflgwqeyeknpyhevhntngiiqmglaenqlcfdlleswlakn
peaaafkkngesifaelalfqdyhglpafkkamvdfmaeirgnkvtfdpnhlvltagats
anetfifcladpgeavliptpyypgfdrdlkwrtgveivpihctssngfqitetaleeay
qeaekrnlrvkgvlvtnpsnplgttmtrnelylllsfvedkgihlisdeiysgtafssps
fisvmevlkdrncdensevwqrvhvvyslskdlglpgfrvgaiysnddmvvaaatkmssf
glvssqtqhllsamlsdkkltknyiaenhkrlkqrqkklvsglqksgisclngnaglfcw
vdmrhllrsntfeaemelwkkivyevhlnispgsschctepgwfrvcfanlpertldlam
qrlkafvg
>d1orda2 3.62.1.5.1 (108-569) Ornithine decarboxylase major domain {Lactobacillus strain 30a}
ppffkslkeyvsrgliqfdcpghqggqyyrkhpagrefydffgetvfradlcnadvalgd
llihegpavaaekhaarvynadktyfvlggssnanntvtsalvsngdlvlfdrnnhksvy
nsalamaggrpvylqtnrnpygfiggiydsdfdekkirelaakvdperakwkrpfrlavi
qlgtydgtiynahevvkrighlcdyiefdsawvgyeqfipmmrnssplliddlgpedpgi
ivvqsvhkqqagfsqtsqihkkdshikgqlrycdhkhfnnsfnlfmstspfypmyaaldv
naamqegeagrklwhdllittiearkklikagsmfrpfvppvvngkkwedgdtedmanni
dywrfekgakwhayegygdnqyyvdpnkfmlttpginpetgdyedfgvpativanylrdh
giipeksdlnsilflmtpaetpakmnnlitqllqlqrlieed
>d1gpma2 3.63.1.1.1 (3-207) GMP synthetase {Escherichia coli}
enihkhrilildfgsqytqlvarrvrelgvycelwawdvteaqirdfnpsgiilsggpes
tteensprapqyvfeagvpvfgvcygmqtmamqlgghveasnerefgyaqvevvndsalv
rgiedaltadgkplldvwmshgdkvtaipsdfitvastescpfaimaneekrfygvqfhp
evthtrqgmrmlerfvrdicqceal
>d1a9xb2 3.63.1.1.2 (1653-1880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1qdlb_ 3.63.1.1.3 Anthranilate synthase GAT subunit TrpG {Sulfolobus solfataricus}
mdltliidnydsfvyniaqivgelgsypivirndeisikgieridpdrliispgpgtpek
redigvsldvikylgkrtpilgvclghqaigyafgakirrarkvfhgkisniilvnnspl
slyygiakefkatryhslvvdevhrplivdaisaedneimaihheeypiygvqfhpesvg
tslgykilynflnrv
>d2bce__ 3.64.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsvdifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptvtsagasll
ppednsqaspvppadnsgaptepsagdsevaqmpvvigf
>d1qe3a_ 3.64.1.1.5 Thermophylic para-nitrobenzyl esterase (PNB esterase) {Bacillus subtilis}
thqivttqygkvkgttengvhkwkgipyakppvgqwrfkapeppevwedvldataygpic
pqpsdllslsytelprqsedclyvnvfapdtpsqnlpvmvwihggafylgagseplydgs
klaaqgevivvtlnyrlgpfgflhlssfdeaysdnlglldqaaalkwvrenisafggdpd
nvtvfgesaggmsiaallampaakglfqkaimesgasrtmtkeqaastaaaflqvlgine
sqldrlhtvaaedllkaadqlriaekenifqlffqpaldpktlpeepeksiaegaasgip
lligttrdegylfftpdsdvhsqetldaaleyllgkplaekaadlyprslesqihmmtdl
lfwrpavayasaqshyapvwmyrfdwhpekppynkafhalelpfvfgnldglermakaei
tdevkqlshtiqsawitfaktgnpsteavnwpayheetretvildseitiendpesekrq
klf
>d1jkma_ 3.64.1.2.1 Brefeldin A esterase {Bacillus subtilis}
pgrlgdessgprtdprfspamvealatfgldavaaappvsasddlptvlaavgashdgfq
avydsialdlptdrddvetstetilgvdgneitlhvfrpagvegvlpglvythgggmtil
ttdnrvhrrwctdlaaagsvvvmvdfrnawtaeghhpfpsgvedclaavlwvdehreslg
lsgvvvqgesgggnlaiattllakrrgrldaidgvyasipyisggyawdherrltelpsl
vendgyfienggmallvraydptgehaedpiawpyfasedelrglppfvvavneldplrd
egiafarrlaragvdvaarvniglvhgadvifrhwlpaalestvrdvagfaadrarlr
>d1qfma2 3.64.1.3.1 (431-710) Prolyl oligopeptidase, C-terminal domain {Porcine}
dasdyqtvqifypskdgtkipmfivhkkgikldgshpaflygyggfnisitpnysvsrli
fvrhmggvlavanirgggeygetwhkggilankqncfddfqcaaeylikegytspkrlti
nggsnggllvatcanqrpdlfgcviaqvgvmdmlkfhkytighawttdygxsdskqhfew
likysplhnvklpeaddiqypsmllltadhddrvvplhslkfiatlqyivgrsrkqnnpl
lihvdtkaghgagkptakvieevsdmfafiarclnidwip
>e1wht.1a 3.64.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
ghaadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpg
cssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiyts
gdnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgf
mvgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvatae
qgnidmyslytpvcni
>e1wht.1b 3.64.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpgq
>d1cpy__ 3.64.1.4.2 Serine carboxypeptidase II {Baker's yeast (Saccharomyces cerevisiae)}
kikdpkilgidpnvtqytgyldvededkhfffwtfesrndpakdpvilwlnggpgcsslt
glffalgpssigpdlkpignpyswnsnatvifldqpvnvgfsysgssgvsntvaagkdvy
nflelffdqfpeyvnkgqdfhiagasyaghyipvfaseilshkdrnfnltsvligngltd
pltqynyyepmacgeggepsvlpseecsamedslerclgliescydsqsvwscvpatiyc
nnaqlapyqrtgrnvydirkdceggnlcyptlqdiddylnqdyvkeavgaevdhyescnf
dinrnflfagdwmkpyhtavtdllnqdlpilvyagdkdficnwlgnkawtdvlpwkydee
fasqkvrnwtasitdevagevksykhftylrvfngghmvpfdvpenalsmvnewihggfs
l
>d1ac5__ 3.64.1.4.3 Serine carboxypeptidase II {Baker's yeast (Saccharomyces cerevisiae), kex1(delta)p}
lpsseeykvayellpglsevpdpsnipqmhaghiplrsedadeqdssdleyffwkftnnd
sngnvdrpliiwlnggpgcssmdgalvesgpfrvnsdgklylnegswiskgdllfidqpt
gtgfsveqnkdegkidknkfdedledvtkhfmdflenyfkifpedltrkiilsgesyagq
yipffanailnhnkfskidgdtydlkalligngwidpntqslsylpfamekklidesnpn
fkhltnahencqnlinsastdeaahfsyqecenilnlllsytressqkgtadclnmynfn
lkdsypscgmnwpkdisfvskffstpgvidslhldsdkidhwkectnsvgtklsnpiskp
sihllpgllesgieivlfngdkdlicnnkgvldtidnlkwggikgfsddavsfdwihksk
stddseefsgyvkydrnltfvsvynashmvpfdkslvsrgivdiysndvmiidnngknvm
itt
>d1ivya_ 3.64.1.4.4 Human 'protective protein', HPP {Homo sapiens}
apdqdeiqrlpglakqpsfrqysgylkssgskhlhywfvesqkdpenspvvlwlnggpgc
ssldglltehgpflvqpdgvtleynpyswnlianvlylespagvgfsysddkfyatndte
vaqsnfealqdffrlfpeyknnklfltgesyagiyiptlavlvmqdpsmnlqglavgngl
ssyeqndnslvyfayyhgllgnrlwsslqthccsqnkcnfydnkdlecvtnlqevarivg
nsglniynlyapcaggvpshfryekdtvvvqdlgniftrlplkrmwhqallrsgdkvrmd
ppctnttaastylnnpyvrkalnipeqlpqwdmcnflvnlqyrrlyrsmnsqylkllssq
kyqillyngdvdmacnfmgdewfvdslnqkmevqrrpwlvkygdsgeqiagfvkefshia
fltikgaghmvptdkplaaftmfsrflnkqpy
>d1qtra_ 3.64.1.5.2 Proline iminopeptidase {Serratia marcescens}
lrglypplaaydsgwldtgdghriywelsgnpngkpavfihggpgggisphhrqlfdper
ykvllfdqrgcgrsrphasldnnttwhlvadierlremagveqwlvfggswgstlalaya
qthpervsemvlrgiftlrkqrlhwyyqdgasrffpekwervlsilsdderkdviaayrq
rltsadpqvqleaaklwsvwegetvtllpsresasfgeddfalafarienhyfthlgfle
sddqllrnvplirhipavivhgrydmacqvqnawdlakawpeaelhivegaghsydepgi
lhqlmiatdrfagk
>d1b6g__ 3.64.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaxlmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqaxidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1bn7a_ 3.64.1.6.2 Haloalkane dehalogenase {Rhodococcus sp.}
igtgfpfdphyvevlgermhyvdvgprdgtpvlflhgnptssylwrniiphvapshrcia
pdligmgksdkpdldyffddhvryldafiealgleevvlvihdwgsalgfhwakrnperv
kgiacmefirpiptwdewpefaretfqafrtadvgreliidqnafiegvlpkcvvrplte
vemdhyrepflkpvdreplwrfpneipiagepanivalveaymnwlhqspvpkllfwgtp
gvlippaeaarlaeslpncktvdigpglhylqednpdligseiarwlpgla
>d1din__ 3.64.1.7.1 Dienelactone hydrolase {Pseudomonas B13}
mltegisiqsydghtfgalvgspakapapviviaqeifgvnafmretvswlvdqgyaavc
pdlyarqapgtaldpqderqreqayklwqafdmeagvgdleaairyarhqpysngkvglv
gyxlggalaflvaakgyvdravgyygvglekqlnkvpevkhpalfhmggqdhfvpapsrq
litegfganpllqvhwyeeaghsfartsssgyvasaaalanertldflaplqs
>d1c4xa_ 3.64.1.8.1 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (BPHD) {Rhodococcus sp. strain rha1}
tveiiekrfpsgtlashalvagdpqspavvllhgagpgahaasnwrpiipdlaenffvva
pdligfgqseypetypghimswvgmrveqilglmnhfgiekshivgnsmggavtlqlvve
aperfdkvalmgsvgapmnarppelarllafyadprltpyrelihsfvydpenfpgmeei
vksrfevandpevrriqevmfesmkagmeslvippatlgrlphdvlvfhgrqdrivpldt
slyltkhlkhaelvvldrcghwaqlerwdamgpmlmehfra
>d1cr6a2 3.64.1.9.1 (226-544) Mammalian epoxide hydrolase, C-terminal domain {Mouse (Mus musculus)}
lpvpcnpndvshgyvtvkpgirlhfvemgsgpalclchgfpeswfswryqipalaqagfr
vlaidmkgygdsssppeieeyamellckemvtfldklgipqavfighdwagvmvwnmalf
ypervravaslntpfmppdpdvspmkvirsipvfnyqlyfqepgvaeaeleknmsrtfks
ffrasdetgfiavhkateiggilvntpedpnlskitteeeiefyiqqfkktgfrgplnwy
rnternwkwsckglgrkilvpalmvtaekdivlrpemsknmekwipflkrghiedcghwt
qiekptevnqilikwlqte
>d1ehya_ 3.64.1.9.2 Bacterial epoxide hydrolase {(Agrobacterium radiobacter)}
airrpedfkhyevqlpdvkihyvregagptllllhgwpgfwwewskvigplaehydvivp
dlrgfgdsekpdlndlskysldkaaddqaalldalgiekayvvghdfaaivlhkfirkys
drvikaaifdpiqpdfgpvyfglghvheswysqfhqldmavevvgssrevckkyfkhffd
hwsyrdellteeelevhvdncmkpdnihggfnyyranirpdaalwtdldhtmsdlpvtmi
wglgdtcvpyapliefvpkyysnytmetiedcghflmvekpeiaidriktafr
>d1qo7a_ 3.64.1.9.3 Bacterial epoxide hydrolase {Aspergillus niger}
kafakfpssasispnpftvsipdeqlddlktlvrlskiapptyeslqadgrfgitsewlt
tmrekwlsefdwrpfearlnsfpqftteiegltihfaalfseredavpiallhgwpgsfv
efypilqlfreeytpetlpfhlvvpslpgytfssgppldkdfglmdnarvvdqlmkdlgf
gsgyiiqggdigsfvgrllgvgfdackavhlnlcamrappegpsieslsaaekegiarme
kfmtdglayamehstrpstighvlssspiallawigekylqwvdkplpsetilemvslyw
ltesfpraihtyrettptasapngatmlqkelyihkpfgfsffpkdlcpvprswiattgn
lvffrdhaegghfaalerprelktdltafveqvw
>d1brt__ 3.64.1.10.1 Bromoperoxidase A2 {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgtgqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfstgtgevaryvssygtariakva
flaslepfllktddnpdgaapqeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a88a_ 3.64.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1thta_ 3.64.1.11.1 Myristoyl-ACP-specific thioesterase {Vibrio harveyi}
qcktiahvlrvnngqelhvwetppkenvpfknntiliasgfarrmdhfaglaeylstngf
hvfrydslhhvglssgsideftmttgknslctvyhwlqtkgtqnigliaaslsarvayev
isdlelsflitavgvvnlrdtlekalgfdylslpidelpndldfeghklgsevfvrdcfe
hhwdtldstldkvantsvpliaftannddwvkqeevydmlahirtghcklysllgsshdl
genlvvlrnfyqsvtkaaiamdggsleidvdfiepdfeqltiatvnerrlkaeienrtpe
ma
>d1auoa_ 3.64.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1qlwa_ 3.64.1.12.2 A novel bacterial esterase {Alcaligenes sp.}
vpktpagpltlsgqgsffvggrdvtsetlslspkydahgtvtvdqmyvryqipqrakryp
itlihgccltgmtwettpdgrmgwdeyflrkgystyvidqsgrgrsatdisainavklgk
apasslpdlfaagheaawaifrfgprypdafkdtqfpvqaqaelwqqmvpdwlgsmptpn
ptvanlsklaikldgtvllshsqsgiypfqtaamnpkgitaivsvepgecpkpedvkplt
sipvlvvfgdhieefprwaprlkachafidalnaaggkgqlmslpalgvhgnshmmmqdr
nnlqvadlildwigrnta
>d1jfra_ 3.64.1.13.1 Lipase {Streptomyces exfoliatus}
npyergpaptnasieasrgpyatsqtsvsslvasgfgggtiyyptstadgtfgavvispg
ftayqssiawlgprlasqgfvvftidtnttldqpdsrgrqllsaldyltqrssvrtrvda
trlgvmghsmggggsleaaksrtslkaaipltgwntdktwpelrtptlvvgadgdtvapv
athskpfyeslpgsldkaylelrgashftpntsdttiakysiswlkrfidsdtryeqflc
piprpsltiaeyrgtcphts
>d1tca__ 3.64.1.14.1 Triacylglycerol lipase {Yeast (Candida antarctica), form b}
lpsgsdpafsqpksvldagltcqgaspssvskpillvpgtgttgpqsfdsnwiplstqlg
ytpcwispppfmlndtqvnteymvnaitalyagsgnnklpvltwsqgglvaqwgltffps
irskvdrlmafapdykgtvlagpldalavsapsvwqqttgsalttalrnaggltqivptt
nlysatdeivqpqvsnspldssylfngknvqaqavcgplfvidhagsltsqfsyvvgrsa
lrsttgqarsadygitdcnplpandltpeqkvaaaallapaaaaivagpkqncepdlmpy
arpfavgkrtcsgivtp
>d3tgl__ 3.64.1.14.2 Triacylglycerol lipase {Rhizomucor miehei}
giraatsqeineltyyttlsansycrtvipgatwdcihcdatedlkiiktwstliydtna
mvargdsektiyivfrgsssirnwiadltfvpvsyppvsgtkvhkgfldsygevqnelva
tvldqfkqypsykvavtghslggatvllcaldlyqreeglsssnlflytqgqprvgdpaf
anyvvstgipyrrtvnerdivphlppaafgflhageeywitdnspetvqvctsdletsdc
snsivpftsvldhlsyfgintglct
>d1tib__ 3.64.1.14.4 Triacylglycerol lipase {Humicola lanuginosa}
evsqdlfnqfnlfaqysaaaycgknndapagtnitctgnacpevekadatflysfedsgv
gdvtgflaldntnklivlsfrgsrsienwignlnfdlkeindicsgcrghdgftsswrsv
adtlrqkvedavrehpdyrvvftghslggalatvagadlrgngydidvfsygaprvgnra
faefltvqtggtlyrithtndivprlpprefgyshsspeywiksgtlvpvtrndivkieg
idatggnnqpnipdipahlwyfgligtcl
>d1thg__ 3.64.1.14.7 Type-B carboxylesterase/lipase {Fungus (Geotrichum candidum), ATCC 34614}
xaptavlngnevisgvlegkvdtfkgipfadpplndlrfkhpqpftgsyqglkandfspa
cmqldpgnsltlldkalglakvipeefrgplydmakgtvsmnedclylnvfrpagtkpda
klpvmvwiyggafvygssaaypgnsyvkesinmgqpvvfvsinyrtgpfgflggdaitae
gntnaglhdqrkglewvsdnianfggdpdkvmifgesagamsvahqliayggdntyngkk
lfhsailqsggplpyhdsssvgpdisynrfaqyagcdtsasandtleclrsksssvlhda
qnsydlkdlfgllpqflgfgprpdgniipdaayelfrsgryakvpyisgnqedegtafap
valnatttphvkkwlqyifydaseasidrvlslypqtlsvgspfrtgilnaltpqfkrva
ailsdmlfqsprrvmlsatkdvnrwtylsthlhnlvpflgtfhgnelifqfnvnigpans
ylryfisfanhhdpnvgtnllqwdqytdegkemleihmtdnvmrtddyriegisnfetdv
nlyg
>e1qge.1e 3.64.1.15.1 Lipase {Pseudomonas Glumae, also known as Pseudomonas gladioli}
vvgatdtstgtldvanvtdpstlallatgavminrasgqndglvsrcsslfgqvistsyh
wnhldeinqllgvrganaedpvavirthvnrlklqgv
>d1cvl__ 3.64.1.15.4 Lipase {Chromobacterium viscosum}
adtyaatrypvilvhglagtdkfanvvdywygiqsdlqshgakvyvanlsgfqsddgpng
rgeqllayvkqvlaatgatkvnlighsqggltsryvaavapqlvasvttigtphrgsefa
dfvqdvlktdptglsstviaafvnvfgtlvssshntdqdalaalrtlttaqtatynrnfp
saglgapgscqtgaatetvggsqhllyswggtaiqptstvlgvtgatdtstgtldvanvt
dpstlallatgavminrasgqndglvsrcsslfgqvistsyhwnhldeinqllgvrgana
edpvavirthvnrlklqgv
>d1bu8a2 3.64.1.16.6 (1-336) Pancreatic lipase, N-terminal domain {Rat (Rattus norvegicus)}
kevcyghlgcfsndkpwagmlqrplkifpwspedidtrfllytnenpnnyqkisatepdt
ikfsnfqldrktrfivhgfidkgedgwlldmckkmfqvekvncicvdwrrgsrteytqas
yntrvvgaeiaflvqvlstemgyspenvhlighslgahvvgeagrrleghvgritgldpa
epcfqglpeevrldpsdamfvdvihtdsapiipylgfgmsqkvghldffpnggkempgcq
knilstivdingiwegtqnfvacnhlrsykyyassilnpdgflgypcssyekfqqndcfp
cpeegcpkmghyadqfegktatveqtvylntgdsgnft
>d1qj4a_ 3.64.1.17.1 Hydroxynitrile lyase {Rubber tree (Hevea brasiliensis)}
afahfvlihtichgawiwhklkpllealghkvtaldlaasgvdprqieeigsfdeysepl
ltflealppgekvilvgescgglniaiaadkycekiaaavfhnsvlpdtehcpsyvvdkl
mevfpdwkdttyftytkdgkeitglklgftllrenlytlcgpeeyelakmltrkgslfqn
ilakrpfftkegygsikkiyvwtdqdeiflpefqlwqienykpdkvykveggdhklqltk
tkeiaeilqevadtyn
>d2masa_ 3.65.1.1.1 Inosine-uridine nucleoside N-ribohydrolase, IU-NH {Crithidia fasciculata}
akkiildcdpglddavaillahgnpeiellaittvvgnqtlakvtrnaqlvadiagitgv
piaagcdkplvrkimtaghihgesgmgtvaypaefknkvderhavnliidlvmshepkti
tlvptggltniamaarleprivdrvkevvlmgggyhegnatsvaefniiidpeaahivfn
eswqvtmvgldlthqalatppilqrvkevdtnparfmleimdyytkiyqsnrymaaaavh
dpcavayvidpsvmttervpvdieltgkltlgmtvadfrnprpehchtqvavkldfekfw
glvldalerigdp
>d1ra9__ 3.66.1.1.1 Dihydrofolate reductase, prokaryotic type {Escherichia coli}
misliaalavdrvigmenampwnlpadlawfkrntldkpvimgrhtwesigrplpgrkni
ilssqpgtddrvtwvksvdeaiaacgdvpeimvigggrvyeqflpkaqklylthidaeve
gdthfpdyepddwesvfsefhdadaqnshsycfeilerr
>d3dfr__ 3.66.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqnrngligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhldqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1vdra_ 3.66.1.1.3 Dihydrofolate reductase, prokaryotic type {Haloferax volcanii}
elvsvaalaenrvigrdgelpwpsipadkkqyrsriaddpvvlgrttfesmrddlpgsaq
ivmsrsersfsvdtahraasveeavdiaasldaetayviggaaiyalfqphldrmvlsrv
pgeyegdtyypewdaaeweldaetdhegftlqewvrs
>d8dfr__ 3.66.1.1.4 Dihydrofolate reductases, eukaryotic type {Chicken (Gallus gallus)}
vrslnsivavcqnmgigkdgnlpwpplrneykyfqrmtstshvegkqnavimgkktwfsi
peknrplkdrinivlsrelkeapkgahylskslddalalldspelkskvdmvwivggtav
ykaamekpinhrlfvtrilhefesdtffpeidykdfkllteypgvpadiqeedgiqykfe
vyqksv
>d1dyr__ 3.66.1.1.6 Dihydrofolate reductases, eukaryotic type {Fungus (Pneumocystis carinii)}
nqqksltlivalttsygigrsnslpwklkkeisyfkrvtsfvptfdsfesmnvvlmgrkt
wesiplqfrplkgrinvvitrnesldlgngihsaksldhalellyrtygsessvqinrif
viggaqlykaamdhpkldrimatiiykdihcdvffplkfrdkewssvwkkekhsdleswv
gtkvphgkinedgfdyefemwtrdl
>d1aoea_ 3.66.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1rkd__ 3.67.1.1.1 Ribokinase {Escherichia coli}
agslvvlgsinadhilnlqsfptpgetvtgnhyqvafggkganqavaagrsganiafiac
tgddsigesvrqqlatdniditpvsvikgestgvalifvngegenvigihaganaalspa
lveaqrerianasallmqlesplesvmaaakiahqnktivalnpaparelpdellalvdi
itpneteaekltgirvendedaakaaqvlhekgirtvlitlgsrgvwasvngegqrvpgf
rvqavdtiaagdtfngalitalleekplpeairfahaaaaiavtrkgaqpsvpwreeida
fldrqr
>d1bx4a_ 3.67.1.1.2 Adenosine kinase {Human (Homo sapiens)}
vrenilfgmgnplldisavvdkdfldkyslkpndqilaedkhkelfdelvkkfkveyhag
gstqnsikvaqwmiqqphkaatffgcigidkfgeilkrkaaeahvdahyyeqneqptgtc
aacitgdnrslianlaaancykkekhldleknwmlvekarvcyiagffltvspesvlkva
hhasennriftlnlsapfisqfykeslmkvmpyvdilfgneteaatfareqgfetkdike
iakktqalpkmnskrqriviftqgrddtimatesevtafavldqdqkeiidtngagdafv
ggflsqlvsdkplteciraghyaasiiirrtgctfpekpdfh
>d1c3qa_ 3.67.1.2.1 Thiazole kinase {Bacillus subtilis}
mdaqsaakcltavrrhsplvhsitnnvvtnftangllalgaspvmayakeevadmakiag
alvlnigtlskesveamiiagksanehgvpvildpvgagatpfrtesardiirevrlaai
rgnaaeiahtvgvtdwlikgvdagegggdiirlaqqaaqklntviaitgevdviadtshv
ytlhnghklltkvtgagclltsvvgafcaveenplfaaiaaissygvaaqlaaqqtadkg
pgsfqiellnklstvteqdvqewatiervtvs
>d1uag_3 3.67.2.1.1 (94-297) UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase, gene MurD {Escherichia coli}
dielfcreaqapivaitgsngkstvttlvgemakaagvnvgvggniglpalmllddecel
yvlelssfqlettsslqavaatilnvtedhmdrypfglqqyraaxlriyenakvcvvnad
daltmpirgadercvsfgvnmgdyhlnhqqgetwlrvkgekvlnvkemklsgqhnytnal
aalaladaaglprasslkalttft
>d1fgs_2 3.67.2.2.1 (1-296) Folylpolyglutamate synthetase {Lactobacillus casei}
mnytetvayihsfprlaktgdhrriltllhalgnpqqqgryihvtgtngkgsaanaiahv
leasgltvglytspfimrfnerimidhepipdaalvnavafvraalerlqqqqadfnvte
fefitalaywyfrqrqvdvavievgiggdtdstnvitpvvsvltevaldhqkllghtita
iakhkagiikrgipvvtgnlvpdaaavvaakvattgsqwlrfdrdfsvpkaklhgwgqrf
tyedqdgrisdlevplvgdyqqrnmaiaiqtakvyakqtewpltpqnirqglaash
>d1b7ba_ 3.68.1.1.1 Carbamate kinase {Enterococcus faecium}
gkkmvvalggnailsndasahaqqqalvqtsaylvhlikqghrlivshgngpqvgnlllq
qqaadseknpampldtcvamtqgsigywlsnalnqelnkagikkqvatvltqvvvdpade
afknptkpigpflteaeakeamqagaifkedagrgwrkvvpspkpidiheaetintlikn
diitiscggggipvvgqelkgveavidkdfaseklaelvdadalviltgvdyvcinygkp
dekqltnvtvaeleeykqaghfapgsmlpkieaaiqfvesqpnkqaiitslenlgsmsgd
eivgtvv
>d1fua__ 3.69.1.1.1 L-fuculose-1-phosphate aldolase {Escherichia coli}
mernklarqiidtclemtrlglnqgtagnvsvryqdgmlitptgipyeklteshivfidg
ngkheegklpssewrfhmaayqsrpdanavvhnhavhctavsilnrsipaihymiaaagg
nsipcapyatfgtrelsehvalalknrkatllqhhgliacevnlekalwlahevevlaql
ylttlaitdpvpvlsdeeiavvlekf
>d1b8ja_ 3.70.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1auk__ 3.70.1.2.1 Arylsulfatase A {Human (Homo sapiens)}
rppnivlifaddlgygdlgcyghpssttpnldqlaagglrftdfyvpvslxtpsraallt
grlpvrmgmypgvlvpssrgglpleevtvaevlaargyltgmagkwhlgvgpegaflpph
qgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpipllanlsveaqppwlpgle
arymafahdlmadaqrqdrpfflyyashhthypqfsgqsfaersgrgpfgdslmeldaav
gtlmtaigdlglleetlviftadngpetmrmsrggcsgllrcgkgttyeggvrepalafw
pghiapgvthelassldllptlaalagaplpnvtldgfdlsplllgtgksprqslffyps
ypdevrgvfavrtgkykahfftqgsahsdttadpachasssltaheppllydlskdpgen
ynllggvagatpevlqalkqlqllkaqldaavtfgpsqvargedpalqicchpgctprpa
cchcp
>d1fsu__ 3.70.1.2.2 Arylsulfatase B (4-sulfatase) {Human (Homo sapiens)}
srpphlvflladdlgwndvgfhgsrirtphldalaaggvlldnyytqplxtpsrsqlltg
ryqirtglqhqiiwpcqpscvpldekllpqllkeagytthmvgkwhlgmyrkeclptrrg
fdtyfgyllgsedyysherctlidalnvtrcaldfrdgeevatgyknmystniftkraia
litnhppekplflylalqsvheplqvpeeylkpydfiqdknrhhyagmvslmdeavgnvt
aalkssglwnntvfifstdnggqtlaggnnwplrgrkwslweggvrgvgfvaspllkqkg
vknrelihisdwlptlvklarghtngtkpldgfdvwktisegspspriellhnidpnfvd
sspcprnsmapakddsslpeysafntsvhaairhgnwklltgypgcgywfpppsqynvse
ipssdpptktlwlfdidrdpeerhdlsreyphivtkllsrlqfyhkhsvpvyfpaqdprc
dpkatgvwgpwm
>d1cnza_ 3.71.1.1.5 3-isopropylmalate dehydrogenase, IPMDH {Salmonella typhimurium}
msknyhiavlpgdgigpevmaqalkvmdavrsrfdmrittshydvggiaidnhghplpka
tvegceqadailfgsvggpkwenlppesqpergallplrkhfklfsnlrpaklyqgleaf
cplradiaangfdilcvreltggiyfgqpkgregsgqyekafdtevyhrfeieriariaf
esarkrrrkvtsidkanvlqssilwreivndvaktypdvelahmyidnatmqlikdpsqf
dvllcsnlfgdilsdecamitgsmgmlpsaslneqgfglyepaggsapdiagknianpia
qilslalllrysldandaataieqainraleegvrtgdlargaaavstdemgdiiaryva
egv
>d1iso__ 3.71.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpmseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdeyalfeathgtapdiagqdkanpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtkdfeslmdgakllkcsefgdaiienm
>d3csua1 3.72.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastrtrlsfe
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqetqg
>d3csua2 3.72.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampqyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d2at2a1 3.72.1.1.2 (1-144) Aspartate carbamoyltransferase catalytic subunit {Bacillus subtilis}
mkhlttmselsteeikdllqtaqelksgktdnqltgkfaanlffepstrtrfsfevaekk
lgmnvlnldgtstsvqkgetlydtirtlesigvdvcvirhsedeyyeelvsqvnipilna
gdgcgqhptqslldlmtiyeefnt
>d2at2a2 3.72.1.1.2 (145-295) Aspartate carbamoyltransferase catalytic subunit {Bacillus subtilis}
fkgltvsihgdikhsrvarsnaevltrlgarvlfsgpsewqdeentfgtyvsmdeavess
dvvmllriqnerhqsavsqegylnkygltveraermkrhaiimhpapvnrgveiddslve
seksrifkqmkngvfirmaviqcalqtnvkr
>d1orta1 3.72.1.1.3 (1-150) Ornithine transcarbamoylase {Pseudomonas aeruginosa}
afnmhnrnllslmhhstrelrylldlsrdlkrakytgteqqhlkrknialifektstrtr
cafevaaydqganvtyidpnssqighkesmkdtarvlgrmydaigyrgfkqeiveelakf
agvpvfngltdeyhptqmladvltmrehsd
>d2otca1 3.72.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
rvpvwngltnefhptqlladlltmqehlpg
>d2otca2 3.72.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1a1s_1 3.72.1.1.5 (1-150) Ornithine transcarbamoylase {Pyrococcus furiosus}
vvslagrdllclqdytaeeiwtiletakmfkiwqkigkphrllegktlamifqkpstrtr
vsfevamahlgghalylnaqdlqlrrgetiadtarvlsryvdaimarvydhkdvedlaky
atvpvinglsdfshpcqaladymtiwekkg
>d1a1s_2 3.72.1.1.5 (151-313) Ornithine transcarbamoylase {Pyrococcus furiosus}
tikgvkvvyvgdgnnvahslmiagtklgadvvvatpegyepdekvikwaeqnaaesggsf
ellhdpvkavkdadviytdvwasmgqeaeaeerrkifrpfqvnkdlvkhakpdymfmhcl
pahrgeevtddvidspnsvvwdqaenrlhaqkavlalvmggik
>d1otha1 3.72.1.1.6 (34-184) Ornithine transcarbamoylase {Human (Homo sapiens)}
kvqlkgrdlltlknftgeeikymlwlsadlkfrikqkgeylpllqgkslgmifekrstrt
rlstetgfallgghpcflttqdihlgvnesltdtarvlssmadavlarvykqsdldtlak
easipiinglsdlyhpiqiladyltlqehys
>d1otha2 3.72.1.1.6 (185-354) Ornithine transcarbamoylase {Human (Homo sapiens)}
slkgltlswigdgnnilhsimmsaakfgmhlqaatpkgyepdasvtklaeqyakengtkl
lltndpleaahggnvlitdtwismgreeekkkrlqafqgyqvtmktakvaasdwtflhcl
prkpeevddevfysprslvfpeaenrkwtimavmvslltdyspqlqkpkf
>d1b74a1 3.72.2.1.1 (1-126) Glutamate racemase {Bacteria (Aquifex pyrophilus)}
mkigifdsgvggltvlkairnryrkvdivylgdtarvpygirskdtiiryslecagflkd
kgvdiivvacntasayalerlkkeinvpvfgviepgvkealkksrnkkigvigtpatvks
gayqrk
>d1b74a2 3.72.2.1.1 (127-252) Glutamate racemase {Bacteria (Aquifex pyrophilus)}
leeggadvfakacplfaplaeegllegeitrkvvehylkefkgkidtlilgcthypllkk
eikkflgdaevvdssealslslhnfikddgssslelfftdlspnlqfliklilgrdypvk
laegvf
>d2tysb_ 3.73.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahttnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdilkargei
>d1oasa_ 3.73.1.1.2 O-acetylserine sulfhydrylase (Cystein synthase) {Bacteria (Salmonella typhimurium)}
skiyednsltightplvrlnrigngrilakvesrnpsfsvkcriganmiwdaekrgvlkp
gvelveptngntgialayvaaargykltltmpetmsierrkllkalganlvltegakgmk
gaiqkaeeivasdpqkylllqqfsnpanpeihekttgpeiwedtdgqvdvfisgvgtggt
ltgvtryikgtkgktdlitvaveptdspviaqalageeikpgphkiqgigagfipgnldl
klidkvvgitneeaistarrlmeeegilagissgaavaaalklqedesftnknivvilps
sgerylstalfadlf
>d1tdj_1 3.73.1.1.3 (5-335) Threonine deaminase N-terminal domain {Escherichia coli}
qplsgapegaeylravlrapvyeaaqvtplqkmeklssrldnvilvkredrqpvhsfklr
gayammaglteeqkahgvitasagnhaqgvafssarlgvkalivmptatadikvdavrgf
ggevllhganfdeakakaielsqqqgftwvppfdhpmviagqgtlalellqqdahldrvf
vpvgggglaagvavlikqlmpqikviaveaedsaclkaaldaghpvdlprvglfaegvav
krigdetfrlcqeylddiitvdsdaicaamkdlfedvravaepsgalalagmkkyialhn
irgerlahilsganvnfhglryvsercelge
>d1moq__ 3.74.1.1.1 "Isomerase domain" of glucosamine 6-phosphate synthase (GLMS) {Escherichia coli}
gdkgiyrhymqkeiyeqpnaikntltgrishgqvdlselgpnadellskvehiqilacgt
synsgmvsrywfeslagipcdveiasefryrksavrrnslmitlsqsgetadtlaglrls
kelgylgslaicnvpgsslvresdlalmtnagteigvastkafttqltvllmlvaklsrl
kgldasiehdivhglqalpsrieqmlsqdkriealaedfsdkhhalflgrgdqypialeg
alklkeisyihaeayaagelkhgplalidadmpvivvapnnelleklksnieevrarggq
lyvfadqdagfvssdnmhiiemphveeviapifytvplqllayhvalikgtdvdqprnla
ksvtve
>d1dqra_ 3.74.1.2.1 Phosphoglucose isomerase, PGI {Rabbit (Oryctolagus cuniculus)}
aaltrnpqfqklqqwhrehgselnlrhlfdtdkerfnhfsltlntnhghilldysknlvt
eevmhmlldlaksrgveaaresmfngekinstedravlhvalrnrsntpivvdgkdvmpe
vnkvldkmkafcqrvrsgdwkgytgktitdvinigiggsdlgplmvtealkpyssggprv
wfvsnidgthiaktlaclnpesslfiiasktfttqetitnaktakdwfllsakdpstvak
hfvalstntakvkefgidpqnmfefwdwvggryslwsaiglsialhvgfdnfeqllsgah
wmdqhfrttpleknapvllamlgiwyincfgcetqavlpydqylhrfaayfqqgdmesng
kyitksgarvdhqtgpivwgepgtngqhafyqlihqgtkmipcdflipvqtqhpirkglh
hkillanflaqtealmkgksteearkelqaagkspedlmkllphkvfegnrptnsivftk
ltpfilgaliamyehkifvqgvvwdinsfdqwgvelgkqlakkiepeldgsspvtshdss
tnglinfikqqreak
>d1b0za_ 3.74.1.2.2 Phosphoglucose isomerase, PGI {Bacillus stearothermophilus}
aisfdysnalpfmqeneldylsefvkaahhmlherkgpgsdflgwvdwpirydknefsri
kqaaerirnhsdalvvigiggsylgaraaiealshtfhnqmndttqiyfagqnisstyis
hlldvlegkdlsinvisksgtttepaiafrifrdymekkygkeearkriyvttdrtkgal
kkladqegyetfvipdniggrysvltavgllpiavaglnidrmmegaasayhkynnpdll
tnesyqyaavrnilyrkgkaiellvnyepslhyvsewwkqlfgesegkdqkglfpasvdf
ttdlhsmgqyvqegrrnlietvlhvkkpqieltiqedpenidglnflagktldevnkkaf
qgtllahvdggvpnliveldemneytfgemvyffekacgisghllgvnpfdqpgveaykk
nmfallgkpgfedekaalmkrl
>d1dmr_2 3.75.1.1.2 (3-625) Dimethylsulfoxide reductase (DMSO reductase) {Rhodobacter capsulatus}
langtvmsgshwgvftatvengrataftpwekdphpspmlagvldsiysptrikypmvrr
eflekgvnadrstrgngdfvrvswdqaldlvaaevkrveetygpegvfggsygwkspgrl
hncttllrrmltlaggyvngagdystgaaqvimphvvgtlevyeqqtawpvlaentevmv
fwaadpiktsqigwvipehgaypglealkakgtkvividpvrtktveffgaehitpkpqt
dvaimlgmahtlvaedlydkdfianytsgfdkflpyldgetdstpktaewaegisgvpae
tikelarlfeskrtmlaagwsmqrmhhgeqahwmlvtlasmlgqiglpgggfglsyhysg
ggtpstsgpalagitdggaatkgpewlaasgasvipvarvvdmlenpgaefdfngtrskf
pdvkmaywvggnpfvhhqdrnrmvkawekletfvvhdfqwtptarhadivlpattsyern
dietigdysntgilamkkiveplyearsdydifaavaerlgkgaeftegkdemgwiksfy
ddaakqgkaagvqmpafdafwaegivefpvtdgadfvryasfredpllnplgtptgliei
yskniekmgyddcpahptwmepl
>d2napa2 3.75.1.1.5 (4-600) Dissimilatory nitrate reductase (NAP) {Desulfovibrio desulfuricans}
rpekwvkgvcrycgtgcgvlvgvkdgkavaiqgnpnnhnagllclkgsllipvlnskerv
tqplvrrhkggklepvswdealdlmasrfrssidmygpnsvawygsgqclteesyvanki
fkggfgtnnvdgnprlcmasavggyvtsfgkdepmgtyadidqatcffiigsntseahpv
lfrriarrkqvepgvkiivadprrtntsriadmhvafrpgtdlafmhsmawviineeldn
prfwqryvnfmdaegkpsdfegykaflenyrpekvaeicrvpveqiygaarafaesaatm
slwcmginqrvqgvfannlihnlhlitgqicrpgatsfsltgqpnacggvrdggalshll
pagraipnakhraemeklwglpegriapepgyhtvalfealgrgdvkcmiicetnpahtl
pnlnkvhkamshpesfivcieafpdavtleyadlvlppafwcerdgvygcgerrysltek
avdppgqcrptvntlvefarragvdpqlvnfrnaedvwnewrmvskgttydfwgmtrerl
rkesgliwpcpsedhpgtslryvrgqdpcvpadhpdrfffygkpdgraviwmrpakg
>d1ad3a_ 3.76.1.1.1 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1euha_ 3.76.1.1.7 Aldehyde reductase (dehydrogenase), ALDH {Streptococcus mutans}
tkqyknyvngewklseneikiyepasgaelgsvpamsteevdyvyasakkaqpawralsy
ieraaylhkvadilmrdkekigailskevakgyksavsevvrtaeiinyaaeeglrmege
vleggsfeaaskkkiavvrrepvglvlaispfnypvnlagskiapaliagnviafkpptq
gsisglllaeafaeaglpagvfntitgrgseigdyivehqavnfinftgstgigerigkm
agmrpimlelggkdsaivledadleltakniiagafgysgqrctavkrvlvmesvadelv
ekirekvlaltignpeddaditplidtksadyveglindandkgatalteikregnlicp
ilfdkvttdmrlaweepfgpvlpiirvtsveeaieisnkseyglqasiftndfprafgia
eqlevgtvhinnktqrgtdnfpflgakksgagiqgvkysieamttvksvvfdik
>d1co3a_ 3.76.1.1.8 Aldehyde reductase (dehydrogenase), ALDH {Vibrio harveyi}
qtdnvfyatnaftgealplafpvhtevevnqaataaakvardfrrlnnskrasllrtias
elearsddiiarahletalpevrltgeiartanqlrlfadvvnsgsyhqaildtpnptra
plpkpdirrqqialgpvavfgasnfplafsaaggdtasalaagcpvivkghtahpgtsqi
vaecieqalkqeqlpqaiftllqgnqralgqalvshpeikavgftgsvgggralfnlahe
rpepipfygelgainptfifpsamrakadladqfvasmtmgcgqfctkpgvvfalntpet
qafietaqslirqqspstlltpgirdsyqsqvvsrgsddgidvtfsqaespcvasalfvt
ssenwrkhpaweeeifgpqslivvcenvadmlslsemlagsltatihateedypqvsqli
prleeiagrlvfngwptevevgyamvhggpypasthsastsvgaeaihrwlrpvayqalp
esllpdslkaenpleiaravdgkaa
>d1aco_2 3.77.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d3pmga1 3.78.1.1.1 (1-190) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
vkivtvktkaypdqkpgtsglrkrvkvfqsstnyaenfiqsiistvepaqrqeatlvvgg
dgrfymkeaiqlivriaaangigrlvigqngilstpavsciirkikaiggiiltashnpg
gpngdfgikfnisnggpapeaitdkifqisktieeyaicpdlkvdlgvlgkqqfdlenkf
kpftveivds
>d3pmga2 3.78.1.1.1 (191-303) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
veayatmlrnifdfnalkellsgpnrlkiridamhgvvgpyvkkilceelgapansavnc
vpledfgghhpdpnltyaadlvetmksgehdfgaafdgdgdrnmilgkhgffv
>d3pmga3 3.78.1.1.1 (304-420) Phosphoglucomutase, first 3 domains {Rabbit (Oryctolagus cuniculus)}
npsdsvaviaanifsipyfqqtgvrgfarsmptsgaldrvanatkialyetptgwkffgn
lmdasklslcgeesfgtgsdhirekdglwavlawlsilatrkqsvedilkdhwhkfg
>d1fuia2 3.79.1.1.1 (1-355) L-fucose isomerase, N-terminal and second domains {Escherichia coli}
mkkislpkigirpvidgrrmgvresleeqtmnmakataallteklrhacgaavecvisdt
ciagmaeaaaceekfssqnvgltitvtpcwcygsetidmdptrpkaiwgfngterpgavy
laaalaahsqkgipafsiyghdvqdaddtsipadveekllrfaraglavasmkgksylsl
ggvsmgiagsivdhnffeswlgmkvqavdmtelrrridqkiydeaelemalawadknfry
gedennkqyqrnaeqsravlresllmamcirdmmqgnskladigrveeslgynaiaagfq
gqrhwtdqypngdtaeailnssfdwngvrepfvvatendslngvamlmghqltgt
>d16pk__ 3.80.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d1qgua_ 3.81.1.1.3 Nitrogenase iron-molybdenum protein {Klebsiella pneumoniae}
tnatgernlaliqevlevfpetarkerrkhmmvsdpkmksvgkciisnrksqpgvmtvrg
cayagskgvvfgpikdmahishgpvgcgqysragrrnyytgvsgvdsfgtlnftsdfqer
divfggdkklsklieemellfpltkgitiqsecpvgligddisavanasskaldkpvipv
rcegfrgvsqslghhiandvvrdwilnnregqpfettpydvaiigdyniggdawasrill
eemglrvvaqwsgdgtlvementpfvklnlvhcyrsmnyiarhmeekhqipwmeynffgp
tkiaeslrkiadqfddtiranaeaviaryegqmaaiiakyrprlegrkvllymgglrprh
vigayedlgmeiiaagyefahnddydrtlpdlkegtllfddassyeleafvkalkpdlig
sgikekyifqkmgvpfrqmhswdysgpyhgydgfaifardmdmtlnnpawneltapwl
>d1qgub_ 3.81.1.1.3 Nitrogenase iron-molybdenum protein {Klebsiella pneumoniae}
sqtidkinscyplfeqdeyqelfrnkrqleeahdaqrvqevfawtttaeyealnfrreal
tvdpakacqplgavlcslgfantlpyvhgsqgcvayfrtyfnrhfkepiacvsdsmteda
avfggnnnmnlglqnasalykpeiiavsttcmaevigddlqafianakkdgfvdssiavp
hahtpsfigshvtgwdnmfegfaktftadyqgqpgklpklnlvtgfetylgnfrvlkrmm
eqmavpcsllsdpsevldtpadghyrmysggttqqemkeapdaidtlllqpwqllkskkv
vqemwnqpatevaiplglaatdellmtvsqlsgkpiadaltlergrlvdmmldshtwlhg
kkfglygdpdfvmgltrfllelgceptvilshnankrwqkamnkmldaspygrdsevfin
cdlwhfrslmftrqpdfmignsygkfiqrdtlakgkafevplirlgfplfdrhhlhrqtt
wgyegamnivttlvnavlekldsdtsqlgktdysfdlvr
>d1c3ja_ 3.82.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1a8i__ 3.82.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
qekrkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgr
wirtqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeie
edaglgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlryg
npwekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsa
kapndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqd
iirrfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawe
vtvktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlr
rmslveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngi
tprrwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfa
aylereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmig
gkaapgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqi
stagteasgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgy
naqeyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqer
vsalyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d4pgaa_ 3.83.1.1.4 Glutaminase-asparaginase {Pseudomonas 7A}
klanvvilatggtiagagasaansatyqaakvgvdkliagvpeladlanvrgeqvmqias
esitnddllklgkrvaeladsndvdgivithgtdtleetayflnlvqktdkpivvvgsmr
pgtamsadgmlnlynavavasnkdsrgkgvlvtmndeiqsgrdvsksinikteafksawg
plgmvvegksywfrlpakrhtvnsefdikqisslpqvdiaysygnvtdtaykalaqngak
alihagtgngsvssrvvpalqqlrkngtqiirsshvnqggfvlrnaeqpddkndwvvahd
lnpekarilamvamtktqdskelqrifwey
>d1pfka_ 3.84.1.1.1 Phosphofructokinase {Escherichia coli}
mikkigvltsggdapgmnaairgvvrsalteglevmgiydgylglyedrmvqldrysvsd
minrggtflgsarfpefrdeniravaienlkkrgidalvviggdgsymgamrltemgfpc
iglpgtidndikgtdytigfftalstvveaidrlrdtssshqrisvvevmgrycgdltla
aaiaggcefvvvpevefsredlvneikagiakgkkhaivaitehmcdvdelahfieketg
retratvlghiqrggspvpydrilasrmgayaidlllagyggrcvgiqneqlvhhdiida
ienmkrpfkgdwldcakkly
>d1cbf__ 3.85.1.1.1 Cobalt precorrin-4 methyltransferase CbiF {Bacillus megaterium}
glvprgshmklyiigagpgdpdlitvkglkllqqadvvlyadslvsqdliakskpgaevl
ktagmhleemvgtmldrmregkmvvrvhtgdpamygaimeqmvllkregvdieivpgvts
vfaaaaaaeaeltipdltqtviltraegrtpvpefekltdlakhkctialflsstltkkv
mkefinagwsedtpvvvvykatwpdekivrttvkdlddamrtngirkqamilagwaldp
>d1ayl__ 3.86.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {Escherichia coli}
mrvnngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtg
iftgrspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfv
vdafcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqw
keqglnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgek
gdvavffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepei
ynairrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifl
tadafgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptq
yaevlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnl
aiptelpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>d1doza_ 3.87.1.1.1 Ferrochelatase {Bacillus subtilis}
srkkmgllvmaygtpykeedieryythirrgrkpepemlqdlkdryeaiggisplaqite
qqahnleqhlneiqdeitfkayiglkhiepfiedavaemhkdgiteavsivlaphfstfs
vqsynkrakeeaeklggltitsveswydepkfvtywvdrvketyasmpederenamlivs
ahslpekikefgdpypdqlhesakliaegagvseyavgwqsegntpdpwlgpdvqdltrd
lfeqkgyqafvyvpvgfvadhlevlydndyeckvvtddigasyyrpempnakpefidala
tvvlkklgr
>d1qgoa_ 3.87.1.2.1 Cobalt chelatase CbiK {Salmonella typhimurium}
kkallvvsfgtsyhdtceknivacerdlaascpdrdlfraftsgmiirklrqrdgididt
plqalqklaaqgyqdvaiqslhiingdeyekivrevqllrplftrltlgvpllsshndyv
qlmqalrqqmpslrqtekvvfmghgashhafaayacldhmmtaqrfparvgavesypevd
ilidslrdegvtgvhlmplmlvagdhaindmasddgdswkmrfnaagipatpwlsglgen
pairamfvahlhqalnm
>d1toaa_ 3.87.2.1.1 Periplasmic zinc binding protein TroA {Treponema pallidum}
gkplvvttigmiadavkniaqgdvhlkglmgpgvdphlytatagdvewlgnadlilyngl
hletkmgevfsklrgsrlvvavsetipvsqrlsleeaefdphvwfdvklwsysvkavyes
lckllpgktreftqryqayqqqldkldayvrrkaqslpaerrvlvtahdafgyfsraygf
evkglqgvstaseasahdmqelaafiaqrklpaifiessiphknvealrdavqarghvvq
iggelfsdamgdagtsegtyvgmvthnidtivaalar
>d2dri__ 3.88.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptdsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d8abp__ 3.88.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmlaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1rpja_ 3.88.1.1.3 D-allose-binding protein {Escherichia coli}
aaeyavvlktlsnpfwvdmkkgiedeaktlgvsvdifaspsegdfqsqlqlfedlsnkny
kgiafaplssvnlvmpvarawkkgiylvnldekidmdnlkkaggnveafvttdnvavgak
gasfiidklgaeggevaiiegkagnasgearrngateafkkasqiklvasqpadwdrika
ldvatnvlqrnpnikaiycandtmamgvaqavanagktgkvlvvgtdgipearkmveagq
mtatvaqnpadigatglklmvdaeksgkvipldkapefklvdsilvtq
>d1gca__ 3.88.1.1.5 Galactose/glucose-binding protein {Salmonella typhimurium, strain lt2}
adtrigvtiykyddnfmsvvrkaiekdgksapdvqllmndsqndqskqndqidvllakgv
kalainlvdpaaagtviekargqnvpvvffnkepsrkaldsydkayyvgtdskesgviqg
dliakhwqanqgwdlnkdgkiqyvllkgepghpdaearttyvvkelndkgiqteqlaldt
amwdtaqakdkmdawlsgpnankievvianndamamgavealkahnkssipvfgvdalpe
alalvksgamagtvlndannqakatfdlaknlaegkgaadgtswkienkivrvpyvgvdk
dnlseftqk
>d1pea__ 3.88.1.1.6 Amide receptor/negative regulator of the amidase operon (AmiC) {Pseudomonas aeruginosa}
pligllfsetgvtadiersqrygallaveqlnreggvggrpietlsqdpggdpdryrlca
edfirnrgvrflvgcymshtrkavmpvveradallcyptpyegfeyspnivyggpapnqn
saplaaylirhygervvfigsdyiypresnhvmrhlyrqhggtvleeiyiplypsdddlq
raveriyqaradvvfstvvgtgtaelyraiarrygdgrrppiaslttseaevakmesdva
egqvvvapyfssidtpasrafvqachgffpenatitawaeaaywqtlllgraaqaagnwr
vedvqrhlydididapqgpvrverqnnhsrlssriaeidargvfqvrwqspepirpdpyv
vvhnlddw
>d1dbqa_ 3.88.1.1.7 Purine repressor (PurR), C-terminal domain {Escherichia coli}
ksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdgl
lvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagrylierghr
eigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqphr
ptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslge
tafnmlldrivnkreepqsievhprlierrsvadgpfrdyrr
>d1tlfa_ 3.88.1.1.8 Lac-repressor (lacR) core (C-terminal domain) {Escherichia coli}
slligvatsslalhapsqivaaiksradqlgasvvvsmversgveackaavhnllaqrvs
gliinyplddqdaiaveaactnvpalfldvsdqtpinsiifshedgtrlgvehlvalghq
qiallagplssvsarlrlagwhkyltrnqiqpiaeregdwsamsgfqqtmqmlnegivpt
amlvandqmalgamraitesglrvgadisvvgyddtedsscyipplttikqdfrllgqts
vdrllqlsqgqavkgnqllpvslvkrkttlapntqtaspraladslmqlarqvsrl
>d1byka_ 3.88.1.1.9 Trehalose repressor, C-terminal domain {Escherichia coli}
sdkvvaiivtrldslsenlavqtmlpafyeqgydpimmesqfspqlvaehlgvlkrrnid
gvvlfgftgiteemlahwqsslvllardakgfasvcyddegaikilmqrlydqghrnisy
lgvphsdvttgkrrheaylafckahklhpvaalpglamkqgyenvakvitpettallcat
dtlalgaskylqeqridtlqlasvgntplmkflhpeivtvdpgyaeagrqaacqliaqvt
grsepqqiiipatls
>d2liv__ 3.88.1.1.10 Leucine-,isoleucine-,valine-binding (LIV) protein {Escherichia coli}
edikvavvgamsgpvaqygdqeftgaeqavadinakggikgnklqiakyddacdpkqava
vankvvndgikyvighlcssstqpasdiyedegilmitpaatapeltargyqlilrttgl
dsdqgptaakyilekvkpqriaivhdkqqygeglaravqdglkkgnanvvffdgitagek
dfstlvarlkkenidfvyyggyhpemgqilrqaraaglktqfmgpegvanvslsniages
aegllvtkpknydqvpankpivdaikakkqdpsgafvwttyaalqslqaglnqsddpaei
akylkansvdtvmgpltwdekgdlkgfefgvfdwhangtatdak
>d1jeta_ 3.89.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1pda_1 3.89.1.1.2 (3-219) Porphobilinogen deaminase (hydroxymethylbilane synthase), N-terminal domain {Escherichia coli}
dnvlriatrqsplalwqahyvkdklmashpglvvelvpmvtrgdvildtplakvggkglf
vkelevallenradiavhsmkdvpvefpqglglvticeredprdafvsnnydsldalpag
sivgtsslrrqcqlaerrpdliirslrgnvgtrlskldngeydaiilavaglkrlglesr
iraalppeislpavgqgavgiecrlddsrtrellaal
>d1lst__ 3.89.1.1.3 Lysine-,arginine-,ornithine-binding (LAO) protein {Salmonella typhimurium}
alpqtvrigtdttyapfsskdakgefigfdidlgnemckrmqvkctwvasdfdalipslk
akkidaiisslsitdkrqqeiafsdklyaadsrliaakgspiqptleslkgkhvgvlqgs
tqeayandnwrtkgvdvvayanqdliysdltagrldaalqdevaasegflkqpagkeyaf
agpsvkdkkyfgdgtgvglrkddtelkaafdkaltelrqdgtydkmakkyfdfnvygdk
>d1sbp__ 3.89.1.1.4 Sulphate-binding protein {Salmonella typhimurium}
kdiqllnvsydptrelyeqynkafsahwkqetgdnvvidqshggsgkqatsvingieadt
vtlalaydvnaiaergridknwikrlpddsapytstivflvrkgnpkqihdwndlikpgv
svitpnpkssggarwnylaawgyalhhnnndqakaedfvkalfknvevldsgargstntf
vergigdvliaweneallatnelgkdkfeivtpsesilaeptvsvvdkvvekkdtkavae
aylkylyspegqeiaaknfyrprdadvakkyddafpklklftidevfggwakaqkdhfad
ggtfdqisk
>d1ixh__ 3.89.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveyayakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d3mbp__ 3.89.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d3thia_ 3.89.1.1.7 Thiaminase I {Bacillus subtilis}
itlkvaiypyvpdparfqaavldqwqrqepgvkleftdwdsysadppddldvfvldsifl
shfvdagyllpfgsqdidqaedvlpfalqgakrngevyglpqilctnllfyrkgdlkigq
vdniyelykkigtshseqipppqnkgllinmaggttkasmylealidvtgqyteydllpp
ldplndkvirglrllinmagekpsqyvpedgdayvraswfaqgsgrafigysesmmrmgd
yaeqvrfkpisssagqdiplfysdvvsvnsktahpelakklanvmasadtveqalrpqad
gqypqyllparhqvyealmqdypiyselaqivnkpsnrvfrlgpevrtwlkdakqvlpea
lg
>d1mrp__ 3.89.1.1.8 Ferric-binding protein {Haemophilus influenzae}
ditvyngqhkeaatavakafeqetgikvtlnsgkseqlagqlkeegdktpadvfyteqta
tfadlseagllapiseqtiqqtaqkgvplapkkdwialsgrsrvvvydhtklsekdmeks
vldyatpkwkgkigyvstsgafleqvvalskmkgdkvalnwlkglkengklyaknsvalq
avengevpaalinnyywynlakekgvenlksrlyfvrhqdpgalvsysgaavlkasknqa
eaqkfvdflaskkgqealvaaraeyplradvvspfnlepyekleapvvsattaqdkehai
klieeaglk
>d1dpe__ 3.89.1.1.10 Dipeptide-binding protein {Escherichia coli}
ktlvycsegspegfnpqlfisgttydassvplynrlvefkigttevipglaekwevsedg
ktytfhlrkgvkwhdnkefkptrelnaddvvfsfdrqknaqnpyhkvsggsyeyfegmgl
pelisevkkvddntvqfvltrpeapfladlamdfasilskeyadammkagtpekldlnpi
gtgpfqlqqyqkdsrirykafdgywgtkpqidtlvfsitpdasvryaklqknecqvmpyp
npadiarmkqdksinlmempglnvgylsynvqkkplddvkvrqaltyavnkdaiikavyq
gagvsaknlipptmwgynddvqdytydpekakallkeaglekgfsidlwampvqrpynpn
arrmaemiqadwakvgvqakivtyewgeylkrakdgehqtvmmgwtgdngdpdnffatef
scaaseqgsnyskwcykpfedliqparatddhnkrvelykqaqvvmhdqapaliiahstv
fepvrkevkgyvvdplgkhhfenvsie
>d1pot__ 3.89.1.1.13 Spermidine/putrescine-binding protein PotD {Escherichia coli}
nntlyfynwteyvppglleqftketgikviystyesnetmyaklktykdgaydlvvpsty
yvdkmrkegmiqkidkskltnfsnldpdmlnkpfdpnndysipyiwgataigvngdavdp
ksvtswadlwkpeykgsllltddarevfqmalrklgysgnttdpkeieaaynelkklmpn
vaafnsdnpanpymegevnlgmiwngsafvarqagtpidvvwpkeggifwmdslaipana
knkegalklinfllrpdvakqvaetigyptpnlaarkllspevandktlypdaetiknge
wqndvgaassiyeeyyqklkag
>d1a99a_ 3.89.1.1.14 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1wdna_ 3.89.1.1.15 Glutamine-binding protein {Escherichia coli}
klvvatdtafvpfefkqgdlyvgfdvdlwaaiakelkldyelkpmdfsgiipalqtknvd
lalagititderkkaidfsdgyyksgllvmvkannndvksvkdldgkvvavksgtgsvdy
akaniktkdlrqfpnidnaymelgtnradavlhdtpnilyfiktagngqfkavgdsleaq
qygiafpkgsdelrdkvngalktlrengtyneiykkwfgtepk
>d1gr2a_ 3.89.1.1.16 Glutamate receptor ligand binding core (GluR2) {Rat (Rattus norvegicus)}
ktvvvttilespyvmmkknhemlegneryegycvdlaaeiakhcgfkykltivgdgkyga
rdadtkiwngmvgelvygkadiaiapltitlvreevidfskpfmslgisimikkpgtdgn
piesaedlskqteiaygtldsgstkeffrrskiavfdkmwtymrsaepsvfvrttaegva
rvrkskgkyayllestmneyieqrkpcdtmkvggnldskgygiatpkgsslgnavnlavl
klneqglldklknkwwydkgec
>d1amf__ 3.89.1.1.17 Molybdate-binding protein, ModA {Escherichia coli}
gkitvfaaasltnamqdiatqfkkekgvdvvssfassstlarqieagapadlfisadqkw
mdyavdkkaidtatrqtllgnslvvvapkasvqkdftidsktnwtsllnggrlavgdpeh
vpagiyakealqklgawdtlspklapaedvrgalalverneaplgivygsdavaskgvkv
vatfpedshkkveypvavveghnnatvkafydylkgpqaaeifkrygftik
>d1atg__ 3.89.1.1.18 Molybdate-binding protein, ModA {Azotobacter vinelandii}
elkvvtatnflgtleqlagqfakqtghavvissgssgpvyaqivngapynvffsadeksp
ekldnqgfalpgsrftyaigklvlwsakpglvdnqgkvlagngwrhiaisnpqiapygla
gtqvlthlglldkltaqeriveansvgqahsqtasgaadlgfvalaqiiqaaakipgshw
fppanyyepivqqavitkstaekanaeqfmswmkgpkavaiikaagyvlpq
>d1al3__ 3.89.1.1.19 Cofactor-binding fragment of CysB {Klebsiella aerogenes}
twpdkgslyvatthtqaryalpgvikgfieryprvslhmhqgsptqiaeavskgnadfai
atealhlyddlvmlpcyhwnrsivvtpehplatkgsvsieelaqyplvtytfgftgrsel
dtafnragltprivftatdadviktyvrlglgvgviasmavdpvsdpdlvkldangifsh
sttkigfrrstflrsymydfiqrfaphltrdvvdtavalrsnedieamfkdiklpek
>d1lfg_2 3.89.1.2.1 (335-691) Lactoferrin {Human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksaqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdpasnlcalcigdeege
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1ovb__ 3.89.1.2.5 Ovotransferrin {Duck (Anas platyrhynchos)}
syyavavvkkgtdfmikdlrgktschtglgrsagwnipigtlihrediewegiesgsveq
avakffsascvpgatieqklcrqckgdaktkclrnapysgysgafqclkdgkgdvafvkh
ttvqenapeekdeyellcldgsrqpvdsyktcnwarvaa
>d1a8e__ 3.89.1.2.8 Transferrin {Human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1afwa1 3.90.1.1.1 (25-293) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwa2 3.90.1.1.1 (294-417) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1dd8a1 3.90.1.1.2 (1-253) Beta-ketoacyl-ACP synthase I {Escherichia coli}
mkrvvitglgivssignnqqevlaslregrsgitfsqelkdsgmrshvwgnvkldttgli
drkvvrfmsdasiyaflsmeqaiadaglspeayqnnprvgliagsgggsprfqvfgadam
rgprglkavgpyvvtkamasgvsaclatpfkihgvnysissacatsahcignaveqiqlg
kqdivfagggeelcwemacefdamgalstkyndtpekasrtydahrdgfviaggggmvvv
eelehalargahi
>d1dd8a2 3.90.1.1.2 (254-406) Beta-ketoacyl-ACP synthase I {Escherichia coli}
yaeivgygatsdgadmvapsgegavrcmkmamhgvdtpidylnshgtstpvgdvkelaai
revfgdkspaisatkamtghslgaagvqeaiysllmlehgfiapsinieeldeqaaglni
vtettdrelttvmsnsfgfggtnatlvmrklkd
>d1kas_1 3.90.1.1.3 (2-251) Beta-ketoacyl-ACP synthase II {Escherichia coli}
krrvvvtglgmlspvgntvestwkallagqsgislidhfdtsayatkfaglvkdfncedi
isrkeqrkmdafiqygivagvqamqdsgleiteenatrigaaigsgigglglieenhtsl
mnggprkispffvpstivnmvaghltimyglrgpsisiatactsgvhnighaariiaygd
advmvaggaekastplgvggfgaaralstrndnpqaasrpwdkerdgfvlgdgagmlvle
eyehakkrga
>d1kas_2 3.90.1.1.3 (252-412) Beta-ketoacyl-ACP synthase II {Escherichia coli}
kiyaelvgfgmssdayhmtsppengagaalamanalrdagieasqigyvnahgtstpagd
kaeaqavktifgeaasrvlvsstksmtghllgaagavesiysilalrdqavpptinldnp
degcdldfvphearqvsgmeytlcnsfgfggtngslifkki
>d1d9ba1 3.90.1.1.4 (1-174) Ketoacyl-ACP synthase III (FabH) {Escherichia coli}
mytkiigtgsylpeqvrtnadlekmvdtsdewivtrtgirerhiaapnetvstmgfeaat
raiemagiekdqiglivvattsathafpsaacqiqsmlgikgcpafdvaaacagftyals
vadqyvksgavkyalvvgsdvlartcdptdrgtiiifgdgagaavlaaseepgi
>d1ebla2 3.90.1.1.4 (175-317) Ketoacyl-ACP synthase III (FabH) {Escherichia coli}
isthlhadgsygelltlpnadrvnpensihltxagnevfkvavtelahivdetlaannnd
rsqldwlvphqanlriisatakklgxsxdnvvvtldrhgntsaasvpcaldeavrdgrik
pgqlvlleafgggftwgsalvrf
>d1bi5a1 3.90.1.2.1 (1-235) Chalcone synthase {Alfalfa (Medicago sativa)}
mvsvseirkaqraegpatilaigtanpancveqstypdfyfkitnsehktelkekfqrmc
dksmikrrymylteeilkenpnvceymapsldarqdmvvvevprlgkeaavkaikewgqp
kskithlivcttsgvdmpgadyqltkllglrpyvkrymmyqqgxfaggtvlrlakdlaen
nkgarvlvvcsevtavtfrgpsdthldslvgqalfgdgaaalivgsdpvpeiekp
>d1bi5a2 3.90.1.2.1 (236-389) Chalcone synthase {Alfalfa (Medicago sativa)}
ifemvwtaqtiapdsegaidghlreagltfhllkdvpgivsknitkalveafeplgisdy
nsifwiahpggpaildqveqklalkpekmnatrevlseygnmssacvlfildemrkkstq
nglkttgeglewgvlfgfgpgltietvvlrsvai
>d1hfel1 3.91.1.1.2 (87-398) Fe-only hydrogenase larger subunit, C-domain {Desulfovibrio vulgaris}
wvpevekklkdgkvkciampapavryalgdafgmpvgsvttgkmlaalqklgfahcwdte
ftadvtiweegsefverltkksdmplpqftsccpgwqkyaetyypellphfstckspigm
ngalaktygaermkydpkqvytvsimpciakkyeglrpelkssgmrdidatlttrelaym
ikkagidfaklpdgkrdslmgestggatifgvtggvmeaalrfayeavtgkkpdswdfka
vrgldgikeatvnvggtdvkvavvhgakrfkqvcddvkagkspyhfieymacpggcvcgg
gqpvmpgvleam
>d1aln_1 3.92.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1aln_2 3.92.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1rgea_ 4.1.1.1.1 RNase Sa {Streptomyces aureofaciens}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriitgeatqedyytgdhyatfslidqtc
>d1fus__ 4.1.1.1.2 RNase F1 {Fusarium moniliforme}
xsattcgstnysasqvraaanaacqyyqnddtagsstyphtynnyegfdfpvdgpyqefp
iksggvytggspgadrvvintnceyagaithtgasgnnfvgcsgtn
>d9rnt__ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyklhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1rtu__ 4.1.1.1.4 RNase U2 {Ustilago sphaerogena}
cdipqstncggnvysnddintaiqgalddvangdrpdnyphqyyxeaseditlccgsgpw
sefplvyngpyyssrdnyvspgpdrviyqtntgefcatvthtgaasydgftqcs
>d1a2pa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d2rbia_ 4.1.1.1.6 Barnase/Binase {Bacillus intermedius}
vintfdgvadylirykrlpdnyitksqasalgwvaskgnlaevapgksiggdvfsnregr
lpsasgrtwreadinyvsgfrnadrlvyssdwliykttdnyatftrir
>d1rds__ 4.1.1.1.7 RNase Ms {Molsin (Aspergillus saitoi)}
esceytcgstcywssdvsaakakgyslyesgdtiddypheyhdyegfdfpvsgtyyeypi
msdydvytggspgadrvifngddelagvithtgasgddfvacsss
>d1aqza_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergillus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1cnsa_ 4.2.1.1.1 Barley endochitinase {Pearled barley (Hordeum vulgare)}
svssivsraqfdrmllhrndgacqakgfytydafvaaaaafsgfgttgsadvqkrevaaf
laqtshettggwatapdgafawgycfkqergassdyctpsaqwpcapgkryygrgpiqls
hnynygpagraigvdllanpdlvatdatvsfktamwfwmtaqppkpsshavivgqwspsg
adraagrvpgfgvitniinggiecghgqdsrvadrigfykrycdilgvgygnnldcysqr
pfa
>d3lzt__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1jsf__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d2eql__ 4.2.1.2.9 Lysozyme {Horse (Equus caballus), milk}
kvfskcelahklkaqemdgfggyslanwvcmaeyesnfntrafngknangssdyglfqln
nkwwckdnkrsssnacnimcsklldenidddiscakrvvrdpkgmsawkawvkhckdkdl
seylascnl
>d1jug__ 4.2.1.2.10 Lysozyme {Australian echidna (Tachyglossus aculeatus)}
kilkkqelcknlvaqgmngyqhitlpnwvctafhessyntratnhntdgstdygilqins
rywchdgktpgsknacniscskllddditddlkcakkiageakgltpwvawkskcrghdl
skfkc
>d1b9oa_ 4.2.1.2.14 alpha-Lactalbumin {Human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivendesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>d1hfx__ 4.2.1.2.15 alpha-Lactalbumin {Guinea pig (Gavia porcellus)}
kqltkcalshelndlagyrditlpewlciifhisgydtqaivknsdhkeyglfqindkdf
cessttvqsrnicdiscdklldddltddimcvkkildikgidywlahkplcsdkleqwyc
eaq
>d119l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlsksrwynqtpnrakrvittfrtgtwdayk
>d1am7a_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d153l__ 4.2.1.5.1 Lysozyme {Goose (Anser anser anser)}
rtdcygnvnridttgascktakpeglsycgvsaskkiaerdlqamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
infiktiqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d1qsaa2 4.2.1.6.1 (451-618) 70 kDa soluble lytic transglycosylase, SLT70 {Escherichia coli}
layndlfkrytsgkeipqsyamaiarqesawnpkvkspvgasglmqimpgtathtvkmfs
ipgysspgqlldpetninigtsylqyvyqqfgnnrifssaaynagpgrvrtwlgnsagri
davafvesipfsetrgyvknvlaydayyryfmgdkptlmsatewgrry
>d1qusa_ 4.2.1.6.2 36 kDa soluble lytic transglycosylase, SLT35 {Escherichia coli}
mvepqhnvmqmggdfannpnaqqfidkmvnkhgfdrqqlqeilsqakrldsvlrlmdnqa
pttsvkppsgpngawlryrkkfitpdnvqngvvfwnqyedalnrawqvygvppeiivgii
gvetrwgrvmgktrildalatlsfnyprraeyfsgeletfllmardeqddplnlkgsfag
amgygqfmpssykqyavdfsgdghinlwdpvdaigsvanyfkahgwvkgdqvavmangqa
pglpngfktkysisqlaaagltpqqplgnhqqasllrldvgtgyqywyglpnfytitryn
hsthyamavwqlgqavalarvq
>d1chka_ 4.2.1.7.1 Endochitosanase {Streptomyces sp., strain N174}
agaglddphkkeiamelvssaenssldwkaqykyiedigdgrgytggiigfcsgtgdmle
lvqhytdlepgnilakylpalkkvngsashsglgtpftkdwataakdtvfqqaqnderdr
vyfdpavsqakadglralgqfayydaivmhgpgndptsfggirktamkkartpaqggdet
tylngfldarkaamlteaahddtsrvdteqrvflkagnldlnpplkwktygdpyvins
>d1qgia_ 4.2.1.7.2 Endochitosanase {(Bacillus circulans)}
aspddnfspetlqflrnntgldgeqwnnimklinkpeqddlnwikyygycediedergyt
iglfgattggsrdthpdgpdlfkaydaakgasnpsadgalkrlgingkmkgsileikdse
kvfcgkikklqndaawrkamwetfynvyirysveqarqrgftsavtigsfvdtalnqgat
ggsdtlqgllarsgsssnektfmknfhakrtlvvdtnkynkppngknrvkqwdtlvdmgk
mnlknvdseiaqvtdwemk
>d1ppn__ 4.3.1.1.2 Papain {Papaya (Carica papaya)}
ipeyvdwrqkgavtpvknqgscgscwafsavvtiegiikirtgnlneyseqelldcdrrs
ygcnggypwsalqlvaqygihyrntypyegvqrycrsrekgpyaaktdgvrqvqpynega
llysianqpvsvvleaagkdfqlyrggifvgpcgnkvdhavaavgygpnyiliknswgtg
wgengyirikrgtgnsygvcglytssfypvkn
>d3gcb__ 4.3.1.1.8 Bleomycin hydrolase, Gal6 {Baker's yeast (Saccharomyces cerevisiae)}
afqgamassidiskinswnkefqsdlthqlattvlknynaddallnktrlqkqdnrvfnt
vvstdstpvtnqkssgrawlfaatnqlrlnvlselnlkefelsqaylffydklekanyfl
dqivssadqdidsrlvqyllaaptedggqysmflnlvkkyglipkdlygdlpysttasrk
wnsllttklrefaetlrtalkersaddsiivtlreqmqreifrlmslfmdippvqpneqf
tweyvdkdkkihtikstplefaskyakldpstpvslindprhpygklikidrlgnvlggd
aviylnvdnetlsklvvkrlqnnkavffgshtpkfmdkktgvmdielwnypaigynlpqq
kasriryheslmthamlitgchvdetsklplryrvenswgkdsgkdglyvmtqkyfeeyc
fqivvdinelpkelaskftsgkeepivlpiwdpmgala
>d1aim__ 4.3.1.1.9 Cruzain {Trypanosoma cruzi}
apaavdwrargavtavkdqgqcgscwafsaignvecqwflaghpltnlseqmlvscdktd
sgcsgglmnnafewivqenngavytedsypyasgegisppcttsghtvgatitghvelpq
deaqiaawlavngpvavavdasswmtytggvmtscvsealdhgvllvgyndsaavpywii
knswttqwgeegyiriakgsnqclvkeeassavvg
>e1csb.1a 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1csb.2d 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1huc.1a 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>e1huc.2c 4.3.1.1.10 (Pro)cathepsin B {Human (Homo sapiens)}
lpasfdareqwpqcptikeirdqgscgscwafgaveaisdricihtn
>d1thea_ 4.3.1.1.11 (Pro)cathepsin B {Rat (Rattus norvegicus)}
lpesfdareqwsncptiaqirdqgscgscwafgaveamsdricihtngrvnvevsaedll
tccgiqcgdgcnggypsgawnfwtrkglvsggvynshigclpytippcehhvngarppct
gegdtpkcnkmceagystsykedkhygytsysvsdsekeimaeiykngpvegaftvfsdf
ltyksgvykheagdvmgghairilgwgiengvpywlvanswnadwgdngffkilrgenhc
gieseivagiprt
>d1icfd_ 4.3.1.1.12 (Pro)cathepsin L {Human (Homo sapiens)}
nnkywlvknswgeewgmggyvkmakdrrnhcgiasaasyptv
>e1icf.1b 4.3.1.1.12 (Pro)cathepsin L {Human (Homo sapiens)}
nnkywlvknswgeewgmggyvkmakdrrnhcgiasaasyptv
>d1mema_ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1deua_ 4.3.1.1.15 (Pro)cathepsin X {Human (Homo sapiens)}
rgqtcyrplrgdglaplgrttyprpheylspadlpkswdwrnvdgvnyasitrnqhipqy
cgscwahastsamadrinikrkgawpstllsvqnvidcgnagsceggndlsvwdyahqhg
ipdetcnnyqakdqecdkfnqcgtcnefkechairnytlwrvgdygslsgrekmmaeiya
ngpiscgimaterlanytggiyaeyqdttyinhvvsvagwgisdgteywivrnswgepwg
ergwlrivtstykdgkgarynlaieehctfgdpiv
>d1cv8__ 4.3.1.1.16 Staphopain {Staphylococcus aureus}
neqyvnklenfkiretqgnngwcagytmsallnatyntnkyhaeavmrflhpnlqgqqfq
ftgltpremiyfgqtqgrspqllnrmttynevdnltknnkgiailgsrvesrngmhagha
mavvgnaklnngqeviiiwnpwdngfmtqdaknnvipvsngdhyqwyssiygy
>d1dkva3 4.3.1.2.1 (2-355) Calpain large subunit, catalytic domain (domain II) {Human (Homo sapiens)}
agiaaklakdreaaeglgsheraikylnqdyealrnecleagtlfqdpsfpaipsalgfk
elgpyssktrgmrwkrpteicadpqfiiggatrtdicqgalgdcwllaaiasltlneeil
arvvplnqsfqenyagifhfqfwqygewvevvvddrlptkdgellfvhsaegsefwsall
ekayakingcyealsggattegfedftgglaewyelkkpppnlfkiiqkalqkgsllgcs
iditsaadseaitfqklvkghaysvtgaeevesngslqklirirnpwgevewtgawndnc
pswntidpeererltrrhedgefwmsfsdflrhysrleicnltpdtltsdtykk
>d1f13a4 4.3.1.3.1 (191-515) Coagulation factor XIII, catalytic domain {Human (Homo sapiens), blood}
davyldnekereeyvlndigvifygevndiktrswsygqfedgildtclyvmdraqmdls
grgnpikvsrvgsamvnakddegvlvgswdniyaygvppsawtgsvdilleyrssenpvr
ygqcwvfagvfntflrclgiparivtnyfsahdndanlqmdifleedgnvnskltkdsvw
nyhcwneawmtrpdlpvgfggwqavdstpqensdgmyrcgpasvqaikhghvcfqfdapf
vfaevnsdliyitakkdgthvvenvdathigklivtkqiggdgmmditdtykfqegqeee
rlaletalmygakkplntegvmksr
>d1uch__ 4.3.1.4.1 Ubiquitin C-terminal hydrolase UCH-l3 {Human (Homo sapiens)}
rwlpleanpevtnqflkqlglhpnwqfvdvygmdpellsmvprpvcavlllfpitekyev
frteeeekiksqgqdvtssvyfmkqtisnacgtiglihaiannkdkmhfesgstlkkfle
esvsmspeerarylenydairvthetsahegqteapsidekvdlhfialvhvdghlyeld
grkpfpinhgetsdetlledaievckkfmerdpdelrfnaialsaa
>d1cmxa_ 4.3.1.4.2 Ubiquitin C-terminal hydrolase UCH-l3 {Synthetic, based on Saccharomyces cerevisiae sequence}
ravvpiesnpevftnfahklglknewayfdiysltepellaflprpvkaivllfpinedr
ksstsqqitssydviwfkqsvknacglyailhslsnnqsllepgsdldnflksqsdtsss
knrfddvttdqfvlnvikenvqtfstgqseapeatadtnlhyityveenggifeldgrnl
sgplylgksdptatdlieqelvrvrvasymenaneedvlnfamlglgpn
>d1avpa_ 4.3.1.5.1 Human adenovirus 2 proteinase {Mastadenovirus h2}
mgsseqelkaivkdlgcgpyflgtydkrfpgfvsphklacaivntagretggvhwmafaw
nprsktcylfepfgfsdqrlkqvyqfeyesllrrsaiasspdrcitlekstqsvqgpnsa
acglfccmflhafanwpqtpmdhnptmnlitgvpnsmlnspqvqptlrrnqeqlysfler
hspyfrshsaqirsatsfchlknm
>d7ceib_ 4.4.1.1.1 DNase domain of colicin E7 {Escherichia coli}
rnkpgkatgkgkpvnnkwlnnagkdlgspvpdrianklrdkefksfddfrkkfweevskd
pelskqfsrnnndrmkvgkapktrtqdvsgkrtsfelhhekpisqnggvydmdnisvvtp
krhidih
>d1bxib_ 4.4.1.1.2 DNase domain of colicin E9 {Escherichia coli}
eskrnkpgkatgkgkpvgdkwlddagkdsgapipdriadklrdkefksfddfrkavweev
skdpelsknlnpsnkssvskgyspftpknqqvggrkvyelhhdkpisqggevydxdnirv
ttpkrhidih
>d1qaea_ 4.4.1.2.1 Endonuclease {Serratia marcescens}
idncavgcptggssnvsivrhaytlnnnsttkfanwvayhitkdtpasgktrnwktdpal
npadtlapadytganaalkvdrghqaplaslagvsdweslnylsnitpqksdlnqgawar
ledqerklidradissvytvtgplyerdmgklpgtqkahtipsaywkvifinnspavnhy
aaflfdqntpkgadfcqfrvtvdeiekrtgliiwaglpddvqaslkskpgvlpelmgckn
>d1a73a_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1en7a_ 4.4.1.4.1 Recombination endonuclease VII {Bacteriophage T4}
mlltgklykeekqkfydaqngkclicqrelnpdvqanhldhdhelngpkagkvrgllcnl
cnaaegqmkhkfnrsglkgqgvdylewlenlltylksdytqnnihpnfvgdkskefsrlg
keemmaemlqrgfeynesdtktqliasfkkqlrkslk
>d7rsa__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1rraa_ 4.5.1.1.2 Ribonuclease A (also ribonuclease B, S) {Rat (Rattus norvegicus)}
aessadkfkrqhmdtegpskssptycnqmmkrqgmtkgsckpvntfvhepledvqaicsq
gqvtckngrnnchkssstlritdcrlkgsskypncdytttdsqkhiiiacdgnpyvpvhf
dasv
>d1onc__ 4.5.1.1.3 P-30 protein {Frog (Rana pipiens)}
xdwltfqkkhitntrdvdcdnimstnlfhckdkntfiysrpepvkaickgiiasknvltt
sefylsdcnvtsrpckyklkkstnkfcvtcenqapvhfvgvgsc
>d1bc4__ 4.5.1.1.4 Cytotoxic ribonuclease {Bullfrog (Rana catesbeiana)}
nwatfqqkhiintpiincntimdnniyivggqckrvntfiissattvkaictgvinmnvl
sttrfqlntctrtsitprpcpyssrtetnyicvkcenqypvhfagigrcp
>d1qmta_ 4.5.1.1.7 Eosinophil cationic protein, ribonuclease 3 {Human (Homo sapiens)}
mrppqftraqwfaiqhislnpprctiamrainnyrwrcknqntflrttfanvvnvcgnqs
ircphnrtlnnchrsrfrvpllhcdlinpgaqnisncryadrpgrrfyvvacdnrdprds
prypvvpvhldtti
>d1rnfa_ 4.5.1.1.8 Ribonuclease 4 {Human (Homo sapiens)}
mqdgmyqrflrqhvhpeetggsdrycnlmmqrrkmtlyhckrfntfihediwnirsicst
tniqckngkmnchegvvkvtdcrdtgssrapncryraiastrrvviacegnpqvpvhfdg
>d1b1ia_ 4.5.1.1.9 Angiogenin {Human (Homo sapiens)}
dnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenkn
gnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsifr
rp
>d1agi__ 4.5.1.1.10 Angiogenin {Bovine (Bos taurus)}
aqddyryihfltqhydakpkgrndeycfnmmknrrltrpckdrntfihgnkndikaiced
rngqpyrgdlrisksefqitickhkggssrppcrygatedsrvivvgcenglpvhfdesf
itprh
>d1qlza_ 4.6.1.1.3 Prion protein domain {Human (Homo sapiens)}
lggymlgsamsrpiihfgsdyedryyrenmhrypnqvyyrpmdeysnqnnfvhdcvniti
kqhtvttttkgenftetdvkmmervveqmcitqyeresqayyqr
>d1a5ka_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5la_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5ma_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5na_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5oa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwaa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwba_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwca_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwda_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwea_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwfa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwga_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwha_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwia_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1fwja_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1kraa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1krba_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1krca_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d2kaua_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1ubpa_ 4.7.1.1.2 Urease, gamma-subunit {Bacillus pasteurii}
mhlnpaekeklqiflaselllrrkarglklnypeavaiitsfimegardgktvamlmeeg
khvltrddvmegvpemiddiqaeatfpdgtklvtvhnpis
>d1icwa_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcantciivklsdgrelaldpkenwvqrvve
kflkraens
>d1icwb_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
cqciktyskpfhpkfikelrviesgphcantciivklsdgrelaldpkenwvqrvvekfl
kraens
>d1ikl__ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrvve
kflkraens
>d1ikm__ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
elrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrvve
kflkraens
>d1il8a_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1il8b_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1ilpa_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1ilpb_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1ilqa_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d1ilqb_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d2il8a_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d2il8b_ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
akelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrv
vekflkraens
>d3il8__ 4.8.1.1.1 Interleukin-8, IL-8 {Human (Homo sapiens)}
lrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpkenwvqrvvek
flkraens
>d1plfa_ 4.8.1.1.2 Platelet factor 4, PF4 {Bovine (Bos taurus)}
lqcvclkttsginprhisslevigaglhcpspqliatlktgrkicldqqnplykkiikrl
lks
>d1plfb_ 4.8.1.1.2 Platelet factor 4, PF4 {Bovine (Bos taurus)}
edlqcvclkttsginprhisslevigaglhcpspqliatlktgrkicldqqnplykkiik
rllks
>d1plfc_ 4.8.1.1.2 Platelet factor 4, PF4 {Bovine (Bos taurus)}
lqcvclkttsginprhisslevigaglhcpspqliatlktgrkicldqqnplykkiikrl
lks
>d1plfd_ 4.8.1.1.2 Platelet factor 4, PF4 {Bovine (Bos taurus)}
edlqcvclkttsginprhisslevigaglhcpspqliatlktgrkicldqqnplykkiik
rllks
>d1pfma_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfmb_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfmc_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfmd_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfna_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfnb_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfnc_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1pfnd_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
msakelrcqcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykk
iikklles
>d1rhpa_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
dlqclcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykkiikk
lles
>d1rhpb_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
dlqclcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykkiikk
lles
>d1rhpc_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
dlqclcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykkiikk
lles
>d1rhpd_ 4.8.1.1.3 Platelet factor 4, PF4 {Human (Homo sapiens)}
dlqclcvkttsqvrprhitslevikagphcptaqliatlkngrkicldlqaplykkiikk
lles
>d1mgsa_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdksn
>d1mgsb_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdksn
>d1msga_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1msgb_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1msha_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1mshb_ 4.8.1.1.4 Melanoma growth stimulating activity (MGSA) {Human (Homo sapiens)}
asvatelrcqclqtlqgihpkniqsvnvkspgphcaqteviatlkngrkaclnpaspivk
kiiekmlnsdks
>d1roda_ 4.8.1.1.5 IL-8/MGSA chimeric protein CIL-8M {Human (Homo sapiens)}
sakelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpaspivkk
iiekmlnsdksn
>d1rodb_ 4.8.1.1.5 IL-8/MGSA chimeric protein CIL-8M {Human (Homo sapiens)}
sakelrcqciktyskpfhpkfikelrviesgphcanteiivklsdgrelcldpaspivkk
iiekmlnsdksn
>d1huma_ 4.8.1.1.6 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-beta}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1humb_ 4.8.1.1.6 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-beta}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1huna_ 4.8.1.1.6 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-beta}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1hunb_ 4.8.1.1.6 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-beta}
apmgsdpptaccfsytarklprnfvvdyyetsslcsqpavvfqtkrskqvcadpseswvq
eyvydleln
>d1b50a_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b50b_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b53a_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1b53b_ 4.8.1.1.7 Macrophage inflammatory protein, MIP {Human (Homo sapiens), 1-alpha}
slaadtptaccfsytsrqipqnfiaayfetssqcskpgvifltkrsrqvcadpseewvqk
yvsdlelsa
>d1cm9a_ 4.8.1.1.8 Macrophage inflammatory protein, MIP {Kaposi's sarcoma herpes virus-8, VMIP-II}
swhrpdkcclgyqkrplpqvllsswyptsqlcskpgvifltkrgrqvcadkskdwvkklx
qqlpvtar
>d1cm9b_ 4.8.1.1.8 Macrophage inflammatory protein, MIP {Kaposi's sarcoma herpes virus-8, VMIP-II}
whrpdkcclgyqkrplpqvllsswyptsqlcskpgvifltkrgrqvcadkskdwvkklxq
qlpvtar
>d1vmpa_ 4.8.1.1.8 Macrophage inflammatory protein, MIP {Kaposi's sarcoma herpes virus-8, VMIP-II}
lgaswhrpdkcclgyqkrplpqvllsswyptsqlcskpgvifltkrgrqvcadkskdwvk
klmqqlpvtar
>d1b3aa_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
pyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvrey
inslems
>d1b3ab_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
pyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvrey
inslems
>d1hrja_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1hrjb_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1rtna_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1rtnb_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1rtoa_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1rtob_ 4.8.1.1.9 RANTES (regulated upon activation, normal T-cell expressed and secreted) {Human (Homo sapiens)}
spyssdttpccfayiarplprahikeyfytsgkcsnpavvfvtrknrqvcanpekkwvre
yinslems
>d1doka_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dokb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkqt
>d1dol__ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
mqpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkw
vqdsmdhldkq
>d1doma_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1domb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1dona_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1donb_ 4.8.1.1.10 Monocyte chemoattractant protein-1 (MCP-1, MCAF) {Human (Homo sapiens)}
qpdainapvtccynftnrkisvqrlasyrritsskcpkeavifktivakeicadpkqkwv
qdsmdhldkqtqtpkt
>d1eot__ 4.8.1.1.11 Eotaxin {Human (Homo sapiens)}
gpasvpttccfnlanrkiplqrlesyrritsgkcpqkavifktklakdicadpkkkwvqd
smkyldqksptpkp
>d2eot__ 4.8.1.1.11 Eotaxin {Human (Homo sapiens)}
gpasvpttccfnlanrkiplqrlesyrritsgkcpqkavifktklakdicadpkkkwvqd
smkyldqksptpkp
>d1bo0__ 4.8.1.1.12 Monocyte chemoattractant protein-3 (MCP-3) {Human (Homo sapiens)}
qpvgintsttccyrfinkkipkqrlesyrrttsshcpreavifktkldkeicadptqkwv
qdfmkhldkktqtpkl
>d1ncva_ 4.8.1.1.12 Monocyte chemoattractant protein-3 (MCP-3) {Human (Homo sapiens)}
qpvgintsttccyrfinkkipkqrlesyrrttsshcpreavifktkldkeicadptqkwv
qdfmkhldkktqtpkl
>d1ncvb_ 4.8.1.1.12 Monocyte chemoattractant protein-3 (MCP-3) {Human (Homo sapiens)}
qpvgintsttccyrfinkkipkqrlesyrrttsshcpreavifktkldkeicadptqkwv
qdfmkhldkktqtpkl
>d1napa_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
aelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivq
kklagd
>d1napb_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
aelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivq
kklagd
>d1napc_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
rclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivqkkl
agd
>d1napd_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
aelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivq
kklagd
>d1tvxa_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
lrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivqkk
lagd
>d1tvxb_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
dsdlyaelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdapri
kkivqkklagd
>d1tvxc_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
lrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdaprikkivqkk
lagd
>d1tvxd_ 4.8.1.1.14 Neutrophil-activating peptide-2 (NAP-2) {Human (Homo sapiens)}
dsdlyaelrclcikttsgihpkniqslevigkgthcnqveviatlkdgrkicldpdapri
kkivqkklagd
>d1a15a_ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
kpvslsyrcpcrffeshvaranvkhlkilntpacalqivarlknnnrqvcidpklkwiqe
ylekaln
>d1a15b_ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
rcpcrffeshvaranvkhlkilntpacalqivarlknnnrqvcidpklkwiqeylek
>d1sdf__ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
kpvslsyrcpcrffeshvaranvkhlkilntpncalqivarlknnnrqvcidpklkwiqe
ylekaln
>d2sdf__ 4.8.1.1.15 Stromal cell-derived factor-1 (SDF-1) {Human (Homo sapiens)}
kpvslsyrcpcrffeshvaranvkhlkilntpncalqivarlknnnrqvcidpklkwiqe
ylekaln
>d1mi2a_ 4.8.1.1.16 Macrophage inflammatory protein-2 {Mouse (Mus musculus)}
avvaselrcqclktlprvdfkniqslsvtppgphcaqteviatlkggqkvcldpeaplvq
kiiqkilnkgkan
>d1mi2b_ 4.8.1.1.16 Macrophage inflammatory protein-2 {Mouse (Mus musculus)}
avvaselrcqclktlprvdfkniqslsvtppgphcaqteviatlkggqkvcldpeaplvq
kiiqkilnkgkan
>d2hcc__ 4.8.1.1.17 Chemokine hcc-2 (macrophage inflammatory protein-5) {Human (Homo sapiens)}
hfaadcctsyisqsipcslmksyfetssecskpgvifltkkgrqvcakpsgpgvqdcmkk
lkpysi
>d1qnka_ 4.8.1.1.18 Gro beta {Human (Homo sapiens)}
telrcqclqtlqgihlkniqsvkvkspgphcaqteviatlkngqkaclnpaspmvkkiie
kmlkngksn
>d1qnkb_ 4.8.1.1.18 Gro beta {Human (Homo sapiens)}
telrcqclqtlqgihlkniqsvkvkspgphcaqteviatlkngqkaclnpaspmvkkiie
kmlkngksn
>d1b4o__ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisatydegggktgrgavsekdapkellqmlek
qk
>d1bbxc_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bbxd_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bf4a_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekevdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bnza_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
matvkfkykgeekevdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmle
kqkk
>d1jic__ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qk
>d1sso__ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekqvdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qk
>d1azpa_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1azqa_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1ca5a_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
vkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlara
erekk
>d1ca6a_ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1sap__ 4.8.2.1.2 DNA-binding protein {Sulfolobus acidocaldarius, Sac7d}
mvkvkfkykgeekevdtskikkvwrvgkmvsftyddngktgrgavsekdapkelldmlar
aerekk
>d1ap0__ 4.8.2.2.1 Modifier protein 1 (HP1 beta) {Mouse (Mus musculus)}
hmveevleeeeeeyvvekvldrrvvkgkveyllkwkgfsdedntwepeenldcpdliaef
lqsqktahetdks
>d1b69a_ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdaislre
kiaelqkdi
>d1bb8__ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdcislre
kiaelqkdihd
>d1tn9a_ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdaislre
kiaelqkdi
>d2bb8__ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdcislre
kiaelqkdihd
>d1gcca_ 4.9.1.2.1 GCC-box binding domain {Mouse-ear cress (Arabidopsis thaliana)}
khyrgvrqrpwgkfaaeirdpakngarvwlgtfetaedaalaydraafrmrgsrallnfp
lrv
>d2gcc__ 4.9.1.2.1 GCC-box binding domain {Mouse-ear cress (Arabidopsis thaliana)}
khyrgvrqrpwgkfaaeirdpakngarvwlgtfetaedaalaydraafrmrgsrallnfp
lrv
>d3gcc__ 4.9.1.2.1 GCC-box binding domain {Mouse-ear cress (Arabidopsis thaliana)}
khyrgvrqrpwgkfaaeirdpakngarvwlgtfetaedaalaydraafrmrgsrallnfp
lrv
>d1qk9a_ 4.9.1.3.1 Methyl-CpG-binding protein 2, MECP2 {Human (Homo sapiens)}
asaspkqrrsiirdrgpmyddptlpegwtrklkqrksgrsagkydvylinpqgkafrskv
eliayfekvgdtsldpndfdftvtgrgsgsgc
>d1pmd_1 4.10.1.1.1 (620-692) Penicillin-binding protein 2x (pbp-2x), c-terminal domain {Streptococcus pneumoniae}
lqttakaleqvsqqspypmpsvkdispgdlaeelrrnlvqpivvgtgtkiknssaeegkn
lapnqqvlilsdk
>d1pmd_2 4.10.1.1.1 (693-750) Penicillin-binding protein 2x (pbp-2x), c-terminal domain {Streptococcus pneumoniae}
aeevpdmygwtketaetlakwlnielefqgsgstvqkqdvrantaikdikkitltlgd
>d1fit__ 4.11.1.1.2 FHIT (fragile histidine triad protein) {Human (Homo sapiens)}
sfrfgqhlikpsvvflktelsfalvnrkpvvpghvlvcplrpverfhdlrpdevadlfqt
tqrvgtvvekhfhgtsltfsxqdgpeagqtvkhvhvhvlprkagdfhrndsiyeelqkhd
kedfpaswrseeexaaeaaalrvyfq
>d1kpf__ 4.11.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {Human (Homo sapiens)}
dtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesllg
hlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1guqa1 4.11.1.2.1 (2-177) Galactose-1-phosphate uridylyltransferase {Escherichia coli}
tqfnpvdhphrrynpltgqwilvsphrakrpwqgaqetpakqvlpahdpdcflcagnvrv
tgdknpdytgtyvftndfaalmsdtpdapeshdplmrcqsargtsrvicfspdhsktlpe
lsvaalteivktwqeqtaelgktypwvqvfenkgaamgcsnphpggqiwansflpn
>d1guqa2 4.11.1.2.1 (178-348) Galactose-1-phosphate uridylyltransferase {Escherichia coli}
eaeredrlqkeyfaeqkspmlvdyvqreladgsrtvvetehwlavvpywaawpfetlllp
kahvlritdltdaqrsdlalalkkltsrydnlfqcsfpysmgwhgapfngeenqhwqlha
hfyppllrsatvrkfmvgyemlaetqrdltaeqaaerlravsdihfresgv
>d1dar_3 4.12.1.1.1 (476-599) Elongation factor G (EF-G), domain IV {Thermus thermophilus}
vgkpqvayretitkpvdvegkfirqtggrgqyghvkikveplprgsgfefvnaivggvip
keyipavqkgieeamqsgpligfpvvdikvtlydgsyhevdssemafkiagsmaikeavq
kgdp
>d1pkp_1 4.12.1.1.2 (78-148) Ribosomal S5 protein, C-terminal domain {Bacillus stearothermophilus}
gttiphevighfgageiilkpasegtgviaggparavlelagisdilsksigsntpinmv
ratfdglkqlk
>d1a6f__ 4.12.1.2.1 RNase P protein {Bacillus subtilis}
ahlkkrnrlkknedfqkvfkhgtsvanrqfvlytldqpendelrvglsvskkignavmrn
rikrlirqafleekerlkekdyiiiarkpasqltyeetkkslqhlfrksslyk
>d1b63a1 4.12.1.3.1 (217-331) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlq
>d1fccc_ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
ttyklvingktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1gb1__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1gb4__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mttfkliingktlkgeitieavdaaeaekifkqyandngidgewtyddatktftvte
>d1igca_ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
avttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvte
>d1igd__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtpavttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvt
e
>d1pga__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1pgb__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d1pgx__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
eltpavttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftv
temvtevpva
>d1qkza_ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
vttyklvingktlkgetttkavdaataekvfkqyandngvdgewtyddatktftvtek
>d2gb1__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d2igd__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtpavttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvt
e
>d2igg__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
ltpavttyklvingktlkgettteavdaataekvfkqyandngvdgewtyddatktftvt
ekpe
>d2igh__ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
ltpavttyklvingktlkgetttkavdaetaekafkqyandngvdgvwtyddatktftvt
e
>d3gb1a_ 4.13.1.1.1 Immunoglobulin-binding protein G, different constituent domains {Group G Streptococcus)}
mtyklilngktlkgettteavdaataekvfkqyandngvdgewtyddatktftvte
>d2ptl__ 4.13.1.1.2 Immunoglobulin light chain-binding domain of protein L {Peptostreptococcus magnus}
enkeetpetpetdseeevtikanlifangstqtaefkgtfekatseayayadtlkkdnge
ytvdvadkgytlnikfag
>d1aara_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aarb_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1c3ta_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqlfvktltgktltvelepsdtvenlkakiqdkegippdqqrlifagkqledgrtlsdyn
lqkestihlvlrlrgg
>d1d3za_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1tbea_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1tbeb_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlr
>d1ubi__ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1ubq__ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1ud7a_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqvflktltgktvtievepsdtvenfkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestihlvlrlrgg
>d1cmxb_ 4.13.2.1.2 Ubiquitin {Synthetic, based on Saccharomyces cerevisiae sequence}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrg
>d1a5r__ 4.13.2.1.3 SUMO-1 {Human (Homo sapiens)}
gsmsdqeakpstedlgdkkegeyiklkvigqdsseihfkvkmtthlkklkesycqrqgvp
mnslrflfegqriadnhtpkelgmeeedvievyqeqtgghstv
>d1ndda_ 4.13.2.1.4 Nedd8 {Human (Homo sapiens)}
mlikvktltgkeieidieptdkverikerveekegippqqqrliysgkqmndektaadyk
ilggsvlhlvlalr
>d1nddb_ 4.13.2.1.4 Nedd8 {Human (Homo sapiens)}
mlikvktltgkeieidieptdkverikerveekegippqqqrliysgkqmndektaadyk
ilggsvlhlvlalrgg
>d1nddc_ 4.13.2.1.4 Nedd8 {Human (Homo sapiens)}
mlikvktltgkeieidieptdkverikerveekegippqqqrliysgkqmndektaadyk
ilggsvlhlvlal
>d1nddd_ 4.13.2.1.4 Nedd8 {Human (Homo sapiens)}
mlikvktltgkeieidieptdkverikerveekegippqqqrliysgkqmndektaadyk
ilggsvlhlvlal
>d1vcba_ 4.13.2.1.5 Elongin B {Human (Homo sapiens)}
mdvflmirrhkttiftdakesstvfelkrivegilkrppdeqrlykddqllddgktlgec
gftsqtarpqapatvglafraddtfealciepfssppe
>d1bt0a_ 4.13.2.1.6 Rub1 {Mouse-ear cress (Arabidopsis thaliana)}
mlikvktltgkeieidieptdtidrikerveekegippvqqrliyagkqladdktakdyn
ieggsvlhlvlal
>d1c1yb_ 4.13.3.1.1 c-Raf1 RBD {Human (Homo sapiens)}
sntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllhehkgkkarldw
ntdaasligeelqvdfl
>d1guab_ 4.13.3.1.1 c-Raf1 RBD {Human (Homo sapiens)}
ntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllhehkgkkarldwn
tdaasligeelqvdfl
>d1rfa__ 4.13.3.1.1 c-Raf1 RBD {Human (Homo sapiens)}
sntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllhehkgkkarldw
ntdaasligeelqvdfld
>d1rrb__ 4.13.3.1.2 c-Raf1 RBD {Rat (Rattus norvegicus)}
ntirvflpnkqrtvvnvrngmslhdclmkalkvrglqpeccavfrllqehkgkkarldwn
tdaasligeelqvdfl
>d1lfda_ 4.13.3.1.3 Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1lfdc_ 4.13.3.1.3 Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1lxda_ 4.13.3.1.3 Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1lxdb_ 4.13.3.1.3 Ral guanosine-nucleotide exchange factor, RalGDS {Rat (Rattus norvegicus)}
gdcciirvsldvdngnmyksilvtsqdkaptvirkamdkhnldedepedyellqiisedh
klkipenanvfyamnsaanydfilkkr
>d1raxa_ 4.13.3.1.4 Ral guanosine-nucleotide exchange factor, RalGDS {Human (Homo sapiens)}
qqvgdcciirvsldvdngnmyksilvtsqdkapavirkamdkhnleeeepedyellqils
ddrklkipenanvfyamnstanydfvlkkrtft
>d2rgf__ 4.13.3.1.4 Ral guanosine-nucleotide exchange factor, RalGDS {Human (Homo sapiens)}
alplynqqvgdcciirvsldvdngnmyksilvtsqdkapavirkamdkhnleeeepedye
llqilsddrklkipenanvfyamnstanydfvlkkrt
>d1rlf__ 4.13.3.1.5 RalGDS-like factor, Rlf {Mouse (Mus musculus)}
gssdcriirvqmelgedgsvyksilvtsqdkapsvisrvlkknnrdsavasefelvqllp
gdreltiphsanvfyamdgashdfllrqrr
>d1ef5a_ 4.13.3.1.6 Rgl {Mouse (Mus musculus)}
edtciirisvednngnmyksimltsqdktpaviqramskhnlesdpaeeyelvqvisedk
elvipdsanvfyamnsqvnfdfilrkkn
>d1d4ba_ 4.13.4.1.1 Cell death-inducing effector B (CIDE-B), N-terminal domain {Human (Homo sapiens)}
meylsalnpsdllrsvsnissefgrrvwtsapppqrpfrvcdhkrtirkgltaatrqell
akaletlllngvltlvleedgtavdsedffqlleddtclmvlqsgqswsptrsgvlhhhh
hh
>d1c9fa_ 4.13.4.1.2 Caspase-activated DNase, N-terminal domain {Mouse (Mus musculus)}
mcavlrqpkcvklralhsackfgvaarscqellrkgcvrfqlpmpgsrlclyedgtevtd
dcfpglpndaelllltagetwhgyvsd
>d2sak__ 4.13.5.1.1 Staphylokinase {Staphylococcus aureus, sakstar variant}
syfeptgpylmvnvtgvdskgnellsphyvefpikpgttltkekieyyvewaldatayke
frvveldpsakievtyydknkkkeetksfpitekgfvvpdlsehiknpgfnlitkvviek
k
>d1bmlc1 4.13.5.1.2 (12-148) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
svnnsqlvvsvagtvegtnqdislkffeidltsrpahggkteqglspkskpfatdsgamp
hklekadllkaiqeqlianvhsnddyfevidfasdatitdrngkvyfadkdgsvtlptqp
vqefllsghvrvrpyke
>d1bmlc3 4.13.5.1.2 (285-372) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
dpfdrshlklftikyvdvntnellkseqlltasernldfrdlydprdkakllynnldafg
imdytltgkvednhddtnriitvymgkr
>d1bmld3 4.13.5.1.2 (285-372) Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
dpfdrshlklftikyvdvntnellkseqlltasernldfrdlydprdkakllynnldafg
imdytltgkvednhddtnriitvymgkr
>d1qqra_ 4.13.5.1.2 Streptokinase {Streptoccocal bacteria (Streptococcus equisimilis)}
iqnqaksvdveytvqftplnpdddfrpglkltkllktlaigdtitsqellaqaqsilnkn
hpgytiyerdssivthdndifrtilpmdqeftyrvknreqayrinkksglneeinntdli
sekyyvlkkgekpydpfd
>d1czpa_ 4.13.6.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena) pcc7119}
atfkvtlineaegtkheievpddeyildaaeeqgydlpfscragacstcagklvsgtvdq
sdqsfldddqieagyvltcvayptsdvviqthkeedly
>d1frd__ 4.13.6.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena) pcc7119}
asyqvrlinkkqdidttieideettildgaeengielpfschsgscsscvgkvvegevdq
sdqiflddeqmgkgfallcvtyprsnctikthqepyla
>d1qoc__ 4.13.6.1.1 2Fe-2S ferredoxin {Cyanobacterium (Anabaena) pcc7119}
atfkvtlineaegtkheievpddeyildaaeeqgydlpfscragacstcagklvsgtvdq
edqsfldkdqieagyvltcvayptsdvviqthkeadly
>d4fxc__ 4.13.6.1.2 2Fe-2S ferredoxin {Spirulina platensis}
atykvtlineaeginetidcdddtyildaaeeagldlpyscragacstcagtitsgtidq
sdqsfldddqieagyvltcvayptsdctikthqeegly
>d1fxia_ 4.13.6.1.3 2Fe-2S ferredoxin {Cyanobacterium (Aphanothece sacrum)}
asykvtlktpdgdnvitvpddeyildvaeeegldlpyscragacstcagklvsgpapded
qsfldddqiqagyiltcvayptgdcviethkeealy
>d1dox__ 4.13.6.1.4 2Fe-2S ferredoxin {Synechocystis PCC 6803}
asytvklitpdgessiecsddtyildaaeeagldlpyscragacstcagkitagsvdqsd
qsfldddqieagyvltcvayptsdctiethkeedly
>d2cjn__ 4.13.6.1.5 2Fe-2S ferredoxin {Synechococcus elongatus}
atykvtlvrpdgsettidvpedeyildvaeeqgldlpfscragacstcagkllegevdqs
dqsfldddqiekgfvltcvayprsdckiltnqeeely
>d1awd__ 4.13.6.1.6 2Fe-2S ferredoxin {Chlorella fusca}
ykvtlktpsgeetiecpedtyildaaeeagldlpyscragacsscagkvesgevdqsdqs
flddaqmgkgfvltcvayptsdvtilthqeaaly
>d1frra_ 4.13.6.1.7 2Fe-2S ferredoxin {Equisetum arvense}
ayktvlktpsgeftldvpegttildaaeeagydlpfscragacssclgkvvsgsvdeseg
sflddgqmeegfvltciaipesdlviethkeeelf
>d1frrb_ 4.13.6.1.7 2Fe-2S ferredoxin {Equisetum arvense}
ayktvlktpsgeftldvpegttildaaeeagydlpfscragacssclgkvvsgsvdeseg
sflddgqmeegfvltciaipesdlviethkeeelf
>d1doi__ 4.13.6.1.8 2Fe-2S ferredoxin {Haloarcula marismortui}
ptveylnyevvddngwdmydddvfgeasdmdlddedygslevnegeyileaaeaqgydwp
fscragacancaaivlegdidmdmqqilsdeevedknvrltcigspdadevkivynakhl
dylqnrvi
>d1pfd__ 4.13.6.1.9 2Fe-2S ferredoxin {Parsley (Petroselinum crispum)}
atynvklitpdgevefkcdddvyvldqaeeegidipyscragscsscagkvvsgsidqsd
qsflddeqmdagyvltchayptsdvviethkeeeiv
>d1a70__ 4.13.6.1.10 2Fe-2S ferredoxin {Spinach (Spinacia oleracea)}
aaykvtlvtptgnvefqcpddvyildaaeeegidlpyscragscsscagklktgslnqdd
qsfldddqidegwvltcaaypvsdvtiethkkeelta
>d1put__ 4.13.6.1.11 Putidaredoxin {Pseudomonas putida}
skvvyvshdgtrrqldvadgvslmqaavsngiydivgdcggsascatchvyvneaftdkv
paanereigmlecvtaelkpnsrlccqiimtpeldgivvdvpdrqw
>d1b9ra_ 4.13.6.1.12 Terpredoxin {Pseudomonas}
prvvfideqsgeyavdaqdgqslmevatqngvpgivaecggscvcatcrieiedawveiv
geanpdendllqstgepmtagtrlscqvfidpsmdglivrvplpa
>d1ayfa_ 4.13.6.1.13 Adrenodoxin {Bovine (Bos taurus)}
kitvhfinrdgetlttkgkigdslldvvvqnnldidgfgacegtlacstchlifeqhife
kleaitdeendmldlaygltdrsrlgcqicltkamdnmtvrvp
>d1feha2 4.13.6.2.1 (1-126) Fe-only hydrogenase, N-terminal domain {Clostridium pasteurianum}
mktiiingvqfntdedttilkfardnnidisalcflnncnndinkceictvevegtglvt
acdtliedgmiintnsdavnekiksrisqlldihefkcgpcnrrenceflklvikykara
skpflp
>d1alo_2 4.13.6.2.2 (1-80) Aldehyde oxidoreductase, N-terminal domain {Desulfovibrio gigas}
miqkvitvngieqnlfvdaeallsdvlrqqlgltgvkvgceqgqcgacsvildgkvvrac
vtkmkrvadgaqittiegvg
>d1qj2a2 4.13.6.2.3 (3-81) Carbone monoxide (CO) dehydrogenase iron-sulfur protein, N-domain {Pseudomonas carboxydovorans}
kahieltinghpvealveprtllihfireqqnltgahigcdtshcgactvdldgmsvksc
tmfavqangasittiegma
>d1qj2g2 4.13.6.2.3 (3-81) Carbone monoxide (CO) dehydrogenase iron-sulfur protein, N-domain {Pseudomonas carboxydovorans}
kahieltinghpvealveprtllihfireqqnltgahigcdtshcgactvdldgmsvksc
tmfavqangasittiegma
>d2pia_3 4.13.6.2.4 (224-321) Phthalate dioxygenase reductase, C-terminal domain {Pseudomonas cepacia, db01}
sfgatntnarentpftvrlsrsgtsfeipanrsilevlrdanvrvpsscesgtcgsckta
lcsgeadhrdmvlrddekgtqimvcvsraksaelvldl
>d1fumb_ 4.13.6.2.5 Fumarate reductase iron-sulfur protein {Escherichia coli}
aemknlkievvrynpevdtaphsafyevpydattslldalgyikdnlapdlsyrwscrma
icgscgmmvnnvpklacktflrdytdgmkvealanfpierdlvvdmthfiesleaikpyi
ignsrtadqgtniqtpaqmakyhqfsgcincglcyaacpqfglnpefigpaaitlahryn
edsrdhgkkermaqlnsqngvwsctfvgycsevcpkhvdpaaaiqqgkvesskdfliatl
kpr
>d1qlab_ 4.13.6.2.6 Fumarate reductase iron-sulfur protein {Wolinella succinogenes}
mgrmltirvfkydpqsavskphfqeykieeapsmtifivlnmiretydpdlnfdfvcrag
icgscgmmingrpslacrtltkdfedgvitllplpafklikdlsvdtgnwfngmsqrves
wihaqkehdiskleeriepevaqevfeldrciecgcciaacgtkimredfvgaaglnrvv
rfmidphdertdedyyeligdddgvfgcmtllachdvcpknlplqskiaylrrkmvsvn
>d1esfa2 4.13.7.1.1 (121-233) Staphylococcal enterotoxin A, SEA {Staphylococcus aureus}
eekkvpinlwldgkqntvpletvktnkknvtvqeldlqarrylqekynlynsdvfdgkvq
rglivfhtstepsvnydlfgaqgqysntllriyrdnktinsenmhidiylyts
>d1ste_2 4.13.7.1.2 (121-238) Staphylococcal enterotoxin C2, SEC2 {Staphylococcus aureus}
nhfdngnlqnvlirvyenkrntisfevqtdkksvtaqeldikarnflinkknlyefnssp
yetgyikfienngntfwydmmpapgdkfdqskylmmyndnktvdsksvkievhlttkn
>d3tss_2 4.13.7.1.3 (94-194) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfkirhqltqthglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d3seb_2 4.13.7.1.4 (122-238) Staphylococcal enterotoxin B, SEB {Staphylococcus aureus}
ngnqldkyrsitvrvfedgknllsfdvqtnkkkvtaqeldyltrhylvknkklyefnnsp
yetgyikfienensfwydmmpapgdkfdqskylmmyndnkmvdskdvkievylttkk
>d1an8_2 4.13.7.1.6 (96-208) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
nkvnhkllgnlfisgesqqnlnnkiilekdivtfqeidfkirkylmdnykiydatspyvs
grieigtkdgkheqidlfdspnegtrsdifakykdnriinmknfshfdiylek
>d1bxta2 4.13.7.1.7 (120-234) Streptococcal superantigen SSA {Streptococcus pyogenes}
qiegkfpnitvkvyednenilsfdittnkkqvtvqeldcktrkilvsrknlyefnnspye
tgyikfiessgdsfwydmmpapgaifdqskylmlyndnktvsssaiaievhltkk
>d1b1za2 4.13.7.1.8 (108-220) Streptococcal pyrogenic exotoxin A1 {Streptococcus pyogenes}
gnhleipkkivvkvsidgiqslsfdietnkkmvtaqeldykvrkyltdnkqlytngpsky
etgyikfipknkesfwfdffpepeftqskylmiykdnetldsntsqievyltt
>d1tif__ 4.13.8.1.1 Translation initiation factor IF3, N-terminal domain {Bacillus stearothermophilus}
kdfiineqirarevrlidqngdqlgikskqealeiaarrnldlvlvapnakppvcrimdy
gkfrfeqqkkekeark
>d1lgr_1 4.13.9.1.1 (1-100) Glutamine synthetase, N-terminal domain {Salmonella typhimurium}
saehvltmlnehevkfvdlrftdtkgkeqhvtipahqvnaeffeegkmfdgssiggwkgi
nesdmvlmpdastavidpffadstliircdilepgtlqgy
>d1coy_2 4.14.1.1.1 (319-450) Cholesterol oxidase {Brevibacterium sterolicum}
gnngnimvgranhmwdatgskqatiptmgidnwadptapifaeiaplpagletyvslyla
itknperarfqfnsgtgkvdltwaqsqnqkgidmakkvfdkinqkegtiyrtdlfgvyyk
twgddftyhplg
>d1b4va2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaeiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyhplg
>d1pbe_2 4.14.1.2.1 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas fluorescens}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1foha4 4.14.1.2.3 (241-341) Phenol hydroxylase {Soil-living yeast (Trichosporon cutaneum)}
geqtdyiwgvldavpasnfpdirsrcaihsaesgsimiiprennlvrfyvqlqaraekgg
rvdrtkftpevvianakkifhpytfdvqqldwftayhigqr
>d1an9a2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1b3ma2 4.14.1.3.2 (218-321) Sarcosine oxidase {Bacillus sp.}
qlpyrqvvgffesdeskysndidfpgfmvevpngiyygfpsfggcglklgyhtfgqkidp
dtinrefgvypedesnlrafleeympgangelkrgavcmytktl
>d1gpea2 4.14.1.4.2 (329-524) Glucose oxidase {Penicillium amagasakiense}
nmqdqttttvssrassagagqgqavffanftetfgdyapqardllntkldqwaeetvarg
gfhnvtalkvqyenyrnwlldedvafaelfmdtegkinfdlwdlipftrgsvhilssdpy
lwqfandpkfflnefdllgqaaasklardltsqgamkeyfagetlpgynlvqnatlsqws
dyvlqnfrpnwhavss
>d1b37a2 4.14.1.5.1 (294-405) Polyamine oxidase {Maize (Zea mays)}
dmavytkiflkfprkfwpegkgrefflyassrrgyygvwqefekqypdanvllvtvtdee
srrieqqsdeqtkaeimqvlrkmfpgkdvpdatdilvprwwsdrfykgtfsn
>d1gnd_2 4.14.1.6.1 (292-388) Guanine nucleotide dissosiation inhibitor, GDI {Bovine (Bos taurus)}
rkagqviriicilshpikntndanscqiiipqnqvnrksdiyvcmisyahnvaaqgkyia
iasttvettdpekevepalellepidqkfvaisdlye
>d1mnl__ 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyenereikgyeyql
yvyasdklfradisedyktrgrkllrfngpv
>d1mola_ 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyenereikgyeyql
yvyasdklfradisedyktrgrkllrfngpvppp
>e3mon.1a 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e3mon.1b 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>e3mon.2c 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e3mon.2d 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>e3mon.3e 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e3mon.3f 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>e3mon.4g 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e3mon.4h 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>e4mon.1a 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e4mon.1b 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>e4mon.2c 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
reikgyeyqlyvyasdklfradisedyktrgrkllrfngpvppp
>e4mon.2d 4.15.1.1.1 Monellin, B & A chains together {Serendipity berry (Dioscoreophyllum cumminsii diels)}
geweiidigpftqnlgkfavdeenkigqygrltfnkvirpcmkktiyene
>d1cewi_ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1dvd__ 4.15.1.2.2 Cystatin A (stefin A) {Human (Homo sapiens)}
mipgglseakpatpeiqeivdkvkpqleektnetygkleavqyktqvvagtnyyikvrag
dnkymhlkvfkslpgqnedlvltgyqvdknkddeltgf
>d1stfi_ 4.15.1.2.3 Cystatin B (stefin B) {Human (Homo sapiens)}
mmsgapsatqpataetqhiadqvrsqleekynkkfpvfkavsfksqvvagtnyfikvhvg
dedfvhlrvfqslphenkpltlsnyqtnkakhdeltyf
>d1d6ua2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1d6ub2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1d6ya2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1d6yb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1d6za2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1d6zb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1oaca2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1oaca3 4.15.2.1.1 (186-300) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
mvllddfasvqniinnseefaaavkkrgitdakkvittpltvgyfdgkdglkqdarllkv
isyldvgdgnywahpienlvavvdleqkkivkieegpvvpvpmtarpfdgrdrva
>d1oacb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qafa2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qafb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qaka2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qakb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qala2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1qalb2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1spua2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1spub2 4.15.2.1.1 (91-185) Copper amine oxidase, domains 1 and 2 {Escherichia coli}
krphplnaltadeikqaveivkasadfkpntrfteisllppdkeavwafalenkpvdqpr
kadvimldgkhiieavvdlqnnkllswqpikdahg
>d1ksia2 4.15.2.1.2 (6-98) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
vqhpldpltkeeflavqtivqnkypisnnrlafhyiglddpekdhvlryethptlvsipr
kifvvaiinsqtheilinlrirsivsdnihngy
>d1ksia3 4.15.2.1.2 (99-206) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
gfpilsvdeqslaiklplkyppfidsvkkrglnlseivcssftmgwfgeeknvrtvrldc
fmkestvniyvrpitgitivadldlmkiveyhdrdieavptaenteyq
>d1ksib2 4.15.2.1.2 (6-98) Copper amine oxidase, domains 1 and 2 {Pea seedling (Pivum sativum)}
vqhpldpltkeeflavqtivqnkypisnnrlafhyiglddpekdhvlryethptlvsipr
kifvvaiinsqtheilinlrirsivsdnihngy
>d1av4_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1av4_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avk_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avl_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1a2va2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2va3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d3stda_ 4.15.3.1.1 Scytalone dehydratase {Fungus (Magnaporthe grisea)}
geitfsdylglmtcvyewadsydskdwdrlrkviaptlridyrsfldklweampaeefvg
mvsskqvlgdptlrtqhfiggtrwekvsedevigyhqlrvphqrykdttmkevtmkghah
sanlhwykkidgvwkfaglkpdirwgefdfdrifedgretfg
>d1ouna_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpf
qkiqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1qjga_ 4.15.3.3.1 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {Comamonas testosteroni (Pseudomonas testosteroni)}
mntpehmtavvqryvaalnagdldgivalfaddatvenpvgseprsgtaairefyanslk
lplaveltqevravaneaafafivsfeyqgrktvvapidhfrfngagkvvsmralfgekn
ihaga
>d1opy__ 4.15.3.3.2 Delta-5-3-ketosteroid isomerase, steroid delta-isomerase, KSI {Pseudomonas putida}
nlptaqevqglmaryielvdvgdieaivqmyaddatvedpfgqppihgreqiaafyrqgl
gggkvracltgpvrashngcgampfrvemvwngqpcaldvidvmrfdehgriqtmqayws
evnlsv
>d1ndob_ 4.15.3.4.1 Napthalene 1,2-dioxygenase beta subunit {Pseudomonas putida}
miniqedklvsahdaeeilrffnchdsalqqeattlltqeahlldiqayrawlehcvgse
vqyqvisrelraaserryklneamnvynenfqqlkvrvehqldpqnwgnspklrftrfit
nvqaamdvndkellhirsnvilhrarrgnqvdvfyaaredkwkrgeggvrklvqrfvdyp
erilqthnlmvfl
>d1udii_ 4.15.4.1.1 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs1}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1euic_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
qlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsdapeykpwalviqd
sngenkikml
>d1euid_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
qlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsdapeykpwalviqd
sngenkikml
>d1ughi_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d1ugia_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugib_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugic_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugid_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d1ugie_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugif_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugig_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1ugih_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d1uugb_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d1uugd_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d2ugia_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d2ugib_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
tnlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsd
apeykpwalviqdsngenkikml
>d2uugc_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d2uugd_ 4.15.4.1.2 Uracil-DNA glycosylase inhibitor protein {Bacteriophage pbs2}
nlsdiieketgkqlviqesilmlpeeveevignkpesdilvhtaydestdenvmlltsda
peykpwalviqdsngenkikml
>d1pcfa_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfb_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfc_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfd_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfe_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcff_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfg_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d1pcfh_ 4.16.1.1.1 Transcriptional coactivator PC4 C-terminal domain {Human (Homo sapiens)}
amfqigkmryvsvrdfkgkvlidireywmdpegemkpgrkgislnpeqwsqlkeqisdid
davrkl
>d3frua2 4.17.1.1.1 (1-178) Fc (IgG) receptor, alpha-1 and alpha-2 domains {Rat (Rattus norvegicus)}
aeprlplmyhlaavsdlstglpsfwatgwlgaqqyltynnlrqeadpcgawiwenqvswy
wekettdlkskeqlfleairtlenqingtftlqgllgcelapdnsslptavfalngeefm
rfnprtgnwsgewpetdivgnlwmkqpeaarkeseflltscperllghlergrqnlew
>d1cd1a2 4.17.1.1.2 (7-185) CD1, alpha-1 and alpha-2 domains {Mouse (Mus musculus)}
nytfrclqmssfanrswsrtdsvvwlgdlqthrwsndsatisftkpwsqgklsnqqwekl
qhmfqvyrvsftrdiqelvkmmspkedypieiqlsagcemypgnasesflhvafqgkyvv
rfwgtswqtvpgapswldlpikvlnadqgtsatvqmllndtcplfvrglleagksdlek
>d1hdma2 4.17.1.1.3 (13-93) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dm}
lqnhtflhtvycqdgspsvglseaydedqlfffdfsqntrvprlpefadwaqeqgdailf
dkefcewmiqqipkldgkipv
>d1hdmb2 4.17.1.1.3 (3-87) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dm}
fvahvestcllddagtpkdftycisfnkdlltcwdpeenkmapcnslanvlsqhlnqkdt
lmqrlnglqncathtqpfwgsltnr
>d1aqda2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdb2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdd2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqde2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdg2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdh2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdj2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdk2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1dlha2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhb2 4.17.1.1.4 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1dlhd2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1dlhe2 4.17.1.1.4 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
trprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywn
sqkdlleqrraavdtycrhnygvgesftvq
>d1seba2 4.17.1.1.4 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
ikeehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgal
aniavdkanleimtkrsnytp
>d1sebb2 4.17.1.1.4 (1-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
gdtrprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaey
wnsqkdlleqrraavdtycrhnygvgesftvq
>d1sebe2 4.17.1.1.4 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
ikeehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgal
aniavdkanleimtkrsnytp
>d2seba2 4.17.1.1.4 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
ikeehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgal
aniavdkanleimtkrsnytp
>d2sebb2 4.17.1.1.4 (2-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
dtrprfleqvkhechffngtervrfldryfyhqeeyvrfdsdvgeyravtelgrpdaeyw
nsqkdlleqkraavdtycrhnygvgesftvq
>d1bx2a2 4.17.1.1.5 (2-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
keehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgala
niavdkanleimtkrsnytp
>d1bx2b2 4.17.1.1.5 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
trprflwqpkrechffngtervrfldryfynqeesvrfdsdvgefravtelgrpdaeywn
sqkdileqaraavdtycrhnygvvesftvq
>d1bx2d2 4.17.1.1.5 (2-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
keehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgala
niavdkanleimtkrsnytp
>d1bx2e2 4.17.1.1.5 (3-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr2}
trprflwqpkrechffngtervrfldryfynqeesvrfdsdvgefravtelgrpdaeywn
sqkdileqaraavdtycrhnygvvesftvq
>d1a6aa2 4.17.1.1.6 (5-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
hviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalania
vdkanleimtkrsnytp
>d1a6ab2 4.17.1.1.6 (5-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
prfleystsechffngtervryldryfhnqeenvrfdsdvgefravtelgrpdaeywnsq
kdlleqkrgrvdnycrhnygvvesftvq
>d1iaka2 4.17.1.1.7 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA i-ak}
ieadhvgsygitvyqspgdigqytfefdgdelfyvdldkketvwmlpefaqlrrfepqgg
lqniatgkhnleiltkrsnstp
>d1iakb2 4.17.1.1.7 (5-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA i-ak}
gsfvhqfqpfcyftngtqrirlviryiynreeyvrfdsdvgeyravtelgrpdaeywnkq
ylertraeldtvcrhnyektetptslr
>d1d9kc2 4.17.1.1.8 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AK}
ieadhvgsygitvyqspgdigqytfefdgdelfyvdldkketvwmlpefaqlrrfepqgg
lqniatgkhnleiltkrsnstp
>d1d9kd2 4.17.1.1.8 (2-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AK}
gserhfvhqfqpfcyftngtqrirlviryiynreeyvrfdsdvgeyravtelgrpdaeyw
nkqylertraeldtvcrhnyektetptslr
>d1d9kg2 4.17.1.1.8 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AK}
ieadhvgsygitvyqspgdigqytfefdgdelfyvdldkketvwmlpefaqlrrfepqgg
lqniatgkhnleiltkrsnstp
>d1d9kh2 4.17.1.1.8 (2-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AK}
gserhfvhqfqpfcyftngtqrirlviryiynreeyvrfdsdvgeyravtelgrpdaeyw
nkqylertraeldtvcrhnyektetptslr
>d1ieaa2 4.17.1.1.9 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1ieab2 4.17.1.1.9 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1ieac2 4.17.1.1.9 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iead2 4.17.1.1.9 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1ieba2 4.17.1.1.9 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iebb2 4.17.1.1.9 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1iebc2 4.17.1.1.9 (1-81) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
ikeehtiiqaefyllpdkrgefmfdfdgdeifhvdieksetiwrleefakfasfeaqgal
aniavdkanldvmkersnntp
>d1iebd2 4.17.1.1.9 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-EK}
rpwfleycksechfyngtqrvrllvryfynleenlrfdsdvgefravtelgrpdaenwns
qpefleqkraevdtvcrhnyeifdnflvp
>d1iaoa2 4.17.1.1.10 (1-82) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AD}
eadhvgfygttvyqspgdigqythefdgdelfyvdldkkktvwrlpefgqlilfepqggl
qniaaekhnlgiltkrsnftpa
>d1iaob2 4.17.1.1.10 (6-93) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AD}
hfvvqfkgecyytngtqrirlvtryiynreeyvrydsdvgeyravtelgrpdaeywnsqp
eildrtraevdtacrhnyegpetstslr
>d2iada2 4.17.1.1.10 (1a-82) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AD}
ieadhvgfygttvyqspgdigqythefdgdelfyvdldkkktvwrlpefgqlilfepqgg
lqniaaekhnlgiltkrsnftpa
>d2iadb2 4.17.1.1.10 (6-93) MHC class II, N-terminal domains of alpha and beta chains {Mouse I-AD}
hfvvqfkgecyytngtqrirlvtryiynreeyvrydsdvgeyravtelgrpdaeywnsqp
eilertraevdtacrhnyegpetstslr
>d1duza2 4.17.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1de4a2 4.17.1.1.20 (4-181) MHC class I, alpha-1 and alpha-2 domains {Human (Homo sapiens), hemochromatosis protein Hfe}
rshslhylfmgaseqdlglslfealgyvddqlfvfydhesrrveprtpwvssrissqmwl
qlsqslkgwdhmftvdfwtimenhnhskeshtlqvilgcemqednstegywkygydgqdh
lefcpdtldwraaeprawptklewerhkirarqnraylerdcpaqlqqllelgrgvld
>d1zaga2 4.17.1.1.26 (5-183) Zinc-alpha-2-glycoprotein, ZAG {Human (Homo sapiens)}
dgrysltyiytglskhvedvpafqalgslndlqffrynskdrksqpmglwrqvegmedwk
qdsqlqkaredifmetlkdiveyyndsngshvlqgrfgceiennrssgafwkyyydgkdy
iefnkeipawvpfdpaaqitkqkweaepvyvqrakayleeecpatlrkylkysknildr
>d1b3ja2 4.17.1.1.27 (1-180) MHC I homolog Mic-a {Human (Homo sapiens)}
ephslrynltvlswdgsvqsgfltevhldgqpflrcdrqkcrakpqgqwaedvlgnktwd
retrdltgngkdlrmtlahikdqkeglhslqeirvceihednstrssqhfyydgelflsq
nletkewtmpqssraqtlamnvrnflkedamktkthyhamhadclqelrrylksgvvlrr
>d1c16a2 4.17.1.1.28 (1-180) MHC I homolog Mic-a {Mouse (Mus musculus) t22}
gshslryfytavsrpglgepwfiivgyvddmqvlrfsskeetprmapwleqeeadnweqq
trivtiqgqlsernlmtlvhfynksmddshtlqwlqgcdvepdrhlclwynqlaydsedl
ptlnenpssctvgnstvphisqdlkshcsdllqkylekgkerll
>d2aak__ 4.18.1.1.1 Ubiquitin conjugating enzyme {Arabidopsis thaliana}
mstparkrlmrdfkrlqqdppagisgapqdnnimlwnavifgpddtpwdggtfklslqfs
edypnkpptvrfvsrmfhpniyadgsicldilqnqwspiydvaailtsiqsllcdpnpns
panseaarmyseskreynrrvrdvveqswt
>d1qcqa_ 4.18.1.1.3 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc4}
mssskriakelsdlerdpptscsagpvgddlyhwqasimgpadspyaggvfflsihfptd
ypfkppkisfttkiyhpninangnicldilkdqwspaltlskvllsicslltdanpddpl
vpeiahiyktdrpkyeatarewtkkyav
>d2ucz__ 4.18.1.1.4 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc7}
sktaqkrllkelqqlikdsppgivagpksennifiwdcliqgppdtpyadgvfnaklefp
kdyplsppkltftpsilhpniypngevcisilhspgddpnmyelaeerwspvqsvekill
svmsmlsepniesganidacilwrdnrpeferqvklsilkslgf
>d1u9aa_ 4.18.1.1.5 Ubiquitin conjugating enzyme {Human/mouse (Homo sapiens/Mus musculus), ubc9}
lnmsgialsrlaqerkawrkdhpfgfvavptknpdgtmnlmnwecaipgkkgtpwegglf
klrmlfkddypssppkckfepplfhpnvypsgtvclsileedkdwrpaitikqillgiqe
llnepniqdpaqaeaytiycqnrveyekrvraqakkfaps
>d1c4zd_ 4.18.1.1.6 Ubiquitin conjugating enzyme {Human (Homo sapiens), ubch7}
srrlmkeleeirkcgmknfrniqvdeanlltwqglivpdnppydkgafrieinfpaeypf
kppkitfktkiyhpnidekgqvclpvisaenwkpatktdqviqslialvndpqpehplra
dlaeeyskdrkkfcknaeeftkky
>d2e2c__ 4.18.1.1.7 Ubiquitin conjugating enzyme {Clam (Spisula solidissima), E-2C}
mttskerhsvskrlqqelrtllmsgdpgitafpdgdnlfkwvatldgpkdtvyeslkykl
tlefpsdypykppvvkfttpcwhpnvdqsgnicldilkenwtasydvrtillslqsllge
pnnasplnaqaadmwsnqteykkvlhekyktaqsdk
>d1bwza1 4.19.1.1.1 (1-130) Diaminopimelate epimerase {Haemophilus influenzae}
mqfskmhglgndfvvvdgvtqnvfftpetirrlanrhcgigfdqlliveapydpeldfhy
rifnadgsevsqcgngarcfarfvtlkgltnkkdisvstqkgnmvltvkdmnqirvnmge
piwepakipf
>d1bwza2 4.19.1.1.1 (131-274) Diaminopimelate epimerase {Haemophilus influenzae}
tankfeknyilrtdiqtvlcgavsmgnphcvvqvddiqtanveqlgpllesherfpervn
agfmqiinkehiklrvyergagetqacgsgacaavavgimqgllnnnvqvdlpggslmie
wngvghplymtgeathiydgfitl
>d1ema__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
skgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptlv
ttfxvqcfsrypdhxkrhdffksaxpegyvqertiffkddgnyktraevkfegdtlvnri
elkgidfkedgnilghkleynynshnvyixadkqkngikvnfkirhniedgsvqladhyq
qntpigdgpvllpdnhylstqsalskdpnekrdhxvllefvtaagi
>d1c8za_ 4.21.1.1.1 Transcriptional factor tubby, C-terminal domain {Mouse (Mus musculus) |A|}
gsvdievqdleefalrpapqgitikcritrdkkgmdrgmfptyflhldredgkkvfllag
rkrkksktsnylisvdptdlsrggdsyigklrsnlmgtkftvydngvnpqkassstlesg
tlrqelaavcyetnvlgfkgprkmsvivpgmnmvhervcirprnehetllarwqnkntes
iielqnktpvwnddtqsyvlnfhgrvtqasvknfqiihgndpdyivmqfgrvaedvftmd
ynyplcalqafaialssfdsklace
>d2pil__ 4.22.1.1.1 Pilin {Gc (Neisseria gonorrhoeae)}
ftlielmiviaivgilaavalpayqdytaraqvseaillaegqksavteyylnhgkwpen
ntsagvaxppsdikgkyvkevevkngvvtatmlssgvnneikgkklslwarrengsvkwf
cgqpvtrtdddtvadakdgkeidtkhlpstcrdnfdak
>d1p32a_ 4.23.1.1.1 Acidic mitochondrial matrix protein p32 {Human (Homo sapiens)}
mhtdgdkafvdflsdeikeerkiqkhktlpkmsggwelelngteaklvrkvagekitvtf
ninnsipptfdgeeepsqgqkveeqepeltstpnfvveviknddgkkalvldchypedev
gqedeaesdifsirevsfqstgesewkdtnytlntdsldwalydhlmdfladrgvdntfa
delvelstalehqeyitfledlksfvksq
>d1bkf__ 4.24.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdknkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatgvpgiipphatlvfdvellkle
>d1yat__ 4.24.1.1.3 FK-506 binding protein (FKBP12), an immunophilin {Yeast}
seviegnvkidrispgdgatfpktgdlvtihytgtlengqkfdssvdrgspfqcnigvgq
vikgwdvgipklsvgekarltipgpyaygprgfpglippnstlvfdvellkvn
>d1pbk__ 4.24.1.1.4 FKBP25 {Human (Homo sapiens)}
pkytksvlkkgdktnfpkkgdvvhcwytgtlqdgtvfdtniqtsakkkknakplsfkvgv
gkvirgwdealltmskgekarleiepewaygkkgqpdakippnakltfevelvdid
>d1rot__ 4.24.1.1.5 FKBP59-I, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
gvdispkqdegvlkvikregtgtetpmigdrvfvhytgwlldgtkfdssldrkdkfsfdl
gkgevikawdiavatmkvgelcritckpeyaygsagsppkippnatlvfevelfefkg
>d1pina_ 4.24.1.1.6 Mitotic rotamase PIN1 {Human (Homo sapiens)}
klppgwekrmsrssgrvyyfnhitnasqwerpsgnsssggkngqgeparvrcshllvkhs
qsrrpsswrqekitrtkeealelingyiqkiksgeedfeslasqfsdcssakargdlgaf
srgqmqkpfedasfalrtgemsgpvftdsgihiilrte
>d1grj_2 4.24.1.2.1 (80-158) GreA transcript cleavage factor, C-terminal domain {Escherichia coli}
mpnngrvifgatvtvlnldsdeeqtyrivgddeadfkqnlisvnspiargligkeeddvv
viktpggevefevikveyl
>d3eipa_ 4.24.2.1.1 Colicin E3 immunity protein {Escherichia coli}
glkldltwfdkstedfkgeeyskdfgddgsvmeslgvpfkdnvnngcfdviaewvpllqp
yfnhqidisdneyfvsfdyrdgdw
>d3eipb_ 4.24.2.1.1 Colicin E3 immunity protein {Escherichia coli}
glkldltwfdkstedfkgeeyskdfgddgsvmeslgvpfkdnvnngcfdviaewvpllqp
yfnhqidisdneyfvsfdyrdgdw
>d1ctn_3 4.24.3.1.1 (444-516) Chitinase A, insertion domain {Serratia marcescens}
ygrgwtgvngyqnnipftgtatgpvkgtwengivdyrqiagqfmsgewqytydataeapy
vfkpstgdlitfd
>d1edqa3 4.24.3.1.1 (444-516) Chitinase A, insertion domain {Serratia marcescens}
ygrgwtgvngyqnnipftgtatgpvkgtwengivdyrqiagqfmsgewqytydataeapy
vfkpstgdlitfd
>d1qkfa_ 4.25.1.1.1 Ribosomal protein S19 {Thermus thermophilus}
gvfvddhllekvlelnakgekrliktwsrrstivpemvghtiavyngkqhvpvyitenmv
ghklgefaptrty
>d1qkha_ 4.25.1.1.1 Ribosomal protein S19 {Thermus thermophilus}
gvfvddhllekvlelnakgekrliktwsrrstivpemvghtiavyngkqhvpvyitenmv
ghklgefaptrty
>d1b33n_ 4.26.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>d1b33o_ 4.26.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>d1qcsa2 4.27.1.1.1 (86-201) C-terminal domain of NSF-N, NSF-Nc {Hamster (Cricetulus griseus)}
dkakqcigtxtieidflqkknidsnpydtdkxaaefiqqfnnqafsvgqqlvfsfndklf
gllvkdieaxdpsilkgepasgkrqkievglvvgnsqvafekaensslnligkakt
>d1cr5a2 4.27.1.1.2 (108-210) C-terminal domain of NSF-N, NSF-Nc {Baker's yeast (Saccharomyces cerevisiae), sec18p}
sgkqsylgsididisfrargkavstvfdqdelakqfvrcyesqifsptqylimefqghff
dlkirnvqaidlgdieptsavatgietkgiltkqtqinffkgr
>d1cz4a2 4.27.1.1.3 (92-185) C-terminal domain of VAT-N, VAT-Nc {Thermoplasma acidophilum}
teiakkvtlapiirkdqrlkfgegieeyvqralirrpmleqdnisvpgltlagqtgllfk
vvktlpskvpveigeetkieireepasevleegg
>d1cz5a2 4.27.1.1.3 (92-185) C-terminal domain of VAT-N, VAT-Nc {Thermoplasma acidophilum}
teiakkvtlapiirkdqrlkfgegieeyvqralirrpmleqdnisvpgltlagqtgllfk
vvktlpskvpveigeetkieireepasevleegg
>d1qipa_ 4.28.1.1.1 Glyoxalase I (lactoylglutathione lyase) {Human (Homo sapiens)}
ggltdeaalsccsdadpstkdfllqqtmlrvkdpkksldfytrvlgmtliqkcdfpimkf
slyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfghi
giavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywieilnpnkmatlm
>d1byla_ 4.28.1.2.1 Bleomycin resistance protein, BRP {Streptoalloteichus hindustanus}
fmakltsavpvltardvagavefwtdrlgfsrdfveddfagvvrddvtlfisavqdqvvp
dntlawvwvrgldelyaewsevvstnfrdasgpamteigeqpwgrefalrdpagncvhfv
ae
>d1dhy_1 4.28.1.3.1 (1-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {Pseudomonas}
sierlgylgfavkdvpawdhfltksvglmaagsagdaalyradqrawriavqpgelddla
yaglevddaaalermadklrqagvaftrgdealmqqrkvmgllclqdpfglpleiyygpa
eifhepflpsap
>d1han_1 4.28.1.3.2 (2-132) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {Pseudomonas cepacia}
sirslgymgfavsdvaawrsfltqklglmeagttdngdlfridsrawriavqqgevddla
fagyevadaaglaqmadklkqagiavttgdaslarrrgvtglitfadpfglpleiyygas
evfekpflpga
>d1han_2 4.28.1.3.2 (133-289) 2,3-Dihydroxybiphenyl dioxygenase (DHDB, BPHC enzyme) {Pseudomonas cepacia}
avsgfltgeqglghfvrcvpdsdkalafytdvlgfqlsdvidmkmgpdvtvpayflhcne
rhhtlaiaafplpkrihhfmlevaslddvgfafdrvdadglitstlgrhtndhmvsfyas
tpsgveveygwsartvdrswvvvrhdspsmwghksvr
>d1mpya1 4.28.1.3.3 (1-145) Catechol 2,3-dioxygenase (metapyrocatechase) {Pseudomonas putida, mt2}
mnkgvmrpghvqlrvldmskalehyvellgliemdrddqgrvylkawtevdkfslvlrea
depgmdfmgfkvvdedalrqlerdlmaygcaveqlpagelnscgrrvrfqapsghhfely
adkeytgkwglndvnpeawprdlkg
>d1mpya2 4.28.1.3.3 (146-307) Catechol 2,3-dioxygenase (metapyrocatechase) {Pseudomonas putida, mt2}
maavrfdhalmygdelpatydlftkvlgfylaeqvldengtrvaqflslstkahdvafih
hpekgrlhhvsfhletwedllraadlismtdtsidigptrhglthgktiyffdpsgnrne
vfcggdynypdhkpvtwttdqlgkaifyhdrilnerfmtvlt
>d1bm8__ 4.29.1.1.1 DNA-binding domain of Mlu1-box binding protein MBP1 {Baker's yeast (Saccharomyces cerevisiae)}
qiysarysgvdvyefihstgsimkrkkddwvnathilkaanfakakrtrilekevlketh
ekvqggfgkyqgtwvplniakqlaekfsvydqlkplfdf
>d1b2va_ 4.30.1.1.1 Heme-binding protein A (HasA) {Serratia marcescens}
afsvnydssfggysihdylgqwastfgdvnhtngnvtdansggfyggslsgsqyaissta
nqvtafvaggnltytlfnepahtlygqldslsfgdglsggdtspysiqvpdvsfgglnls
slqaqghdgvvhqvvyglmsgdtgaletalngilddyglsvnstfdqvaaata
>d1b3ob2 4.31.1.1.1 (112-159) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
qgfitdpvvlspkdrvrdvfeakarhgfcgipitdtgrmgsrlvgiis
>d1b3ob3 4.31.1.1.1 (178-231) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
imtkredlvvapagitlkeaneilqrskkgklpivneddelvaiiartdlkknr
>d1bvqa_ 4.32.1.1.1 4-hydroxybenzoyl-CoA thioesterase {Pseudomonas CBS-3}
arsitmqqriefgdcdpagivwypnyhrwldaasrnyfikcglppwrqtvvergivgtpi
vscnasfvctasyddvltietcikewrrksfvqrhsvsrttpggdvqlvmradeirvfam
ndgerlraievpadyielc
>d1mkaa_ 4.32.1.2.1 beta-Hydroxydecanol thiol ester dehydrase {Escherichia coli}
vdkresytkedllasgrgelfgakgpqlpapnmlmmdrvvkmtetggnfdkgyveaeldi
npdlwffgchfigdpvmpgclgldamwqlvgfylgwlggegkgralgvgevkftgqvlpt
akkvtyrihfkrivnrrlimgladgevlvdgrliytasdlkvglfqdtsaf
>d1cmia_ 4.33.1.1.1 PIN, a protein inhibitor of neuronal nitric oxide synthase {Human (Homo sapiens)}
kaviknadmseemqqdsvecatqalekyniekdiaahikkefdkkynptwhcivgrnfgs
yvthetkhfiyfylgqvaillfksg
>d1cmib_ 4.33.1.1.1 PIN, a protein inhibitor of neuronal nitric oxide synthase {Human (Homo sapiens)}
kaviknadmseemqqdsvecatqalekyniekdiaahikkefdkkynptwhcivgrnfgs
yvthetkhfiyfylgqvaillfksg
>d1bkq__ 4.33.1.1.2 PIN, a protein inhibitor of neuronal nitric oxide synthase {Rabbit (Oryctolagus cuniculus)}
mcdrkaviknadmseemqqdsvecatqalekyniekdiaahikkefdkkynptwhcivgr
nfgsyvthetkhfiyfylgqvaillfksg
>d1acbi_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1csei_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d1egl__ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
tefgselksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgt
nvvnhvphvg
>d1meei_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhv
phvg
>d1sbni_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqynvyflpegspvtrdlrynrvrvfynpgtnvvnhvp
hvg
>d1sibi_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvkvfynpgtnvvnhvp
hvg
>d1teci_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d2seci_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtldlrynrvrvfynpgtnvvnhv
phvg
>d2teci_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>d3teci_ 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>e1egp.1a 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
lksfpevvgktvdqareyftlhypqynvyflpegspvtl
>e1egp.1b 4.34.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ynrvrvfynpgtnvvnhvphvg
>d1a10i_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtpeyridrvrlfvdkldniaevp
rvg
>d1a1yi_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaevp
rvg
>d1coai_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldnvaev
prvg
>d1ypai_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgkavaaakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaqv
prvg
>d1ypbi_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgkgvaaakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaqv
prvg
>d1ypci_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgksvaaakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaqv
prvg
>d2ci2i_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
nlktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniae
vprvg
>d2snii_ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
lktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaev
prvg
>d3ci2__ 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
lktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaqv
prvg
>e1ciq.1a 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtiv
>e1ciq.1b 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
eyridrvrlfvdkldniaqvprvg
>e1cir.1a 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
mktewpelvgksveeakkvilqdkpeaqiivlpvgtivt
>e1cir.1b 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
eyridrvrlfvdkldniaqvprvg
>e1cq4.1a 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtiv
>e1cq4.1b 4.34.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
yridrvrlfvdkldniaqvprvg
>d1mit__ 4.34.1.1.3 Trypsin inhibitor V {Pumpkin (Cucurbita maxima)}
gsscpgksswphlvgvggsvakaiierqnpnvkavileegtpvtkdfrcnrvriwvnkrg
lvvspprig
>d1tin__ 4.34.1.1.3 Trypsin inhibitor V {Pumpkin (Cucurbita maxima)}
xsscpgksswphlvgvggsvakaiierqnpnvkavileegtpvtkdfrcnrvriwvnkrg
lvvspprig
>e1hym.1a 4.34.1.1.3 Trypsin inhibitor V {Pumpkin (Cucurbita maxima)}
xsscpgksswphlvgvggsvakaiierqnpnvkavileegtpvtk
>e1hym.1b 4.34.1.1.3 Trypsin inhibitor V {Pumpkin (Cucurbita maxima)}
dfrcnrvriwvnkrglvvspprig
>d1dwma_ 4.34.1.1.4 Trypsin inhibitor LUTI {Flax (Linum usitatissimum)}
srrcpgknawpelvgksgnmaaatverenrnvhaivlkegsamtkdfrcdrvwvivndhg
vvtsvphit
>d1alo_3 4.35.1.1.1 (194-310) Aldehyde oxidoreductase, domain 3 {Desulfovibrio gigas}
dygadlglkmpagtlhlamvqakvshanikgidtsealtmpgvhsvithkdvkgknritg
litfptnkgdgwdrpilcdekvfqygdcialvcadseanaraaaekvkvdleelpay
>d1qj2b1 4.35.1.1.2 (10-146) Carbon monoxide (CO) dehydrogenase molybdoprotein, N-domain {Pseudomonas carboxydovorans}
tsaeraeklqgmgckrkrvedirftqgkgnyvddvklpgmlfgdfvrsshahariksidt
skakalpgvfavltaadlkplnlhymptlagdvqavladekvlfqnqevafvvakdryva
adaielvevdyeplpvl
>d1qapa2 4.35.2.1.1 (8-129) Quinolinic acid phosphoribosyltransferase, N-terminal domain {Salmonella typhimurium}
ddrrdallerinldipaavaqalredlggevdagnditaqllpadtqahatvitredgvf
cgkrwveevfiqlagddvrltwhvddgdaihanqtvfelqgparvlltgertalnfvqtl
sg
>d1qpoa2 4.35.2.1.2 (2-116) Quinolinic acid phosphoribosyltransferase, N-terminal domain {Mycobacterium tuberculosis}
glsdwelaaaraaiargldedlrygpdvttlatvpasatttaslvtreagvvagldvall
tlnevlgtngyrvldrvedgarvppgealmtleaqtrglltaertmlnlvghlsg
>d2tpt_3 4.35.3.1.1 (336-440) Thymidine phosphorylase {Escherichia coli}
tamltkavyadtegfvsemdtralgmavvamgggrrqasdtidysvgftdmarlgdqvdg
qrplavihakdennwqeaakavkaaikladkapestptvyrrise
>d1brwa3 4.35.3.1.2 (331-433) Pyrimidine nucleoside phosphorylase {Bacillus stearothermophilus}
kaaytstvtaaadgyvaemaaddigtaamwlgagrakkedvidlavgivlhkkigdrvqk
gealatihsnrpdvldvkekieaairlspqpvarppliyetiv
>d1buoa_ 4.36.1.1.1 Promyelocytic leukemia zinc finger (PLZF) protein BTB domain {Human (Homo sapiens)}
mgmiqlqnpshptgllckanqmrlagtlcdvvimvdsqefhahrtvlactskmfeilfhr
nsqhytldflspktfqqileyaytatlqakaedlddllyaaeileieyleeqclkmleti
q
>d1vcbb_ 4.36.1.1.2 Elongin C {Human (Homo sapiens)}
myvklissdghefivkrehaltsgtikamlsgpgqfaenetnevnfreipshvlskvcmy
ftykvrytnssteipefpiapeialellmaanfldc
>d1vcbe_ 4.36.1.1.2 Elongin C {Human (Homo sapiens)}
myvklissdghefivkrehaltsgtikamlsgpgqfaenetnevnfreipshvlskvcmy
ftykvrytnssteipefpiapeialellmaanfldc
>d1vcbh_ 4.36.1.1.2 Elongin C {Human (Homo sapiens)}
myvklissdghefivkrehaltsgtikamlsgpgqfaenetnevnfreipshvlskvcmy
ftykvrytnssteipefpiapeialellmaanfldc
>d1vcbk_ 4.36.1.1.2 Elongin C {Human (Homo sapiens)}
myvklissdghefivkrehaltsgtikamlsgpgqfaenetnevnfreipshvlskvcmy
ftykvrytnssteipefpiapeialellmaanfldc
>d1a68__ 4.36.1.2.1 Shaker potassium channel {California sea hare (Aplysia californica)}
ervvinvsglrfetqlktlnqfpdtllgnpqkrnryydplrneyffdrnrpsfdailyfy
qsggrlrrpvnvpldvfseeikfyelg
>d1t1da_ 4.36.1.2.1 Shaker potassium channel {California sea hare (Aplysia californica)}
ervvinvsglrfetqlktlnqfpdtllgnpqkrnryydplrneyffdrnrpsfdailyfy
qsggrlrrpvnvpldvfseeikfyelgenaferyredegf
>d3kvt__ 4.36.1.2.2 akv3.1 voltage-gated potassium channel {California sea hare (Aplysia californica)}
enrviinvggirhetykatlkkipatrlsrltegmlnydpvlneyffdrhpgvfaqiiny
yrsgklhyptdvcgplfeeelefwgldsnqvepccwmtytahr
>d1efub1 4.37.1.1.1 (1-139) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
aeitaslvkelrertgagmmdckkalteangdielaienmrksgaikaakkagnvaadgv
iktkidgnygiilevncqtdfvakdagfqafadkvldaavagkitdvevlkaqfeeerva
lvakigeninirrvaaleg
>d1efub2 4.37.1.1.1 (140-282) Elongation factor Ts (EF-Ts), dimerisation domain {Escherichia coli}
dvlgsyqhgarigvlvaakgadeelvkhiamhvaaskpefikpedvsaevvekeyqvqld
iamqsgkpkeiaekmvegrmkkftgevsltgqpfvmepsktvgqllkehnaevtgfirfe
vgegiekvetdfaaevaamskqs
>d1tfe__ 4.37.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
aregiighyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeip
aeelekerqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliq
qaiakigenivvrrfcrfelga
>d1vewa2 4.38.1.1.1 (91-205) Mn superoxide dismutase (MnSOD) {Escherichia coli}
gttlqgdlkaaierdfgsvdnfkaefekaaasrfgsgwawlvlkgdklavvstanqdspl
mgeaisgasgfpimgldvwehayylkfqnrrpdyikefwnvvnwdeaaarfaakk
>d1mnga2 4.38.1.1.2 (93-203) Mn superoxide dismutase (MnSOD) {Thermus thermophilus}
ggakepvgelkkaideqfggfqalkekltqaamgrfgsgwawlvkdpfgklhvlstpnqd
npvmegftpivgidvwehayylkyqnrradylqaiwnvlnwdvaeeffkka
>d1ap6a2 4.38.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d3sdpa2 4.38.1.1.4 (84-190) Fe superoxide dismutase (FeSOD) {Pseudomonas ovalis}
daggqptgaladainaafgsfdkfkeeftktsvgtfgsgwawlvkadgslalcstigaga
pltsgdtplltcdvwehayyidyrnlrpkyveafwnlvnwafvaeeg
>d1isaa2 4.38.1.1.5 (83-192) Fe superoxide dismutase (FeSOD) {Escherichia coli}
naggeptgkvaeaiaasfgsfadfkaqftdaaiknfgsgwtwlvknsdgklaivstsnag
tplttdatplltvdvwehayyidyrnarpgylehfwalvnwefvaknlaa
>d1idsa2 4.38.1.1.6 (86-199) Fe superoxide dismutase (FeSOD) {Mycobacterium tuberculosis}
nggdkptgelaaaiadafgsfdkfraqfhaaattvqgsgwaalgwdtlgnkllifqvydh
qtnfplgivplllldmwehafylqyknvkvdfakafwnvvnwadvqsryaaats
>d1coja2 4.38.1.1.7 (91-212) Fe superoxide dismutase (FeSOD) {Aquifex pyrophilus}
ggkgepsealkkkieediggldactnelkaaamafrgwailgldifsgrlvvngldahnv
ynltgliplividtyehayyvdyknkrppyidaffkninwdvvnerfekamkayealkdf
ik
>d1b06a2 4.38.1.1.9 (93-210) Fe superoxide dismutase (FeSOD) {Sulfolobus acidocaldarius}
pagkgggkpggaladlidkqygsfdrfkqvfsesanslpgsgwtvlyydnesgnlqimtv
enhfmnhiaelpvilivdefehayylqyknkrgdylnawwnvvnwddaekrlqkylnk
>d1bsma2 4.38.1.1.10 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ctf__ 4.39.1.1.1 Ribosomal protein L7/12, C-terminal fragment {Escherichia coli}
efdvilkaagankvavikavrgatglglkeakdlvesapaalkegvskddaealkkalee
agaevevk
>d1aa3__ 4.40.1.1.1 RecA protein, C-terminal domain {Escherichia coli}
infygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrell
lsn
>d1rea_2 4.40.1.1.1 (269-328) RecA protein, C-terminal domain {Escherichia coli}
nfygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrelll
>d2reb_2 4.40.1.1.1 (269-328) RecA protein, C-terminal domain {Escherichia coli}
nfygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrelll
>d1914__ 4.41.1.1.1 Signal recognition particle alu RNA binding heterodimer, SRP9/14 {Mouse (Mus musculus)}
mvlleseqflteltrlfqkcrssgsvfitlkkydgrtkpiprkssveglepaenkcllra
tdgkrkistvvsskevnkfqmaysnllranmdglkkrdkknkskkskpaqggeqklisee
ddsagspmpqfqtweefsraaeklyladpmkvrvvlkyrhvdgnlcikvtddlvclvyrt
dqaqdvkkiekfhsqlmrlmvakesrnv
>d1di2a_ 4.42.1.1.1 Double-stranded RNA-binding protein A, second dsRBD {Xenopus laevis}
mpvgslqelavqkgwrlpeytvaqesgpphkreftitcrvetfvetgsgtskqvakrvaa
eklltkfkt
>d1di2b_ 4.42.1.1.1 Double-stranded RNA-binding protein A, second dsRBD {Xenopus laevis}
mpvgslqelavqkgwrlpeytvaqesgpphkreftitcrvetfvetgsgtskqvakrvaa
eklltkfkt
>d1stu__ 4.42.1.1.2 Staufen, domain III {Fruit fly (Drosophila melanogaster)}
pisqvheigikrnmtvhfkvlreegpahmknfitacivgsivtegegngkkvskkraaek
mlvelqkl
>d1qu6a1 4.42.1.1.3 (1-90) dsRNA-dependent protein kinase pkr {Human (Homo sapiens)}
gshmemagdlsagffmeelntyrqkqgvvlkyqelpnsgpphdrrftfqviidgrefpeg
egrskkeaknaaaklaveilnkekkavspl
>d1qu6a2 4.42.1.1.3 (91-179) dsRNA-dependent protein kinase pkr {Human (Homo sapiens)}
lltttnsseglsmgnyiglinriaqkkrltvnyeqcasgvhgpegfhykckmgqkeysig
tgstkqeakqlaaklaylqilseetgsgc
>d1pkp_2 4.42.1.2.1 (4-77) Ribosomal S5 protein, N-terminal domain {Bacillus stearothermophilus}
inpnkleleervvavnrvakvvkggrrlrfsalvvvgdknghvgfgtgkaqevpeairka
iedakknlievpiv
>d1ah5_2 4.42.2.1.1 (220-313) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeraxntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqxgislaeellnngareilaevyngdapa
>d1pda_2 4.42.2.1.1 (220-307) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeramntrlegacqvpigsyaelidgeiwlrglvgapdgsqiirgerrga
pqdaeqmgislaeellnngareilaevy
>d1ypn_2 4.42.2.1.1 (220-306) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeramntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqmgislaeellnngareilaev
>d2ypna2 4.42.2.1.1 (220-313) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeramntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqmgislaeellnngareilaevyngdapa
>d1dt4a_ 4.43.1.1.1 Neuro-oncological ventral antigen 1, nova-1, KH3 {Human (Homo sapiens)}
mkdvveiavpenlvgailgkggktlveyqeltgcriqiskkgeflpgtrnrkvtitgtpa
atqaaqylitqri
>d1dtja_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelvemavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrvt
>d1dtjb_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelvemavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrvtye
>d1dtjc_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelvemavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrvt
>d1dtjd_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelvemavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrv
>d1ec6a_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelveiavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrvtyeqgvrasnpqkv
>d1ec6b_ 4.43.1.1.2 Neuro-oncological ventral antigen 2, nova-2, KH3 {Human (Homo sapiens)}
mkelveiavpenlvgailgkggktlveyqeltgariqiskkgeflpgtrnrrvtitgspa
atqaaqylisqrvtyeqgvrasnp
>d1vig__ 4.43.1.1.3 Vigilin, KH6 {Human (Homo sapiens)}
inrmdyveinidhkfhrhligksganinrikdqykvsvrippdseksnliriegdpqgvq
qakrellelas
>d1vih__ 4.43.1.1.3 Vigilin, KH6 {Human (Homo sapiens)}
inrmdyveinidhkfhrhligksganinrikdqykvsvrippdseksnliriegdpqgvq
qakrellelas
>d2fmr__ 4.43.1.1.4 Fragile X protein, KH1 {Human (Homo sapiens)}
asrfheqfivredlmglaigthganiqqarkvpgvtaidldedtctfhiygedqdavkka
rsfle
>d1khma_ 4.43.1.1.5 HnRNP K, KH3 {Human (Homo sapiens)}
gspnsygdlggpiittqvtipkdlarsiigkggqrikqirhesgasikideplegsedri
ititgtqdqiqnaqyllqnsvkqysgkff
>d2proa1 4.44.1.1.1 (5-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
dpqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfklv
aatsgarksstlggvevrnvr
>d2proa2 4.44.1.1.1 (86-158) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvries
>d2prob1 4.44.1.1.1 (4-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
vdpqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfkl
vaatsgarksstlggvevrnvr
>d2prob2 4.44.1.1.1 (86-158) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvries
>d2proc1 4.44.1.1.1 (18-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
ifptqlpqylqteklartqaaaierefgaqfagswiernedgsfklvaatsgarksstlg
gvevrnvr
>d2proc2 4.44.1.1.1 (86-158) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvries
>d3proc1 4.44.1.1.1 (6-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
pqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfklva
atsgarksstlggvevrnvr
>d3proc2 4.44.1.1.1 (86-163) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvriesspgkl
>d3prod1 4.44.1.1.1 (3-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
qvdpqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfk
lvaatsgarksstlggvevrnvr
>d3prod2 4.44.1.1.1 (86-163) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvriesspgkl
>d4proc1 4.44.1.1.1 (6-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
pqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfklva
atsgarksstlggvevrnvr
>d4proc2 4.44.1.1.1 (86-166) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvriesspgklqtt
>d4prod1 4.44.1.1.1 (5-85) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
dpqlkfamqrdlgifptqlpqylqteklartqaaaierefgaqfagswiernedgsfklv
aatsgarksstlggvevrnvr
>d4prod2 4.44.1.1.1 (86-166) Alpha-lytic protease prodomain {Lysobacter enzymogenes}
yslkqlqsameqldaganarvkgvskpldgvqswyvdprsnavvvkvddgatdagvdfva
lsgadsaqvriesspgklqtt
>d1gpma3 4.44.2.1.1 (405-525) GMP synthetase, C-terminal, dimerisation domain {Escherichia coli}
gpglgvrvlgevkkeycdllrradaifieelrkadlydkvsqaftvflpvrsvgvmgdgr
kydwvvslravetidfmtahwahlpydflgrvsnriinevngisrvvydisgkppatiew
e
>d1egaa2 4.44.3.1.1 (183-295) GTPase Era C-terminal domain {Escherichia coli}
dyitdrsqrfmaseiireklmrflgaelpysvtveierfvsnerggydinglilveregq
kkmvignkgakiktigiearkdmqemfeapvhlelwvkvksgwadderalrsl
>d1onea2 4.45.1.1.1 (1-141) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
avskvyarsvydsrgnptvevelttekgvfrsivpsgastgvhealemrdgdkskwmgkg
vlhavknvndviapafvkanidvkdqkavddflisldgtanksklganailgvslaasra
aaaeknvplykhladlskskt
>d1pdz_2 4.45.1.1.2 (1-139) Enolase {Lobster (Homarus vulgaris)}
sitkvfartifdsrgnptvevdlytskglfraavpsgastgvhealemrdgdkskyhgks
vfnavknvndvivpeiiksglkvtqqkecdefmckldgtenksslganailgvslaicka
gaaelgiplyrhianlany
>d1bqg_2 4.45.1.1.3 (12-143) D-glucarate dehydratase {Pseudomonas putida}
gapvitdlkvvpvaghdsmllnlsgahgplftrnililtdssghvgvgevpggegirktl
edarhllinqsignyqsllnkvrnafadrdvggrglqtfdlriavhavtavesalldllg
qhlqvpvaallg
>d1muca2 4.45.1.1.4 (4-130) Muconate-lactonizing enzyme (cis muconate cycloisomerase) {Pseudomonas putida}
alieridaiivdlptirphklamhtmqqqtlvvlrvrcsdgvegigeattigglaygyes
pegikanidahlapaliglaadninaamlkldklakgntfaksgiesalldaqgkrlglp
vsellgg
>d2mnr_2 4.45.1.1.5 (3-132) Mandelate racemase {Pseudomonas putida}
evlitglrtravnvplaypvhtavgtvgtaplvlidlatsagvvghsylfaytpvalksl
kqllddmaamivneplapvsleamlakrfclagytglirmaaagidmaawdalgkvhetp
lvkllganar
>d2chr_2 4.45.1.1.6 (1-126) Chlormuconate cycloisomerase {Alcaligenes eutrophus}
mkidaieavivdvptkrpiqmsittvhqqsyvivrvyseglvgvgeggsvggpvwsaeca
etikiiverylaphllgtdafnvsgalqtmaravtgnasakaavemalldlkaralgvsi
aellgg
>d1bxea_ 4.46.1.1.1 Ribosomal protein L22 {Thermus acuaticus, subsp. Thermus thermophilus}
eakaiaryvrisprkvrlvvdlirgksleearnilrytnkrgayfvakvlesaaanavnn
hdxledrlyvkaayvdegpalkrvlprargradiikkrtshitvilgek
>d1aona3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonb3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonc3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aond3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aone3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonf3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aong3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonh3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aoni3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonj3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonk3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonl3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonm3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonn3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dera3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derb3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derc3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derd3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dere3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derf3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derg3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derh3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1deri3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derj3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derk3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derl3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1derm3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1dern3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1grl_3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oela3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oelb3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oelc4 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oeld3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oele3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oelf3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1oelg3 4.47.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1a6da3 4.47.1.2.1 (146-214,368-403) Thermosome {Thermoplasma acidophilum}
tddatlrkialtalsgkntglsndfladlvvkavnavaevrdgktivdtanikvdkkngg
svndtqfisXavsilirggtdhvvseveralndairvvaitkedgk
>d1a6db3 4.47.1.2.1 (145-215,368-403) Thermosome {Thermoplasma acidophilum}
gadekalllkmaqtslnsksasvakdklaeisyeavksvaelrdgkyyvdfdniqvvkkq
ggaiddtqlinXkavsilvrgetehvvdemersitdslhvvasaledg
>d1f2g__ 4.48.1.1.1 Ferredoxin II {Desulfovibrio gigas}
pievnddcmaceacveicpdvfemneegdkavvinpdsdldcveeaidscpaeaivrs
>d1fxd__ 4.48.1.1.1 Ferredoxin II {Desulfovibrio gigas}
pievnddcmaceacveicpdvfemneegdkavvinpdsdldcveeaidscpaeaivrs
>d1fdx__ 4.48.1.1.2 Ferredoxin II {Peptococcus aerogenes}
ayvindsciacgackpecpvniiqgsiyaidadscidcgscasvcpvgapnped
>d1fca__ 4.48.1.1.3 Ferredoxin II {Closridium acidi-urici}
ayvineaciscgacepecpvdaisqggsryvidadtcidcgacagvcpvdapvqa
>d1fdn__ 4.48.1.1.3 Ferredoxin II {Closridium acidi-urici}
ayvineaciscgacepecpvnaissgddryvidadtcidcgacagvcpvdapvqa
>d2fdn__ 4.48.1.1.3 Ferredoxin II {Closridium acidi-urici}
ayvineaciscgacepecpvnaissgddryvidadtcidcgacagvcpvdapvqa
>d1clf__ 4.48.1.1.4 Ferredoxin II {Closridium pasteurianum}
aykiadscvscgacasecpvnaisqgdsifvidadtcidcgncanvcpvgapvqe
>d1blu__ 4.48.1.1.5 Ferredoxin II {Cromatium vinosum}
almitdecincdvcepecpngaisqgdetyviepslctecvghyetsqcvevcpvdciik
dpsheetedelrakyeritg
>d7fd1a_ 4.48.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1bc6__ 4.48.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bd6__ 4.48.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bqxa_ 4.48.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkcascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bwea_ 4.48.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkcascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1xer__ 4.48.1.3.1 Ferredoxin {Sulfolobus}
gidpnyrtnrqvvgehsghkvygpveppxvlgihgtivgvdfdlciadgscinacpvnvf
qwydtpghpasekkadpvneqacifcmacvnvcpvaaidvkpp
>d1rof__ 4.48.1.4.1 Ferredoxin {Thermotoga maritima}
mkvrvdadacigcgvcenlcpdvfqlgddgkakvlqpetdlpcakdaadscptgaisvee
>d1vjw__ 4.48.1.4.1 Ferredoxin {Thermotoga maritima}
mkvrvdadacigcgvcenlcpdvfqlgddgkakvlqpetdlpcakdaadscptgaisve
>d1dax__ 4.48.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1dfd__ 4.48.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1fxra_ 4.48.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d1fxrb_ 4.48.1.4.2 Ferredoxin I {Sulfate-reducing bacteria (Desulfovibrio africanus)}
arkfyvdqdeciacescveiapgafamdpeiekayvkdvegasqeeveeamdtcpvqcih
wede
>d2fxb__ 4.48.1.4.3 Ferredoxin {Bacillus thermoproteolyticus}
pkytivdketciacgacgaaapdiydydedgiayvtlddnqgivevpdiliddmmdafeg
cptdsikvadepfdgdpnkfe
>d1c4aa3 4.48.1.5.1 (127-209) Fe-only hydrogenase, second domain {Clostridium pasteurianum}
kdkteyvdersksltvdrtkcllcgrcvnacgkntetyamkflnkngktiigaedekcfd
dtncllcgqciiacpvaalseks
>d1c4ca3 4.48.1.5.1 (127-209) Fe-only hydrogenase, second domain {Clostridium pasteurianum}
kdkteyvdersksltvdrtkcllcgrcvnacgkntetyamkflnkngktiigaedekcfd
dtncllcgqciiacpvaalseks
>d1feha3 4.48.1.5.1 (127-209) Fe-only hydrogenase, second domain {Clostridium pasteurianum}
kdkteyvdersksltvdrtkcllcgrcvnacgkntetyamkflnkngktiigaedekcfd
dtncllcgqciiacpvaalseks
>d1hfel2 4.48.1.5.2 (2-86) Fe-only hydrogenase larger subunit, N-domain {Desulfovibrio vulgaris}
srtvmerieyemhtpdpkadpdklhfvqideakcigcdtcsqycptaaifgemgephsip
hieacincgqclthcpenaiyeaqs
>d1hfem2 4.48.1.5.2 (2-86) Fe-only hydrogenase larger subunit, N-domain {Desulfovibrio vulgaris}
srtvmerieyemhtpdpkadpdklhfvqideakcigcdtcsqycptaaifgemgephsip
hieacincgqclthcpenaiyeaqs
>d1b0pa5 4.48.1.5.3 (669-785) Pyruvate-ferredoxin oxidoreductase, PFOR, domain V {Desulfovibrio africanus}
tsqfekrgvainvpqwvpenciqcnqcafvcphsailpvlakeeelvgapanftaleakg
kelkgykfriqintldcmgcgncadicppkekalvmqpldtqrdaqvpnleyaarip
>d1acmb1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1acmd1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1d09b1 4.48.2.1.1 (1-100) Aspartate carbamoyltransferase {Escherichia coli}
mthdnklqveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlik
ientflsedqvdqlalyapqatvnridnyevvgksrpslp
>d1raid1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
qveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d2at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d2at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d2atcb1 4.48.2.1.1 (1-100) Aspartate carbamoyltransferase {Escherichia coli}
mthndklqvaeikrgtvinhipaeigfkllslfkltetqdritiglnlpsgemgrkdlik
ientflsedevdelalyapqatvnrindyevvgksrpslp
>d3at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d3at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d4at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d4at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d5at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d5at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d6at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d6at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d7at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d7at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d8at1b1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d8at1d1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d8atcb1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d8atcd1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d9atcb1 4.48.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
qveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1pca_2 4.48.3.1.1 (4a-99a) Procarboxypeptidase A {Porcine (Sus scrofa)}
kedfvghqvlrisvddeaqvqkvkeledlehlqldfwrgparpgfpidvrvpfpsiqavk
vfleahgirytimiedvqllldeeqeqmfasqgr
>d1pyta_ 4.48.3.1.2 Procarboxypeptidase A {Bovine (Bos taurus)}
kedfvghqvlritaadeaevqtvkeledlehlqldfwrgpgqpgspidvrvpfpslqavk
vfleahgiryrimiedvqslldeeqeqmfasqsr
>d1aye_2 4.48.3.1.3 (4a-99a) Procarboxypeptidase A {Human (Homo sapiens)}
letfvgdqvleivpsneeqiknllqleaqehlqldfwkspttpgetahvrvpfvnvqavk
vflesqgiaysimiedvqvlldkeneemlfnrrr
>d1nsa_2 4.48.3.1.4 (7a-95a) Procarboxypeptidase B {Porcine (Sus scrofa)}
fegekvfrvnvedendiselhelastrqidfwkpdsvtqikphstvdfrvkaedilaved
fleqnelqyevlinnlrsvleaqfdsvsr
>d1pba__ 4.48.3.1.4 Procarboxypeptidase B {Porcine (Sus scrofa)}
hhsgehfegekvfrvnvedendiselhelastrqidfwkpdsvtqikphstvdfrvkaed
ilavedfleqnelqyevlinn
>d1spbp_ 4.48.3.2.1 Subtilisin prosegment {Bacillus amyloliquefaciens}
ekkyivgfkqtmstmsaakkkdvisekggkvqkqfkyvdaasatlnekavkelkkdpsva
yveedhvahay
>d1scjb_ 4.48.3.2.2 Subtilisin prosegment {Bacillus subtilis}
ekkyivgfkqtmsamssakkkdvisqkggkvekqfkyvnaaaatldekavkelkkdpsva
yveedhiahey
>d1mli__ 4.48.4.1.1 Muconalactone isomerase {Pseudomonas putida}
mlfhvkmtvklpvdmdpakatqlkadekelaqrlqregtwrhlwriaghyanysvfdvps
vealhdtlmqlplfpymdievdglcrhpssihsddr
>d2pii__ 4.48.5.1.1 PII (product of glnB) {Escherichia coli}
mkkidaiikpfklddvrealaevgitgmtvtevkgfgrqkghtelyrgaeymvdflpkvk
ieivvpddivdtcvdtiirtaqtgkigdgkifvfdvarvirirtgeeddaai
>d1gnka_ 4.48.5.1.2 PII-homolog GlnK {Escherichia coli}
mklvtviikpfkledvrealssigiqgltvtevkgfgrqkghaelyrgaeysvnflpkvk
idvaiaddqldevidivskaaytgkigdgkifvaelqrvirirtgeadeaal
>d1nuea_ 4.48.6.1.1 Nucleoside diphosphate kinases {Human (Homo sapiens)}
anlertfiaikpdgvqrglvgeiikrfeqkgfrlvamkflraseehlkqhyidlkdrpff
pglvkymnsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svksaekeislwfkpeelvdykscahdwvye
>d1npk__ 4.48.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1nhkl_ 4.48.6.1.5 Nucleoside diphosphate kinases {Myxococcus xanthus}
aiertlsiikpdglekgvigkiisrfeekglkpvairlqhlsqaqaegfyavhkarpffk
dlvqfmisgpvvlmvlegenavlanrdimgatnpaqaaegtirkdfatsidkntvhgsds
lenakieiayffreteihsypyq
>d1ha1_1 4.48.7.1.1 (8-92) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
epeqlrklfigglsfettdeslrshfeqwgtltdcvvmrdpntkrsrgfgfvtyatveev
daamnarphkvdgrvvepkravsre
>d1ha1_2 4.48.7.1.1 (99-180) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
ahltvkkifvggikedteehhlrdyfeqygkievieimtdrgsgkkrgfafvtfddhdsv
dkiviqkyhtvnghncevrkal
>d1up1_1 4.48.7.1.1 (7-92) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
pkepeqlrklfigglsfettdeslrshfeqwgtltdcvvmrdpntkrsrgfgfvtyatve
evdaamnarphkvdgrvvepkravsr
>d1up1_2 4.48.7.1.1 (99-182) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
gahltvkkifvggikedteehhlrdyfeqygkievieimtdrgsgkkrgfafvtfddhds
vdkiviqkyhtvnghncevrkals
>d2up1a1 4.48.7.1.1 (8-98) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
kepeqlrklfigglsfettdeslrshfeqwgtltdcvvmrdpntkrsrgfgfvtyatvee
vdaamnarphkvdgrvvepkravsredsqrp
>d2up1a2 4.48.7.1.1 (99-190) Nuclear ribonucleoprotein A1, RNP A1, UP1 {Human (Homo sapiens)}
gahltvkkifvggikedteehhlrdyfeqygkievieimtdrgsgkkrgfafvtfddhds
vdkiviqkyhtvnghncevrkalskqemasas
>d1auda_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfv
>d1cx0a_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
petrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkxrgqafvifkevs
satnalrsxqgfpfydkpxriqyaktdsdiiakxa
>d1drza_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
petrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkxrgqafvifkevs
satnalrsxqgfpfydkpxriqyaktdsdiiakxk
>d1nrca_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
trpnhtiyinnlnekikkdelkkslyaifsqfgqildilvsrslkmrgqafvifkevssa
tnalrsmqgfpfydkpmricyaktd
>d1nrcb_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
trpnhtiyinnlnekikkdelkkslyaifsqfgqildilvsrslkmrgqafvifkevssa
tnalrsmqgfpfydkpmricyak
>d1urna_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakm
>d1urnb_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakm
>d1urnc_ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakm
>d2u1a__ 4.48.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
mapaqplsenppnhilfltnlpeetnelmlsmlfnqfpgfkevrlvpgrhdiafvefdne
vqagaardalqgfkitqnnamkisfakk
>d1a9nb_ 4.48.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmrg
>d1a9nd_ 4.48.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmr
>d1u2fa_ 4.48.7.1.4 Splicing factor U2AF 65 KDa subunit {Human (Homo sapiens)}
arrlyvgnipfgiteeammdffnaqmrlggltqapgnpvlavqinqdknfaflefrsvde
ttqamafdgiifqgqslkirrphdyqplpg
>d2u2fa_ 4.48.7.1.4 Splicing factor U2AF 65 KDa subunit {Human (Homo sapiens)}
ahklfigglpnylnddqvkelltsfgplkafnlvkdsatglskgyafceyvdinvtdqai
aglngmqlgdkkllvqrasvgakna
>d1b7fa1 4.48.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fa2 4.48.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1b7fb1 4.48.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fb2 4.48.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1sxl__ 4.48.7.1.5 Sex-lethal protein {Drosophila melanogaster}
msyarpggesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafv
rynkreeaqeaisalnnvipeggsqplsvrlaeehgk
>d2sxl__ 4.48.7.1.5 Sex-lethal protein {Drosophila melanogaster}
asntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqr
aikvlngitvrnkrlkvsyarpggesik
>d3sxla1 4.48.7.1.5 (124-203) Sex-lethal protein {Drosophila melanogaster}
ntnlivnylpqdxtdrelyalfraigpintcrixrdyktgysfgyafvdftsexdsqrai
kvlngitvrnkrlkvsyarp
>d3sxla2 4.48.7.1.5 (206-289) Sex-lethal protein {Drosophila melanogaster}
esikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkreea
qeaisalnnvipeggsqplsvrla
>d3sxlb1 4.48.7.1.5 (124-203) Sex-lethal protein {Drosophila melanogaster}
ntnlivnylpqdxtdrelyalfraigpintcrixrdyktgysfgyafvdftsexdsqrai
kvlngitvrnkrlkvsyarp
>d3sxlb2 4.48.7.1.5 (206-289) Sex-lethal protein {Drosophila melanogaster}
esikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkreea
qeaisalnnvipeggsqplsvrla
>d3sxlc1 4.48.7.1.5 (124-203) Sex-lethal protein {Drosophila melanogaster}
ntnlivnylpqdxtdrelyalfraigpintcrixrdyktgysfgyafvdftsexdsqrai
kvlngitvrnkrlkvsyarp
>d3sxlc2 4.48.7.1.5 (206-289) Sex-lethal protein {Drosophila melanogaster}
esikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkreea
qeaisalnnvipeggsqplsvrla
>d1cvja1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvja2 4.48.7.1.6 (91-179) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrker
>d1cvjb1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjb2 4.48.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvjc1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjc2 4.48.7.1.6 (91-178) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrke
>d1cvjd1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjd2 4.48.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvje1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvje2 4.48.7.1.6 (91-178) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfksrke
>d1cvjf1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjf2 4.48.7.1.6 (91-173) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrf
>d1cvjg1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjg2 4.48.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
aeraiekmngmllndrkvfvgrfks
>d1cvjh1 4.48.7.1.6 (11-90) Poly(A)-binding protein {Human (Homo sapiens)}
aslyvgdlhpdvteamlyekfspagpilsirvcrdmitrrslgyayvnfqqpadaerald
tmnfdvikgkpvrimwsqrd
>d1cvjh2 4.48.7.1.6 (91-175) Poly(A)-binding protein {Human (Homo sapiens)}
pslrksgvgnifiknldksidnkalydtfsafgnilsckvvcdengskgygfvhfetqea
ae
>d1dbda_ 4.48.8.1.1 Papillomavirus-1 E2 protein {Bovine papillomavirus-1, BPV-1}
rrttndgfhllkaggscfalisgtanqvkcyrfrvkknhrhryenctttwftvadngaer
qgqaqilitfgspsqrqdflkhvplppgmnisgftasldf
>d2bopa_ 4.48.8.1.1 Papillomavirus-1 E2 protein {Bovine papillomavirus-1, BPV-1}
scfalisgtanqvkcyrfrvkknhrhryenctttwftvadngaerqgqaqilitfgspsq
rqdflkhvplppgmnisgftasldf
>d1a7ge_ 4.48.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
attpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsqr
ddflntvvipntvsvstgymti
>d1dhma_ 4.48.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1dhmb_ 4.48.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
mattpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsq
rddflntvkipntvsvstgymti
>d1by9__ 4.48.8.1.3 Papillomavirus-1 E2 protein {Human papillomavirus, type 16}
ttpivhlkgdantlkclryrfkkhctlytavsstwhwtghnvkhksaivtltydsewqrd
qflsqvkipktitvstgfms
>d1b3ta_ 4.48.8.1.4 Epstein barr virus nuclear antigen-1 (ebna1) {Epstein-Barr virus}
kggwfgkhrgqggsnpkfeniaeglrallarshverttdegtwvagvfvyggsktslynl
rrgtalaipqcrltplsrlpfgmapgpgpqpgplresivcyfmvflqthifaevlkdaik
dlvmtkpaptcnirvtvcsfddgvdlp
>d1bura2 4.48.9.1.2 (12-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
efkagvkdykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwt
dgltnldrykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalr
alrledlripvayvkt
>d1bwva2 4.48.9.1.3 (7-149) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
riknsryesgvipyakmgywnpdyqvkdtdvlalfrvtpqpgvdpieaaaavagesstat
wtvvwtdlltaadlyrakaykvdqvpnnpeqyfayiayeldlfeegsianltasiignvf
gfkavkalrledmrlplaylktfq
>d5ruba2 4.48.9.1.6 (2-137) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Rhodospirillum rubrum}
dqssryvnlalkeedliaggehvlcayimkpkagygyvataahfaaesstgtnvevcttd
dftrgvdalvyevdeareltkiaypvalfdrnitdgkamiasfltltmgnnqgmgdveya
kmhdfyvpeayralfd
>d2acy__ 4.48.10.1.1 Acylphosphatase {Bovine (Bos taurus)}
aegdtlisvdyeifgkvqgvffrkytqaegkklglvgwvqntdqgtvqgqlqgpaskvrh
mqewletkgspkshidrasfhnekvivkldytdfqivk
>d1aps__ 4.48.10.1.2 Acylphosphatase {Horse (Equus caballus)}
starplksvdyevfgrvqgvcfrmyaedearkigvvgwvkntskgtvtgqvqgpeekvns
mkswlskvgspssridrtnfsnektiskleysnfsvry
>d1dar_4 4.48.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1efga4 4.48.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1elo_4 4.48.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d2efga4 4.48.11.1.1 (600-689) Elongation factor G (EF-G), domain V {Thermus thermophilus}
vilepimrvevttpeeymgdvigdlnarrgqilgmeprgnaqvirafvplaemfgyatdl
rsktqgrgsfvmffdhyqevpkqvqeklik
>d1b64__ 4.48.12.1.1 Guanine nucleotide exchange factor domain from elongation factor-1 beta {Human (Homo sapiens)}
mlvakssilldvkpwddetdmakleecvrsiqadglvwgssklvpvgygikklqiqcvve
ddkvgtdmleeqitafedyvqsmdvaafnki
>d1b70b4 4.48.13.1.1 (682-775) Phenylalanyl-tRNA synthetase {Thermus thermophilus (Thermus aquaticus)}
lafqdpsrhpaafrdlavvvpaptpygevealvreaagpyleslalfdlyqgpplpeghk
slafhlrfrhpkrtlrdeeveeavsrvaealrar
>d1b7yb4 4.48.13.1.1 (682-775) Phenylalanyl-tRNA synthetase {Thermus thermophilus (Thermus aquaticus)}
lafqdpsrhpaafrdlavvvpaptpygevealvreaagpyleslalfdlyqgpplpeghk
slafhlrfrhpkrtlrdeeveeavsrvaealrar
>d1pysb4 4.48.13.1.1 (682-785) Phenylalanyl-tRNA synthetase {Thermus thermophilus (Thermus aquaticus)}
lafqdpsrhpaafrdlavvvpaptpygevealvreaagpyleslalfdlyqgpplpeghk
slafhlrfrhpkrtlrdeeveeavsrvaealrargfglrgldtp
>d1loua_ 4.48.14.1.1 Ribosomal protein S6 {Thermus thermophilus}
mrryevnivlnpnldqsqlalekeiiqraaenygarvekveelglrrlaypiakdpqgyf
lwyqvempedrvndlarelrirdnvrrvmvvksqepf
>d1ris__ 4.48.14.1.1 Ribosomal protein S6 {Thermus thermophilus}
mrryevnivlnpnldqsqlalekeiiqralenygarvekveelglrrlaypiakdpqgyf
lwyqvempedrvndlarelrirdnvrrvmvvksqepf
>d1bxya_ 4.48.15.1.1 Ribosomal protein L30 {Thermus thermophilus}
mprlkvklvkspigypkdqkaalkalglrrlqqervledtpairgnvekvahlvrvevve
>d1bxyb_ 4.48.15.1.1 Ribosomal protein L30 {Thermus thermophilus}
mprlkvklvkspigypkdqkaalkalglrrlqqervledtpairgnvekvahlvrvevve
>d1afi__ 4.48.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afj__ 4.48.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d2hqi__ 4.48.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1aw0__ 4.48.16.1.2 Menkes copper-transporting ATPase {Human (Homo sapiens)}
ltqetvinidgmtcnscvqsiegviskkpgvksirvslansngtveydplltspetlrga
iedmgfdatlsd
>d2aw0__ 4.48.16.1.2 Menkes copper-transporting ATPase {Human (Homo sapiens)}
ltqetvinidgmtcnscvqsiegviskkpgvksirvslansngtveydplltspetlrga
iedmgfdatlsd
>d1cc7a_ 4.48.16.1.3 ATX1 metallochaperone protein {Baker's yeast (Saccharomyces cerevisiae)}
aeikhyqfnvvmtcsgcsgavnkvltklepdvskidislekqlvdvyttlpydfilekik
ktgkevrsgkql
>d1cc8a_ 4.48.16.1.3 ATX1 metallochaperone protein {Baker's yeast (Saccharomyces cerevisiae)}
aeikhyqfnvvmtcsgcsgavnkvltklepdvskidislekqlvdvyttlpydfilekik
ktgkevrsgkql
>d1cpza_ 4.48.16.1.4 Copper chaperone {Enterococcus hirae}
aqefsvkgmscnhcvarieeavgrisgvkkvkvqlkkekavvkfdeanvqateicqaine
lgyqaevi
>d1qupa2 4.48.16.1.5 (2-73) Copper chaperone for superoxide dismutase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
ttndtyeatyaipxhcencvndikaclknvpginslnfdieqqixsvessvapstiintl
rncgkdaiirga
>d1qupb2 4.48.16.1.5 (5-73) Copper chaperone for superoxide dismutase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dtyeatyaipxhcencvndikaclknvpginslnfdieqqixsvessvapstiintlrnc
gkdaiirga
>d1psda3 4.48.17.1.1 (327-410) Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain {Escherichia coli}
fpevslplhggrrlmhihenrpgvltalnkifaeqgvniaaqylqtsaqmgyvvidiead
edvaekalqamkaipgtirarlly
>d1psdb3 4.48.17.1.1 (327-410) Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain {Escherichia coli}
fpevslplhggrrlmhihenrpgvltalnkifaeqgvniaaqylqtsaqmgyvvidiead
edvaekalqamkaipgtirarlly
>d1tdj_2 4.48.17.2.1 (336-423) Threonine deaminase C-terminal domain {Escherichia coli}
qreallavtipeekgsflkfcqllggrsvtefnyrfadaknacifvgvrlsrgleerkei
lqmlndggysvvdlsddemaklhvrymv
>d1tdj_3 4.48.17.2.1 (424-514) Threonine deaminase C-terminal domain {Escherichia coli}
ggrpshplqerlysfefpespgallrflntlgtywnislfhyrshgtdygrvlaafelgd
hepdfetrlnelgydchdetnnpafrfflag
>d1phza1 4.48.17.3.1 (19-115) Phenylalanine hydroxylase N-terminal domain {Rat (Rattus norvegicus)}
gqetsyiednsnqngaislifslkeevgalakvlrlfeendinlthiesrpsrlnkdeye
fftyldkrtkpvlgsiikslrndigatvhelsrdkek
>d2phma1 4.48.17.3.1 (19-115) Phenylalanine hydroxylase N-terminal domain {Rat (Rattus norvegicus)}
gqetsyiednsnqngaislifslkeevgalakvlrlfeendinlthiesrpsrlnkdeye
fftyldkrtkpvlgsiikslrndigatvhelsrdkek
>d1cg2a2 4.48.18.1.1 (214-326) Carboxypeptidase G2, dimerisation domain {Pseudomonas strain rs-16}
sgiayvqvnitgkashagaapelgvnalveasdlvlrtmniddkaknlrfnwtiakagnv
sniipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgrpa
>d1qaxa1 4.48.19.1.1 (111-220) NAD-binding domain of HMG-CoA reductase {Pseudomonas mevalonii}
lmhaqvqivgiqdplnarlsllrrkdeiielanrkdqllnslgggcrdievhtfadtprg
pmlvahlivdvrdamgantvntmaeavaplmeaitggqvrlrilsnladl
>d1mla_2 4.48.20.1.1 (128-197) Probable ACP-binding domain of malonyl-CoA ACP transacylase {Escherichia coli}
gtgamaaiiglddasiakaceeaaegqvvspvnfnspgqvviaghkeaveragaackaag
akralplpvs
>d1a0ob_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetvev
>d1a0od_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1a0of_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetve
>d1a0oh_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1eayc_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfet
>d1eayd_ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
sprriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfvie
adqitfetv
>d1fwp__ 4.48.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetve
>d1kp6a_ 4.48.22.1.1 Killer toxin KP6 alpha-subunit {Smut fungus (Ustilago maydis)}
nnafcagfglsckwecwctahgtgnelryataagcgdhlsksyydaraghclfsddlrnq
fyshcsslnnnmscrslsk
>d1regx_ 4.48.23.1.1 Translational regulator protein regA {Bacteriophage T4}
mieitlkkpedflkvketltrmgiannkdkvlyqschilqkkglyyivhfkemlrmdgrq
vemteedevrrdsiawlledwglieivpgqrtfmkdltnnfrvisfkqkhewklvpkyti
gn
>d1azsa_ 4.48.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
dmmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclri
kilgdcyycvsglpearadhahccvemgmdmieaislvremtgvnvnmrvgihsgrvhcg
vlglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylk
ehsietflil
>d1azsb_ 4.48.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
hqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvekik
tigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklrv
ginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytctc
rgiinvkgkgdlktyfvnt
>d1hka__ 4.48.25.1.1 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK {Escherichia coli}
tvayiaigsnlaspleqvnaalkalgdipeshiltvssfyrtpplgpqdqpdylnaaval
etslapeellnhtqrielqqgrvrkaerwgprtldldimlfgnevinterltvphydmkn
rgfmlwplfeiapelvfpdgemlrqilhtrafdklnkw
>d1mroc_ 4.48.26.1.1 Methyl-coenzyme M reductase gamma chain {Methanobacterium thermoautotrophicum}
aqyypgttkvaqnrrnfcnpeyeleklreisdedvvkilghrapgeeypsvhppleemde
pedairemvepidgakagdrvryiqftdsmyfapaqpyvrsraylcryrgadagtlsgrq
iietrerdlekiskelleteffdparsgvrgksvhghslrldedgmmfdmlrrqiynkdt
grvemvknqigdeldepvdlgepldeetlmekttiyrvdgeayrddveaveimqrihvlr
sqggfnl
>d1mroa2 4.48.26.2.1 (2-269) Alpha chain {Methanobacterium thermoautotrophicum}
adklfinalkkkfeespeekkttfytlggwkqserktefvnagkevaakrgipqynpdig
tplgqrvlmpyqvsttdtyvegddlhfvnnaamqqmwddirrtvivglnhahaviekrlg
kevtpetithyletvnhampgaavvqehmvethpalvadsyvkvftgndeiadeidpafv
idinkqfpedqaetlkaevgdgiwqvvriptivsrtcdgattsrwsamqigmsmisaykq
aageaatgdfayaakxaevihmgtylpv
>d1mrob2 4.48.26.2.2 (2-188) Beta chain {Methanobacterium thermoautotrophicum}
akfedkvdlyddrgnlveeqvplealsplrnpaiksivqgikrtvavnlegienalktak
vggpackimgreldldivgnaesiaaaakemiqvtedddtnvellgggkralvqvpsarf
dvaaeysaaplvtatafvqaiinefdvsmydanmvkaavlgrypqsveymganiatmldi
pqklegp
>d1qlta1 4.48.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
ggyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngaalffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1diqa1 4.48.27.1.2 (243-521) Flavoprotein subunit of p-cresol methylhydroxylase {Pseudomonas putida}
pvfkpfevifedeadiveivdalrplrmsntipnsvviastlweagsahltraqyttepg
htpdsvikqmqkdtgmgawnlyaalygtqeqvdvnwkivtdvfkklgkgrivtqeeagdt
qpfkyraqlmsgvpnlqefglynwrggggsmwfapvseargseckkqaamakrvlhkygl
dyvaefivaprdmhhvidvlydrtnpeetkradacfnelldefekegyavyrvntrfqdr
vaqsygpvkrklehaikravdpnnilapgrsgidlnndf
>d1ftra1 4.48.28.1.1 (1-148) Formylmethanofuran:tetrahydromethanopterin formyltransferase {Methanopyrus kandleri}
meingveiedtfaeafeakmarvlitaashkwamiavkeatgfgtsvimcpaeagidcgy
vppeetpdgrpgvtimighndedelkeqlldrigqcvmtaptasafdampeaekededrv
gyklsffgdgyqeedeldgrkvwkipvv
>d1ftra2 4.48.28.1.1 (149-296) Formylmethanofuran:tetrahydromethanopterin formyltransferase {Methanopyrus kandleri}
egefivedsfgittgvaggnfyimaesqpaglqaaeaavdaikgvegayapfpggivasa
skvgskqydflpastndaycptvednelpegvkcvyeivinglneeavkeamrvgieaac
qqpgvvkisagnfggklgqyeihlhdlf
>d1qd1a1 4.48.28.2.1 (2-180) Formiminotransferase domain of formiminotransferase-cyclodeaminase. {Pig (Sus scrofa)}
sqlvecvpnfsegknqevidaisravaqtpgcvlldvdsgpstnrtvytfvgrpedvveg
alnaaraayqlidmsrhhgehprmgaldvcpfipvrgvtmdecvrcaqafgqrlaeelgv
pvylygeaartagrqslpalrageyealpeklkqaewapdfgpsafvpswgatvagark
>d1qd1a2 4.48.28.2.1 (181-326) Formiminotransferase domain of formiminotransferase-cyclodeaminase. {Pig (Sus scrofa)}
fllafninllstreqahrialdlreqgrgkdqpgrlkkvqaigwyldeknlaqvstnlld
fevtglhtvfeetcreaqelslpvvgsqlvglvplkalldaaafycekenlfllqdehri
rlvvnrlgldslapfkpkeriieylv
>d1aop_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d1aop_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d2aop_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d2aop_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d2gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d2gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d3aop_1 4.48.29.1.1 (82-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
lrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsvg
ldal
>d3aop_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d3geo_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d3geo_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d4aop_1 4.48.29.1.1 (82-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
lrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsvg
ldal
>d4aop_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d4gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d4gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d5aop_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d5aop_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d5gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d5gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d6gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d6gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d7gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d7gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d8gep_1 4.48.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d8gep_2 4.48.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d1bowa_ 4.49.1.1.1 Multidrug-binding domain of transcription activator BmrR {Bacillus subtilis}
rlgevfvldeeeiriiqteaegigpenvlnasysklkkfiesadgftnnsygatfsfqpy
tsidemtyrhiftpvltnkqissitpdmeittipkgryaciaynfspehyflnlqkliky
iadrqltvvsdvyeliipihyspkkqeeyrvemkiril
>d1d8ia_ 4.50.1.1.1 mRNA triphosphatase CET1 {Baker's yeast (Saccharomyces cerevisiae)}
hmyrnvpiwaqkwkptikalqsinvkdlkidpsflniipdddltksvqdwvyatiysiap
elrsfielemkfgviidakgpdrvnppvssqcvfteldahltpnidaslfkelskyirgi
sevtentgkfsiiesqtrdsvyrvglstqrprflrmstdiktgrvgqfiekrhvaqllly
spkdsydvkislnlelpvpdndppekyksqspisertkdrvsyihndsctriditkvenh
nqnsksrqsettheveleintpallnafdnitndskeyaslirtflnngtiirrklssls
y
>d2if1__ 4.51.1.1.1 Eukaryotic translation initiation factor eIF-1 (SUI1) {Human (Homo sapiens)}
mrgshhhhhhtdpmsaiqnlhsfdpfadaskgddllpagtedyihiriqqrngrktlttv
qgiaddydkkklvkafkkkfacngtviehpeygeviqlqgdqrknicqflveiglakddq
lkvhgf
>d1d1ra_ 4.51.1.1.2 YciH {Escherichia coli}
kgdgvvriqrqtsgrkgkgvclitgvdlddaeltklaaelkkkcgcggavkdgvieiqgd
krdllkslleakgmkvklaggle
>d1lbu_2 4.52.1.1.1 (84-213) Zn2+ DD-carboxypeptidase, C-terminal, catalytic domain {Streptomyces albus G}
vnftyaelnrcnsdwsggkvsaataranalvtmwklqamrhamgdkpitvnggfrsvtcn
snvggasnsrhmyghaadlgagsqgfcalaqaarnhgfteilgpgypghndhthvaggdg
rfwsapscgi
>d1vhh__ 4.52.1.2.1 Sonic hedgehog {Murine (Mus musculus)}
kltplaykqfipnvaektlgasgryegkitrnserfkeltpnynpdiifkdeentgadrl
mtqrckdklnalaisvmnqwpgvklrvtegwdedghhseeslhyegravdittsdrdrsk
ygmlarlaveagfdwvyyeskahihcsvkaensvaak
>d1qf6a2 4.53.1.1.1 (2-62) Threonyl-tRNA synthetase (ThrRS), N-terminal 'additional' domain {Escherichia coli}
pvitlpdgsqrhydhavspmdvaldigpglakaciagrvngelvdacdliendaqlsiit
a
>d1c06a_ 4.53.1.2.1 Ribosomal protein S4 {Bacillus stearothermophilus}
mklseyglqlqekqklrhmygvnerqfrktfeeagkmpgkhgenfmillesrldnlvyrl
glartrrqarqlvthghilvdgsrvnipsyrvkpgqtiavreksrnlqvikealeannyi
pdylsfdpekmegtytrlperselpaeinealivefysr
>d1dm9a_ 4.53.1.3.1 Heat shock protein 15 kD {Bacteria (Escherichia coli)}
pavevrldkwlwaarfyktralaremieggkvhyngqrskpskivelnatltlrqgnder
tvivkaiteqrrpaseaallyeetaesvekrekmalarklnalt
>d1qf6a3 4.54.1.1.1 (63-242) Threonyl-tRNA synthetase (ThrRS), second 'additional' domain {Escherichia coli}
kdeegleiirhscahllghaikqlwphtkmaigpvidngfyydvdldrtltqedvealek
rmhelaeknydvikkkvswhearetfanrgesykvsildeniahddkpglyfheeyvdmc
rgphvpnmrfchhfklmktagaywrgdsnnkmlqriygtawadkkalnaylqrleeaakr
>d1bs2a3 4.54.2.1.1 (5-135) Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain {Baker's yeast (Saccharomyces cerevisiae)}
anmisqlkklsiaepavakdshpdvnivdlmrnyisqelskisgvdsslifpalewtntm
ergdllipiprlrikganpkdlavqwaekfpcgdflekveangpfiqfffnpqflaklvi
pdiltrkedyg
>d1dd5a_ 4.54.3.1.1 Ribosome recycling factor, RRF {Thermotoga maritima}
vnpfikeakekmkrtlekiedelrkmrtgkpspaileeikvdyygvptpvnqlatisise
ertlvikpwdksvlsliekainasdlglnpindgnvirlvfpsptteqrekwvkkakeiv
eegkiairnirreilkkikedqkeglipeddakrleneiqkltdefiekldevfeikkee
imef
>d1tig__ 4.55.1.1.1 Translation initiation factor IF3 {Bacillus stearothermophilus}
invkevrlsptieehdfntklrnarkflekgdkvkatirfkgraithkeigqrvldrlse
acadiavvetapkmdgrnmflvlapknd
>d2ifea_ 4.55.1.1.2 Translation initiation factor IF3 {Escherichia coli}
viqvkeikfrpgtdegdyqvklrslirfleegdkakitlrfrgremahqqigmevlnrvk
ddlqelavvesfptkiegrqmimvlapkkkq
>d1qmha_ 4.55.2.1.1 RNA 3'-terminal phosphate cyclase, RPTC {Escherichia coli}
mialdgaqgegggqilrsalslsmitgqpftitsiragrakpgllrqhltavkaateicg
atvegaelgsqrllfrpgtvrggdyrfaigsagsctlvlqtvlpalwfadgpsrvevsgg
tdnpsappadfirrvlepllakigihqqttllrhgfypagggvvatevspvasfntlqlg
ergnivqmrgevllagvprhvaereiatlagsfslheqnihnlprdqgpgntvslevese
niterffvvgekrvsaevvaaqlvkevkrylastaavgeyladqlvlpmalagageftva
hpschlltniavverflpvrfslietdgvtrvsi
>d1uae__ 4.55.2.2.1 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) {Escherichia coli}
mdkfrvqgptklqgevtisgaknaalpilfaallaeepveiqnvpklkdvdtsmkllsql
gakverngsvhidardvnvfcapydlvktmrasiwalgplvarfgqgqvslpggctigar
pvdlhisgleqlgatikleegyvkasvdgrlkgahivmdkvsvgatvtimcaatlaegtt
iienaarepeivdtanflitlgakisgqgtdriviegverlgggvyrvlpdrietgtflv
aaaisrgkiicrnaqpdtldavlaklrdagadievgedwisldmhgkrpkavnvrtaphp
afptdmqaqftllnlvaegtgfitetvfenrfmhvpelsrmgahaeiesntvichgvekl
sgaqvmatdlrasaslvlagciaegttvvdriyhidrgyeriedklralganiervkg
>d1eps__ 4.55.2.2.3 5-enol-pyruvyl shikimate-3-phosphate(EPSP) synthase {Escherichia coli}
mesltlqpiarvdgtinlpgsktvsnralllaalahgktvltnlldsddvrhmlnaltal
gvsytlsadrtrceiignggplhaegalelflgnagtamrplaaalclgsndivltgepr
mkerpighlvdalrlggakityleqenypplrlqggftggnvdvdgsvssqfltallmta
plapedtvirikgdlvskpyiditlnlmktfgveienqhyqqfvvkggqsyqspgtylve
gdassasyflaaaaikggtvkvtgigrnsmqgdirfadvlekmgaticwgddyisctrge
lnaidmdmnhipdaamtiataalfakgttrlrniynwrvketdrlfamatelrkvgaeve
eghdyiritppeklnfaeiatyndhrmamcfslvalsdtpvtildpkctaktfpdyfeql
arisqaa
>d1tola2 4.56.1.1.1 (125-216) C-terminal domain of TolA {Escherichia coli}
sgadinnyagqiksaieskfydassyagktctlriklapdgmlldikpeggdpalcqaal
aaaklakipkppsqavyevfknapldfkpaaa
>d1kpta_ 4.57.1.1.1 Virally encoded KP4 toxin {Ustilago maydis, P4 strain}
lgincrgssqcglsggnlmvrirdqacgnqgqtwcpgerrakvcgtgnsisayvqstnnc
isgteacrhltnlvnhgcrvcgsdplyagndvsrgqltvnyvnsc
>e1kvd.1a 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kvd.1b 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kvd.2c 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kvd.2d 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kve.1a 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kve.1b 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>e1kve.2c 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
wslrwrmqksttiaaiagcsgaatfgglaggivgciaagilailqgfevnwhnggggdrs
npv
>e1kve.2d 4.57.1.2.1 SMK toxin {Halotolerant yeast (Pichia farinosa)}
geattiwgvgadeaidkgtpskndlqnmsadlakngfkghqgvacstvkdgnkdvymikf
slaggsndpggspcsdd
>d1burs_ 4.58.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilgmkkyetlsylppltteqllaevnyllvnnwipclefevkdgfvyrehlkspg
yydgrywtmwklpmfgctdpaqvlneleeckkaypdafiriigfdnkrqvqcisfiaykp
agy
>d1bwvs_ 4.58.1.1.3 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Galdieria partita}
vritqgtfsflpdltdeqikkqidymiskklaigieytndihprnayweiwglplfdvtd
paavlfeinacrkarsnfyikvvgfssvrgiestiisfivnrpkhepgfnlmrqedksrs
ikytihsyesykpedery
>d1bxni_ 4.58.1.1.4 Ribulose 1,5-bisphosphate carboxylase-oxygenase {(Alcaligenes eutrophus)}
mritqgtfsflpeltdeqitkqleyclnqgwavgleytddphprntywemfglpmfdlrd
aagilmeinnarntfpnhyirvtafdsthtvesvvmsfivnrpadepgfrlvrqeepgrt
lrysiesya
>d1rblm_ 4.58.1.1.5 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Synechococcus strain pcc 6301}
smktlpkerrfetfsylpplsdrqiaaqieymieqgfhpliefnehsnpeefywtmwklp
lfacaapqqvldevrecrseygdcyirvagfdnikecqtssfivhrpgr
>d1dcpa_ 4.59.1.1.1 Pterin-4a-carbinolamine dehydratase (PCD)/dimerization cofactor of HNF1 (DCoH) {Rat (Rattus rattus)}
hrlsaeerdqllpnlravgwnelegrdaifkqfhfkdfnrafgfmtrvalqaekldhhpe
wfnvynkvhitlsthecaglserdinlasfieqvavsmt
>d1xxaa_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxab_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxac_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelfd
>d1xxad_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxae_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxaf_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxba_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxbb_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxbc_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxbd_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxbe_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxbf_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
lknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangftv
kdlyeailelf
>d1xxca_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxcb_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxcc_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxcd_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxce_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1xxcf_ 4.59.2.1.1 C-terminal domain of arginine repressor {Escherichia coli}
plknlvldidyndavvvihtspgaaqliarlldslgkaegilgtiagddtifttpangft
vkdlyeailelf
>d1b4aa2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ab2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ac2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ad2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ae2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4af2 4.59.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ba_ 4.59.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bb_ 4.59.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bc_ 4.59.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1bdfa1 4.59.3.1.1 (2-52,179-232) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
qgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriayn
veaarveqrtdldklviemetngtidpeeairraatilaeqleafv
>d1c0aa2 4.59.4.1.1 (288-420) Rrokaryotic AspRS, insert domain {Escherichia coli}
npmeltdvadllksvefavfagpandpkgrvaalrvpggasltrkqideygnfvkiygak
glayikvnerakgleginspvakflnaeiiedildrtaaqdgdmiffgadnkkivadamg
alrlkvgkdlglt
>d1a79a2 4.60.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79b2 4.60.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79c2 4.60.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79d2 4.60.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1gyfa_ 4.61.1.1.1 GYF domain from cd2bp2 protein {Human (Homo sapiens)}
dvmweykwentgdaelygpftsaqmqtwvsegyfpdgvycrkldppggqfynskridfdl
yt
>d1hmja_ 4.62.1.1.1 RNA polymerase subunit H {Methanococcus jannaschii}
pkheivpkeeveeilkrynikiqqlpkiyeddpviqeigakegdvvrvirksptagvsia
yrlvikri
>d1qkla_ 4.63.1.1.1 HRPABC14.4, essential subunit of RNA polymerases I, II and III (RPB6) {Human (Homo sapiens)}
msdnednfdgddfddveedeglddlenaeeegqenveilpsgerpqanqkrittpymtky
erarvlgtralqiamcapvmvelegetdplliamkelkarkipiiirrylpdgsyedwgv
deliitd
>d1qu9a_ 4.64.1.1.1 Conserved 'hypothetical' protein YjgF {Escherichia coli}
sktiatenapaaigpyvqgvdlgnmiitsgqipvnpktgevpadvaaqarqsldnvkaiv
eaaglkvgdivkttvfvkdlndfatvnatyeafftehnatfparsxvevarlpkdvkiei
eaiavrr
>d1qd9a_ 4.64.1.1.2 Purine regulatory protein YabJ {Bacillus subtilis}
tkavhtkhapaaigpysqgiivnnmfyssgqipltpsgemvngdikeqthqvfsnlkavl
eeagasfetvvkatvfiadmeqfaevnevygqyfdthkparscvevarlpkdalveievi
alvk
>d2chsa_ 4.64.1.2.1 Chorismate mutase {Bacillus subtilis}
mirgirgattverdteeeilqktkqllekiieenhtkpedvvqmllsatpdlhavfpaka
vrelsgwqyvpvtcmqemdvtgglkkcirvmmtvqtdvpqdqirhvylekavvl
>d1fsz_2 4.64.2.1.1 (232-356) Cell-division protein FtsZ {Methanococcus jannaschii}
invdfadvkavmnngglamigigesdsekrakeavsmalnsplldvdidgatgalihvmg
pedltleearevvatvssrldpnatiiwgatidenlentvrvllvitgvqsrieftdtgl
krkkl
>d1tuba2 4.64.2.1.2 (246-440) Tubulin alpha-subunit {Bovine (Bos taurus)}
galnvdltefqtnlvpyprghfplatyapvisaekayheqlsvaeitnacfepanqmvkc
dprhgkymaccllyrgdvvpkdvnaaiatiktkrtiqfvdwcptgfkvginyepptvvpg
gdlakvqravcmlsnttaiaeawarldhkfdlmyakrafvhwyvgegmeegefsearedm
aalekdyeevgvdsv
>d1tubb2 4.64.2.1.3 (246-437) Tubulin beta-subunit {Bovine (Bos taurus)}
gqlnadlrklavnmvpfprlhffmpgfapltsrgsqqyraltvpeltqqmfdaknmmaac
dprhgryltvaavfrgrmsmkevdeqmlnvqnknssyfvewipnnvktavcdipprglkm
satfignstaiqelfkriseqftamfrrkaflhwytgegmdemefteaesnmndlvseyq
qyqd
>d1ck9a_ 4.64.3.1.1 Eukaryotic ribosomal protein L30 (eL30) {Baker's yeast (Saccharomyces cerevisiae)}
apvksqesinqklalviksgkytlgykstvkslrqgkskliiiaantpvlrkseleyyam
lsktkvyyfqggnnelgtavgklfrvgvvsileagdsdilttla
>d1clia1 4.64.4.1.1 (5-170) Aminoimidazole ribonucleotide synthetase (PurM) N-terminal domain {(Escherichia coli) |A,B,C,D|}
tslsykdagvdidagnalvgrikgvvkktrrpevmgglggfgalcalpqkyrepvlvsgt
dgvgtklrlamdlkrhdtigidlvamcvndlvvqgaeplffldyyatgkldvdtasavis
giaegclqsgcslvggetaempgmyhgedydvagfcvgvvekseii
>d1bjpa_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1bjpb_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1bjpc_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelas
>d1bjpd_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
>d1bjpe_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqihilegrsdeqketlirevseaisrsldapltsvrviitemakghfgiggelaskv
rr
>d1otfa_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otfb_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otfc_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otfd_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otfe_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otff_ 4.65.1.1.1 4-oxalocrotonate tautomerase {Pseudomonas}
piaqlyiiegrtdeqketlirqvseamansldaplervrvlitempknhfgiggepask
>d1otga_ 4.65.1.2.1 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) {Escherichia coli}
phfivecsdnireeadlpglfakvnptlaatgifplagirsrvhwvdtwqmadgqhdyaf
vhmtlkigagrslesrqqagemlfelikthfaalmesrllalsfeieelhptlnfkqnnv
halfk
>d1mfia_ 4.65.1.3.3 Microphage migration inhibition factor (MIF) {Mouse (Mus musculus)}
pmfivntnvprasvpegflseltqqlaqatgkpaqyiavhvvpdqlmtfsgtndpcalcs
lhsigkiggaqnrnyskllcgllsdrlhispdrvyinyydmnaanvgwngstfa
>d1dpta_ 4.65.1.3.4 D-dopachrome tautomerase {Human (Homo sapiens)}
pfleldtnlpanrvpaglekrlcaaaasilgkpadrvnvtvrpglamalsgstepcaqls
issigvvgtaednrshsahffefltkelalgqdrilirffpleswqigkigtvmtfl
>d1gd1o2 4.66.1.1.2 (149-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Bacillus stearothermophilus, nca 1503}
cttnclapfakvlheqfgivrgmmttvhsytndqrildlphkdlrraraaaesiiptttg
aakavalvlpelkgklngmamrvptpnvsvvdlvaelekevtveevnaalkaaaegelkg
ilayseeplvsrdyngstvsstidalstmvidgkmvkvvswyd
>d1b7go2 4.66.1.1.5 (139-300) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
cnttallrtictvnkvskvekvrativrraadqkevkkgpinslvpdpatvpshhakdvn
svirnldiatmaviapttlmhmhfinitlkdkvekkdilsvlentprivlisskydaeat
aelvevardlkrdrndipevmifsdsiyvkddevmlmyavhq
>d1dssg2 4.66.1.1.9 (150-312) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Lobster (Palinurus versicolor)}
ttnclapvakvlhenfeiveglmttvhavtatqktvdgpsakdwrggrgaaqniipsstg
aakavgkvipeldgkltgmafrvptpnvsvvdltvrlgkecsyddikaamkaasegplqg
vlgyteddvvscdftgdnrssifdakagiqlsktfvkvvswyd
>d1brma2 4.66.1.1.11 (134-354) Aspartate beta-semialdehyde dehydrogenase {Escherichia coli}
nctvslmlmslgglfandlvdwvsvatyqaasgggarhmrelltqmghlyghvadelatp
ssaildierkvttltrsgelpvdnfgvplagslipwidkqldngqsreewkgqaetnkil
ntssvipvdglcvrvgalrchsqaftiklkkdvsiptveellaahnpwakvvpndreitm
reltpaavtgtlttpvgrlrklnmgpeflsaftvgdqllwg
>d2dap_2 4.66.1.2.1 (119-268) Diaminopimelic acid dehydrogenase (DAPDH) {Corynebacterium glutamicum}
wdpgmfsinrvyaaavlaehqqhtfwgpglsqghsdalrripgvqkavqytlpsedalek
arrgeagdltgkqthkrqcfvvadaadheriendirtmpdyfvgyevevnfideatfdse
htgmphgghvittgdtggfnhtveyilkld
>d1dih_2 4.66.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1ofga2 4.66.1.3.1 (161-322) Glucose-fructose oxidoreductase {Zymomonas mobilis}
dpmnraavklirenqlgklgmvttdnsdvmdqndpaqqwrlrrelagggslmdigiygln
gtryllgeepievraytysdpnderfvevedriiwqmrfrsgalshgassysttttsrfs
vqgdkavllmdpatgyyqnlisvqtpghanqsmmpqfimpan
>d1dpga2 4.66.1.3.2 (182-412,427-485) Glucose 6-phosphate dehydrogenase {Leuconostoc mesenteroides}
kemvqniaalrfgnpifdaawnkdyiknvqvtlsevlgveeragyydtagalldmiqnht
mqivgwlamekpesftdkdiraaknaafnalkiydeaevnkyfvraqygagdsadfkpyl
eeldvpadsknntfiagelqfdlprwegvpfyvrsgkrlaakqtrvdivfkagtfnfgse
qeaqeavlsiiidpkgaielklnaksvedafntrtidlgwtvsdedkkntpXgsnfadwn
gvsiawkfvdaisavytadkapletyksgsmgpeasdkllaangdawvfkg
>d1d6ua4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1d6ub4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1d6ya4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1d6yb4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1d6za4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1d6zb4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1oaca4 4.67.1.1.1 (5-90) Copper amine oxidase, domain N {Escherichia coli}
ahmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmk
dnkawvsdtfindvfqsgldqtfqve
>d1oacb4 4.67.1.1.1 (5-90) Copper amine oxidase, domain N {Escherichia coli}
ahmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmk
dnkawvsdtfindvfqsgldqtfqve
>d1qafa4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1qafb4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1qaka4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1qakb4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1qala4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1qalb4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1spua4 4.67.1.1.1 (7-90) Copper amine oxidase, domain N {Escherichia coli}
mvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkdn
kawvsdtfindvfqsgldqtfqve
>d1spub4 4.67.1.1.1 (6-90) Copper amine oxidase, domain N {Escherichia coli}
hmvpmdktlkefgadvqwddyaqlftlikdgayvkvkpgaqtaivngqplalqvpvvmkd
nkawvsdtfindvfqsgldqtfqve
>d1dlxa_ 4.67.2.1.1 C-terminal domain of frataxin {Human (Homo sapiens) |A|}
dettyerlaeetldslaeffedladkpytfedydvsfgsgvltvklggdlgtyvinkqtp
nkqiwlsspssgpkrydwtgknwvyshdgvslhellaaeltkalktkldlsslaysgkda
>d1bp1_1 4.68.1.1.1 (1-217) Bactericidal permeability-increasing protein, BPI {Human (Homo sapiens)}
vnpgvvvrisqkgldyasqqgtaalqkelkrikipdysdsfkikhlgkghysfysmdire
fqlpssqismvpnvglkfsisnanikisgkwkaqkrflkmsgnfdlsiegmsisadlklg
snptsgkptitcsscsshinsvhvhiskskvgwliqlfhkkiesalrnkmnsqvcekvtn
svssklqpyfqtlpvmtkidsvaginyglvappatta
>d1bp1_2 4.68.1.1.1 (218-456) Bactericidal permeability-increasing protein, BPI {Human (Homo sapiens)}
etldvqmkgefysenhhnpppfappvmefpaahdrmvylglsdyffntaglvyqeagvlk
mtlrddmipkeskfrlttkffgtflpevakkfpnmkiqihvsastpphlsvqptgltfyp
avdvqafavlpnsalaslfligmhttgsmevsaesnrlvgelkldrlllelkhsnigpfp
vellqdimnyivpilvlprvneklqkgfplptparvqlynvvlqphqnfllfgadvvyk
>d2sici_ 4.69.1.1.2 Subtilisin inhibitor {Streptomyces albogriseolus, s-3253}
yapsalvltvgkgvsattaaperavtltcapgpsgthpaagsacadlaavggdlnaltrg
edvmcpmvydpvlltvdgvwqgkrvsyervfsnecemnahgssvfaf
>d1msc__ 4.70.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkyti
kvevpkvatqtvggvelpvaarrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1unaa_ 4.70.1.1.2 GA coat protein {Bacteriophage GA}
atlhsfvlvdnggtgnvtvvpvsnangvaewlsnnsrsqayrvtasyrasgadkrkytik
levpkivtqvvngvelpvsawkayasidltipifaatddvtvisksltglfkvgnpiaea
issqsgfya
>d1qbea_ 4.70.1.1.4 Qbeta coat protein {Bacteriophage Qbeta}
akletvtlgnigkdgkqtlvlnprgvnptngvaslsqagavpalekrvtvsvsqpsrnrk
nykvqvkiqnptactangscdpsvtrqayadvtfsftqystdeerafvrtelaallaspl
lidaidqlnpay
>d1dwna_ 4.70.1.1.5 PP7 coat protein {Bacteriophage PP7}
sktivlsvgeatrtlteiqstadrqifeekvgplvgrlrltaslrqngaktayrvnlkld
qadvvdcstsvcgelpkvrytqvwshdvtivansteasrkslydltkslvatsqvedlvv
nlvplgr
>d1ap8__ 4.71.1.1.1 Translation initiation factor eIF4e {Baker's yeast (Saccharomyces cerevisiae)}
msveevskkfeenvsvddttatpktvlsdsahfdvkhplntkwtlwytkpavdkseswsd
llrpvtsfqtveefwaiiqnipephelplksdyhvfrndvrpewedeanakggkwsfqlr
gkgadidelwlrtllavigetideddsqingvvlsirkggnkfalwtksedkepllrigg
kfkqvlkltddghleffphssangrhpqpsitl
>d3grs_3 4.72.1.1.1 (364-478) Glutathione reductase {Human (Homo sapiens)}
ynniptvvfshppigtvgltedeaihkygienvktystsftpmyhavtkrktkcvmkmvc
ankeekvvgihmqglgcdemlqgfavavkmgatkadfdntvaihptsseelvtlr
>d1gesa3 4.72.1.1.2 (336-450) Glutathione reductase {Escherichia coli}
ysniptvvfshppigtvgltepqareqygddqvkvykssftamytavtthrqpcrmklvc
vgseekivgihgigfgmdemlqgfavalkmgatkkdfdntvaihptaaeefvtmr
>d1feca3 4.72.1.1.3 (358-485) Trypanothione reductase {Crithidia fasciculata}
htkvacavfsippmgvcgyveedaakkydqvavyessftplmhnisgstykkfmvrivtn
hadgevlgvhmlgdsspeiiqsvaiclkmgakisdfyntigvhptsaeelcsmrtpayfy
ekgkrvek
>d1nhp_3 4.72.1.1.5 (322-447) NADH peroxidase {Enterococcus faecalis}
gvqgssglavfdykfastginevmaqklgketkavtvvedylmdfnpdkqkawfklvydp
ettqilgaqlmskadltaninaislaiqakmtiedlayadfffqpafdkpwniintaale
avkqer
>d1lvl_3 4.72.1.1.6 (336-458) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
paaiaavcftdpevvvvgktpeqasqqgldcivaqfpfaangramslesksgfvrvvarr
dnhlilgwqavgvavselstafaqslemgacledvagtihahptlgeavqeaalralgha
lhi
>d3lada3 4.72.1.1.6 (349-472) Dihydrolipoamide dehydrogenase {Pseudomonas putida}
ydlipaviythpeiagvgkteqalkaegvainvgvfpfaasgramaandtagfvkviada
ktdrvlgvhvigpsaaelvqqgaiamefgtsaedlgmmvfahpalsealheaalavsgha
ihva
>d1ebda3 4.72.1.1.7 (347-461) Dihydrolipoamide dehydrogenase {Bacillus stearothermophilus}
aipavvfsdpecasvgyfeqqakdegidviaakfpfaangralalndtdgflklvvrked
gviigaqiigpnasdmiaelglaieagmtaedialtihahptlgeiameaaeval
>d1ojt_3 4.72.1.1.8 (471-598) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
arvipgvaytspevawvgetelsakasarkitkanfpwaasgraiangcdkpftklifda
etgriigggivgpnggdmigevclaiemgcdaadigktihphptlgesigmaaevalgtc
tdlppqkk
>d1fcda3 4.72.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
pgtpsylntcysilapaygisvaaiyrpnadgsaiesvpdsggvtpvdapdwvlerevqy
ayswynnivhdtfg
>d1fcdb3 4.72.1.1.9 (328-401) Flavocytochrome c sulfide dehydrogenase, FCSD, flavin-binding subunit {Purple phototrophic bacterium (Chromatium vinosum)}
pgtpsylntcysilapaygisvaaiyrpnadgsaiesvpdsggvtpvdapdwvlerevqy
ayswynnivhdtfg
>d1qj2c1 4.72.2.1.1 (178-285) Carbon monoxide (CO) dehydrogenase flavoprotein C-domain {Pseudomonas carboxydovorans}
ghgyayeklkrkigdyataaaavvltmsggkcvtasigltnvantplwaeeagkvlvgta
ldkpaldkavalaeaitapasdgrgpaeyrtkmagvmlrraverakar
>d1srsa_ 4.73.1.1.1 Serum response factor (SRF) core {Human (Homo sapiens)}
trgrvkikmefidnklrryttfskrktgimkkayelstltgtqvlllvasetghvytfat
rklqpmitsetgkaliqtclnspd
>d1srsb_ 4.73.1.1.1 Serum response factor (SRF) core {Human (Homo sapiens)}
trgrvkikmefidnklrryttfskrktgimkkayelstltgtqvlllvasetghvytfat
rklqpmitsetgkaliqtcl
>d1mnma_ 4.73.1.1.2 MCM1 transcriptional regulator {Baker's yeast (Saccharomyces cerevisiae)}
qkerrkieikfienktrrhvtfskrkhgimkkafelsvltgtqvlllvvsetglvytfst
pkfepivtqqegrnliqaclnapdd
>d1mnmb_ 4.73.1.1.2 MCM1 transcriptional regulator {Baker's yeast (Saccharomyces cerevisiae)}
rrkieikfienktrrhvtfskrkhgimkkafelsvltgtqvlllvvsetglvytfstpkf
epivtqqegrnliqaclnapd
>d1tbd__ 4.74.1.1.1 The origin DNA-binding domain of SV40 T-antigen {Simian virus 40, SV40}
gskvedpkdfpsellsflshavfsnrtlacfaiyttkekaallykkimekysvtfisrhn
synhnilffltphrhrvsainnyaqklctfsflickgvnkeylmysaltrdpfsvieesl
pgglkehdfnpess
>d1nox__ 4.75.1.1.1 NADH oxidase {Thermus thermophilus, HB8}
pvldaktaalkrrsirryrkdpvpegllreileaalrapsawnlqpwrivvvrdpatkra
lreaafgqahveeapvvlvlyadledalahldevihpgvqgerreaqkqaiqrafaamgq
earkawasgqsyillgyllllleayglgsvpmlgfdpervrailglpsraaipalvalgy
paeegypshrlplervvlwr
>d1bkja_ 4.75.1.1.2 Flavin reductase P (NADPH:FMN oxidoreductase) {Vibrio harveyi}
nntietilahrsirkftavpitdeqrqtiiqaglaassssmlqvvsivrvtdsekrnela
qfagnqayvesaaeflvfcidyqrhatinpdvqadfteltligavdsgimaqncllaaes
mglggvyigglrnsaaqvdellglpensavlfgmclghpdqnpevkprlpahvvvhenqy
qelnlddiqsydqtmqayyasrtsnqklstwsqevtgklagesrphilpylnskglakr
>d1vfra_ 4.75.1.1.3 Flavin reductase P (NADPH:FMN oxidoreductase) {Vibrio fischeri}
thpiihdlenrytskkydpskkvsqedlavllealrlsassinsqpwkfiviesdaakqr
mhdsfanmhqfnqphikacshvilfanklsytrddydvvlskavadkriteeqkeaafas
fkfvelncdengehkawtkpqaylalgnalhtlarlnidsttmegidpellseifadelk
gyechvalaigyhhpsedynaslpksrkafedvitil
>d1kuh__ 4.76.1.1.1 Zinc protease {Streptomyces caespitosus}
tvtvtydpsnapsfqqeianaaqiwnssvrnvqlraggnadfsyyegndsrgsyaqtdgh
grgyifldyqqnqqydstrvtahetghvlglpdhyqgpcselmsgggpgpsctnpypnaq
ersrvnalwang
>d1ezm_2 4.76.1.2.1 (1-153) Elastase {Pseudomonas aeruginosa}
aeaggpggnqkigkytygsdygplivndrcemddgnvitvdmnsstddskttpfrfacpt
ntykqvngaysplndahffggvvfklyrdwfgtsplthklymkvhygrsvenaywdgtam
lfgdgatmfyplvsldvaahevshgfteqnsgl
>d8tlne2 4.76.1.2.2 (1-155) Thermolysin {Bacillus thermoproteolyticus}
itgtstvgvgrgvlgdqkninttystyyylqdntrgdgiftydakyrttlpgslwadadn
qffasydapavdahyyagvtydyyknvhnrlsydgnnaairssvhysqgynnafwngsem
vygdgdgqtfiplsggidvvahelthavtdytagl
>d1bqba2 4.76.1.2.4 (1-154) Aureolysin {Staphylococcus aureus}
aaatgtgkgvlgdtkdininsidggfsledlthqgklsaynfndqtgqatlitnedenfv
kddqragvdanyyakqtydyykntfgresydnhgspivslthvnhyggqdnrnnaawigd
kmiygdgdgrtftnlsgandvvaheithgvtqqt
>d1lml__ 4.76.1.3.1 Leishmanolysin {Leishmania major}
vvrdvnwgalriavstedltdpayhcarvgqhvkdhagaivtctaediltnekrdilvkh
lipqavqlhterlkvqqvqgkwkvtdmvgdicgdfkvpqahitegfsntdfvmyvasvps
eegvlawattcqtfsdghpavgvinipaaniasrydqlvtrvvthemahalgfsgpffed
arivanvpnvrgknfdvpvinsstavakareqygcdtleylevedqggagsagshikmrn
aqdelmapaaaagyytaltmaifqdlgfyqadfskaevmpwgqnagcafltnkcmeqsvt
qwpamfcnesedaircptsrlslgacgvtrhpglppywqyftdpslagvsafmdycpvvv
pysdgsctqraseahasllpfnvfsdaarcidgafrpkatdgivksyaglcanvqcdtat
rtysvqvhgsndytnctpglrvelstvsnafegggyitcppyvevcqgnvqaakd
>d1kapp2 4.76.1.4.1 (1-246) Metallo protease, catalytic (N-terminal) domain {Pseudomonas aeruginosa, alkaline protease}
grsdaytqvdnflhayarggdelvnghpsytvdqaaeqilreqaswqkapgdsvltlsys
fltkpndffntpwkyvsdiyslgkfsafsaqqqaqaklslqswsdvtnihfvdagqgdqg
dltfgnfsssvggaafaflpdvpdalkgqswylinssysanvnpangnygrqtltheigh
tlglshpgdynagegdptyadatyaedtraysvmsyweeqntgqdfkgayssapllddia
aiqkly
>d3btaa3 4.76.1.5.1 (1-546) Botulinum neurotoxin serotype A {(Clostridium botulinum)}
pfvnkqfnykdpvngvdiayikipnvgqmqpvkafkihnkiwviperdtftnpeegdlnp
ppeakqvpvsyydstylstdnekdnylkgvtklferiystdlgrmlltsivrgipfwggs
tidtelkvidtncinviqpdgsyrseelnlviigpsadiiqfecksfghevlnltrngyg
stqyirfspdftfgfeeslevdtnpllgagkfatdpavtlahelihaghrlygiainpnr
vfkvntnayyemsglevsfeelrtfgghdakfidslqenefrlyyynkfkdiastlnkak
sivgttaslqymknvfkekyllsedtsgkfsvdklkfdklykmlteiytednfvkffkvl
nrktylnfdkavfkinivpkvnytiydgfnlrntnlaanfngqnteinnmnftklknftg
lfefykllcvrgiitsktksldkgynkalndlcikvnnwdlffspsednftndlnkgeei
tsdtnieaaeenisldliqqyyltfnfdnepenisienlssdiigqlelmpnierfpngk
kyeldk
>d1ast__ 4.76.1.6.1 Astacin {European fresh water crayfish (Astacus astacus)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1atla_ 4.76.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1buda_ 4.76.1.7.3 Snake venom metalloprotease {Five-pace snake (Agkistrodon acutus), acutolysin A}
fqrymeivivvdhsmvkkyngdsdsikawvyemintitesysylkidislsgleiwsgkd
lidveasagntlksfgewrakdlihrishdnaqlltatdfdgatiglayvasmcnpkrsv
gviqdhssvnrlvaitlahemahnlgvshdegscscggkscimspsisdetikyfsdcsy
iqcrdyiskenppciln
>d1bkca_ 4.76.1.8.1 TNF-alpha converting enzyme, TACE, catalytic domain {Human (Homo sapiens)}
dpmkntckllvvadhrfyrymgrgeestttnylielidrvddiyrntawdnagfkgygiq
ieqirilkspqevkpgekhynmaksypneekdawdvkmlleqfsfdiaeeaskvclahlf
tyqdfdmgtlglayvgspranshggvcpkayyspvgkkniylnsgltstknygktiltke
adlvtthelghnfgaehdpdglaecapnedqggkyvmypiavsgdhennkmfsqcskqsi
yktieskaqecfqer
>d1hfc__ 4.76.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
prweqthltyrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadimisfvrg
dhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahelghslgl
shstdigalmypsytfsgdvqlaqddidgiqaiygrs
>d1qiba_ 4.76.1.9.3 Gelatinase A {Human (Homo sapiens)}
rkpkwdknqityriigytpdldpetvddafarafqvwsdvtplrfsrihdgeadiminfg
rwehgdgypfdgkdgllahafapgtgvggdshfdddelwslgkgvgyslflvaahefgha
mglehsqdpgalmapiytytknfrlsqddikgiqelygasp
>d1mmq__ 4.76.1.9.6 Matrilysin (MMP-9) {Human (Homo sapiens)}
yslfpnspkwtskvvtyrivsytrdlphitvdrlvskalnmwgkeiplhfrkvvwgtadi
migfargahgdsypfdgpgntlahafapgtglggdahfdederwtdgsslginflyaath
elghslgmghssdpnavmyptygngdpqnfklsqddikgiqklygk
>d1bqqm_ 4.76.1.9.8 Membrane-type matrix metalloproteinase (CDMT1-MMP) {Human (Homo sapiens)}
iqglkwqhneitfciqnytpkvgeyatyeairkafrvwesatplrfrevpyayireghek
qadimiffaegfhgdstpfdgeggflahayfpgpniggdthfdsaepwtvrnedlngndi
flvavhelghalglehssdpsaimapfyqwmdtenfvlpdddrrgiqqlygges
>d1qba_4 4.76.2.1.1 (201-337) Bacterial chitobiase, Domain 2 {Serratia marcescens}
snadlqtlpagalrgkivptpmqvkvhaqdadlrkgvaldlstlvkpaadvvsqrfallg
vpvqtngypiktdiqpgkfkgamavsgayelkigkkeaqvigfdqagvfyglqsilslvp
sdgsgkiatldasdapr
>d1lkka_ 4.77.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
lepepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhy
kirnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1shaa_ 4.77.1.1.2 v-src tyrosine kinase {Rous sarcoma virus, Schmidt-ruppin strain a}
aeewyfgkitrreserlllnpenprgtflvresettkgayclsvsdfdnakglnvkhyki
rkldsggfyitsrtqfsslqqlvayyskhadglchrltnvcpt
>d1aotf_ 4.77.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1ayaa_ 4.77.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ghu__ 4.77.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {Human (Homo sapiens)}
gswffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvlrdgagk
yflwvvkfnslnelvdyhrstsvsrnqqiflrdie
>d1zfpe_ 4.77.1.1.7 Growth factor receptor-bound protein 2 (GRB2) {Human (Homo sapiens)}
kphpwffgkiprakaeemlskqrhdgafliresesapgdfslsvkfgndvqhfkvlrdga
gkyflwvvkfnslnelvdyhrstsvsrnqqiflrdieq
>d1qcfa2 4.77.1.1.8 (146-248) Hemopoetic cell kinase Hck {Human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1mil__ 4.77.1.1.9 Shc adaptor protein {Human (Homo sapiens)}
gsqlrgepwfhgklsrreaeallqlngdflvrestttpgqyvltglqsgqpkhlllvdpe
gvvrtkdhrfesvshlisyhmdnhlpiisagselclqqpverkl
>d1qada_ 4.77.1.1.10 Phosphatidylinositol 3-kinase, p85-alpha subunit {Bovine (Bos taurus)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvya
>d2pna__ 4.77.1.1.10 Phosphatidylinositol 3-kinase, p85-alpha subunit {Bovine (Bos taurus)}
lqdaewywgdisreevneklrdtadgtflvrdastkmhgdytltlrkggnnklikifhrd
gkygfsdpltfnsvvelinhyrneslaqynpkldvkllypvsky
>d1a81a_ 4.77.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1csya_ 4.77.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
gsrrasvgshekmpwfhgkisreeseqivligsktngkflirardnngsyalcllhegkv
lhyridkdktgklsipegkkfdtlwqlvehysykadgllrvltvpcqkigtq
>d2plda_ 4.77.1.1.14 Phospholipase C-gamma-1 {Bovine (Bos taurus)}
gspgiheskewyhasltraqaehmlmrvprdgaflvrkrnepnsyaisfraegkikhcrv
qqegqtvmlgnsefdslvdlisyyekhplyrkmklrypineenss
>d1blk__ 4.77.1.1.15 P55 Blk protein tyrosine kinase {Mouse (Mus musculus)}
gsvapvetlevekwffrtisrkdaerqllapmnkagsfliresesnkgafslsvkdittq
gevvkhykirsldnggyyispritfptlqalvqhyskkgdglcqkltlpcvnla
>d2abl_2 4.77.1.1.16 (140-237) Bcr-abl tyrosine kinase {Human (Homo sapiens)}
slekhswyhgpvsrnaaeyllssgingsflvresesspgqrsislryegrvyhyrintas
dgklyvssesrfntlaelvhhhstvadglittlhypap
>d1bf5a3 4.77.1.1.17 (569-710) STAT-1 {Human (Homo sapiens)}
llplwndgcimgfiskererallkdqqpgtfllrfsessregaitftwversqnggepdf
havepytkkelsavtfpdiirnykvmaaenipenplkylypnidkdhafgkyysrgxikt
elisvs
>d1bg1a3 4.77.1.1.18 (576-716) STAT3b {Mouse (Mus musculus)}
ilalwnegyimgfiskererailstkppgtfllrfsesskeggvtftwvekdisgstqiq
svepytkqqlnnmsfaeiimgykimdatnilvsplvylypdipkeeafgkycrpesqehp
eadpgsaapxlktkficvtpf
>d1b47a3 4.77.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47b3 4.77.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47c3 4.77.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d2cbla3 4.77.1.1.19 (264-351) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdltg
>d2shpa3 4.77.1.1.20 (111-218) Tyrosine phoshatase shp-2 {Human (Homo sapiens)}
rwfhghlsgkeaeklltekgkhgsflvresqshpgdfvlsvrtgddkgesndgkskvthv
mircqelkydvgggerfdsltdlvehykknpmvetlgtvlqlkqplnt
>d1d4ta_ 4.77.1.1.21 The Xlp protein Sap {Human (Homo sapiens)}
mdavavyhgkisretgeklllatgldgsyllrdsesvpgvyclcvlyhgyiytyrvsqte
tgswsaetapgvhkryfrkiknlisafqkpdqgiviplqypvek
>d1jem__ 4.78.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {Bacillus subtilis}
aqktfkvtadsgixarpatvlvqtaskydadvnleyngktvnlksimgvvslgiakgaei
tisasgadendalnaleetmkseglge
>d1spha_ 4.78.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {Bacillus subtilis}
aqktfkvtadsgiharpatvlvqtaskydadvnleyngktvnlkdimgvmslgiakgaei
tisasgadendalnaleetmkseglge
>d1sphb_ 4.78.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {Bacillus subtilis}
aqktfkvtadsgiharpatvlvqtaskydadvnleyngktvnlkdimgvmslgiakgaei
tisasgadendalnaleetmkseglge
>d2hid__ 4.78.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {Bacillus subtilis}
aqktfkvtadsgiharpatvlvqtaskydadvnleyngktvnlksimgvvslgiakgaei
tisasgadendalnaleetmkseglge
>d2hpr__ 4.78.1.1.1 Histidine-containing phosphocarrier proteins (HPr) {Bacillus subtilis}
aqktfkvtadsgiharpatvlvqtaskydadvnleyngktvnlksimgvvslgiakgaei
tisasgadendalnaleetmkceglge
>d1ptf__ 4.78.1.1.2 Histidine-containing phosphocarrier proteins (HPr) {Streptococcus faecalis}
mekkefhivaetgiharpatllvqtaskfnsdinleykgksvnlksimgvmslgvgqgsd
vtitvdgadeaegmaaivetlqkegla
>d1hdn__ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d1opd__ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfeqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakdlfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d1pfh__ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d1poh__ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d2jelp_ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d3ezab_ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d3ezbb_ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d3ezeb_ 4.78.1.1.3 Histidine-containing phosphocarrier proteins (HPr) {Escherichia coli}
mfqqevtitapnglhtrpaaqfvkeakgftseitvtsngksasakslfklqtlgltqgtv
vtisaegedeqkavehlvklmaele
>d1pch__ 4.78.1.1.4 Histidine-containing phosphocarrier proteins (HPr) {Mycoplasma capricolum}
akfsaiitdkvglharpasvlakeaskfssnitiianekqgnlksimnvmamaiktgtei
tiqadgndadqaiqaikqtmidtaliqg
>d1zer__ 4.78.1.1.5 Histidine-containing phosphocarrier proteins (HPr) {Staphylococcus aureus}
meqnsyviidetgiharpatmlvqtaskfdsdiqleyngkkvnlksimgvmslgvgkdae
itiyadgsdesdaiqaisdvlskeglt
>d1iba__ 4.79.1.1.1 Glucose permease domain IIB {Escherichia coli}
mapalvaafggkenitnldacitrlrvsvadvskvdqaglkklgaagvvvagsgvqaifg
tksdnlktemdeyirnfg
>d1bp7a_ 4.79.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
ntkynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwfldklvde
igvgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlpsakespdk
flevctwvdqiaalndsktrkttsetvravld
>d1b24a1 4.79.2.1.2 (7-99) I-dmoI {Desulfurococcus mobilis}
vsgisayllgliigdgglyklkykgnrseyrvvitqksenlikqhiaplxqflidelnvk
skiqivkgdtryelrvsskklyyyfanxlerir
>d1b24a2 4.79.2.1.2 (100-179) I-dmoI {Desulfurococcus mobilis}
lfnxreqiafikglyvaegdktlkrlriwnknkalleivsrwlnnlgvrntihlddhrhg
vyvlnislrdrikfvhtils
>d1dfaa2 4.79.2.2.1 (181-298) PI-SceI {Baker's yeast (Saccharomyces cerevisiae)}
pilyendhffdymqkskfhltiegpkvlayllglwigdglsdratfsvdsrdtslmervt
eyaeklnlcaeykdrkepqvaktvnlyskvvrgngirnnlntenplwdaivglgflkd
>d1dfaa3 4.79.2.2.1 (299-415) PI-SceI {Baker's yeast (Saccharomyces cerevisiae)}
gvknipsflstdnigtretflaglidsdgyvtdehgikatiktihtsvrdglvslarslg
lvvsvnaepakvdmngtkhkisyaiymsggdvllnvlskcagskkfrpapaaafare
>d1a8ra_ 4.80.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1b66a_ 4.80.1.2.1 6-pyruvoyl tetrahydropterin synthase {Rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1dhn__ 4.80.1.3.1 7,8-dihidroneopterin aldolase {Staphylococcus aureus}
mqdtiflkgmrfygyhgalsaeneigqifkvdvtlkvdlseagrtdnvidtvhygevfee
vksimegkavnllehlaerianrinsqynrvmetkvritkenppipghydgvgieivren
k
>d1b9la_ 4.80.1.3.2 7,8-dihydroneopterin triphosphate epimerase {Escherichia coli}
aqpaaiiriknlrlrtfigikeeeinnrqdivinvtihypadkartsedindalnyrtvt
kniiqhvennrfsllekltqdvldiarehhwvtyaeveidklhalryadsvsmtlswqr
>d1uox_1 4.80.1.4.1 (1-136) Urate oxidase (uricase) {Aspergillus flavus}
savkaarygkdnvrvykvhkdektgvqtvyemtvcvllegeietsytkadnsvivatdsi
kntiyitakqnpvtppelfgsilgthfiekynhihaahvnivchrwtrmdidgkphphsf
irdseekrnvqvdvve
>d1uox_2 4.80.1.4.1 (137-295) Urate oxidase (uricase) {Aspergillus flavus}
gkgidiksslsgltvlkstnsqfwgflrdeyttlketwdrilstdvdatwqwknfsglqe
vrshvpkfdatwatarevtlktfaednsasvqatmykmaeqilarqqlietveyslpnkh
yfeidlswhkglqntgknaevfapqsdpnglikctvgrs
>d1puc__ 4.81.1.1.1 suc1 {Yeast (Saccharomyces pombe)}
sksgvprlltasererlepfidqihyspryaddeyeyrhvmlpkamlkaiptdyfnpetg
tlrilqeeewrglgitqslgwemyevhvpephillfkrekd
>d1cksa_ 4.81.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpk
>d1cksb_ 4.81.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1cksc_ 4.81.1.1.2 CksHs2 {Human (Homo sapiens)}
ahkqiyysdkyfdehyeyrhvmlprelskqvpkthlmseeewrrlgvqqslgwvhymihe
pephillfrrplpkdqqk
>d1buhb_ 4.81.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplp
>d1dksa_ 4.81.1.1.3 CksHs1 {Human (Homo sapiens)}
shkqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihe
pephillfrrplpkkp
>d1dksb_ 4.81.1.1.3 CksHs1 {Human (Homo sapiens)}
kqiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepe
phillfrrplpkk
>d1dkta_ 4.81.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpkk
>d1dktb_ 4.81.1.1.3 CksHs1 {Human (Homo sapiens)}
qiyysdkyddeefeyrhvmlpkdiaklvpkthlmsesewrnlgvqqsqgwvhymihepep
hillfrrplpk
>d1div_1 4.83.1.1.1 (56-149) Ribosomal protein L9 C-domain {Bacillus stearothermophilus}
rqaaeelanakklkeqlekltvtipakageggrlfgsitskqiaeslqaqhglkldkrki
eladairalgytnvpvklhpevtatlkvhvteqk
>d1div_2 4.84.1.1.1 (1-55) Ribosomal protein L9 N-domain {Bacillus stearothermophilus}
mkviflkdvkgkgkkgeiknvadgyannflfkqglaieatpanlkaleaqkqkeq
>d1qhka_ 4.84.1.2.1 N-terminal domain of RNase HI {Baker's yeast (Saccharomyces cerevisiae)}
gnfyavrkgretgiyntwnecknqvdgyggaiykkfnsyeqaksflg
>d1efnb_ 4.85.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
rpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1cby__ 4.86.1.1.1 Mosquitocidal delta-endotoxin CytB {Bacillus thuringiensis, strain Kyushuensis}
csapiirkpfkhivltvpssdldnfntvfyvqpqyinqalhlanafqgaidplnlnfnfe
kalqiangipnsaivktlnqsviqqtveisvmveqlkkiiqevlglvinstsfwnsveat
ikgtftnldtqideawifwhslsahntsyyynilfsiqnedtgavmavlplafevsvdve
kqkvlfftikdsaryevkmkaltlvqalhssnapivdifnvnnynly
>d1seta2 4.87.1.1.1 (111-421) Seryl-tRNA synthetase (SerRS) {Thermus thermophilus, strain hb27}
vggeeanreikrvggppefsfppldhvalmekngwweprisqvsgsrsyalkgdlalyel
allrfamdfmarrgflpmtlpsyarekaflgtghfpayrdqvwaiaetdlyltgtaevvl
nalhsgeilpyealplryagyapafrseagsfgkdvrglmrvhqfhkveqyvlteaslea
sdrafqellenaeeilrllelpyrlvevatgdmgpgkwrqvdievylpsegryrethscs
alldwqarranlryrdpegrvryaytlnntalatprilamllenhqlqdgrvrvpqalip
ymgkevlepcg
>d1lyla2 4.87.1.1.2 (161-502) Lysyl-tRNA synthetase (LysRS) {Escherichia coli, gene lysU}
dqevryrqryldliandksrqtfvvrskilaairqfmvargfmevetpmmqvipggasar
pfithhnaldldmylriapelylkrlvvggfervfeinrnfrnegisvrhnpeftmmely
mayadyhdlielteslfrtlaqevlgttkvtygehvfdfgkpfekltmreaikkyrpetd
madldnfdaakalaesigitvekswglgrivteifdevaeahliqptfiteypaevspla
rrndvnpeitdrfeffiggreigngfselndaedqaerfqeqvnakaagddeamfydedy
vtaleyglpptaglgigidrmimlftnshtirdvilfpamrp
>d1adja2 4.87.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1atia2 4.87.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1b76a2 4.87.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnakarywtppryfnmmfqdlrgprggrglla
ylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmeieyf
vrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfphgsl
elegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviepsag
vdrgvlallaeaftreelpngeerivlklkp
>d1qf6a4 4.87.1.1.6 (243-532) Threonyl-tRNA synthetase (ThrRS) {Escherichia coli}
dhrkigkqldlyhmqeeapgmvfwhndgwtifrelevfvrsklkeyqyqevkgpfmmdrv
lwektghwdnykdamfttssenreycikpmncpghvqifnqglksyrdlplrmaefgsch
rnepsgslhglmrvrgftqddahifcteeqirdevngcirlvydmystfgfekivvklst
rpekrigsdemwdraeadlavaleennipfeyqlgegafygpkieftlydcldrawqcgt
vqldfslpsrlsasyvgednerkvpvmihrailgsmerfigilteefagf
>d1b8aa2 4.87.1.1.8 (104-438) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
plpldptgkvkaeldtrlnnrfmdlrrpevmaifkirssvfkavrdffhengfieihtpk
iiatateggtelfpmkyfeedaflaespqlykeimmasgldrvyeiapifraeehnttrh
lneawsidsemafiedeeevmsflerlvahainyvrehnakeldilnfeleepklpfprv
sydkaleilgdlgkeipwgedidtegerllgkymmenenaplyflyqypseakpfyimky
dnkpeicrafdleyrgveissggqrehrhdilveqikekglnpesfefylkafrygmpph
ggfglgaerlikqmldlpnirevilfprdrrrltp
>d1c0aa3 4.87.1.1.9 (107-287,421-585) Aspartyl-tRNA synthetase (AspRS) {Escherichia coli}
vlpldsnhvnteearlkyryldlrrpemaqrlktrakitslvrrfmddhgfldietpmlt
katpegardylvpsrvhkgkfyalpqspqlfkqllmmsgfdryyqivkcfrdedlradrq
peftqidvetsfmtapqvrevmealvrhlwlevkgvdlgdfpvmtfaeaerrygsdkpdl
rXdeskwaplwvidfpmfeddgeggltamhhpftspkdmtaaelkaapenavanaydmvi
ngyevgggsvrihngdmqqtvfgilgineeeqrekfgflldalkygtpphaglafgldrl
tmlltgtdnirdviafpkttaaaclmteapsfanptalaelsiqvvk
>d1pysa_ 4.87.1.1.11 Phenyl-tRNA synthetase (PheRS) alpha subunit, PheS {Thermus thermophilus (Thermus aquaticus)}
rvdvslpgaslfsgglhpitlmerelveifralgyqavegpeveseffnfdalnipehhp
ardmwdtfwltgegfrlegplgeevegrlllrthtspmqvrymvahtppfrivvpgrvfr
feqtdatheavfhqleglvvgegiamahlkgaiyelaqalfgpdskvrfqpvyfpfvepg
aqfavwwpeggkwlelggagmvhpkvfqavdayrerlglppayrgvtgfafglgverlam
lrygipdiryffggrlkfleqfkgvl
>d1pysb5 4.87.1.1.12 (475-681) Phenyl-tRNA synthetase (PheRS) beta subunit, PheT, central domain {Thermus thermophilus (Thermus aquaticus)}
alpaffpapdnrgveapyrkeqrlrevlsglgfqevytysfmdpedarrfrldpprllll
nplapekaalrthlfpglvrvlkenldldrperallfevgrvfrereethlagllfgegv
glpwakerlsgyfllkgylealfarlglafrveaqafpflhpgvsgrvlvegeevgflga
lhpeiaqelelppvhlfelrlplpdkp
>d12asa_ 4.87.1.1.13 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d1bia_3 4.87.1.2.1 (64-270) Biotin repressor/biotin holoenzyme synthetase, catalytic (central) domain {Escherichia coli}
iqllnakqilgqldggsvavlpvidstnqylldrigelksgdaciaeyqqagrgrrgrkw
fspfganlylsmfwrleqgpaaaiglslvigivmaevlrklgadkvrvkwpndlylqdrk
lagilveltgktgdaaqivigaginmamrrveesvvnqgwitlqeaginldrntlaamli
relraalelfeqeglapylsrwekldn
>d1qtsa2 4.88.1.1.1 (825-938) Alpa-adaptin AP2, C-terminal subdomain {Mouse (Mus musculus)}
ffqptemasqdffqrwkqlsnpqqevqnifkakhpmdteitkakiigfgsalleevdpnp
anfvgagiihtkttqigcllrlepnlqaqmyrltlrtskdtvsqrlcellseqf
>d1b87a_ 4.89.1.1.1 Aminoglycoside 6'-N-acetyltransferase {Enterococcus faecium}
miisefdrnnpvlkdqlsdllrltwpeeygdssaeeveemmnperiavaavdqdelvgfi
gaipqygitgwelhplvvessrrknqigtrlvnylekevasrggitiylgtddldhgttl
sqtdlyehtfdkvasiqnlrehpyefyeklgykivgvlpnangwdkpdiwmaktiiprpd
s
>d1bo4a_ 4.89.1.1.2 Aminoglycoside 3-N-acetyltransferase {Serratia marcescens}
giirtcrlgpdqvksmraaldlfgrefgdvatysqhqpdsdylgnllrsktfialaafdq
eavvgalaayvlpkfeqprseiyiydlavsgehrrqgiatalinllkheanalgayviyv
qadygddpavalytklg
>d1cm0a_ 4.89.1.1.3 Histone acetyltransferase domain of P300/CBP associating factor, PCAF {Human (Homo sapiens)}
kviefhvvgnslnqkpnkkilmwlvglqnvfshqlprmpkeyitrlvfdpkhktlalikd
grviggicfrmfpsqgfteivfcavtsneqvkgygthlmnhlkeyhikhdilnfltyade
yaigyfkkqgfskeikipktkyvgyikdyegatlmgcelnpri
>d1ygha_ 4.89.1.1.4 Catalytic domain of GCN5 histone acetyltransferase {Baker's yeast (Saccharomyces cerevisiae)}
kiefrvvnndntkenmmvltglknifqkqlpkmpkeyiarlvydrshlsmavirkpltvv
ggityrpfdkrefaeivfcaissteqvrgygahlmnhlkdyvrntsnikyfltyadnyai
gyfkkqgftkeitldksiwmgyikdyeggtlmqcsmlpriryld
>d1qsta_ 4.89.1.1.5 Catalytic domain of GCN5 histone acetyltransferase {Tetrahymena thermophila}
ldfdiltndgthrnmkllidlknifsrqlpkmpkeyivklvfdrhhesmvilknkqkvig
gicfrqykpqrfaevaflavtaneqvrgygtrlmnkfkdhmqkqnieylltyadnfaigy
fkkqgftkehrmpqekwkgyikdydggtlmecyihpyvdy
>d1qsma_ 4.89.1.1.6 Histone acetyltransferase HPA2 {Baker's yeast (Saccharomyces cerevisiae)}
dnitvrfvtendkegwqrlwksyqdfyevsfpddlddfnfgrfldpnikmwaavavesss
ekiigminffnhmttwdfkdkiyindlyvdensrvkgaggkliqfvydeadklgtpsvyw
ctdesnhraqllyvkvgykapkilykrkgy
>d1bob__ 4.89.1.1.7 Histone acetyltransferase HAT1 {Baker's yeast (Saccharomyces cerevisiae)}
fkpetwtssanealrvsivgenavqfsplftypiygdsekiygykdliihlafdsvtfkp
yvnvkysaklgddnivdvekkllsflpkddvivrdeakwvdcfaeerkthnlsdvfekvs
eyslngeefvvyksslvddfarrmhrrvqifsllfieaanyidetdpswqiywllnkktk
eligfvttykywhylgaksfdedidkkfrakisqflifppyqnkghgsclyeaiiqswle
dksiteitvedpneafddlrdrndiqrlrklgydavfqkhsdlsdeflessrkslkleer
qfnrlvemllllnns
>d1cjwa_ 4.89.1.1.8 Serotonin N-acetyltranferase {Sheep (Ovis aries)}
htlpanefrcltpedaagvfeiereafisvsgncplnldevqhfltlcpelslgwfvegr
lvafiigslwdeerltqeslalhrprghsahlhalavhrsfrqqgkgsvllwrylhhvga
qpavrravlmcedalvpfyqrfgfhpagpcaivvgsltftemhcsl
>d1nmta1 4.89.1.2.2 (60-224) N-myristoyl transferase, NMT {Yeast (Candida albicans)}
egpidklktpedvpndplplisdfewstldiddnlqldelykllydnyvedidatfrfky
sheffqwalkppgwrkdwhvgvrvkstgklvafiaatpvtfklnksnkvidsveinflci
hkklrnkrlapvlikeitrrvnkqniwqalytggsilptplttcr
>d1nmta2 4.89.1.2.2 (225-451) N-myristoyl transferase, NMT {Yeast (Candida albicans)}
yqhrpinwsklhdvgfshlppnqtkssmvasytlpnnpklkglrpmtgkdvstvlsllyk
yqerfdivqlfteeefkhwmlghdensdsnvvksyvvedengiitdyfsyyllpftvldn
aqhdelgiaylfyyasdsfekpnykkrlnelitdalitskkfgvdvfncltcqdntyflk
dckfgsgdgflnyylfnyrtfpmdggidkktkevvedqtsgigvvll
>d2vik__ 4.90.1.1.1 Villin, domain 1 (res. 1-126) {Chicken (Gallus gallus)}
velskkvtgkldkttpgiqiwrienmemvpvptksygnfyegdcyvllstrktgsgfsyn
ihywlgknssqdeqgaaaiyttqmdeylgsvavqhrevqghesetfrayfkqgliykqgg
vasgmk
>d1svq__ 4.90.1.1.2 Severin, domain 2 {Dictyostelium discoideum}
eykprllhisgdknakvaevplatsslnsgdcflldagltiyqfngsksspqeknkaaev
araidaerkglpkvevfcetdsdipaefwkllgg
>d1svr__ 4.90.1.1.2 Severin, domain 2 {Dictyostelium discoideum}
eykprllhisgdknakvaevplatsslnsgdcflldagltiyqfngsksspqeknkaaev
araidaerkglpkvevfcetdsdipaefwkllgg
>d1svy__ 4.90.1.1.2 Severin, domain 2 {Dictyostelium discoideum}
eykprllhisgdknakvaevplatsslnsgdcflldagltiyqfngsksspqeknkaaev
araidaerkglpkvevfxetdsdipaefwkllggkgaiaakh
>d1d0na2 4.90.1.1.3 (153-262) Gelsolin {Horse (Equus caballus)}
vpnevvvqrllqvkgrrvvratevpvswesfnngdcfildlgnniyqwcgsksnrferlk
atqvskgirdnersgraqvsvfeegaepeamlqvlgpkptlpeatedtvk
>d1d0na3 4.90.1.1.3 (263-383) Gelsolin {Horse (Equus caballus)}
edaanrklaklykvsngagpmvvslvadenpfaqgalrsedcfildhgkdgkifvwkgkq
anmeerkaalktasdfiskmdypkqtqvsvlpeggetplfrqffknwrdpdqteglglay
l
>d1d0na4 4.90.1.1.3 (384-532) Gelsolin {Horse (Equus caballus)}
sshiahvervpfdaatlhtstamaaqhgmdddgtgqkqiwrvegsnkvpvdpatygqfyg
gdsyiilynyrhgsrqgqiiynwqgaqstqdevaasailtaqldeelggtpvqsrvvqgk
epahlmslfggkpmivykggtsreggqta
>d1d0na5 4.90.1.1.3 (533-628) Gelsolin {Horse (Equus caballus)}
pastrlfqvrasssgatraveiipkagalnsndafvlktpsaaylwvgagaseaektgaq
ellrvlraqpvqvaegsepdsfwealggkatyrtsp
>d1d0na6 4.90.1.1.3 (629-755) Gelsolin {Horse (Equus caballus)}
rlkdkkmdahpprlfacsnkigrfvieevpgefmqedlatddvmlldtwdqvfvwvgkds
qdeektealtsakryidtdpahrdrrtpitvvkqgfeppsfvgwflgwddsywsvdpldr
alaelaa
>d1d0nb5 4.90.1.1.3 (533-628) Gelsolin {Horse (Equus caballus)}
pastrlfqvrasssgatraveiipkagalnsndafvlktpsaaylwvgagaseaektgaq
ellrvlraqpvqvaegsepdsfwealggkatyrtsp
>d1db0b2 4.90.1.1.4 (533-628) Gelsolin {Human (Homo sapiens)}
pastrlfqvransagatraveiipkagalnsndafvlktpsaaylwvgtgaseaektgaq
ellrvlraqpvqvaegsepdsfwealggkaayrtsp
>d1yagg_ 4.90.1.1.4 Gelsolin {Human (Homo sapiens)}
mvvehpeflkagkepglqiwrvekfdlvpvptnlygdfftgdayvilktvqlrngnlqyd
lhywlgnecsqdesgaaaiftvqlddylngravqhrevqgfesatflgyfksglkykkgg
vasgf
>d1cfya_ 4.90.1.2.1 Yeast cofilin, monoclinic crystal form {Baker's yeast (Saccharomyces cerevisiae)}
vavadesltafndlklgkkykfilfglndakteivvketstdpsydafleklpendclya
iydfeyeingnegkrskivfftwspdtapvrskmvyasskdalrralngvstdvqgtdfs
evsydsvlervsr
>d1cnua_ 4.90.1.2.2 Actophorin {Amoeba (Acanthamoeba castellanii)}
giavsddcvqkfnelklghqhryvtfkmnasntevvvehvggpnatyedfksqlperdcr
yaifdyefqvdggqrnkitfilwapdsapikskmmytstkdsikkklvgiqvevqatdaa
eisedavserakkd
>d1ak7__ 4.90.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1pne__ 4.91.1.1.1 Profilin (actin-binding protein) {Bovine (Bos taurus)}
xagwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgilvgkdrssff
vngltlggqkcsvirdsllqdgeftmdlrtkstggaptfnitvtmtaktlvllmgkegvh
ggminkkcyemashlrrsqy
>d1d1ja_ 4.91.1.1.3 Profilin (actin-binding protein) {Human (Homo sapiens), isoform II}
agwqsyvdnlmcdgccqeaaivgycdakyvwaataggvfqsitpieidmivgkdregfft
ngltlgakkcsvirdslyvdgdctmdirtksqggeptynvavgragralvivmgkegvhg
gtlnkkayelalylrrsd
>d1acf__ 4.91.1.1.4 Profilin (actin-binding protein) {Acanthamoeba castellanii}
swqtyvdtnlvgtgavtqaailgldgntwatsagfavtpaqgttlagafnnadairaggf
dlagvhyvtlraddrsiygkkgssgvitvktskailvgvynekiqpgtaanvvekladyl
igqgf
>d1ypra_ 4.91.1.1.5 Profilin (actin-binding protein) {Baker's yeast (Saccharomyces cerevisiae)}
swqaytdnligtgkvdkaviysragdavwatsgglslqpneigeivqgfdnpaglqsngl
hiqgqkfmllraddrsiygrhdaegvvcvrtkqtviiahypptvqageatkiveqladyl
igvqy
>d3nul__ 4.91.1.1.7 Profilin (actin-binding protein) {Mouse-ear cress (Arabidopsis thaliana)}
swqsyvddhlxcdvegnhltaaailgqdgsvwaqsakfpqlkpqeidgikkdfeepgfla
ptglflggekyxviqgeqgavirgkkgpggvtikktnqalvfgfydepxtggqcnlvver
lgdyliesel
>d3pyp__ 4.91.2.1.1 Photoactive yellow protein, PYP {Ectothiorhodospira halophila}
mehvafgsedientlakmddgqldglafgaiqldgdgnilqynaaegditgrdpkqvigk
nffkdvapctdspefygkfkegvasgnlntmfeytfdyqmtptkvkvhmkkalsgdsywv
fvkrv
>d1drma_ 4.91.2.2.1 Histidine kinase FixL heme domain {Bradyrhizobium japonicum}
ipdamividghgiiqlfstaaerlfgwseleaigqnvnilmpepdrsrhdsyisryrtts
dphiigigrivtgkrrdgttfpmhlsigemqsggepyftgfvrdltehqqtqarlqelq
>d1bywa_ 4.91.2.3.1 Erg potassium channel, N-terminal domain {Human (Homo sapiens)}
srkfiianarvencaviycndgfcelcgysraevmqrpctcdflhgpctqrraaaqiaqa
llgaeerkveiafyrkdgscflclvdvvpvknedgavimfilnfevvmek
>d1cfe__ 4.92.1.1.1 P14a {Tomato (Lycopersicon esculentum)}
qnspqdylavhndaraqvgvgpmswdanlasraqnyansragdcnlihsgagenlakggg
dftgraavqlwvserpsynyatnqcvggkkcrhytqvvwrnsvrlgcgrarcnngwwfis
cnydpvgnwigqrpy
>d1a6ja_ 4.93.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {Escherichia coli}
lqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekmgstgign
giaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkthlhtlslv
akrladkticrrlraaqsdeelyqiitdte
>d1a3aa_ 4.93.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
lfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiav
phgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnald
desvierlahttsvdevlellagrk
>d1mut__ 4.94.1.1.1 Nucleoside triphosphate pyrophosphorylase (MutT) {Escherichia coli}
mkklqiavgiirnenneifitrraadahmanklefpggkiemgetpeqavvrelqeevgi
tpqhfslfekleyefpdrhitlwfwlverwegepwgkegqpgewmslvglnaddfppane
pviaklkrl
>d1ush_1 4.95.1.1.1 (363-550) 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain {Escherichia coli}
kigetngrlegdrdkvrfvqtnmgrlilaaqmdrtgadfavmsgggirdsieagdisykn
vlkvqpfgnvvvyadmtgkevidyltavaqmkpdsgaypqfanvsfvakdgklndlkikg
epvdpaktyrmatlnfnatggdgyprldnkpgyvntgfidaevlkayiqksspldvsvye
pkgevswq
>d1qqqa_ 4.96.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrxhlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdsrriivsawnvgeldkmalapxhaffqfyvadgklscqlyqrsxdvflglpfniasy
allvhmmaqqxdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydshpgikapvai
>d1bkpa_ 4.96.1.1.3 Thymidylate synthase {Bacillus subtilis}
tqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpilttk
kvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrslng
ekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevrar
sndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqfe
apelwinpevkdfydftiddfklinykhgdkllfevav
>d1b5ea_ 4.96.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1lba__ 4.97.1.1.1 Bacteriophage T7 lysozyme (Zn amidase) {Bacteriophage T7}
akqrestdaifvhcsatkpsqnvgvreirqwhkeqgwldvgyhfiikrdgtveagrdema
vgshakgynhnsigvclvggiddkgkfdanftpaqmqslrsllvtllakyegavlrahhe
vapkacpsfdlkrwweknelvtsdrg
>d1cyo__ 4.99.1.1.1 Cytochrome b5 {Bovine (Bos taurus)}
skavkyytleeiqkhnnskstwlilhykvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktfiigelhpddrskit
>d1wdb__ 4.99.1.1.1 Cytochrome b5 {Bovine (Bos taurus)}
skavkyytleeiqkhnnskstwlilhykvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktfiigelhpddr
>d3b5c__ 4.99.1.1.1 Cytochrome b5 {Bovine (Bos taurus)}
avkyytleeiqkhnnskstwlilhykvydltkfleehpggeevlreqaggdatenfedvg
hstdarelsktfiigelhpddrskit
>d1aqa__ 4.99.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
kyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfedvghs
tdarelsktyiigelhpddrskia
>d1awpa_ 4.99.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1awpb_ 4.99.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1axx__ 4.99.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5m__ 4.99.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
avtyyrleevakrntaeetwmvihgrvyditrflsehpggeevlleqagadatesfedvg
hspdaremlkqyyigdvhpndlkp
>d1do9a_ 4.99.1.1.3 Cytochrome b5 {Rabbit (Oryctolagus cuniculus)}
dkdvkyytleeikkhnhskstwlilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktfiigelhpddrsklskpmetl
>d1cxya_ 4.99.1.1.4 Cytochrome b558 {Ectothiorhodospira vacuolata}
tlpvftleqvaehhspddcwmaihgkvydltpyvpnhpgpagmmlvwcgqesteawetks
ygephsslaarllqryligtl
>d1fcba2 4.99.1.1.5 (1-97) Flavocytochrome b2, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
epkldmnkqkispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvta
ifeplhapnvidkyiapekklgplqgsmppelvcppy
>d1lcoa2 4.99.1.1.5 (10-97) Flavocytochrome b2, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1ldca2 4.99.1.1.5 (10-97) Flavocytochrome b2, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1ltda2 4.99.1.1.5 (10-97) Flavocytochrome b2, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kispaevakhnkpddcwvvingyvydltrflpnhpggqdvikfnagkdvtaifeplhapn
vidkyiapekklgplqgsmppelvcppy
>d1soxa2 4.99.1.1.6 (3-93) Sulfite oxidase, N-terminal domain {Chicken (Gallus gallus)}
sypeytreevgrhrspeervwvthgtdvfdvtdfvelhpggpdkillaaggalepfwaly
avhgephvlellqqykvgelspdeapaapda
>d1soxb2 4.99.1.1.6 (3-93) Sulfite oxidase, N-terminal domain {Chicken (Gallus gallus)}
sypeytreevgrhrspeervwvthgtdvfdvtdfvelhpggpdkillaaggalepfwaly
avhgephvlellqqykvgelspdeapaapda
>d1vcc__ 4.100.1.1.1 Vaccinia DNA topoisomerase I, 9 kDa N-terminal fragment {Vaccinia virus, strain WR}
mralfykdgklftdnnflnpvsddnpayevlqhvkipthltdvvvyeqtweealtrlifv
gsdskgrrqyfygkmhv
>d1byqa_ 4.101.1.1.2 HSP90 {Human (Homo sapiens)}
pmeeeevetfafqaeiaqlmsliintfysnkeiflrelisnssdaldkiryetltdpskl
dsgkelhinlipnkqdrtltivdtgigmtkadlinnlgtiaksgtkafmealqagadism
igqfgvgfysaylvaekvtvitkhnddeqyawessaggsftvrtdtgepmgrgtkvilhl
kedqteyleerrikeivkkhsqfigypitlfve
>d1aj6__ 4.101.1.2.1 DNA gyrase B {Escherichia coli}
vlkgldavrkrpgmyigdtddgtglhhmvfevvdnaidealaghckeiivtihadnsvsv
qddgrgiptgihpeegvsaaevimtvlhaggkfddnsykvsgglhgvgvsvvnalsqkle
lviqhegkihrqiyehgvpqaplavtgetektgtmvrfwpsletftnvtefeyeilakrl
relsflnsgvsirlrdkrdgkedhfh
>d1b63a2 4.101.1.2.2 (1-216) DNA mismatch repair protein MutL {Escherichia coli}
mpiqvlppqlanqiaagevverpasvvkelvensldagatrididierggaklirirdng
cgikkdelalalarhatskiaslddleaiislgfrgealasissvsrltltsrtaeqqea
wqayaegrdmnvtvkpaahpvgttlevldlfyntparrkflrtektefnhideiirrial
arfdvtinlshngkivrqyravpeggqkerrlgaic
>d1bxda_ 4.101.1.3.1 Histidine kinase domain of the osmosensor EnvZ {(Escherichia coli)}
tgqempmemadlnavlgeviaaesgyereietalypgsievkmhplsikravanmvvnaa
rygngwikvssgtepnrawfqveddgpgiapeqrkhlfqpfvrgdsartisgtglglaiv
qrivdnhngmlelgtsergglsirawlpvpvtraqgttkeg
>d1b3qa3 4.101.1.3.2 (355-539) Histidine kinase CheA {Thermotoga maritima}
mvpisfvfnrfprmvrdlakkmnkevnfimrgedteldrtfveeigepllhllrnaidhg
iepkeeriakgkppigtlilsarhegnnvvieveddgrgidkekiirkaiekglideska
atlsdqeilnflfvpgfstkekvsevsgrgvgmdvvknvveslngsmgiesekdkgtkvt
irlpl
>d1ixma_ 4.102.1.1.1 Sporulation responce regulatory protein Spo0B {Bacillus subtilis}
sdtaltnelihllghsrhdwmnklqlikgnlslqkydrvfemieemvidakhesklsnlk
tphlafdfltfnwkthymtleyevlgeikdlsaydqklaklmrklfhlfdqavsresenh
ltvslqtdhpdrqlilyldfhgafadpsafddirqngyedvdimrfeitsheclieigl
>d1bola_ 4.103.1.1.1 Ribonuclease Rh {Rhizopus niveus}
sscsstalscsnsansdtccspeyglvvlnmqwapgygpdnaftlhglwpdkcsgayaps
ggcdsnrasssiasvikskdsslynsmltywpsnqgnnnvfwshewskhgtcvstydpdc
ydnyeegedivdyfqkamdlrsqynvykafssngitpggtytatemqsaiesyfgakaki
dcssgtlsdvalyfyvrgrdtyvitdalstgscsgdveyptk
>d1bk7a_ 4.103.1.1.2 Ribonuclease MC1 {Bitter gourd (Momordica charantia)}
fdsfwfvqqwppavcsfqksgscpgsglrtftihglwpqqsgtsltncpgspfditkish
lqsqlntlwpnvlrannqqfwshewtkhgtcsestfnqaayfklavdmrnnydiigalrp
haagpngrtksrqaikgflkakfgkfpglrcrtdpqtkvsylvqvvacfaqdgstlidct
rdtcganfif
>d1orda3 4.104.1.1.1 (570-730) Ornithine decarboxylase C-terminal domain {Lactobacillus strain 30a}
aplkqvlpsiyaaneeryngytirelcqelhdfyknnntftyqkrlflreffpeqgmlpy
earqefirnhnklvplnkiegeialegalpyppgvfcvapgekwsetavkyftilqdgin
nfpgfapeiqgvyfkqegdkvvaygevydaevaknddrynn
>d1jdw__ 4.105.1.1.1 L-arginine: glycine amidinotransferase {Human (Homo sapiens)}
cpvssynewdpleevivgraenacvppftievkantyekywpfyqkqgghyfpkdhlkka
vaeieemcnilktegvtvrrpdpidwslkyktpdfestglysamprdilivvgneiieap
mawrsrffeyrayrsiikdyfhrgakwttapkptmadelynqdypihsvedrhklaaqgk
fvttefepcfdaadfiragrdifaqrsqvtnylgiewmrrhlapdyrvhiisfkdpnpmh
idatfniigpgivlsnpdrpchqidlfkkagwtiitpptpiipddhplwmsskwlsmnvl
mldekrvmvdanevpiqkmfeklgittikvnirnanslgggfhcwtcdvrrrgtlqsyld
>d1chma2 4.106.1.1.1 (157-402) Creatinase, catalytic (C-terminal) domain {Pseudomonas putida}
miksaeehvmirhgariadiggaavvealgdqvpeyevalhatqamvraiadtfedvelm
dtwtwfqsgintdgahnpvttrkvnkgdilslncfpmiagyytalertlfldhcsddhlr
lwqvnvevheaglklikpgarcsdiarelneiflkhdvlqyrtfgyghsfgtlshyygre
aglelredidtvlepgmvvsmepmimlpeglpgaggyrehdilivnengaenitkfpygp
ekniir
>d1c22a_ 4.106.1.1.2 Methionine aminopeptidase {Escherichia coli}
aisiktpediekmrvagrlaaevlemiepyvkpgvstgeldricndyivneqhavsaclg
yhgypksvcisinevvchgipddakllkdgdivnidvtvikdgfhgdtskmfivgkptim
gerlcritqeslylalrmvkpginlreigaaiqkfveaegfsvvreycghgigqgfheep
qvlhydsretnvvlkpgmtftiepmvnagkkeirtmkdgwtvktkdrslsaqyehtivvt
dngceiltlrkddtipaiishd
>d1xgsa2 4.106.1.1.3 (1-194,272-295) Methionine aminopeptidase {Pyrococcus furiosus}
mdteklmkageiakkvrekaiklarpgmlllelaesiekmimelggkpafpvnlsineia
ahytpykgdttvlkegdylkidvgvhidgfiadtavtvrvgmeedelmeaakealnaais
varagveikelgkaieneirkrgfkpivnlsghkieryklhagisipniyrphdnyvlke
gdvfaiepfatigaXrngivaqfehtiivekdsvivtte
>d1b6a_2 4.106.1.1.4 (110-374,449-478) Methionine aminopeptidase {Human (Homo sapiens)}
kvqtdppsvpicdlypngvfpkgqeceypptqdgrtaawrttseekkaldqaseeiwndf
reaaeahrqvrkyvmswikpgmtmieicekledcsrklikenglnaglafptgcslnnca
ahytpnagdttvlqyddickidfgthisgriidcaftvtfnpkydtllkavkdatntgik
cagidvrlcdvgeaiqevmesyeveidgktyqvkpirnlnghsigqyrihagktvpivkg
geatrmeegevyaietfgstgkgvvXdikgsytaqfehtillrptckevvsrgddy
>d1az9__ 4.106.1.1.5 Aminopeptidase P {Escherichia coli}
seisrqefqrrrqalveqmqpgsaalifaapevtrsadseypyrqnsdfwyftgfnepea
vlvliksddthnhsvlfnrvrdltaeiwfgrrlgqdaapeklgvdralafseinqqlyql
lngldvvyhaqgeyayadvivnsaleklrkgsrqnltapatmidwrpvvhemrlfkspee
iavlrrageitamahtramekcrpgmfeyhlegeihhefnrhgarypsyntivgsgengc
ilhytenecemrdgdlvlidagceykgyagditrtfpvngkftqaqreiydivleslets
lrlyrpgtsilevtgevvrimvsglvklgilkgdvdeliaqnahrpffmhglshwlgldv
hdvgvygqdrsrilepgmvltvepglyiapdaevpeqyrgigirieddivitetgnenlt
asvvkkpeeiealmvaarkq
>d1lgr_2 4.107.1.1.1 (101-468) Glutamine synthetase, C-terminal domain {Salmonella typhimurium}
drdprsiakraedylratgiadtvlfgpepefflfddirfgasisgshvaiddiegawns
stkyeggnkghrpgvkggyfpvppvdsaqdirsemclvmeqmglvveahhhevatagqne
vatrfntmtkkadeiqiykyvvhnvahrfgktatfmpkpmfgdngsgmhchmslakngtn
lfsgdkyaglseqalyyiggvikhakainalanpttnsykrlvpgyeapvmlaysarnrs
asiripvvaspkarrievrfpdpaanpylcfaallmagldgiknkihpgepmdknlydlp
peeakeipqvagsleealnaldldreflkaggvftdeaidayialrreeddrvrmtphpv
efelyysv
>d1qh4a2 4.107.1.2.2 (103-381) Creatine kinase, C-terminal domain {Chicken (Gallus gallus), brain-type}
tdehktdlnadnlqggddldpnyvlssrvrtgrsirgfclpphcsrgerraieklsveal
gslggdlkgkyyalrnmtdaeqqqliddhflfdkpvsplllasgmardwpdargiwhndn
ktflvwineedhlrvismqkggnmkevftrfctgltqietlfksknyefmwnphlgyilt
cpsnlgtglragvhiklpnlgkhekfgevlkrlrlqkrgtggvdtaavggvfdvsnadrl
gfsevelvqmvvdgvklliemekrlekgqsiddlmpaqk
>d1c9bb1 4.108.1.1.1 (158-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
gsgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssg
kmvctgakseeqsrlaarkyarvvqklgfpakfld
>d1c9bb2 4.108.1.1.1 (253-337) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
fkiqnmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvl
tgakvraeiyeafeniypilkgfrk
>d1c9bf1 4.108.1.1.1 (158-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
gsgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssg
kmvctgakseeqsrlaarkyarvvqklgfpakfld
>d1c9bf2 4.108.1.1.1 (253-337) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
fkiqnmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvl
tgakvraeiyeafeniypilkgfrk
>d1c9bj1 4.108.1.1.1 (158-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
gsgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssg
kmvctgakseeqsrlaarkyarvvqklgfpakfld
>d1c9bj2 4.108.1.1.1 (253-337) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
fkiqnmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvl
tgakvraeiyeafeniypilkgfrk
>d1c9bn1 4.108.1.1.1 (158-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
gsgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssg
kmvctgakseeqsrlaarkyarvvqklgfpakfld
>d1c9bn2 4.108.1.1.1 (253-337) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
fkiqnmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvl
tgakvraeiyeafeniypilkgfrk
>d1c9br1 4.108.1.1.1 (158-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
gsgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssg
kmvctgakseeqsrlaarkyarvvqklgfpakfld
>d1c9br2 4.108.1.1.1 (253-337) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
fkiqnmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvl
tgakvraeiyeafeniypilkgfrk
>d1cdwa1 4.108.1.1.1 (155-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
sgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssgk
mvctgakseensrlaarkyarvvqklgfpakfldfkiq
>d1cdwa2 4.108.1.1.1 (253-333) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
nmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvltgak
vraeiyeafeniypilkgfrk
>d1tgha1 4.108.1.1.1 (155-252) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
sgivpqlqnivstvnlgckldlktialrarnaeynpkrfaavimrireprttalifssgk
mvctgakseeqsrlaarkyarvvqklgfpakfldfkiq
>d1tgha2 4.108.1.1.1 (253-334) TATA-box binding protein (TBP), C-terminal domain {Human (Homo sapiens)}
nmvgscdvkfpirleglvlthqqfssyepelfpgliyrmikprivllifvsgkvvltgak
vraeiyeafeniypilkgfrkt
>d1qn3a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn3b2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn4a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn4b2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn5a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn5b2 4.108.1.1.2 (116-197) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrk
>d1qn6a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn6b2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn7a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn7b2 4.108.1.1.2 (116-197) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrk
>d1qn8a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn8b2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn9a2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qn9b2 4.108.1.1.2 (116-197) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrk
>d1qnaa1 4.108.1.1.2 (17-115) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
hpsgivptlqnivstvnldckldlkaialqarnaeynpkrfaavimrirepkttalifas
gkmvctgaksedfskmaarkyarivqklgfpakfkdfki
>d1qnaa2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qnab2 4.108.1.1.2 (116-197) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrk
>d1qnba2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qnbb2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qnca2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qncb2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qnea2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1qneb2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1voka2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1vokb2 4.108.1.1.2 (116-199) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrkiq
>d1volb2 4.108.1.1.2 (116-198) TATA-box binding protein (TBP), C-terminal domain {Arabidopsis thaliana}
qnivgscdvkfpirleglayshaafssyepelfpgliyrmkvpkivllifvsgkivitga
kmrdetykafeniypvlsefrki
>d1tbab1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
sgivptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgk
mvvtgakseddsklasrkyariiqkigfaakftdf
>d1tbab2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1tbpa1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
givptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgkm
vvtgakseddsklasrkyariiqkigfaakftdf
>d1tbpa2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1tbpb1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
givptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgkm
vvtgakseddsklasrkyariiqkigfaakftdf
>d1tbpb2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1ytba1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
sgivptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgk
mvvtgakseddsklasrkyariiqkigfaakftdf
>d1ytba2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1ytbb1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
sgivptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgk
mvvtgakseddsklasrkyariiqkigfaakftdf
>d1ytbb2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1ytfa1 4.108.1.1.3 (61-155) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
sgivptlqnivatvtlgcrldlktvalharnaeynpkrfaavimrirepkttalifasgk
mvvtgakseddsklasrkyariiqkigfaakftdf
>d1ytfa2 4.108.1.1.3 (156-240) TATA-box binding protein (TBP), C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
kiqnivgscdvkfpirleglafshgtfssyepelfpgliyrmvkpkivllifvsgkivlt
gakqreeiyqafeaiypvlsefrkm
>d1aisa1 4.108.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
mvdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallif
ssgklvvtgaksvqdieravaklaqklksigv
>d1aisa2 4.108.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldky
>d1d3ua1 4.108.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
mvdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallif
ssgklvvtgaksvqdieravaklaqklksigv
>d1d3ua2 4.108.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldky
>d1pcza1 4.108.1.1.4 (2-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
vdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallifs
sgklvvtgaksvqdieravaklaqklksigv
>d1pcza2 4.108.1.1.4 (93-184) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldkygll
>d1pczb1 4.108.1.1.4 (2-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
vdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallifs
sgklvvtgaksvqdieravaklaqklksigv
>d1pczb2 4.108.1.1.4 (93-184) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldkygll
>d1mpga2 4.108.1.2.1 (1-99) 3-Methyladenine DNA glycosylase II (gene alkA or aidA), N-terminal domain {Escherichia coli}
mytlnwqppydwswmlgflaaravssvetvadsyyarslavgeyrgvvtaipdiarhtlh
inlsaglepvaaeclakmsrlfdlqcnpqivngalgrlg
>d3pmga4 4.108.2.1.1 (421-561) Phosphoglucomutase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
rnfftrydyeeveaegatkmmkdlealmfdrsfvgkqfsandkvytvekadnfeyhdpvd
gsvsknqglrlifadgsriifrlsgtgsagatirlyidsyekdnakinqdpqvmlaplis
ialkvsqlqertgrtaptvit
>d1bv1__ 4.108.3.1.1 Major birch pollen allergen Bet v 1 {White birch (Betula verrucosa)}
gvfnyetettsvipaarlfkafildgdnlfpkvapqaissveniegnggpgtikkisfpe
glpfkyvkdrvdevdhtnfkynysvieggpigdtlekisneikivatpdggsilkisnky
htkgdhevkaeqvkaskemgetllravesyllahsdayn
>d1ndoa2 4.108.3.2.1 (155-447) Napthalene 1,2-dioxygenase alpha subunit, C-domain {Pseudomonas putida}
eapplmdylgdaawylepmfkhsgglelvgppgkvvikanwkapaenfvgdayhvgwtha
sslrsgesifsslagnaalppegaglqmtskygsgmgvlwdgysgvhsadlvpelmafgg
akqerlnkeigdvrariyrshlnctvfpnnsmltcsgvfkvwnpidanttevwtyaivek
dmpedlkrrladsvqrtfgpagfwesddndnmetasqngkkyqsrdsdllsnlgfgedvy
gdavypgvvgksaigetsyrgfyrayqahvsssnwaefehasstwhteltktt
>d1mxa_1 4.109.1.1.1 (1-102) S-adenosylmethionine synthetase. MAT {Escherichia coli}
akhlftsesvseghpdkiadqisdavldaileqdpkarvacetyvktgmvlvggeittsa
wvdieeitrntvreigyvhsdmgfdanscavlsaigkqspdi
>d1mxa_2 4.109.1.1.1 (108-231) S-adenosylmethionine synthetase. MAT {Escherichia coli}
radpleqgagdqglmfgyatnetdvlmpapityahrlvqrqaevrkngtlpwlrpdaksq
vtfqyddgkivgidavvlstqhseeidqkslqeavmeeiikpilpaewltsatkffinpt
grfv
>d1mxa_3 4.109.1.1.1 (232-383) S-adenosylmethionine synthetase. MAT {Escherichia coli}
iggpmgdcgltgrkiivdtyggmarhgggafsgkdpskvdrsaayaaryvaknivaagla
drceiqvsyaigvaeptsimvetfgtekvpseqltllvreffdlrpygliqmldllhpiy
ketaayghfgrehfpwektdkaqllrdaaglk
>d2pola1 4.110.1.1.1 (1-122) DNA polymerase III, beta subunit {Escherichia coli}
mkftverehllkplqqvsgplggrptlpilgnlllqvadgtlsltgtdlememvarvalv
qphepgattvparkffdicrglpegaeiavqlegermlvrsgrsrfslstlpaadfpnld
dw
>d2pola2 4.110.1.1.1 (123-244) DNA polymerase III, beta subunit {Escherichia coli}
qseveftlpqatmkrlieatqfsmahqdvryylngmlfetegeelrtvatdghrlavcsm
pigqslpshsvivprkgvielmrmldggdnplrvqigsnnirahvgdfiftsklvdgrfp
dy
>d2pola3 4.110.1.1.1 (245-366) DNA polymerase III, beta subunit {Escherichia coli}
rrvlpknpdkhleagcdllkqafaraailsnekfrgvrlyvsenqlkitannpeqeeaee
ildvtysgaemeigfnvsyvldvlnalkcenvrmmltdsvssvqiedaasqsaayvvmpm
rl
>d1b77a1 4.110.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77a2 4.110.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1plq_1 4.110.1.2.2 (1-126) Prolifirating cell nuclear antigen (PCNA) {Baker's yeast (Saccharomyces cerevisiae)}
mleakfeeaslfkriidgfkdcvqlvnfqckedgiiaqavddsrvllvsleigveafqey
rcdhpvtlgmdltslskilrcgnntdtltliadntpdsiillfedtkkdriaeyslklmd
idadfl
>d1plq_2 4.110.1.2.2 (127-258) Prolifirating cell nuclear antigen (PCNA) {Baker's yeast (Saccharomyces cerevisiae)}
kieelqydstlslpssefskivrdlsqlsdsinimitketikfvadgdigsgsviikpfv
dmehpetsiklemdqpvdltfgakylldiikgsslsdrvgirlsseapalfqfdlksgfl
qfflapkfndee
>d1axca1 4.110.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axca2 4.110.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1bcca_ 4.111.1.1.2 Core 1 subunit {Chicken (Gallus gallus)}
yaqalqsvpetqvsqldngvrvaseqssqptctvgvwidagsryeseknngagyflehla
fkgtknrpqnalekevesmgahlnayssrehtayyikalskdvpkavelladivqncsle
dsqiekerdvivrelqendtsmrevvfnylhatafqgtglaqsvegpsenirklsradlt
eylsthytaprmvlaaaggvehqqllelaqkhfggvpftydddavptlskcrftgsqirh
redglplahvaiavegpgwahpdlvalqvanaiighydrtyggglhsssplasiavtnkl
cqsfqtfsicysetglfgfyfvcdrmsiddmmfvlqgqwmrlctsisesevlrgknflrn
alvshldgttpvcedigrelltygrripleeweerlaevdarmvrevcskyiydqcpava
gpgpieqlpdynrirsgmfwlr
>d1bccb_ 4.111.1.1.4 Core 2 subunit {Chicken (Gallus gallus)}
pphpqdleitklpnglviaslenyspgstigvfikagsryenssnlgtshllrlassltt
kgassfkitrgieavggklsvestrenmaytveclrddveilmefllnvttapefrpwev
adlqpqlkidkavafqnpqthvienlhaaayrnaladslycpdyrigkvtsvelhdfvqn
hftsarmalvglgvshpvlknvaeqllnirgglglsgakakyrggeireqngdslvhaai
vaesaaiggaeanafsvlqhvlganphvkrglnatsslyqavakgvhqpfdvsafnasys
dsglfgfytisqaayagqvikaaynqvktiaqgnvsnenvqaaknklkakylmsvesseg
fleevgsqalaagsynppstvlqqidavadadvikaakkfvsrqksmaasgnlghtpfvd
el
>d1alo_4 4.112.1.1.1 (311-907) Aldehyde oxidoreductase {Desulfovibrio gigas}
msgpaaaaedaieihpgtpnvyfeqpivkgedtgpifasadvtvegdfyvgrqphmpiep
dvafaymgddgkcyihsksigvhlhlymiapgvglepdqlvlvanpmggtfgykfsptse
alvavaamatgrpvhlrynyqqqqqytgkrspwemnvkfaakkdgtllamesdwlvdhgp
ysefgdlltlrgaqfigagynipnirglgrtvatnhvwgsafrgygapqsmfaseclmdm
laeklgmdplelryknayrpgdtnptgqepevfslpdmidqlrpkyqaalekaqkestat
hkkgvgisigvygsgldgpdaseawaelnadgtitvhtawedhgqgadigcvgtahealr
pmgvapekikftwpntattpnsgpsggsreqvmtgnairvacenllkacekpgggyytyd
elkaadkptkitgnwtasgathcdavtglgkpfvvymygvfmaevtvdvatgqttvdgmt
lmadlgslcnqlatdgqiygglaqgiglalsedfedikkhatlvgagfpfikqipdkldi
vyvnhprpdgpfgasgvgelpltsphaaiinaiksatgvriyrlpaypekvlealka
>d1qj2b2 4.112.1.1.2 (147-809) Carbon monoxide (CO) dehydrogenase molybdoprotein {Pseudomonas carboxydovorans}
vdpfkamepdapllredikdkmtgahgarkhhnhifrweigdkegtdatfakaevvskdm
ftyhrvhpspletcqcvasmdkikgeltlwgtfqaphvirtvvslisglpehkihviapd
igggfgnkvgaysgyvcavvasivlgvpvkwvedrmenlsttsfardyhmttelaatkdg
kilamrchvladhgafdacadpskwpagfmnictgsydmpvahlavdgvytnkasggvay
rxsfrvteavyaieraietlaqrlemdsadlriknfiqpeqfpymaplgweydsgnypla
mkkamdtvgyhqlraeqkakqeafkrgetreimgigisffteivgagpskncdilgvsmf
dsaeirihptgsviarmgtksqgqghettyaqiiatelgipaddimieegntdtapyglg
tygsrstptagaatavaarkikakaqmiaahmlevhegdlewdvdrfrvkglpekfktmk
elawasynspppnlepgleavnyydppnmtypfgayfcimdididtgvaktrrfyalddc
gtrinpmiiegqvhgglteafavamgqeirydeqgnvlgasfmdfflptavetpkwetdy
tvtpsphhpigakgvgesphvggvpcfsnavndayaflnaghiqmphdawrlwkvgeqlg
lhv
>d1aop_3 4.113.1.1.1 (149-345) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
ndmnrnvlctsnpyesqlhaeayewakkisehllprtrayaeiwldqekvattdeepilg
qtylprkfkttvvippqndidlhandmnfvaiaengklvgfnllvggglsiehgnkktya
rtasefgylplehtlavaeavvttqrdwgnrtdrknaktkytlervgvetfkaeverrag
ikfepirpyeftgrgdr
>d1aop_4 4.113.1.1.1 (426-570) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
pqrensmacvsfptcplamaeaerflpsfidnidnlmakhgvsdehivmrvtgcpngcgr
amlaevglvgkapgrynlhlggnrigtriprmykenitepeilasldeligrwakereag
egfgdftvragiirpvldpardlwd
>d1byra_ 4.114.1.1.1 Nuclease Nuc {(Salmonella typhimurium) |A|}
epsvqvgyspegsarvlvlsaidsaktsirmmaysftapdimkalvaakkrgvdvkivid
ergntgrasiaamnyiansgiplrtdsnfpiqhdkviivdnvtvetgsfnftkaaetkns
enavviwnmpklaesflehwqdrwnqgrdyrs
>d1qhla_ 4.115.1.1.1 Cell division protein MukB, N-terminal domain {Escherichia coli}
rgkfrsltlinwngffartfdldelvttlsggngagksttmaafvtalipdltllhfrnt
teagatsgsrdkglhgklkagvcysmldtinsrhqrvvvgvrlqqvagrdrkvdikpfai
qglpmsvqptqlvtetlnerqarvlplnelkdkleamegvqfkqfnsitdyhslmfdlgi
iarrlrsasdrskfyrlieaslyggissaitrslrdyllpen
>d1ckv__ 4.116.1.1.1 Soluble methane monooxygenase regulatory protein B {Escherichia coli}
msvnsnaydagimglkgkdfadqffadenqvvhesdtvvlvlkksdeintfieeilltdy
kknvnptvnvedragywwikangkievdcdeisellgrqfnvydflvdvsstigraytlg
nkftitselmgldrkledyha
>d2moba_ 4.116.1.1.2 Soluble methane monooxygenase regulatory protein B {Methylosinus trichosporium}
snavvlvlmksdeidaiiedivlkggkaknpsivvedkagfwwikadgaieidaaeagel
lgkpfsvydllinvsstvgraytlgtkftitsel
>d1hqi__ 4.116.1.1.3 Phenol hydroxylase P2 protein {Pseudomonas CF600}
msslvyiafqdndnaryvveaiiqdnphavvqhhpamirieaekrleirretveenlgra
wdvqemlvdvitiggnvdedddrfvlewkn
>d1pysb6 4.117.1.1.1 (191-399) B3/B4 domain of PheRS, PheT {Thermus thermophilus (Thermus aquaticus)}
lkaealplpfalkvedpegaphftlgyafglrvapsplwmqralfaagmrpinnvvdvtn
yvmleraqpmhafdlrfvgegiavrraregerlktldgvertlhpedlviagwrgeesfp
lglagvmggaesevredteaialevacfdpvsirktarrhglrteashrfergvdplgqv
paqrralsllqalagarvaealleagspk
>d1clia2 4.118.1.1.1 (171-345) Aminoimidazole ribonucleotide synthetase (PurM) C-terminal domain {(Escherichia coli) |A,B,C,D|}
dgskvsdgdvlialgssgphsngyslvrkilevsgcdpqtteldgkpladhllaptriyv
ksvleliekvdvhaiahltgggfweniprvlpdntqavidesswqwpevfnwlqtagnve
hhemyrtfncgvgmiialpapevdkalallnangenawkigiikasdseqrvvie
>d1seia_ 4.119.1.1.1 Ribosomal protein S8 {Bacillus stearothermophilus}
vmtdpiadmltairnanmvrheklevpaskikreiaeilkregfirdyeyiednkqgilr
iflkygpnervitglkriskpglrvyvkahevprvlnglgiailstsqgvltdkearqkg
tggeiiayvi
>d1an7a_ 4.119.1.1.2 Ribosomal protein S8 {Thermus thermophilus}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1rl6a1 4.120.1.1.1 (7-81) Ribosomal protein L6 {Bacillus stearothermophilus}
pieipagvtvtvngntvtvkgpkgeltrtfhpdmtitvegnvitvtrpsdekhhralhgt
trsllanmvegvskg
>d1rl6a2 4.120.1.1.1 (82-170) Ribosomal protein L6 {Bacillus stearothermophilus}
yekalelvgvgyraskqgkklvlsvgyshpveiepeegleievpsqtkiivkgadkqrvg
elaaniravrppepykgkgiryegelvrl
>d1gsa_2 4.121.1.1.1 (123-314) Glutathione synthetase {Escherichia coli}
neklftawfsdltpetlvtrnkaqlkafwekhsdiilkpldgmggasifrvkegdpnlgv
iaetltehgtrycmaqnylpaikdgdkrvlvvdgepvpyclaripqggetrgnlaaggrg
eprpltesdwkiarqigptlkekglifvgldiigdrlteinvtsptcireieaefpvsit
gmlmdaiearlq
>d1iow_2 4.121.1.1.2 (97-306) D-ala-D-ala ligase {Escherichia coli, gene ddlB}
klrskllwqgaglpvapwvaltraefekglsdkqlaeisalglpvivkpsregssvgmsk
vvaenalqdalrlafqhdeevliekwlsgpeftvailgeeilpsiriqpsgtfydyeakf
lsdetqyfcpagleasqeanlqalvlkawttlgckgwgridvmldsdgqfylleantspg
mtshslvpmaarqagmsfsqlvvrilelad
>d1bnca3 4.121.1.2.1 (115-330) Biotin carboxylase subunit of acetyl-CoA carboxylase {Escherichia coli}
dkvsaiaamkkagvpcvpgsdgplgddmdknraiakrigypviikasgggggrgmrvvrg
daelaqsismtraeakaafsndmvymekylenprhveiqvladgqgnaiylaerdcsmqr
rhqkvveeapapgitpelrryigercakacvdigyrgagtfeflfengefyfiemntriq
vehpvtemitgvdlikeqlriaagqplsikqeevhv
>d1gsoa3 4.121.1.2.2 (104-327) Glycinamide ribonucleotide synthetase (GAR-syn) {Escherichia coli}
skaftkdflarhkiptaeyqnftevepalaylrekgapivikadglaagkgvivamtlee
aeaavhdmlagnafgdaghrivieefldgeeasfivmvdgehvlpmatsqdhkrvgdkdt
gpntggmgayspapvvtddvhqrtmeriiwptvkgmaaegntytgflyaglmidkqgnpk
viefncrfgdletqpimlrmksdlvelclaaceskldektsewd
>d1b6ra3 4.121.1.2.3 (79-276) N5-carboxyaminoimidazole ribonucleotide synthetase, AIRC, PurK {Escherichia coli}
drltqkqlfdklhlptapwqllaersewpavfdrlgelaivkrrtggydgrgqwrlrane
teqlpaecygeciveqginfsgevslvgargfdgstvfyplthnlhqdgilrtsvafpqa
naqqqaraeemlsaimqelgyvgvmamecfvtpqgllinelaprvhnsghwtqngasisq
felhlraitdlplpqpvv
>d1a9xa5 4.121.1.2.4 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xa6 4.121.1.2.4 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1auva2 4.121.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d2scub2 4.121.1.4.1 (1-244) Succinyl-CoA synthetase, beta-chain, N-terminal domain {Escherichia coli}
mnlheyqakqlfaryglpapvgyacttpreaeeaaskigagpwvvkcqvhaggrgkaggv
kvvnskedirafaenwlgkrlvtyqtdangqpvnqilveaatdiakelylgavvdrssrr
vvfmasteggveiekvaeetphlihkvaldpltgpmpyqgrelafklglegklvqqftki
fmglatiflerdlalieinplvitkqgdlicldgklgadgnalfrqpdlremrdqsqedp
reaq
>d1dik_3 4.121.1.5.1 (2-376) Pyruvate phosphate dikinase, N-terminal domain {Escherichia coli}
akwvykfeegnasmrnllggkgcnlaemtilgmpipqgftvtteacteyynsgkqitqei
qdqifeaitwleelngkkfgdtedpllvsvrsaarasmpgmmdtilnlglndvavegfak
ktgnprfaydsyrrfiqmysdvvmevpkshfekiidamkeekgvhfdtdltaddlkelae
kfkavykeamngeefpqepkdqlmgavkavfrswdnpraivyrrmndipgdwgtavnvqt
mvfgnkgetsgtgvaftrnpstgekgiygeylinaqgedvvagvrtpqpitqlendmpdc
ykqfmdlamklekhfrdmqdmeftieegklyflqtrngkrtapaalqiacdlvdegmite
eeavvrieaksldql
>d2hgsa2 4.121.1.6.1 (304-474) Eukaryotic glutathione synthetase {Human (Homo sapiens)}
tkkvqqelsrpgmlemllpgqpeavarlratfaglysldvgeegdqaiaealaapsrfvl
kpqregggnnlygeemvqalkqlkdseerasyilmekiepepfencllrpgsparvvqci
selgifgvyvrqektlvmnkhvghllrtkaiehadggvaagvavldnpypv
>d2hgsa3 4.121.1.6.1 (3-201) Eukaryotic glutathione synthetase {Human (Homo sapiens)}
tnwgsllqdkqqleelarqavdralaegvllrtsqeptssevvsyapftlfpslvpsall
eqayavqmdfnllvdavsqnaafleqtlsstikqddftarlfdihkqvlkegiaqtvflg
lnrsdymfqrsadgspalkqieintisasfgglasrtpavhrhvlsvlsktkeagkilsn
npskglalgiakawelygs
>d1a0i_2 4.121.2.1.1 (2-240) ATP-dependent DNA ligase, N-terminal domain {Bacteriophage T7}
vniktnpfkavsfvesaikkaldnagyliaeikydgvrgnicvdntansywlsrvsktip
alehlngfdvrwkrllnddrcfykdgfmldgelmvkgvdfntgsgllrtkwtdtknqefh
eelfvepirkkdkvpfklhtghlhiklyailplhivesgedcdvmtllmqehvknmlpll
qeyfpeiewqaaesyevydmvelqqlyeqkraegheglivkdpmciykrgkksgwwkmk
>d1b04a_ 4.121.2.2.1 Adenylation domain of NAD+-dependent DNA ligase {Bacillus stearothermophilus}
drqqaerraaelrellnrygyeyyvldrpsvpdaeydrlmqeliaieeqypelktsdspt
qriggppleafrkvahrvpmmslanafgegdlrdfdrrvrqevgeaayvcelaidglavs
vryedgyfvqgatrgdgttgeditenlktirslplrlkepvsleargeafmpkasflrln
eerkargeelfanprnaaagslrqldpkvaasrqldlfvygladaealgiashsealdyl
qalgfkvnperrrcanideviafvsewhdkrpqlpyeidgivikvdsfaqqralgataks
prwaiaykfpae
>d1ckma2 4.121.2.3.1 (11-238) RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain {Chlorella virus, PBCV-1}
nitteravltlnglqiklhkvvgesrddivakmkdlamddhkfprlpgpnpvsierkdfe
klkqnkyvvsektdgirfmmfftrvfgfkvctiidramtvyllpfkniprvlfqgsifdg
elcvdivekkfafvlfdavvvsgvtvsqmdlasrffamkrslkefknvpedpailrykew
iplehptiikdhlkkanaiyhtdgliimsvdepviygrnfnlfklkpg
>d1a48__ 4.122.1.1.1 SAICAR synthase {Baker's yeast (Saccharomyces cerevisiae)}
sitkteldgilplvargkvrdiyevdagtllfvatdrisaydvimensipekgilltkls
efwfkflsndvrnhlvdiapgktifdylpaklsepkyktqledrsllvhkhklipleviv
rgyitgsawkeyvktgtvhglkqpqglkesqefpepiftpstkaeqgehdenispaqaae
lvgedlsrrvaelavklyskckdyakekgiiiadtkfefgidektneiilvdevltpdss
rfwngasykvgesqdsydkqflrdwltanklngvngvkmpqdivdrtrakyieayetltg
skwsh
>d1bo1a_ 4.122.1.2.1 Phosphatidylinositol phosphate kinase IIbeta, PIPK IIbeta {Human (Homo sapiens)}
klfrasepilsvlmwgvnhtinelsnvpvpvmlmpddfkayskikvdnhlfnkenlpsrf
kfkeycpmvfrnlrerfgiddqdyqnsvtrsapinsdsqgrcgtrflttydrrfviktvs
sedvaemhnilkkyhqfivechgntllpqflgmyrltvdgvetymvvtrnvfshrltvhr
kydlkgstvareasdkekakdlptfkdndflnegqklhvgeeskknfleklkrdveflaq
lkimdysllvgihdvdraeqeemeveeraedeecendgvggnllcsygtppdspgnllsf
prffgpgefdpsvdvyamkshesspkkevyfmaiidiltpydtkkkaahaaktvkhgaga
eistvnpeqyskrfnefmsnilt
>d1hcl__ 4.123.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1apme_ 4.123.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
seqesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhy
amkildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemf
shlrrigrfaepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfak
rvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyek
ivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrk
veapfipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1phk__ 4.123.1.1.7 gamma-subunit of glycogen phosphorylase kinase (Phk) {Rabbit (Oryctolagus cuniculus)}
fyenyepkeilgrgvssvvrrcihkptckeyavkiidvtgggsfsaeevqelreatlkev
dilrkvsghpniiqlkdtyetntffflvfdlmkkgelfdyltekvtlseketrkimrall
evicalhklnivhrdlkpenilldddmnikltdfgfscqldpgeklrevcgtpsylapei
iecsmndnhpgygkevdmwstgvimytllagsppfwhrkqmlmlrmimsgnyqfgspewd
dysdtvkdlvsrflvvqpqkrytaeealahpffqqyv
>d1tkia_ 4.123.1.1.8 Titin, kinase domain {Human (Homo sapiens)}
kelyekymiaedlgrgefgivhrcvetsskktymakfvkvkgtdqvlvkkeisilniarh
rnilhlhesfesmeelvmifefisgldiferintsafelnereivsyvhqvcealqflhs
hnighfdirpeniiyqtrrsstikiiefgqarqlkpgdnfrllftapeyyapevhqhdvv
statdmwslgtlvyvllsginpflaetnqqiienimnaeytfdeeafkeisieamdfvdr
llvkerksrmtasealqhpwlkqkiervstkvirtlkhrryyhtlikkdlnmvvsaaris
cggairsqkgvsvakvkvasi
>d1pme__ 4.123.1.1.13 MAP kinase Erk2 {Human (Homo sapiens)}
gqvfdvgprytnlsyigegaygmvcsaydnvnkvrvaikkispfehqtycqrtlreikil
lrfrheniigindiiraptieqmkdvylvthlmgadlykllktqhlsndhicyflyqilr
glkyihsanvlhrdlkpsnlllnttxdlkicdfglarvadpdhdhtgflteyvatrwyra
peimlnskgytksidiwsvgcilaemlsnrpifpgkhyldqlnhilgilgspsqedlnci
inlkarnyllslphknkvpwnrlfpnadskaldlldkmltfnphkrieveqalahpyleq
yydpsdepiaeapfkfdmelddlpkeklkelifeetarfqpgyrs
>d1csn__ 4.123.1.1.17 Casein kinase-1, CK1 {Schizosaccharomyces pombe}
nvvgvhykvgrrigegsfgvifegtnllnnqqvaikfeprrsdapqlrdeyrtykllagc
tgipnvyyfgqeglhnvlvidllgpsledlldlcgrkfsvktvamaakqmlarvqsihek
slvyrdikpdnfligrpnsknanmiyvvdfgmvkfyrdpvtkqhipyrekknlsgtarym
sinthlgreqsrrddlealghvfmyflrgslpwqglkaatnkqkyerigekkqstplrel
cagfpeefykymhyarnlafdatpdydylqglfskvlerlnttedenfdwnll
>d1a6o__ 4.123.1.1.18 Protein kiase CK2, alpha subunit {Maize (Zea mays)}
skarvyadvnvlrpkeywdyealtvqwgeqddyevvrkvgrgkysevfeginvnnnekci
ikilkpvkkkkikreikilqnlcggpnivklldivrdqhsktpslifeyvnntdfkvlyp
tltdydiryyiyellkaldychsqgimhrdvkphnvmidhelrklrlidwglaefyhpgk
eynvrvasryfkgpellvdlqdydysldmwslgcmfagmifrkepffyghdnhdqlvkia
kvlgtdglnvylnkyrieldpqlealvgrhsrkpwlkfmnadnqhlvspeaidfldkllr
ydhqerltaleamthpyfqqvraaens
>d1b6cb_ 4.123.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1fmk_3 4.123.1.2.3 (249-533) c-src tyrosine kinase {Human (Homo sapiens)}
kpqtqglakdaweipreslrlevklgqgcfgevwmgtwngttrvaiktlkpgtmspeafl
qeaqvmkklrheklvqlyavvseepiyivteymskgslldflkgetgkylrlpqlvdmaa
qiasgmayvermnyvhrdlraanilvgenlvckvadfglarliedneytarqgakfpikw
tapeaalygrftiksdvwsfgilltelttkgrvpypgmvnrevldqvergyrmpcppecp
eslhdlmcqcwrkepeerptfeylqafledyftstepqxqpgenl
>d1ir3a_ 4.123.1.2.6 Insulin receptor {Human (Homo sapiens)}
ssvfvpdewevsrekitllrelgqgsfgmvyegnardiikgeaetrvavktvnesaslre
rieflneasvmkgftchhvvrllgvvskgqptlvvmelmahgdlksylrslrpeaennpg
rppptlqemiqmaaeiadgmaylnakkfvhrdlaarncmvahdftvkigdfgmtrdixet
dxxrkggkgllpvrwmapeslkdgvfttssdmwsfgvvlweitslaeqpyqglsneqvlk
fvmdggyldqpdncpervtdlmrmcwqfnpkmrptfleivnllkddlhpsfpevsffhse
enk
>d1cjaa_ 4.123.1.3.1 Actin-fragmin kinase {Slime mold (Physarum polycephalum)}
agalweiekelftklpapssainshlqpakpkvpqkkpskwdppaefkvdlstavsyndi
gdinwknlqqfkgiersekgteglffvetesgvfivkrstniesetfcsllcmrlglhap
kvrvvssnseegtnmleclaaidksfrvittlanqanillmelvrgitlnkltttsapev
ltkstmqqlgslmaldvivnnsdrlpiawtnegnldnimlsergatvvpidskiipldas
hphgervrellrtliahpghessqfhsirdiitlytgydvgtegsismqegflatvreca
sfdldaferellswqeslqkchnlsispqaipfilrmlrifh
>d1qmma4 4.123.1.4.1 (726-1092) Phoshoinositide 3-kinase (PI3K), catalytic domain {Pig (Sus scrofa)}
tamlhdftqqvqvidmlqkvtidikslsaekydvssqvisqlkqklenlqnlnlpqsfrv
pydpglkagalviekckvmaskkkplwlefkcadptalsnetigiifkhgddlrqdmlil
qilrimesiwetesldlcllpygcistgdkigmieivkdattiakiqqstvgntgafkde
vlshwlkekcpieekfqaaverfvyscagycvatfvlgigdrhndnimisetgnlfhidf
ghilgnyksflginkervpfvltpdflfvmgtsgkktslhfqkfqdvcvkaylalrhhtn
lliilfsmmlmtgmpqltskedieyirdaltvgkseedakkyfldqievcrdkgwtvqfn
wflhlvl
>d1qlta2 4.124.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1diqa2 4.124.1.1.3 (7-242) Flavoprotein subunit of p-cresol methylhydroxylase {Pseudomonas putida}
avlpkgvtqgefnkavqkfrallgddnvlvesdqlvpynkimmpvenaahapsaavtatt
veqvqgvvkicnehkipiwtistgrnfgygsaapvqrgqvildlkkmnkiikidpemcya
lvepgvtfgqmydyiqennlpvmlsfsapsaiagpvgntmdrgvgytpygehfmmqcgme
vvlangdvyrtgmggvpgsntwqifkwgygptldgmftqanygictkmgfwlmpkp
>d1uxy_1 4.124.1.2.1 (3-200) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase (MurB), N-terminal domain {Escherichia coli}
hslkpwntfgidhnaqhivcaedeqqllnawqyataegqpvlilgegsnvlfledyrgtv
iinrikgieihdepdawylhvgagenwhrlvkytlqegmpglenlalipgcvgsspiqni
gaygvelqrvcayvdsvelatgkqvrltakecrfgyrdsifkheyqdrfaivavglrlpk
ewqpvltygdltrldptt
>d1qj2c2 4.124.1.3.1 (1-177) Carbon monoxide (CO) dehydrogenase flavoprotein N-domain {Pseudomonas carboxydovorans}
mipgsfdyhrpksiadavalltklgedarplagghslipimktrlatpehlvdlrdigdl
vgireegtdvvigamttqhaligsdflaaklpiiretslliadpqirymgtiggnaangd
pgndmpalmqclgaayeltgpegarivaardyyqgayftaiepgelltairipvppt
>d1uxy_2 4.125.1.1.1 (201-342) Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain {Escherichia coli}
vtpqqvfnavchmrttklpdpkvngnagaffknpvvsaetakallsqfptapnypqadgs
vklaagwlidqcqlkgmqiggaavhrqqalvlinednaksedvvqlahhvrqkvgekfnv
wlepevrfigasgevsavetis
>d1qlma_ 4.126.1.1.1 Methenyltetrahydromethanopterin cyclohydrolase {Methanopyrus kandleri}
mvsvnenalplvermieraellnvevqelengttvidcgveaaggfeagllfsevcmggl
atveltefehdglclpavqvttdhpavstlaaqkagwqvqvgdyfamgsgparalalkpk
etyeeidyeddadvailclesselpdedvaehvadecgvdpenlyllvaptasivgsvqv
sarvvetglykllevleydvtrvkyatgtapiapvadddgeamgrtndcilyggtvylyv
egddelpevveelpseasedygkpfmkifeeadydfykidpgvfaparvvvndlstgkty
tageinvdvlkesfsl
>d1c4za_ 4.127.1.1.1 Ubiquitin-protein ligase E3a, Hect catalytic domain (E6ap) {Human (Homo sapiens)}
npylrlkvrrdhiiddalvrlemiamenpadlkkqlyvefegeqgvdeggvskeffqlvv
eeifnpdigmftydestklfwfnpssfetegqftligivlglaiynncildvhfpmvvyr
klmgkkgtfrdlgdshpvlyqslkdlleyegnveddmmitfqisqtdlfgnpmmydlken
gdkipitnenrkefvnlysdyilnksvekqfkafrrgfhmvtnesplkylfrpeeielli
cgsrnldfqaleetteydggytrdsvlirefweivhsftdeqkrlflqfttgtdrapvgg
lgklkmiiakngpdterlptshtcfnvlllpeysskeklkerllkaitya
>d2ahja_ 4.128.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
idhttenaapaqapvsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvara
wtdpefrqllltdgtaavaqygylgpqgeyivavedtptlknvivcslxsxtawpilglp
ptwyksfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsq
eqlqeivtkdcligvaipqv
>d1qr0a_ 4.129.1.1.1 4'-Phosphopantetheinyl transferase SFP {Bacillus subtilis}
mkiygiymdrplsqeenerfmtfispekrekcrrfyhkedahrtllgdvlvrsvisrqyq
ldksdirfstqeygkpcipdlpdahfnishsgrwvigafdsqpigidiektkpisleiak
rffskteysdllakdkdeqtdyfyhlwsmkesfikqegkglslpldsfsvrlhqdgqvsi
elpdshspcyiktyevdpgykmavcaahpdfpeditmvsyeellraaa
>d1ako__ 4.130.1.1.1 DNA-repair enzyme exonuclease III {Escherichia coli}
mkfvsfninglrarphqleaivekhqpdviglqetkvhddmfpleevaklgynvfyhgqk
ghygvalltketpiavrrgfpgddeeaqrriimaeipsllgnvtvingyfpqgesrdhpi
kfpakaqfyqnlqnyletelkrdnpvlimgdmnisptdldigigeenrkrwlrtgkcsfl
peerewmdrlmswglvdtfrhanpqtadrfswfdyrskgfddnrglridlllasqplaec
cvetgidyeirsmekpsdhapvwatfrr
>d1bix__ 4.130.1.1.2 DNA repair endonuclease Hap1 {Human (Homo sapiens)}
lyedppdqktspsgkpatlkicswnvdglrawikkkgldwvkeeapdilclqetkcsenk
lpaelqelpglshqywsapsdkegysgvgllsrqcplkvsygigdeehdqegrvivaefd
sfvlvtayvpnagrglvrleyrqrwdeafrkflkglasrkplvlcgdlnvaheeidlrnp
kgnkknagftpqerqgfgellqavpladsfrhlypntpyaytfwtymmnarsknvgwrld
yfllshsllpalcdskirskalgsdhcpitlylal
>d2dnja_ 4.130.1.1.4 Deoxyribonuclease I {Bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcescgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1b25a2 4.131.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1gdoa_ 4.132.1.1.1 Glucosamine 6-phosphate synthase, N-terminal domain {Escherichia coli}
cgivgaiaqrdvaeilleglrrleyrgydsaglavvdaeghmtrlrrlgkvqmlaqaaee
hplhggtgiahtrwathgepsevnahphvsehivvvhngiienheplreelkargytfvs
etdteviahlvnwelkqggtlreavlraipqlrgaygtvimdsrhpdtllaarsgsplvi
glgmgenfiasdqlallpvtrrfifleegdiaeitrrsvnifdktgaevkrqdiesnl
>d1gph12 4.132.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ecfa2 4.132.1.1.3 (1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs
>d1ct9a2 4.132.1.1.4 (1-192) Asparagine synthetase B, N-terminal domain {Escherichia coli}
asifgvfdiktdavelrkkalelsrlmrhrgpdwsgiyasdnailaherlsivdvnagaq
plynqqkthvlavngeiynhqalraeygdryqfqtgsdcevilalyqekgpeflddlqgm
fafalydsekdayligrdhlgiiplymgydehgqlyvasemkalvpvcrtikefpagsyl
wsqdgeirsyyh
>e1pnk.1a 4.132.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqes
>e1pnk.1b 4.132.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqewtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d3pvaa_ 4.132.1.3.1 Penicillin V acylase {Bacillus sphaericus}
csslsirttddkslfartmdftmepdskviivprnygirllekenvvinnsyafvgmgst
ditspvlydgvnekglmgamlyyatfatyadepkkgttginpvyvisqvlgncvtvddvi
ekltsytllneaniilgfapplhytftdasgesiviepdktgitihrktigvmtnspgye
whqtnlrayigvtpnppqdimmgdldltpfgqgagglglpgdftpsarflrvaywkkyte
kaknetegvtnlfhilssvnipkgvvltnegktdytiytsamcaqsknyyfklydnsris
avslmaenlnsqdlitfewdrkqdikqlnqvnvm
>d1pma1_ 4.132.1.4.1 Proteasome beta subunit (catalytic) {Thermoplasma acidophilum}
tttvgitlkdavimaterrvtmenfimhkngkklfqidtytgmtiaglvgdaqvlvrymk
aelelyrlqrrvnmpieavatllsnmlnqvkympymvqllvggidtaphvfsidaaggsv
ediyastgsgspfvygvlesqysekmtvdegvdlviraisaakqrdsasggmidvavitr
kdgyvqlptdqiesrirklglil
>d1ryp1_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
qfnpygdnggtilgiagedfavlagdtrnitdysinsryepkvfdcgdnivmsangfaad
gdalvkrfknsvkwyhfdhndkklsinsaarniqhllygkrffpyyvhtiiagldedgkg
avysfdpvgsyereqcraggaaaslimpfldnqvnfknqyepgtngkvkkplkylsveev
iklvrdsftsaterhiqvgdgleilivtkdgvrkefyelkrd
>d1ryp2_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
tqqpivtgtsvismkydngviiaadnlgsygsllrfngverlipvgdntvvgisgdisdm
qhierllkdlvtenaydnpladaeealepsyifeylatvmyqrrskmnplwnaiivagvq
sngdqflryvnllgvtyssptlatgfgahmanpllrkvvdresdipkttvqvaeeaivna
mrvlyyrdarssrnfslaiidkntgltfkknlqvenmkwdfakdikgygtqki
>d1ryph_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
lkkgevslgasimavtfkdgvilgadsrtttgayianrvtdkltrvhdkiwccrsgsaad
tqaiadivqyhlelytsqygtpstetaasvfkelcyenkdnltagiivagyddknkgevy
tiplggsvhklpyaiagsgstfiygycdknfrenmskeetvdfikhslsqaikwdgssgg
virmvvltaagverlifypdeyeql
>d1rypi_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
ttivgvkfnngvviaadtrstqgpivadkncaklhrispkiwcagagtaadteavtqlig
snielhslytsreprvvsalqmlkqhlfkyqghigaylivagvdptgshlfsihahgstd
vgyylslgsgslaamavleshwkqdltkeeaiklasdaiqagiwndlgsgsnvdvcvmei
gkdaeylrnyltpnvreekqksykfprgttavlkesivnicd
>d1rypj_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
sdpssinggivvamtgkdcvaiacdlrlgsqslgvsnkfekifhyghvflgitglatdvt
tlnemfryktnlyklkeeraiepetftqlvssslyerrfgpyfvgpvvaginsksgkpfi
agfdligcideakdfivsgtasdqlfgmceslyepnlepedlfetisqallnaadrdals
gwgavvyiikkdevvkrylkmrqd
>d1rypk_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
mdiilgirvqdsvilasskavtrgisvlkdsddktrqlsphtlmsfageagdtvqfaeyi
qaniqlysiredyelspqavssfvrqelaksirsrrpyqvnvliggydkkknkpelyqid
ylgtkvelpygahgysgfytfslldhhyrpdmtteegldllklcvqelekrmpmdfkgvi
vkivdkdgirqvddfqaq
>d1rypl_ 4.132.1.4.2 Proteasome beta subunit (catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
tttlafrfqggiivavdsratagnwvasqtvkrvieinpfllgtmaggaadcqfwetwlg
sqcrlhelrekerisvaaaskilsnlvyqykgaglsmgtmicgytrkegptiyyvdsdgt
rlkgdifcvgsgqtfaygvldsnykwdlsvedalylgkrsilaaahrdaysggsvnlyhv
tedgwiyhgnhdvgelfwkvkeeegsfnnvig
>d1pmaa_ 4.132.1.4.3 Proteasome alpha subunit (non-catalytic) {Thermoplasma acidophilum}
tvfspdgrlfqveyareavkkgstalgmkfangvllisdkkvrsrlieqnsiekiqlidd
yvaavtsglvadarvlvdfarisaqqekvtygslvnienlvkrvadqmqqytqyggvrpy
gvslifagidqigprlfdcdpagtineykataigsgkdavvsflereykenlpekeavtl
gikalkssleegeelkapeiasitvgnkyriydqeevkkfl
>d1rypa_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
agydrhitifspegrlyqveyafkatnqtninslavrgkdctvvisqkkvpdklldpttv
syifcisrtigmvvngpipdarnaalrakaeaaefrykygydmpcdvlakrmanlsqiyt
qraymrplgviltfvsvdeelgpsiyktdpagyyvgykatatgpkqqeittnlenhfkks
kidhineeswekvvefaithmidalgtefskndlevgvatkdkfftlsaenieerlvaia
eqd
>d1rypb_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
mtdrysfslttfspsgklgqidyaltavkqgvtslgikatngvviatekksssplamset
lskvslltpdigavysgmgpdyrvlvdksrkvahtsykriygeypptkllvsevakimqe
atqsggvrpfgvslliaghdefngfslyqvdpsgsyfpwkataigkgsvaaktflekrwn
deleledaihialltlkesvegefngdtielaiigdenpdllgytgiptdkgprfrklts
qeindrleal
>d1rypc_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
gsrrydsrttifspegrlyqveyalesishagtaigimasdgivlaaerkvtstlleqdt
steklyklndkiavavagltadaeilintarihaqnylktynedipveilvrrlsdikqg
ytqhgglrpfgvsfiyagyddrygyqlytsnpsgnytgwkaisvgantsaaqtllqmdyk
ddmkvddaielalktlskttdssaltydrlefatirkgandgevyqkifkpqeikdilvk
tgit
>d1rypd_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
gydralsifspdghifqveyaleavkrgtcavgvkgkncvvlgcerrstlklqdtritps
kvskidshvvlsfsglnadsriliekarveaqshrltledpvtveyltryvagvqqrytq
sggvrpfgvstliagfdprddepklyqtepsgiysswsaqtigrnsktvrefleknydrk
eppatveecvkltvrsllevvqtgaknieitvvkpdsdivalsseeinqyvtqieqekqe
q
>d1rype_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
drgvstfspegrlfqveysleaiklgstaigiatkegvvlgvekratspllesdsiekiv
eidrhigcamsgltadarsmiehartaavthnlyydedinvesltqsvcdlalrfgegas
geerlmsrpfgvalliaghdaddgyqlfhaepsgtfyrynakaigsgsegaqaellnewh
ssltlkeaellvlkilkqvmeekldennaqlscitkqdgfkiydnektaelikelkekea
ae
>d1rypf_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
frnnydgdtvtfsptgrlfqveyaleaikqgsvtvglrsnthavlvalkrnadelssyqk
kiikcdehmglslaglapdarvlsnylrqqcnysslvfnrklaveraghllcdkaqkntq
syggrpygvglliigydksgahllefqpsgnvtelygtaigarsqgaktylertldtfik
idgnpdelikagveaisqslrdesltvdnlsiaivgkdtpftiydgeavakyi
>d1rypg_ 4.132.1.4.4 Proteasome alpha subunit (non-catalytic) {Baker's yeast (Saccharomyces cerevisiae)}
gtgydlsnsvfspdgrnfqveyavkavengttsigikcndgvvfaveklitskllvpqkn
vkiqvvdrhigcvysglipdgrhlvnrgreeaasfkklyktpipipafadrlgqyvqaht
lynsvrpfgvstifggvdkngahlymlepsgsywgykgaatgkgrqsakaeleklvdhhp
eglsareavkqaakiiylahednkekdfeleiswcslsetnglhkfvkgdllqeaidfaq
kein
>d1dooa_ 4.132.1.4.5 HslV (ClpQ) protease {Escherichia coli}
ttivsvrrnghvviagdgqatlgntvmkgnvkkvrrlyndkviagfaggtadaftlfelf
erklemhqghlvkaavelakdwrtdrmlrkleallavadetasliitgngdvvqpendli
aigsggpyaqaaarallentelsareiaekaldiagdiciytnhfhtieelsy
>e1apy.1a 4.132.1.5.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.1b 4.132.1.5.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e2gac.1a 4.132.1.5.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
nkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdgr
vtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkken
lltaesekewkewlkt
>e2gac.1b 4.132.1.5.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
cigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletp
>d1b65a_ 4.133.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>e1pya.1a 4.134.1.1.1 Histidine decarboxylase {Lactobacillus strain 30a}
seldaklnklgvdriaispykqwtrgymepgnigngyvtglkvdagvrdksdddvldgiv
sydraetknayigqinmttas
>e1pya.1b 4.134.1.1.1 Histidine decarboxylase {Lactobacillus strain 30a}
ftgvqgrvigydilrspevdkakplftetqwdgselpiydakplqdalveyfgteqdrrh
ypapgsfivcankgvtaerpkndadmkpgqgygvwsaiaisfakdptkdssmfvedagvw
etpnedelleylegrrkamaksiaecgqdahasfesswigfaytmmepgqignaitvapy
vslpidsipggsiltpdkdmeimenltmpewlekmgykslsannalky
>e1pya.2c 4.134.1.1.1 Histidine decarboxylase {Lactobacillus strain 30a}
seldaklnklgvdriaispykqwtrgymepgnigngyvtglkvdagvrdksdddvldgiv
sydraetknayigqinmttas
>e1pya.3e 4.134.1.1.1 Histidine decarboxylase {Lactobacillus strain 30a}
seldaklnklgvdriaispykqwtrgymepgnigngyvtglkvdagvrdksdddvldgiv
sydraetknayigqinmttas
>e1jen.1a 4.135.1.1.1 S-adenosylmethionine decarboxylase {Human (Homo sapiens)}
smfvskrrfilktcgttlllkalvpllklardysgfdsiqsffysrknfmkpshqgyphr
nfqeeieflnaifpngaaycmgrmnsdcwylytldfpesrvisqpdqtleilmseldpav
mdqfymkdgvtakdvtresgirdlipgsvidatmfnpcgysmngmksdgtywtihitpep
efsyvsfetnlsqtsyddlirkvvevfkpgkfvttlfvnqsskcrtvlrspqkiegfkrl
dcqsamfndynfvftsfakkq
>e1jen.1b 4.135.1.1.1 S-adenosylmethionine decarboxylase {Human (Homo sapiens)}
ahffegtekllevwfsrqqpdanqgsgdlrtiprsewdillkdvqcsiisvtktdkqeay
vlse
>e1jen.2d 4.135.1.1.1 S-adenosylmethionine decarboxylase {Human (Homo sapiens)}
hffegtekllevwfsrqqpdanqgsgdlrtiprsewdillkdvqcsiisvtktdkqeayv
ls
>d2bc2a_ 4.136.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggxlvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1a7ta_ 4.136.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1smla_ 4.136.1.1.3 Zn metallo-beta-lactamase {Xanthomonas maltophilia}
evplpqlraytvdaswlqpmaplqiadhtwqigtedltallvqtpdgavlldggmpqmas
hlldnmkargvtprdlrlillshahadhagpvaelkrrtgakvaanaesavllarggsdd
lhfgdgityppanadrivmdgevitvggivftahfmaghtpgstawtwtdtrngkpvria
yadslsapgyqlqgnpryphliedyrrsfatvralpcdvlltphpgasnwdyaagaraga
kaltckayadaaeqkfdgqlaketag
>d1qh5a_ 4.136.1.2.1 Glyoxalase II (hydroxyacylglutathione hydrolase) {Human (Homo sapiens) |A,B|}
mkvevlpaltdnymylviddetkeaaivdpvqpqkvvdaarkhgvklttvltthhhwdha
ggneklvklesglkvyggddrigalthkithlstlqvgslnvkclatpchtsghicyfvs
kpggseppavftgdtlfvagcgkfyegtademckallevlgrlppdtrvycgheytinnl
kfarhvepgnaaireklawakekysigeptvpstlaeeftynpfmrvrektvqqhagetd
pvttmravrrekdqfkmprd
>d1a6q__ 4.137.1.1.1 Protein serine/threonine phosphatase 2C {Human (Homo sapiens)}
gafldkpkmekhnaqgqgnglryglssmqgwrvemedahtaviglpsgleswsffavydg
hagsqvakyccehlldhitnnqdfkgsagapsvenvkngirtgfleidehmrvmsekkhg
adrsgstavgvlispqhtyfincgdsrgllcrnrkvhfftqdhkpsnplekeriqnaggs
vmiqrvngslavsralgdfdykcvhgkgpteqlvspepevhdierseeddqfiilacdgi
wdvmgneelcdfvrsrlevtddlekvcnevvdtclykgsrdnmsvilicfpnapkvspea
vkkeaeldkylecrveeiikkqgegvpdlvhvmrtlasenipslppggelaskrnvieav
ynrlnpy
>d4kbpa2 4.138.1.1.1 (121-432) Plant purple acid phosphatase, catalytic domain {Kidney bean (Phaseolus vulgaris)}
qtgldvpytfgligdlgqsfdsnttlshyelspkkgqtvlfvgdlsyadrypnhdnvrwd
twgrftersvayqpwiwtagnheiefapeinetepfkpfsyryhvpyeasqstspfwysi
krasahiivlssysaygrgtpqytwlkkelrkvkrsetpwlivlmhsplynsynhhfmeg
eamrtkfeawfvkykvdvvfaghvhayerservsniaykitdglctpvkdqsapvyitig
dagnygvidsnmiqpqpeysafreasfghgmfdiknrthahfswnrnqdgvaveadsvwf
fnrhwypvddst
>d1utea_ 4.138.1.1.3 Mammalian purple acid phosphatase {Pig (Sus scrofa)}
ptpilrfvavgdwggvpnapfhtaremanakaiattvktlgadfilslgdnfyftgvhda
kdkrfqetfedvfsdpslrnvpwhvlagnhdhlgnvsaqiayskiskrwnfpspyyrlrf
kiprsnvsvaifmldtvtlcgnsddfvsqqperprnlalartqlawikkqlaaakedyvl
vaghypvwsiaehgpthclvkqllplltthkvtaylcghdhnlqylqdenglgfvlsgag
nfmdpskkhlrkvpngylrfhfgaenslggfayveitpkemsvtyieasgkslfktklpr
ra
>d1ush_2 4.138.1.2.1 (26-362) 5'-nucleotidase (syn. UDP-sugar hydrolase), N-terminal domain {Escherichia coli}
yeqdktykitvlhtndhhghfwrneygeyglaaqktlvdgirkevaaeggsvlllsggdi
ntgvpesdlqdaepdfrgmnlvgydamaignhefdnpltvlrqqekwakfpllsaniyqk
stgerlfkpwalfkrqdlkiaviglttddtakignpeyftdiefrkpadeaklviqelqq
tekpdiiiaathmghydngehgsnapgdvemaralpagslamivgghsqdpvcmaaenkk
qvdyvpgtpckpdqqngiwivqahewgkyvgradfefrngemkmvnyqlipvnlkkkvtw
edgkservlytpeiaenqqmisllspfqnkgkaqlev
>d1fjma_ 4.138.1.3.1 Protein phosphatase-1 (PP-1) {Rabbit (Oryctolagus cuniculus)}
lnldsiigrllevqgsrpgknvqlteneirglclksreiflsqpilleleaplkicgdih
gqyydllrlfeyggfppesnylflgdyvdrgkqsleticlllaykikypenffllrgnhe
casinriygfydeckrryniklwktftdcfnclpiaaivdekifcchgglspdlqsmeqi
rrimrptdvpdqgllcdllwsdpdkdvqgwgendrgvsftfgaevvakflhkhdldlicr
ahqvvedgyeffakrqlvtlfsapnycgefdnagammsvdetlmcsfqilkpad
>d1qdla_ 4.139.1.1.1 Anthranilate synthase aminodeoxyisochorismate synthase/lyase subunit TrpE {Sulfolobus solfataricus}
amevhpisefaspfevfkcierdfkvagllesiggpqykarysviawstngylkihddpv
nilngylkdlkladipglfkggmigyisydavrfwekirdlkpaaedwpyaefftpdnii
iydhnegkvyvnadlssvggcgdigefkvsfydeslnknsyerivsesleyirsgyifqv
vlsrfyryifsgdplriyynlrrinpspymfylkfdekyligsspellfrvqdnivetyp
iagtrprgadqeedlklelelmnsekdkaehlmlvdlarndlgkvcvpgtvkvpelmyve
kyshvqhivskvigtlkkkynalnvlsatfpagtvsgapkpmamniietleeykrgpyag
avgfisadgnaefaiairtaflnkellrihagagivydsnpeseyfetehklkalktaig
vr
>d1mlda2 4.140.1.1.1 (145-313) Malate dehydrogenase {Porcine (Sus scrofa)}
vttldivranafvaelkgldparvsvpvigghagktiiplisqctpkvdfpqdqlstltg
riqeagtevvkakagagsatlsmayagarfvfslvdamngkegvvecsfvksqetdcpyf
stplllgkkgieknlgigkispfeekmiaeaipelkasikkgeefvknm
>d5mdha2 4.140.1.1.1 (155-333) Malate dehydrogenase {Porcine (Sus scrofa)}
trldhnrakaqialklgvtsddvknviiwgnhsstqypdvnhakvklqakevgvyeavkd
dswlkgefittvqqrgaavikarklssamsaakaicdhvrdiwfgtpegefvsmgiisdg
nsygvpddllysfpvtikdktwkiveglpindfsrekmdltakelaeeketafeflssa
>d7mdha2 4.140.1.1.2 (198-385) Malate dehydrogenase {Sorghum (Sorghum vulgare), chloroplast}
trldenrakcqlalkagvfydkvsnvtiwgnhsttqvpdflnakidgrpvkevikrtkwl
eeeftitvqkrggaliqkwgrssaastavsiadaikslvtptpegdwfstgvyttgnpyg
iaedivfsmpcrskgdgdyelatdvsnddflwerikkseaellaekkcvahltgegnayc
dvpedtml
>d2cmd_2 4.140.1.1.3 (146-312) Malate dehydrogenase {Escherichia coli}
vttldiirsntfvaelkgkqpgevevpvigghsgvtilpllsqvpgvsfteqevadltkr
iqnagtevveakagggsatlsmgqaaarfglslvralqgeqgvvecayvegdgqyarffs
qplllgkngveerksigtlsafeqnalegmldtlkkdialgqefvnk
>d1bdma2 4.140.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d2hlpa2 4.140.1.1.5 (163-330) Malate dehydrogenase {Haloarcula marismortui}
fggrldsarfryvlseefdapvqnvegtilgehgdaqvpvfskvrvdgtdpefsgdekeq
llgdlqesamdvierkgatewgpargvahmveailhdtgrvlpasvklegefghedtafg
vpvrlgsngveeivewdlddyeqdlmadaaeklsdqydkis
>d1b8pa2 4.140.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1hyha2 4.140.1.1.7 (167-329) L-2-hydroxyisocapronate dehydrogenase, L-HICDH {Lactobacillus confusus}
gtlldtarmqravgeafdldprsvsgynlgehgnsqfvawstvrvmgqpivtladagdid
laaieeearkggftvlngkgytsygvatsairiakavmadahaelvvsnrrddmgmylsy
paiigrdgvlaettldlttdeqekllqsrdyiqqrfdeivdtl
>d1ldm_2 4.140.1.1.10 (161-329) Lactate dehydrogenase {Dogfish (Squalus acanthias)}
sgcnldsarfrylmgerlgvhscschgwvigehgdsvpsvwsgmnvasiklhpldgtnkd
kqdwkklhkdvvdsayeviklkgytswaiglsvadlaetimknlcrvhpvstmvkdfygi
kdnvflslpcvlndhgisnivkmklkpneeqqlqksattlwdiqkdlkf
>d1ceqa2 4.140.1.1.11 (164-329) Lactate dehydrogenase {Malarial parasite (Plasmodium falciparum)}
ggvldtsrlkyyisqklnvcprdvnahivgahgnkmvllkryitvggiplqefinnklis
daeleaifdrtvntaleivnlhaspyvapaaaiiemaesylkdlkkvlicstllegqygh
sdifggtpvvlgangveqvielqlnseekakfdeaiaetkrmkala
>d1ldna2 4.140.1.1.12 (163-330) Lactate dehydrogenase {Bacillus stearothermophilus}
tildtarfrfllgeyfsvapqnvhayiigehgdtelpvwsqayigvmpirklveskgeea
qkdlerifvnvrdaayqiiekkgatyygiamglarvtrailhnenailtvsayldglyge
rdvyigvpavinrngirevieielnddeknrfhhsaatlksvlaraft
>d1llc_2 4.140.1.1.13 (165-334) Lactate dehydrogenase {Lactobacillus casei}
tsldtarfrqsiaemvnvdarsvhayimgehgdtefpvwshaniggvtiaewvkahpeik
edklvkmfedvrdaayeiiklkgatfygiatalariskailndenavlplsvymdgqygi
ndlyigtpavinrngiqnileipltdheeesmqksasqlkkvltdafakndi
>d1llda2 4.140.1.1.14 (150-319) Lactate dehydrogenase {Bifidobacterium longum, strain am101-2}
tnldsarlrfliaqqtgvnvknvhayiagehgdsevplwesatiggvpmsdwtplpghdp
ldadkreeihqevknaaykiingkgatnyaigmsgvdiieavlhdtnrilpvssmlkdfh
gisdicmsvptllnrqgvnntintpvsdkelaalkrsaetlketaaqfgf
>d1a5z_2 4.140.1.1.15 (164-333) Lactate dehydrogenase {Thermotoga maritima}
gtvldtarlrtliaqhcgfsprsvhvyvigehgdsevpvwsgamiggiplqnmcqvcqkc
dskilenfaektkraayeiierkgathyaialavadivesiffdekrvltlsvyledylg
vkdlcisvpvtlgkhgverilelnlneeeleafrksasilknaineitaeen
>d1aiha_ 4.141.1.1.1 Integrase {Bacteriophage HP1}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1ae9a_ 4.141.1.1.2 Integrase (Int) {Bacteriophage lambda}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d4crxa2 4.141.1.1.3 (130-341) Cre recombinase {Bacteriophage P1}
rakqalafertdfdqvrslmensdrcqdirnlaflgiayntllkiaeiarirvkdisrtd
ggrmlihigrtktlvstagvekalslgvtklverwisvsgvaddpnnylfcrvrkngvaa
psatsqlstralegifeathrliygakddsgqrylawsghsarvgaardmaragvsipei
mqaggwtnvnivmnyirnldsetgamvrlled
>d1a0p_2 4.141.1.1.4 (111-292) Recombinase XerD {Escherichia coli}
kdlseaqverllqaplidqplelrdkamlevlyatglrvselvgltmsdislrqgvvrvi
gkgnkerlvplgeeavywletylehgrpwllngvsidvlfpsqraqqmtrqtfwhrikhy
avlagidseklsphvlrhafathllnhgadlrvvqmllghsdlsttqiythvaterlrql
hq
>d1a31a1 4.141.1.2.1 (431-626,720-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravXklnxldpritvawckkwgvpiekiynktqrekfawaidmaded
yef
>d1a41__ 4.141.1.2.2 Eukaryotic DNA topoisomerase I, catalytic core {Vaccinia virus}
nakrdrifvrvynvmkrincfinknikksstdsnyqlavfmlmetmffirfgkmkylken
etvglltlknkhieispdeivikfvgkdkvshefvvhksnrlykpllkltddsspeeflf
nklserkvyecikqfgirikdlrtygvnytflynfwtnvksisplpspkklialtikqta
evvghtpsiskraymattilemvkdknfldvvskttfdeflsivvdhvks
>d1mhda_ 4.142.1.1.1 SMAD MH1 domain {Human (Homo sapiens)}
pivkrllgwkkgeqngqeekwcekavkslvkklkktgqldelekaittqnvntkcitipr
sldgrlqvshrkglphviycrlwrwpdlhshhelramelcefafnmkkdevcvnpyhyqr
vet
>d1mrj__ 4.143.1.1.1 alpha-Trichosanthin {Mongolian snake gourd (Trichosanthes kirillowii maxim)}
dvsfrlsgatsssygvfisnlrkalpnerklydipllrsslpgsqryalihltnyadeti
svaidvtnvyimgyragdtsyffneasateaakyvfkdamrkvtlpysgnyerlqtaagk
ireniplglpaldsaittlfyynansaasalmvliqstseaarykfieqqigkrvdktfl
pslaiislenswsalskqiqiastnngqfespvvlinaqnqrvtitnvdagvvtsniall
lnrnnma
>d1abra_ 4.143.1.1.5 Abrin A-chain {Abrus precatorius}
edrpikfstegatsqsykqfiealrerlrgglihdipvlpdpttlqernryitvelsnsd
tesievgidvtnayvvayragtqsyflrdapssasdylftgtdqhslpfygtygdlerwa
hqsrqqiplglqalthgisffrsggndneekartliviiqmvaeaarfryisnrvrvsiq
tgtafqpdaamislennwdnlsrgvqesvqdtfpnqvtltnirnepvivdslshptvavl
almlfvcnppn
>d1d6aa_ 4.143.1.1.6 Pokeweed antiviral protein alpha {Pokeweed (Phytolacca americana)}
vntiiynvgsttiskyatflndlrneakdpslkcygipmlpntntnpkyvlvelqgsnkk
titlmlrrnnlyvmgysdpfetnkcryhifndisgterqdvettlcpnansrvskninfd
sryptleskagvksrsqvqlgiqildsnigkisgvmsftekteaefllvaiqmvseaarf
kyienqvktnfnrafnpnpkvlnlqetwgkistaihdakngvlpkplelvdasgakwivl
rvdeikpdvallnyvggscqtt
>d1ift__ 4.143.1.1.7 Ricin A-chain {Castor bean (Ricinus communis)}
ypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilvelsnh
aelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafggnydr
leqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaarfqyie
gemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskfsvydv
silipiialmvyrcappp
>d1dm0a_ 4.143.1.2.1 Shiga toxin, A-chain {Shigella dysenteriae}
keftldfstaktyvdslnvirsaigtplqtissggtsllmidsgtgdnlfavdvrgidpe
egrfnnlrlivernnlyvtgfvnrtnnvfyrfadfshvtfpgttavtlsgdssyttlqrv
agisrtgmqinrhslttsyldlmshsgtsltqsvaramlrfvtvtaealrfrqiqrgfrt
tlddlsgrsyvmtaedvdltlnwgrlssvlpdyhgqdsvrvgrisfgsinailgsvalil
nchhhasrvarmasdefpsmcpadgrvrgithnkilwdsstlgailm
>e1htl.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1lta.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1ltb.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdi
>e1ltg.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1lti.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1lts.1a 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
rlyradsrppdeikrsgglmprghneyfdrgtqmninlydhargtqtgfvryddgyvsts
lslrsahlagqsilsgystyyiyviatapnmfnvndvlgvysphpyeqevsalggipysq
iygwyrvnfgviderlhrnreyrdryyrnlniapaedgyrlagfppdhqawreepwihha
pqgcg
>e1lts.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1ltt.1c 4.144.1.1.1 Heat-labile toxin, A-chain {Escherichia coli, type IB}
gdtcneetqnlstiylreyqskvkrqifsdyqsevdiynri
>e1tii.1c 4.144.1.1.2 Heat-labile toxin, A-chain {Escherichia coli, type IIB}
ttcasltnklsqhdladfkkyikrkftlmtllsinn
>d1ddt_2 4.144.1.1.3 (1-187) Diphtheria toxin, N-terminal domain {Corynebacterium diphtheriae}
gaddvvdssksfvmenfssyhgtkpgyvdsiqkgiqkpksgtqgnydddwkgfystdnky
daagysvdnenplsgkaggvvkvtypgltkvlalkvdnaetikkelglslteplmeqvgt
eefikrfgdgasrvvlslpfaegsssveyinnweqakalsveleinfetrgkrgqdamye
ymaqaca
>d1aera_ 4.144.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
aflgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvraa
iwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltlaapeaa
geverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvggdldp
ssipdkeqaisalpdyasqpgkppr
>d1prta_ 4.144.1.1.5 Pertussis toxin, S1 subunit {Bordetella pertussis}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>e1xtc.1c 4.144.1.1.6 Cholera toxin {Vibrio cholerae}
sntcdektqslgvkfldeyqskvkrqifsgyqsdidthnrikdel
>d1qs1a1 4.144.1.1.7 (60-264) Vegetative insecticidal protein 2 (VIP2) {Bacillus cereus}
tdkvedfkedkekakewgkekekewkltatekgkmnnfldnkndiktnykeitfsmagsf
edeikdlkeidkmfdktnlsnsiityknvepttigfnksltegntinsdamaqfkeqfld
rdikfdsyldthltaqqvsskervilkvtvpsgkgsttptkagvilnnseykmlidngym
vhvdkvskvvkkgveclqiegtlkk
>d1qs1a2 4.144.1.1.7 (265-461) Vegetative insecticidal protein 2 (VIP2) {Bacillus cereus}
sldfkndinaeahswgmknyeewakdltdsqrealdgyarqdykeinnylrnqggsgnek
ldaqiknisdalgkkpipenitvyrwcgmpefgyqisdplpslkdfeeqflntikedkgy
mstslsserlaafgsrkiilrlqvpkgstgaylsaiggfasekeilldkdskyhidkvte
viikgvkryvvdatllt
>d1a26_2 4.144.1.2.1 (797-1012) Poly(ADP-ribose) polymerase, C-terminal domain {Chicken (Gallus gallus)}
lrtdikvvdkdseeakiikqyvknthaathnaydlkvveifrieregesqrykpfkqlhn
rqllwhgsrttnfagilsqglriappeapvtgymfgkgiyfadmvsksanychtsqadpi
glillgevalgnmyelknashitklpkgkhsvkglgktapdptatttldgvevplgngis
tgindtcllyneyivydvaqvnlkyllklkfnykts
>d1bs4a_ 4.145.1.1.1 Peptide deformylase {Escherichia coli}
svlqvlhipderlrkvakpveevnaeiqrivddmfetmyaeegiglaatqvdihqriivi
dvsenrderlvlinpelleksgetgieegclsipeqralvpraekvkiraldrdgkpfel
eadgllaiciqhemdhlvgklfmdylsplkqqrirqkvekldrlkara
>d1chua3 4.146.1.1.1 (238-353) L-aspartate oxidase {Escherichia coli}
lefnqfhptalyhpqarnflltealrgegaylkrpdgtrfmpdfdergelaprdivarai
dhemkrlgadcmfldishkpadfirqhfpmiyekllglgidltqepvpivpaahyt
>d1fuma3 4.146.1.1.2 (226-357) Fumarate reductase flavoprotein subunit {Escherichia coli}
mefvqyhptglpgsgilmtegcrgeggilvnkngyrylqdygmgpetplgepknkymelg
prdkvsqafwhewrkgntistprgdvvyldlrhlgekklherlpficelakayvgvdpvk
epipvrptahyt
>d1qlaa3 4.146.1.1.3 (251-371) Fumarate reductase flavoprotein subunit {Wolinella succinogenes}
meavqfhptplfpsgilltegcrgdggilrdvdghrfmpdyepekkelasrdvvsrrmie
hirkgkgvqspygqhlwldisilgrkhietnlrdvqeiceyfagidpaekwapvlpmqhy
s
>d1qjda3 4.146.1.1.4 (360-505) Flavocytochrome c3 (respiratory fumarate reductase) {Shewanella frigidimarina}
qyiqahptlsvkggvmvteavrgngailvnregkrfvneittrdkasaailaqtgksayl
ifddsvrkslskidkyiglgvaptadslvklgkmegidgkaltetvarynslvssgkdtd
ferpnlpralnegnyyaievtpgvhh
>d1d4ca3 4.146.1.1.5 (360-505) Flavocytochrome c3 (respiratory fumarate reductase) {Shewanella putrefaciens}
yiqahptyspaggvmiteavrgngaivvnregnrfmneittrdkasaailqqkgesaylv
fddsirkslkaiegyvhlnivkegktieelakqidvpaaelaktvtayngfvksgkdaqf
erpdlprelvvapfyaleiapavhht
>d1qdda_ 4.147.1.1.1 Lithostathine, inhibitor of stone formation {Human (Homo sapiens)}
qeaqtelpqariscpegtnayrsycyyfnedretwvdadlycqnmnsgnlvsvltqaega
fvaslikesgtddfnvwiglhdpkknrawhwssgslvsykswgigapssvnpgycvslts
stgfqkwkdvpcedkfsfvckfkn
>d1b6e__ 4.147.1.1.2 CD94 {Human (Homo sapiens)}
cscqekwvgyrcncyfisseqktwnesrhlcasqkssllqlqntdeldfmsssqqfywig
lsyseehtawlwengsalsqylfpsfetfntknciaynpngnaldescedknryickqql
i
>d1ixxa_ 4.147.1.1.3 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dclsgwssyeghcykafekyktwedaervcteqakgahlvsiessgeadfvaqlvtqnmk
rldfyiwiglrvqgkvkqcnsewsdgssvsyenwieaesktclgleketdfrkwvniycg
qqnpfvcea
>d1ixxb_ 4.147.1.1.3 Coagulation factors IX/X-binding protein (IX/X-BP) {Habu snake (Trimeresurus flavoviridis)}
dcpsdwssyeghcykpfsepknwadaenfctqqhagghlvsfqsseeadfvvklafqtfg
hsifwmglsnvwnqcnwqwsnaamlrykawaeesycvyfkstnnkwrsracrmmaqfvce
fqa
>d2afpa_ 4.147.1.1.4 Type II antifreeze protein {Sea raven (Hemitripterus americanus)}
qragpncpagwqplgdrciyyettamtwalaetncmklgghlasihsqeehsfiqtlnag
vvwiggsaclqagawtwsdgtpmnfrswcstkpddvlaaccmqmtaaadqcwddlpcpas
hksvcamtf
>d1qo3c_ 4.147.1.1.5 NK cell receptor ly49a {Mouse (Mus musculus)}
stvldslqhtgrgdkvywfcygmkcyyfvmdrktwsgckqtcqssslsllkiddedelkf
lqlvvpsdscwvglsydnkkkdwawidnrpsklalntrkynirdggcmllsktrldngnc
dqvficicgkrld
>d1esl_1 4.147.1.1.6 (1-118) E-selectin {Human (Homo sapiens)}
wsyntsteamtydeasaycqqrythlvaiqnkeeieylnsilsyspsyywigirkvnnvw
vwvgtqkplteeaknwapgepnnrqkdedcveiyikrekdvgmwndercskkklalcy
>d1hup_1 4.147.1.1.7 (112-228) Mannose-binding protein A, lectin domain {Human (Homo sapiens)}
kqvgnkffltngeimtfekvkalcvkfqasvatprnaaengaiqnlikeeaflgitdekt
egqfvdltgnrltytnwnegepnnagsdedcvlllkngqwndvpcstshlavcefpi
>d1rdl1_ 4.147.1.1.8 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kyfmssvrrmplnrakalcselqgtvatprnaeenraiqnvakdvaflgitdqrtenvfe
dltgnrvrytnwnegepnnvgsgencvvlltngkwndvpcsdsflvvcefs
>d2msba_ 4.147.1.1.8 Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevtegqf
myvtggrltysnwkkdepndhgsgedcvtivdnglwndiscqashtavcefp
>d1b08a1 4.147.1.1.9 (235-355) Lung surfactant protein D (SP-D), lectin domain {Human (Homo sapiens)}
pngqsvgekifktagfvkpfteaqllctqaggqlasprsaaenaalqqlvvakneaafls
mtdsktegkftyptgeslvysnwapgepnddggsedcveiftngkwndracgekrlvvce
f
>d1byfa_ 4.147.1.1.10 Lectin TC14 {Tunicate (Polyandrocarpa misakiensis)}
dyeilfsdetmnyadagtycqsrgmalvssamrdstmvkailaftevkghdywvgadnlq
dgaynflwndgvslptdsdlwspnepsnpqswqlcvqiwskynllddvgcggarrvicek
eld
>d1tn3__ 4.147.1.1.11 Tetranectin {Human (Homo sapiens)}
alqtvclkgtkvhmkcflaftqtktfheasedcisrggtlstpqtgsendalyeylrqsv
gneaeiwlglndmaaegtwvdmtgariayknweteitaqpdggktencavlsgaangkwf
dkrcrdqlpyicqfgiv
>d1bcpb2 4.147.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpc2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1bcph2 4.147.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpi2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1prtb2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgtyl
ggeyggvikdgtpggafdlkttfcim
>d1prtc2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1prth2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgtyl
ggeyggvikdgtpggafdlkttfcim
>d1prti2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1ptob2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgtyl
ggeyggvikdgtpggafdlkttfcim
>d1ptoc2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1ptoh2 4.147.1.2.1 (2-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
tpgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgt
ylggeyggvikdgtpggafdlkttfcim
>d1ptoi2 4.147.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1prea1 4.147.1.2.2 (2-84) Proaerolysin, N-terminal domain {Aeromonas hydrophila}
epvypdqlrlfslgqgvcgdkyrpvnreeaqsvksnivgmmgqwqisglangwvimgpgy
ngeikpgtasntwcyptnpvtge
>d1preb1 4.147.1.2.2 (2-84) Proaerolysin, N-terminal domain {Aeromonas hydrophila}
epvypdqlrlfslgqgvcgdkyrpvnreeaqsvksnivgmmgqwqisglangwvimgpgy
ngeikpgtasntwcyptnpvtge
>d1inma3 4.147.1.3.1 (183-280) Intimin {Escherichia coli}
livpnmskrvtyndavntcknfggklpssqnelenvfkawgaankyeyykssqtiiswvq
qtaqdvksgvastydlvkqnplnnikasesnayatcvk
>d1cwva5 4.147.1.3.2 (887-986) Invasin {(Yersinia pseudotuberculosis)}
nrwiydggrslvssleasrqcqgsdmsavlessratngtrapdgtlwgewgsltayssdw
qsgeywvkktstdfetmnmdtgalqpgpaylafplcalsi
>d1tsg__ 4.147.1.4.1 TSG-6, Link module {Human (Homo sapiens)}
gvyhrearsgkykltyaeakavcefegghlatykqleaarkigfhvcaagwmakgrvgyp
ivkpgpncgfgktgiidygirlnrserwdaycynphak
>d1koe__ 4.147.1.5.2 Endostatin {Mouse (Mus musculus)}
qpvlhlvalntplsggmrgirgadfqcfqqaravglsgtfraflssrlqdlysivrradr
gsvpivnlkdevlspswdslfsgsqgqlqpgarifsfdgrdvlrhpawpqksvwhgsdps
grrlmesycetwrtettgatgqassllsgrlleqkaaschnsyivlciensf
>d1by2__ 4.148.1.1.1 M2BP {Human (Homo sapiens)}
avndgdmrladggatnqgrveifyrgqwgtvcdnlwdltdasvvcralgfenatqalgra
afgqgsgpimldevqctgteasladckslgwlksncrherdagvvctnetrsthtl
>d1fid__ 4.149.1.1.1 Fibrinogen C-terminal domains {Human (Homo sapiens), beta and gamma}
qihditgkdcqdiankgakqsglyfikplkanqqflvyceidgsgngwtvfqkrldgsvd
fkknwiqykegfghlsptgttefwlgnekihlistqsaipyalrveledwngrtstadya
mfkvgpeadkyrltyayfaggdagdafdgfdfgddpsdkfftshngmqfstwdndndkfe
gncaeqdgsgwwmnkchaghlngvyyqggtyskastpngydngiiwatwktrwysmkktt
mkiipfnrltigegqqhhl
>d1fzda_ 4.149.1.1.2 Fibrinogen C-terminal domains {Human (Homo sapiens), fibrinogen-420, alpha-E}
ggwlliqqrmdgslnfnrtwqdykrgfgslndegegefwlgndylhlltqrgsvlrvele
dwagneayaeyhfrvgseaegyalqvssyegtagdaliegsveegaeytshnnmqfstfd
rdadqweencaevygggwwynncqaanlngiyypggsydprnnspyeiengvvwvsfrga
dyslravrmkirplvtq
>d1gc1g_ 4.150.1.1.1 gp120 core {Human immunodeficiency virus, type 1, HIV-1}
tenfnmwkndmveqmhediislwdqslkpcvkltplcvgagscntsvitqacpkvsfepi
pihycapagfailkcnnktfngtgpctnvstvqcthgirpvvstqlllngslaeeevvir
svnftdnaktiivqlntsveinctgaghcnisrakwnntlkqiasklreqfgnnktiifk
qssggdpeivthsfncggeffycnstqlfnstwfnstwstkgsnntegsdtitlpcrikq
iinmwqkvgkamyappisgqircssnitgllltrdggnsnneseifrpgggdmrdnwrse
lykykvvkie
>d1msk__ 4.151.1.1.1 Methionine synthase (activation domain) {Escherichia coli}
tppvtleaardndfafdwqaytppvahrlgvqeveasietlrnyidwtpffmtwslagky
priledevvgveaqrlfkdandmldklsaektlnprgvvglfpanrvgddieiyrdetrt
hvinvshhlrqqtektgfanycladfvapklsgkadyigafavtggleedaladafeaqh
ddynkimvkaladrlaeafaeylhervrkvywgyapnenlsneelirenyqgirpapgyp
acpehtekatiwellevekhtgmkltesfamwpgasvsgwyfshpdskyyavaqiqrdqv
edyarrkgmsvteverwlapnlgydad
>d1nsea_ 4.152.1.1.2 Nitric oxide (NO) synthase oxygenase domain {Bovine (Bos taurus)}
gpkfprvknwelgsitydtlcaqsqqdgpctprrclgslvlprklqtrpspgpppaeqll
sqardfinqyyssikrsgsqaheerlqeveaevastgtyhlreselvfgakqawrnaprc
vgriqwgklqvfdardcssaqemftyicnhikyatnrgnlrsaitvfpqrapgrgdfriw
nsqlvryagyrqqdgsvrgdpanveitelciqhgwtpgngrfdvlplllqapdeapelfv
lppelvlevplehptlewfaalglrwyalpavsnmlleigglefsaapfsgwymsteigt
rnlcdphryniledvavcmdldtrttsslwkdkaaveinlavlhsfqlakvtivdhhaat
vsfmkhldneqkarggcpadwawivppisgsltpvfhqemvnyilspafryqpdpw
>d1pmd_3 4.153.1.1.1 (76-263) Penicillin-binding protein 2x (pbp-2x), N-terminal domain {Streptococcus pneumoniae}
rgtiydrngvpiaedatsynvyavidenyksatgkilyvektqfnkvaevfhkyldmees
yvreqlsqpnlkqvsfgakgngityanmmsikkeleaaevkgidfttspnrsypngqfas
sfiglaqlhenedgsksllgtsgmesslnsilagtdgiityekdrlgnivpgteqvsqrt
mdgkdvyt
>d1soxa3 4.154.1.1.1 (94-343) Sulfite oxidase, middle catalytic domain {Chicken (Gallus gallus)}
qdpfagdpprhpglrvnsqkpfnaeppaellaerfltpnelfftrnhlpvpavepssyrl
rvdgpgggtlslslaelrsrfpkhevtatlqcagnrrsemsrvrpvkglpwdigaistar
wggarlrdvllhagfpeelqgewhvcfegldadpggapygasipygralspaadvllaye
mngtelprdhgfpvrvvvpgvvgarsvkwlrrvavspdespshwqqndykgfspcvdwdt
vdyrtapaiq
>d3pah__ 4.155.1.1.2 Phenylalanine hydroxylase {Human (Homo sapiens)}
tvpwfprtiqeldrfanqilsygaeldadhpgfkdpvyrarrkqfadiaynyrhgqpipr
veymeeekktwgtvfktlkslykthacyeynhifpllekycgfhednipqledvsqflqt
ctgfrlrpvagllssrdflgglafrvfhctqyirhgskpmytpepdichellghvplfsd
rsfaqfsqeiglaslgapdeyieklatiywftvefglckqgdsikaygagllssfgelqy
clsekpkllplelektaiqnytvtefqplyyvaesfndakekvrnfaatiprpfsvrydp
ytqrievl
>d1qaxa2 4.156.1.1.1 (4-110,221-428) Substrate-binding domain of HMG-CoA reductase {Pseudomonas mevalonii}
dsrlpafrnlspaarldhigqllglshddvsllanagalpmdiangmienvigtfelpya
vasnfqingrdvlvplvveepsivaaasymaklaranggfttsssapXrlaraqvritpq
qletaefsgeaviegildayafaavdpyraathnkgimngidplivatgndwraveagah
ayacrsghygslttwekdnnghlvgtlempmpvglvggatkthplaqlslrilgvktaqa
laeiavavglaqnlgamralategiqrghmalharniavvagargdevdwvarqlveyhd
vradravallkqkrgq
>d16vpa_ 4.157.1.1.1 Conserved core of transcriptional regulatory protein vp16 {Herpes simplex virus, type 1, HSV-1}
srmpsppmpvppaalfnrllddlgfsagpalctmldtwnedlfsalptnadlyreckfls
tlpsdvvewgdayvpertqidirahgdvafptlpatrdglglyyealsrffhaelraree
syrtvlanfcsalyrylrasvrqlhrqahmrgrdrdlgemlratiadryyretarlarvl
flhlylfltreilwaayaeqmmrpdlfdclccdleswrqlaglfqpfmfvngaltvrgvp
iearrlrelnhirehlnlplvrsaateepgaplttpptlhgnqarasgyfmvliraklds
yssfttspseavmrehaysraptknnygstieglldlpdddapeeaglaaprlsfl
>d1bdfa2 4.158.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1qgwa_ 4.159.1.1.1 Phycoerythrin 545 alpha-subunits {Red alga (Porphyridium sordium)}
amdxsakapqitifdhrgcsrapkestggkaggqddemmvkvastkvtvsesdaakklqe
fitfekgidgpftskn
>d1qgwb_ 4.159.1.1.1 Phycoerythrin 545 alpha-subunits {Red alga (Porphyridium sordium)}
amdxsakapvitifdhrgcsrapkeytgakaggkddemmvkaqsvkievstgtaegvlat
slakmtk
>e1hle.1b 5.1.1.1.1 Elastase inhibitor {Horse (Equus caballus)}
eenfnadhpfiffirhnpsanilflgrfssp
>d1ovaa_ 5.1.1.1.2 Ovalbumin {Hen (Gallus domesticus)}
xgsigaasmefcfdvfkelkvhhanenifycpiaimsalamvylgakdstrtqinkvvrf
dklpgfgdsieaqcgtsvnvhsslrdilnqitkpndvysfslasrlyaeerypilpeylq
cvkelyrgglepinfqtaadqarelinswvesqtngiirnvlqpssvdsqtamvlvnaiv
fkglwekafkdedtqampfrvteqeskpvqmmyqiglfrvasmasekmkilelpfasgtm
smlvllpdevsgleqlesiinfekltewtssnvmeerkikvylprmkmeekynltsvlma
mgitdvfsssanlsgissaeslkisqavhaahaeineagrevvgsaeagvdaasvseefr
adhpflfcikhiatnavlffgrcvsp
>e1as4.1a 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
glasanvdfafslykqlvlkapdknvifsplsistalaflslgahnttlteilkglkfnl
tetseaeihqsfqhllrtlnqssdelqlsmgnamfvkeqlslldrftedakrlygseafa
tdfqdsaaakklindyvkngtrgkitdlikdldsqtmmvlvnyiffkakwempfdpqdth
qsrfylskkkwvmvpmmslhhltipyfrdeelsctvvelkytgnasalfilpdqdkmeev
eamllpetlkrwrdslefreigelylpkfsisrdynlndillqlgieeaftskadlsgit
garnlavsqvvhkavldvfeegteasratavkitll
>e1as4.1b 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
gtivrfnrpflmiivptdtqniffmskvtnpkq
>e2ach.1b 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
trtivrfnrpflmiivptdtqniffmskvtnpkqa
>e3caa.1b 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
rtivrfnrpflmiivptdtqniffmskvtnpk
>e4caa.1b 5.1.1.1.3 Antichymotrypsin, alpha-1 {Human (Homo sapiens)}
rtivrfnrpflmiivptdtqniffmskvtnpkq
>e1qmb.1b 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
leaiprsippevkfnapfvflmieqntksplfmgkvvnptqk
>e7api.1b 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
sippevkfnkpfvflmieqntksplfmgkvvnptqk
>e8api.1b 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
sippevkfnkpfvflmieqntksplfmgkvvnptqk
>e9api.1b 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
sippevkfnkpfvflmieqntksplfmgkvvnptqk
>d1azxi_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
gspvdictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfatt
fyqhladskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihf
ffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeq
sraainkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfyk
adgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltp
evlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrdd
lyvsdafhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntii
fmgrvanpcv
>d1a7ca_ 5.1.1.1.7 Plasminogen activator inhibitor-1 {Human (Homo sapiens)}
hhppsyvahlasdfgvrvfqqvaqaskdrnvvfspygvasvlamlqlttggetqqqiqaa
mgfkiddkgmapalrhlykelmgpwnkdeisttdaifvqrdlklvqgfmphffrlfrstv
kqvdfseverarfiindwvkthtkgmisnllgkgavdqltrlvlvnalyfngqwktpfpd
ssthrrlfhksdgstvsvpmmaqtnkfnytefttpdghyydilelpyhgdtlsmfiaapy
ekevplsaltnilsaqlishwkgnmtrlprllvlpkfsletevdlrkplenlgmtdmfrq
fqadftslsdqeplhvaqalqkvkievnesgtvessstavivsarmapeeiimdrpflfv
vrhnptgtvlfmgqvmep
>d1sek__ 5.1.1.1.9 Serpin K {Tobacco hawkmoth (Manduca sexta)}
getdlqkilresndqftaqmfsevvkanpgqnvvlsafsvlpplgqlalasvgeshdell
ralalpndnvtkdvfadlnrgvravkgvdlkmaskiyvakglelnddfaavsrdvfgsev
qnvdfvksveaagainkwvedqtnnriknlvdpdaldettrsvlvnaiyfkgswkdkfnk
ertmdrdfhvskdktikvptmigkkdvryadvpeldakmiemsyegdqasmiiilpnqvd
gitaleqklkdpkalsraeerlynteveiylpkfkietttdlkevlsnmnikklftpgaa
rlenllktkeslyvdaaiqkafievneegaeaaaanafkittysfhfvpkveinkpfffs
lkynrnsmfsgvcvqp
>d1ecra_ 5.2.1.1.1 Replication terminator protein (Tus) {Escherichia coli}
dlvdrlnttfrqmeqelaifaahleqhkllvarvfslpevkkedehnplnrievkqhlgn
daqslalrhfrhlfiqqqsenrsskaavrlpgvlcyqvdnlsqaalvshiqhinklkttf
ehivtveselptaarfewvhrhlpglitlnayrtltvlhdpatlrfgwankhiiknlhrd
evlaqlekslksprsvapwtreewqrklereyqdiaalpqnaklkikrpvkvqpiarvwy
kgdqkqvqhacptplialinrdngagvpdvgellnydadnvqhrykpqaqplrliiprlh
lyvad
>d1skf__ 5.3.1.1.1 D-ala carboxypeptidase/transpeptidase {Streptomyces K15}
vtkptiaavggyamnngtgttlytkaadtrrstgsttkimtakvvlaqsnlnldakvtiq
kaysdyvvannasqahlivgdkvtvrqllyglmlpsgcdaayaladkygsgstraarvks
figkmntaatnlglhnthfdsfdgignganystprdltkiassamknstfrtvvktkayt
aktvtktgsirtmdtwkntngllssysgaigvktgsgpeakyclvfaatrggktvigtvl
astsiparesdatkimnygfal
>d3pte__ 5.3.1.1.2 D-ala carboxypeptidase/transpeptidase {Streptomyces R61}
adlpapddtglqavlhtalsqgapgamvrvddngtihqlsegvadratgraitttdrfrv
gsvtksfsavvllqlvdegkldldasvntylpgllpddritvrqvmshrsglydytndmf
aqtvpgfesvrnkvfsyqdlitlslkhgvtnapgaaysysntnfvvagmliekltghsva
teyqnriftplnltdtfyvhpdtvipgthangyltpdeaggalvdsteqtvswaqsagav
isstqdldtffsalmsgqlmsaaqlaqmqqwttvnstqgyglglrrrdlscgisvyghtg
tvqgyytyafaskdgkrsvtalantsnnvnvlntmartlesafcgkp
>d1btl__ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1alq__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
sepivlviftnkdnksdkpndklisetaksvmkefaagsknaakelndlekkynahigvy
aldtksgkevkfnsdkrfayastskainsailleqvpynklnkkvhinkddivayspile
kyvgkditlkalieasmtysdntannkiikeiggikkvkqrlkelgdkvtnpvryeieln
yyspkskkdtstpaafgktlnkliangklskenkkflldlmlnnksgdtlikdgvpkdyk
vadksgqaityasrndvafvypk
>d1dja__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
mkelndlekkynahigvyaldtksgkevkfnsdkrfayastshainsailleqvpynkln
kkvhinkddivayspilekyvgkditlkalieasmtysdntannkiikeiggikkvkqrl
kelgdkvtnpvryeielnyyspkskkdtstpaafgktlnkliangklskenkkflldlml
nnksgdtlikdgvpkdykvadksgqaityasrndvafvypkgqsepivlviftnkdnksd
kpndklisetaksvmkef
>d1bsg__ 5.3.1.1.9 beta-Lactamase, class A {Streptomyces albus G}
sdaerrlaglerasgarlgvyaydtgsgrtvayradelfpmcsvfktlssaavlrdldrn
geflsrrilytqddveqadgapetgkpqnlangmtveelcevsitasdncaanlmlrelg
gpaavtrfvrslgdrvtrldrwepelnsaepgrvtdttspraitrtygrlvlgdalnprd
rrlltswllanttsgdrfraglpddwtlgdktgagrygtnndagvtwppgrapivltvlt
akteqdaarddglvadaarvlaetlg
>d1mfoa_ 5.3.1.1.10 beta-Lactamase, class A {Mycobacterium fortuitum}
apiddqlaelerrdnvliglyaanlqsgrrithrpdemfamcstfkgyvaarvlqmaehg
eisldnrvfvdadalvpnspvtearagaemtlaelcqaalqrsdntaanlllktiggpaa
vtafarsvgdertrldrwevelnsaipgdprdtstpaalavgyrailagdalsppqrgll
edwmranqtssmraglpegwttadktgsgdygstndagiafgpdgqrlllvmmtrsqahd
pkaenlrpligeltalvlpsll
>d1gcea_ 5.3.1.1.12 AMPC beta-Lactamase, class C {Enterobacter cloacae, P99, cephalosporinase}
tpvsekqlaevvantvtplmkaqsvpgmavaviyqgkphyytfgkadiaankpvtpqtlf
elgsisktftgvlggdaiargeislddpvtrywpqltgkqwqgirmldlatytagglplq
vpdevtdnasllrfyqnwqpqwkpgttrlyanasiglfgalavkpsgmpyeqamttrvlk
plkldhtwinvpkaeeahyawgyrdgkavravrvspgmldaqaygvktnvqdmanwvman
mapenvadaslkqgialaqsrywrigsmyqglgwemlnwpveantvvegsdskvalaplp
vaevnppappvkaswvhktgstggfgsyvafipekqigivmlantsypnparveaayhil
ealq
>d1pmd_4 5.3.1.1.14 (264-619) Penicillin-binding protein 2x (pbp-2x), transpeptidase domain {Streptococcus pneumoniae}
tissplqsfmetqmdafqekvkgkymtatlvsaktgeilattqrptfdadtkegitedfv
wrdilyqsnyepgstmkvmmlaaaidnntfpggevfnsselkiadatirdwdvnegltgg
rmmtfsqgfahssnvgmtlleqkmgdatwldylnrfkfgvptrfgltdeyagqlpadniv
niaqssfgqgisvtqtqmiraftaiandgvmlepkfisaiydpndqtarksqkeivgnpv
skdaasltrtnmvlvgtdpvygtmynhstgkptvtvpgqnvalksgtaqiadeknggylv
gltdyifsavsmspaenpdfilyvtvqqpehysgiqlgefanpilerasamkdsln
>d1lbea_ 5.4.1.1.1 ADP ribosyl cyclase {Sea hare (Aplysia californica)}
ivptrelenvflgrckdyeitryldilprvrsdcsalwkdffkafsfknpcdldlgsykd
fftsaqqqlpknkvmfwsgvydeahdyantgrkyitledtlpgymlnslvwcgqranpgf
nekvcpdfktcpvqaresfwgmasssyahsaegevtymvdgsnpkvpayrpdsffgkyel
pnltnkvtrvkvivlhrlgekiiekcgagslldleklvkakhfafdcvenpravlfllcs
dnpnarecrl
>d1dgfa_ 5.5.1.1.2 Catalase I {Human (Homo sapiens)}
rdpasdqmqhwkeqraaqkadvlttgagnpvgdklnvitvgprgpllvqdvvftdemahf
dreripervvhakgagafgyfevthditkyskakvfehigkktpiavrfstvagesgsad
tvrdprgfavkfytedgnwdlvgnntpiffirdpilfpsfihsqkrnpqthlkdpdmvwd
fwslrpeslhqvsflfsdrgipdghrhmngygshtfklvnangeavyckfhyktdqgikn
lsvedaarlsqedpdygirdlfnaiatgkypswtfyiqvmtfnqaetfpfnpfdltkvwp
hkdyplipvgklvlnrnpvnyfaeveqiafdpsnmppgieaspdkmlqgrlfaypdthrh
rlgpnylhipvncpyrarvanyqrdgpmcmqdnqggapnyypnsfgapeqqpsalehsiq
ysgevrrfntanddnvtqvrafyvnvlneeqrkrlceniaghlkdaqifiqkkavknfte
vhpdygshiqalldkyn
>d1buca2 5.6.1.1.1 (1-232) Butyryl-CoA dehydrogenase {Megasphaera elsdenii}
mdfnltdiqqdflklahdfgekklaptvterdhkgiydkelidellslgitgayfeekyg
gsgddggdvlsyilaveelakydagvaitlsatvslcanpiwqfgteaqkekflvplveg
tklgafgltepnagtdasgqqtiatknddgtytlngskifitnggaadiyivfamtdksk
gnhgitafiledgtpgftygkkedkmgihtsqtmelvfqdvkvpaenmlgee
>d3mdda2 5.6.1.1.2 (11-241) Medium chain acyl-CoA dehydrogenase {Pig (Sus scrofa)}
gfsfelteqqkefqatarkfareeiipvaaeydrtgeypvpllkrawelglmnthipesf
gglglgiidscliteelaygctgvqtaieantlgqvpliiggnyqqqkkylgrmteeplm
caycvtepgagsdvagiktkaekkgdeyiingqkmwitnggkanwyfllarsdpdpkapa
skaftgfiveadtpgvqigrkeinmgqrcsdtrgivfedvrvpkenvltge
>d1ivha2 5.6.1.1.4 (6-241) Isovaleryl-coa dehydrogenase {Human (Homo sapiens)}
vddainglseeqrqlrqtmakflqehlapkaqeidrsnefknlrefwkqlgnlgvlgita
pvqyggsglgylehvlvmeeisrasgavglsygahsnlcinqlvrngneaqkekylpkli
sgeyigalamsepnagsdvvsmklkaekkgnhyilngnkfwitngpdadvlivyaktdla
avpasrgitafivekgmpgfstskkldklgmrgsntcelifedckipaanilghen
>d1frpa_ 5.7.1.1.1 Fructose-1,6-bisphosphatase {Pig (Sus scrofa)}
nivtltrfvmeqgrkargtgemtqllnslctavkaistavrkagiahlygiagatnvtgd
qvkkldvlsndlvinvlkssfatcvlvteedknaiivepekrgkyvvcfdpldgssnidc
lvsigtifgiyrknstdepsekdalqpgrnlvaagyalygsatmlvlamvngvncfmldp
aigefilvdrnvkikkkgsiysinegyakefdpaiteyiqrkkfppdnsapygaryvgsm
vadvhrtlvyggifmypankkspkgklrllyecnpmayvmekagglattgkeavldivpt
dihqrapiilgspedvtelleiyqkha
>d2hhma_ 5.7.1.2.1 Inositol monophosphatase {Human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1inp__ 5.7.1.3.1 Inositol polyphosphate 1-phospatase {Bovine (Bos taurus), brain}
msdilqellrvsekaaniaracrqqetlfqllieekkegeknkkfavdfktladvlvqev
ikenmenkfpglgkkifgeesneltndlgekiimrlgpteeetvallskvlngnklasea
lakvvhqdvffsdpaldsveinipqdilgiwvdpidstyqyikgsaditpnqgifpsglq
cvtvligvydiqtgvplmgvinqpfvsqdlhtrrwkgqcywglsylgtnihsllppvstr
snseaqsqgtqnpssegscrfsvvistseketikgalshvcgerifraagagykslcvil
gladiyifsedttfkwdscaahailramgggmvdlkeclernpdtgldlpqlvyhvgneg
aagvdqwankggliayrsekqletflsrllqhlapvatht
>d1qgxa_ 5.7.1.4.1 3';5'-adenosine bisphosphatase, PAP phosphatase {Yeast (Candida albicans)}
alerellvatqavrkaslltkriqsevishkdsttitkndnspvttgdyaaqtiiinaik
snfpddkvvgeesssglsdafvsgilneikandevynknykkddflftndqfplksledv
rqiidfgnyeggrkgrfwcldpidgtkgflrgeqfavclalivdgvvqlgcigcpnlvls
sygaqdlkghesfgyifravrglgafyspssdaeswtkihvrhlkdtkdmitlegvekgh
sshdeqtaiknklniskslhldsqakycllalgladvylrlpiklsyqekiwdhaagnvi
vheaggihtdamedvpldfgngrtlatkgviassgprelhdlvvstscdviqsr
>d1xwl_2 5.8.1.1.3 (493-876) DNA polymerase I (Klenow fragment) {Bacillus stearothermophilus, newly identified strain as yet unnamed}
vkvdtkrleqmgkelaeqlgtveqriyelagqefninspkqlgvilfeklqlpvlkktkt
gystsadvleklapyheivenilhyrqlgklqstyiegllkvvrpdtkkvhtifnqaltq
tgrlsstepnlqnipirleegrkirqafvpsesdwlifaadysqielrvlahiaeddnlm
eafrrdldihtktamdifqvsedevtpnmrrqakavnfgivygisdyglaqnlnisrkea
aefieryfesfpgvkrymenivqeakqkgyvttllhrrrylpditsrnfnvrsfaermam
ntpiqgsaadiikkamidlnarlkeerlqahlllqvhdelileapkeemerlcrlvpevm
eqavtlrvplkvdyhygstwydak
>d1t7pa2 5.8.1.1.4 (211-704) T7 phage DNA polymerase {Bacteriophage T7}
leavdiehraawllakqerngfpfdtkaieelyvelaarrsellrkltetfgswyqpkgg
temfchprtgkplpkypriktpkvggifkkpknkaqregrepceldtreyvagapytpve
hvvfnpssrdhiqkklqeagwvptkytdkgapvvddevlegvrvddpekqaaidlikeyl
miqkrigqsaegdkawlryvaedgkihgsvnpngavtgrathafpnlaqipgvrspygeq
craafgaehhldgitgkpwvqagidasglelrclahfmarfdngeyaheilngdihtknq
iaaelptrdnaktfiygflygagdekigqivgagkergkelkkkflentpaiaalresiq
qtlvessqwvageqqvkwkrrwikgldgrkvhvrsphaalntllqsagalicklwiikte
emlvekglkhgwdgdfaymawvhdeiqvgcrteeiaqvvietaqeamrwvgdhwnfrcll
dtegkmgpnwaich
>d1clqa2 5.8.1.1.5 (376-903) T4-like DNA polymerase {Bacteriophage RB69}
qnkvipqgrshpvqpypgafvkepipnrykyvmsfdltslypsiirqvnispetiagtfk
vaplhdyinavaerpsdvyscspngmmyykdrdgvvpteitkvfnqrkehkgymlaaqrn
geiikealhnpnlsvdepldvdyrfdfsdeikekikklsakslnemlfraqrtevagmta
qinrkllinslygalgnvwfryydlrnataittfgqmalqwierkvneylnevcgtegea
fvlygdtdsiyvsadkiidkvgeskfrdtnhwvdfldkfarermepaidrgfremceymn
nkqhlmfmdreaiagpplgskgiggfwtgkkryalnvwdmegtryaepklkimgletqks
stpkavqkalkecirrmlqegeeslqeyfkefekefrqlnyisiasvssanniakydvgg
fpgpkcpfhirgiltynraikgnidapqvvegekvyvlplregnpfgdkciawpsgteit
dlikddvlhwmdytvllektfikplegftsaakldyekkaslfdmfdf
>d1tgoa2 5.8.1.1.6 (348-773) T4-like DNA polymerase {Thermococcus gorgonarius}
stgnlvewfllrkayernelapnkpderelarrresyaggyvkeperglwenivyldfrs
lypsiiithnvspdtlnregceeydvapqvghkfckdfpgfipsllgdlleerqkvkkkm
katidpiekklldyrqraikilansfygyygyakarwyckecaesvtawgrqyiettire
ieekfgfkvlyadtdgffatipgadaetvkkkakefldyinaklpglleleyegfykrgf
fvtkkkyavideedkittrgleivrrdwseiaketqarvleailkhgdveeavrivkevt
eklskyevppeklviyeqitrdlkdykatgphvavakrlaargikirpgtvisyivlkgs
grigdraipfdefdpakhkydaeyyienqvlpaverilrafgyrkedlryqktrqvglga
wlkpkt
>d1mml__ 5.8.1.2.1 MMLV reverse transcriptase {Moloney murine leukemia virus, MMLV}
twlsdfpqawaetggmglavrqapliiplkatstpvsikqypmsqearlgikphiqrlld
qgilvpcqspwntpllpvkkpgtndyrpvqdlrevnkrvedihptvpnpynllsglppsh
qwytvldlkdaffclrlhptsqplfafewrdpemgisgqltwtrlpqgfknsptlfdeal
hrdladfriqhpdlillqyvddlllaatseldcqqgtrallqtlgnlgyrasakkaqicq
kqvkylgyllk
>d1vrta2 5.8.1.2.2 (4-429) HIV-1 reverse transcriptase {Human immunodeficiency virus, type 1, HIV-1}
pietvpvklkpgmdgpkvkqwplteekikalveictemekegkiskigpenpyntpvfai
kkkdstkwrklvdfrelnkrtqdfwevqlgiphpaglkkkksvtvldvgdayfsvplded
frkytaftipsinnetpgiryqynvlpqgwkgspaifqssmtkilepfrkqnpdiviyqy
mddlyvgsdleigqhrtkieelrqhllrwglttpdkkhqkeppflwmgyelhpdkwtvqp
ivlpekdswtvndiqklvgklnwasqiypgikvrqlckllrgtkalteviplteeaelel
aenreilkepvhgvyydpskdliaeiqkqgqgqwtyqiyqepfknlktgkyarmrgahtn
dvkqlteavqkittesiviwgktpkfklpiqketwetwwteywqatwipewefvntpplv
klwyql
>d1ceza_ 5.8.1.3.1 T7 RNA polymerase {Bacteriophage T7}
iakndfsdielaaipfntladhygerlareqlalehesyemgearfrkmferqlkageva
dnaaakplittllpkmiarindwfeevkakrgkrptafqflqeikpeavayitikttlac
ltsadnttvqavasaigraiedearfgrirdleakhfkknveeqlnkrvghvykkafmqv
veadmlskgllggeawsswhkedsihvgvrciemliestgmvslhrqnagvvgqdsetie
lapeyaeaiatragalagispmfqpcvvppkpwtgitgggywangrrplalvrthskkal
mryedvympevykainiaqntawkinkkvlavanvitkwkhcpvedipaiereelpmkpe
didmnpealtawkraaaavyrkdkarksrrislefmleqankfanhkaiwfpynmdwrgr
vyavsmfnpqgndmtkglltlakgkpigkegyywlkihgancagvdkvpfperikfieen
henimacaksplentwwaeqdspfcflafcfeyagvqhhglsyncslplafdgscsgiqh
fsamlrdevggravnllpsetvqdiygivakkvneilqadaingtdnevvtvtdentgei
sekvklgtkalagqwlaygvtrsvtkrsvmtlaygskefgfrqqvledtiqpaidsgkgl
mftqpnqaagymakliwesvsvtvvaaveamnwlksaakllaaevkdkktgeilrkrcav
hwvtpdgfpvwqeykkpiqtrlnlmflgqfrlqptintnkdseidahkqesgiapnfvhs
qdgshlrktvvwahekygiesfalihdsfgtipadaanlfkavretmvdtyescdvladf
ydqfadqlhesqldkmpalpakgnlnlrdilesdfafa
>d1rdr__ 5.8.1.4.1 RNA-dependent RNA-polymerase {Poliovirus type 1, mahoney strain}
vgypiinapsktklepsafhyvfegvkepavltkndprlktdfeeaifskyvgnkitevd
eymkeavdhyagqlmsldinteqmcledamygtdglealdlstsagypyvamgkkkrdil
nkqtrdtkemqklldtyginlplvtyvkdelrsktkveqgksrlieasslndsvamrmaf
gnlyaafhknpgvitgsavgcdpdlfwskipvlmeeklfafdytgydaslspawfealkm
vlekigfgdrvdyidylnhshhlyknktycvkggmpsgcsgtsifnsminnliirtlllk
tykgidldhlkmiaygddviasyphevdasllaqsgkdygltmtpadksatfetvtwenv
tflkrffradekypflihpvmpmkeihesirwtkdprntqdhvrslcllawhngeeeynk
flakirsvpigralllpeystlyrrwldsf
>d1quva_ 5.8.1.4.2 RNA-dependent RNA-polymerase {Hepatitis C virus}
smsytwtgalitpcaaeesklpinalsnsllrhhnmvyattsrsaglrqkkvtfdrlqvl
ddhyrdvlkemkakastvkakllsveeackltpphsakskfgygakdvrnlsskavnhih
svwkdlledtvtpidttimaknevfcvqpekggrkparlivfpdlgvrvcekmalydvvs
tlpqvvmgssygfqyspgqrveflvntwkskknpmgfsydtrcfdstvtendirveesiy
qccdlapearqaikslterlyiggpltnskgqncgyrrcrasgvlttscgntltcylkas
aacraaklqdctmlvngddlvvicesagtqedaaslrvfteamtrysappgdppqpeydl
elitscssnvsvahdasgkrvyyltrdpttplaraawetarhtpvnswlgniimyaptlw
armilmthffsillaqeqlekaldcqiygacysiepldlpqiierlhglsafslhsyspg
einrvasclrklgvpplrvwrhrarsvrarllsqggraatcgkylfnwavktklkltpip
aasqldlsgwfvagys
>d1rpl__ 5.9.1.1.2 DNA polymerase beta, catalytic (31 kD) fragment {Rat (Rattus norvegicus)}
ssinfltrvtgigpsaarklvdegiktledlrknedklnhhqriglkyfedfekripree
mlqmqdivlnevkkldpeyiatvcgsfrrgaessgdmdvllthpnftsesskqpkllhrv
veqlqkvrfitdtlskgetkfmgvcqlpsendeneyphrridirlipkdqyycgvlyftg
sdifnknmrahalekgftineytirplgvtgvageplpvdseqdifdyiqwryrepkdrs
e
>d1knya_ 5.9.1.2.1 Kanamycin nucleotidyltransferase (KNTase) {Staphylococcus aureus}
mngpiimtreermkivheikerildkygddvkaigvygslgrqtdgpysdiemmcvmste
eaefshewttgewkvevnfyseeilldyasqvesdwplthgqffsilpiydsggylekvy
qtaksveaqtfhdaicaliveelfeyagkwrnirvqgpttflpsltvqvamagamliglh
hricyttsasvlteavkqsdlpsgydhlcqfvmsgqlsdseklleslenfwngiqewter
hgyivdvskripf
>d1ecl__ 5.10.1.1.1 DNA topoisomerase I, 67K N-terminal domain {Escherichia coli}
gkalvivespakaktinkylgsdyvvkssvghirdltsgsaakksadststktakkpkkp
dergalvnrmgvdpwhnweahyevlpgkekvvselkqlaekadhiylatdldregeaiaw
hlreviggddarysrvvfneitknairqafnkpgelnidrvnaqqarrfmdrvvgymvsp
llwkkiarglsagrvqsvavrlvverereikafvpeefwevdastttpsgealalqvthq
ndkpfrpvnkeqtqaavsllekarysvleredkpttskpgapfitstlqqaastrlgfgv
kktmmmaqrlyeagyitymrtdstnlsqdavnmvrgyisdnfgkkylpespnqyaskgns
qeaheairpsdvnvmaeslkdmeadaqklyqliwrqfvacqmtpakydsttltvgagdfr
lkargrilrfdgwtkvmpalrkgdedrilpavnkgdaltlveltpaqhftkpparfseas
lvkelekrgigrpstyasiistiqdrgyvrvenrrfyaekmgeivtdrleenfrelmnyd
ftaqmensldqvanheaewkavldhffsdftqqldkaekdpeeggmrpn
>d1bjt__ 5.11.1.1.1 DNA topoisomerase II, C-terminal fragment (residues 410-1202) {Baker's yeast (Saccharomyces cerevisiae)}
rksritnypkledankagtkegykctlvltegdsalslavaglavvgrdyygcyplrgkm
lnvreasadqilknaeiqaikkimglqhrkkyedtkslryghlmimtdqdhdgshikgli
inflessflglldiqgfllefitpiikvsitkptkntiafynmpdyekwreeeshkftwk
qkyykglgtslaqevreyfsnldrhlkifhslqgndkdyidlafskkkaddrkewlrqye
pgtvldptlkeipisdfinkelilfsladnirsipnvldgfkpgqrkvlygcfkknlkse
lkvaqlapyvsectayhhgeqslaqtiiglaqnfvgsnniylllpngafgtratggkdaa
aaryiytelnkltrkifhpaddplykyiqedektvepewylpilpmilvngaegigtgws
tyippfnpleiiknirhlmndeeleqmhpwfrgwtgtieeieplryrmygrieqigdnvl
eitelpartwtstikeylllglsgndkikpwikdmeeqhddnikfiitlspeemaktrki
gfyerfklispislmnmvafdphgkikkynsvneilsefyyvrleyyqkrkdhmserlqw
evekysfqvkfikmiiekeltvtnkprnaiiqelenlgfprfnkegkpyygspndeiaeq
indvkgatsdeedeesshedtenvingpeelygtyeyllgmriwsltkeryqkllkqkqe
ketelenllklsakdiwntdlkafevgyqeflqrdaearg
>d1ab4__ 5.11.1.1.2 DNA Gyrase A {Escherichia coli}
vgralpdvrdglkpvhrrvlyamnvlgndwnkaykksarvvgdvigkyhphgdsavydti
vrmaqpfslrymlvdgqgnfgsidgdsaaamryteirlakiahelmadleketvdfvdny
dgtekipdvmptkipnllvngssgiavgmatnipphnltevingclayiddedisieglm
ehipgpdfptaaiingrrgieeayrtgrgkvyiraraevevetiivheipyqvnkarlie
kiaelvkekrvegisalrdesdkdgmriviegevvlnnlysqtqlqvsfginmvalhhgq
pkimnlkdiiaafvrhrrevvtrrtifelrkardrahilealavalanidpiielirhap
tpaeaktalvanpwqlgnvaamledaarpewlepefgvrdglyylteqqaqaildlrlqk
ltgleheklldeykelldqiaellrilgsadrlmevireelelvreqfgdkrrteit
>d1d3ya_ 5.12.1.1.1 DNA topoisomerase IV, alpha subunit {Methanococcus jannaschii}
qakifaqttkmlefakqlletddfstlreayyvsknwgearfddqqasnnviedleaalg
vlrehlgfipeedgssvvgplkiieetpegelvvdctklgtgaynipndvtklnletdad
filaietsgmfarlnaerfwdkhncilvslkgvparatrrfikrlheehdlpvlvftdgd
pygylniyrtlkvgsgkaihladklsipaarligvtpqdiidydlpthplkeqdikrikd
glknddfvrsfpewqkalkqmldmgvraeqqslakyglkyvvntylpekikdestwlp
>d1ois__ 5.13.1.1.2 Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Baker's yeast (Saccharomyces cerevisiae)}
dtikwvtlkhngvifpppyqplpshiklyydgkpvdlppqaeevagffaallesdhaknp
vfqknffndflqvlkesggplngieikefsrcdftkmfdyfqlqkeqkkqltsqekkqir
lerekfeedykfceldgrreqvgnfkveppdlfrgrgahpktgklkrrvnpedivlnlsk
dapvppapeghkwgeirhdntvqwlamwrenifnsfkyvrlaa
>d1daaa_ 5.14.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmilkgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkip
>d1a3ga_ 5.14.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1h2rl_ 5.15.1.1.2 Nickel-iron hydrogenase, large subunit {Desulfovibrio vulgaris}
ssysgpivvdpvtrieghlrievevengkvknayssstlfrgleiilkgrdprdaqhftq
rtcgvctythalastrcvdnavgvhipknatyirnlvlgaqylhdhivhfyhlhaldfvd
vtaalkadpakaakvassisprkttaadlkavqdklktfvetgqlgpftnayflgghpay
yldpetnliatahylealrlqvkaaramavfgaknphtqftvvggvtcydaltpqriaef
ealwketkafvdevyipdllvvaaaykdwtqyggtdnfitfgefpkdeydlnsrffkpgv
vfkrdfknikpfdkmqieehvrhswyegaearhpwkgqtqpkytdlhgddryswmkapry
mgepmetgplaqvliaysqghpkvkavtdavlaklgvgpealfstlgrtaargietavia
eyvgvmlqeykdniakgdnvicapwempkqaegvgfvnaprgglshwiriedgkignfql
vvpstwtlgprcdknnvspveasligtpvadakrpveilrtvhsfdpciacgvh
>d1h2rs_ 5.16.1.1.2 Nickel-iron hydrogenase, small subunit {Desulfovibrio vulgaris}
lmgprrpsvvylhnaectgcsesvlrafepyidtlildtlsldyhetimaaagdaaeaal
eqavnsphgfiavveggiptaangiygkvanhtmldicsrilpkaqaviaygtcatfggv
qaakpnptgakgvndalkhlgvkainiagcppnpynlvgtivyylknkaapeldslnrpt
mffgqtvheqcprlphfdagefapsfeseearkgwclyelgckgpvtmnncpkikfnqtn
wpvdaghpcigcsepdfwdamtpfyqn
>d1cc1s_ 5.16.1.1.3 Nickel-iron hydrogenase, small subunit {Desulfomicrobium baculatum}
kkapviwvqgqgctgcsvsllnavhprikeilldvislefhptvmasegemalahmyeia
ekfngnffllvegaiptakegrycivgetldakahhhevtmmelirdlapkslatvavgt
csayggipaaegnvtgsksvrdffadekiekllvnvpgcpphpdwmvgtlvaawshvlnp
tehplpeldddgrpllffgdnihencpyldkydnsefaetftkpgckaelgckgpstyad
cakrrwnnginwcvenavcigcvepdfpdgkspfyvae
>d1dkza_ 5.17.1.1.1 DnaK {Escherichia coli}
vllldvtplslgietmggvmttliaknttiptkhsqvfstaednqsavsihvlqgerkra
adnkslgqfnldginpaprgmpqievtfdidadgilhvsakdknsgkeqkitikassgln
edeiqkmvrdaeanaeadrkfeelvqtrnqgdhllhstrkqveeagdklpaddktaiesa
ltaletalkgedkaaieakmqelaqvsqklmeiaq
>d1ckra_ 5.17.1.1.2 DnaK {Rat (Rattus norvegicus)}
senvqdlllldvtplslgietaggvmtvlikrnttiptkqtqtfttysdnqpgvliqvye
geramtkdnnllgkfeltgippaprgvpqievtfdidangilnvsavdkstgkenkitit
ndkgrlskediermvqeaekykaedekqrdkvssknsle
>d1zrn__ 5.18.1.1.1 L-2-Haloacid dehalogenase {Pseudomonas}
yikgiafdlygtlfdvhsvvgrcdeafpgrgreisalwrqkqleytwlrslmnryvnfqq
atedalrftcrhlgldldartrstlcdaylrlapfsevpdslrelkrrglklailsngsp
qsidavvshaglrdgfdhllsvdpvqvykpdnrvyelaeqalgldrsailfvasnawdat
garyfgfptcwinrtgnvfeemgqtpdwevtslravvelf
>d1qq5a_ 5.18.1.1.2 L-2-Haloacid dehalogenase {Xanthobacter autotrophicus}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfws
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1dqsa_ 5.19.1.1.1 Dehydroquinate synthase, DHQS {Aspergillus nidulans (Emericella nidulans)}
ptkisilgresiiadfglwrnyvakdlisdcssttyvlvtdtnigsiytpsfeeafrkra
aeitpsprlliynrppgevsksrqtkadiedwmlsqnppcgrdtvvialgggvigdltgf
vastymrgvryvqvpttllamvdssiggktaidtplgknligaiwqptkiyidlefletl
pvrefingmaeviktaaisseeeftaleenaetilkavrrevtpgehrfegteeilkari
lasarhkayvvsaderegglrnllnwghsighaieailtpqilhgecvaigmvkeaelar
hlgilkgvavsrivkclaayglptslkdarirkltagkhcsvdqlmfnmaldkkndgpkk
kivllsaigtpyetrasvvanedirvvl
>d1lci__ 5.20.1.1.1 Luciferase {Firefly (Phontinus pyralis)}
aknikkgpapfypledgtageqlhkamkryalvpgtiaftdahievnityaeyfemsvrl
aeamkryglntnhrivvcsenslqffmpvlgalfigvavapandiynerellnsmnisqp
tvvfvskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfvp
esfdrdktialimnssgstglpkgvalphrtacvrfshardpifgnqiipdtailsvvpf
hhgfgmfttlgylicgfrvvlmyrfeeelflrslqdykiqsallvptlfsffakstlidk
ydlsnlheiasggaplskevgeavakrfhlpgirqgygltettsailitpegddkpgavg
kvvpffeakvvdldtgktlgvnqrgelcvrgpmimsgyvnnpeatnalidkdgwlhsgdi
aywdedehffivdrlkslikykgyqvapaelesillqhpnifdagvaglpdddagelpaa
vvvlehgktmtekeivdyvasqvttakklrggvvfvdevpkgltgkldarkireilikak
k
>d1amua_ 5.20.1.1.2 Phenylalanine activating domain of gramicidin synthetase 1 {Bacillus brevis}
gtheeeqylfavnntkaeyprdktihqlfeeqvskrpnnvaivceneqltyhelnvkanq
larifiekgigkdtlvgimmeksidlfigilavlkaggayvpidieypkeriqyilddsq
armlltqkhlvhlihniqfngqveifeedtikiregtnlhvpskstdlayviytsgttgn
pkgtmlehkgisnlkvffenslnvtekdrigqfasisfdasvwemfmalltgaslyiilk
dtindfvkfeqyinqkeitvitlpptyvvhldperilsiqtlitagsatspslvnkwkek
vtyinaygptetticattwvatketighsvpigapiqntqiyivdenlqlksvgeagelc
iggeglargywkrpeltsqkfvdnpfvpgeklyktgdqarwlsdgnieylgridnqvkir
ghrveleevesillkhmyisetavsvhkdhqeqpylcayfvsekhipleqlrqfsseelp
tymipsyfiqldkmpltsngkidrkqlpepdltf
>d1ad2__ 5.21.1.1.1 Ribosomal protein L1 {Thermus thermophilus}
kryrallekvdpnkiytideaahlvkelatakfdetvevhaklgidprrsdqnvrgtvsl
phglgkqvrvlaiakgekikeaeeagadyvggeeiiqkildgwmdfdavvatpdvmgavg
sklgrilgprgllpnpkagtvgfnigeiireikagriefrndktgaihapvgkacfppek
ladnirafiraleahkpegakgtflrsvyvtttmgpsvrinphs
>d1dt9a_ 5.22.1.1.1 Eukaryotic peptide chain release factor subunit 1, ERF1 {Human (Homo sapiens)}
psaadrnveiwkikkliksleaargngtsmisliippkdqisrvakmladefgtasniks
rvnrlsvlgaitsvqqrlklynkvppnglvvycgtivteegkekkvnidfepfkpintsl
ylcdnkfhtealtallsddskfgfividgsgalfgtlqgntrevlhkftvdlpkkhgrgg
qsalrfarlrmekrhnyvrkvaetavqlfisgdkvnvaglvlagsadfktelsqsdmfdq
rlqskvlklvdisyggengfnqaielstevlsnvkfiqekkligryfdeisqdtgkycfg
vedtlkalemgaveilivyenldimryvlhcqgteeekilyltpeqekdkshftdketgq
eheliesmpllewfannykkfgatleivtdksqegsqfvkgfggiggilryrvdfqgm
>d2btva_ 5.23.1.1.1 BTV inner layer core protein vp3 {Bluetongue virus, strain 1}
vdftvpdvqqilddikalaaeqvykivkvpstsfrhivtqsrdrvlrvdtyyeemsqvgd
vitedepekfystiikkvrfirgkgsfilhdipardhrgmevaepevlgvefknvlpvlt
aehramiqnaldgsiiengnvatrdvdvfigacsepiyriynrlqgyieavqlqelrnsi
gwlerlgqrkritysqevltdfrrqdmiwvlalqlpvnpqvvwdvprssianlimniatc
lptgeyiapnprissitltqritttgpfailtgstptaqqlndvrkiylalmfpgqiild
lkidpgermdpavrmvagvvghllftaggrftnltqnmarqldialndyllymyntrvqv
nygptgepldfqigrnqydcnvfradfatgtgyngwatidveyrdpapyvhaqryirycg
idsrelinpttygigmtyhcynemlrmlvaagkdseaayfrsmlpfhmvrfarinqiine
dlhsvfslpddmfnallpdliagahqnadpvvldvswislwfafnrsfepthrnemleia
pliesvyaselsvmkvdmrhlslmqrrfpdvliqarpshfwkavlndspeavkavmnlsh
shnfinirdmmrwvllpslqpslklvleeeawaaandfedlmltdqvymhrdmlpeprld
dierfrqegfyytnmleappeidrvvqytyeiarlqanmgqfraalrrimddddwvrfgg
vlrtvrvkffdarppddilqglpfsydtnekgglsyatikyatettifyliynvefsntp
dslvlinptytmtkvfinkrivervrvgqilavlnrrfvaykgkmrimditqslkmgtkl
aaptv
>d1cola_ 6.1.1.1.1 Colicin A {Escherichia coli}
akderellektseliagmgdkigehlgdkykaiakdiadniknfqgktirsfddamasln
kitanpamkinkadrdalvnawkhvdaqdmanklgnlskafkvadvvmkvekvreksieg
yetgnwgplmleveswvlsgiassvalgifsatlgayalslgvpaiavgiagillaavvg
aliddkfadalnneiir
>d1cii_1 6.1.1.1.3 (451-624) Colicin Ia {Escherichia coli}
dainftteflksvsekygakaeqlaremagqakgkkirnveealktyekyradinkkina
kdraaiaaalesvklsdissnlnrfsrglgyagkftsladwitefgkavrtenwrplfvk
tetiiagnaatalvalvfsiltgsalgiigygllmavtgalideslvekankfw
>d1ddt_3 6.1.2.1.1 (200-380) Diphtheria toxin, middle domain {Corynebacterium diphtheriae}
scinldwdvirdktktkieslkehgpiknkmsespnktvseekakqyleefhqtalehpe
lselktvtgtnpvfaganyaawavnvaqvidsetadnlekttaalsilpgigsvmgiadg
avhhnteeivaqsialsslmvaqaiplvgelvdigfaaynfvesiinlfqvvhnsynrpa
y
>d1dlc_3 6.1.3.1.1 (61-289) delta-Endotoxin (insectocide), N-terminal domain {Bacillus thuringiensis tenebrionis, CRYIIIA (BT13)}
ttkdviqkgisvvgdllgvvgfpfggalvsfytnflntiwpsedpwkafmeqvealmdqk
iadyaknkalaelqglqnnvedyvsalsswqknpvssrnphsqgrirelfsqaeshfrns
mpsfaisgyevlflttyaqaanthlfllkdaqiygeewgyekediaefykrqlkltqeyt
dhcvkwynvgldklrgssyeswvnfnryrremtltvldlialfplydvr
>d1ciy_3 6.1.3.1.2 (33-255) delta-Endotoxin (insectocide), N-terminal domain {Bacillus thuringiensis, CRYIA (A)}
ytpidislsltqfllsefvpgagfvlglvdiiwgifgpsqwdaflvqieqlinqrieefa
rnqaisrleglsnlyqiyaesfreweadptnpalreemriqfndmnsalttaipllavqn
yqvpllsvyvqaanlhlsvlrdvsvfgqrwgfdaatinsryndltrlignytdyavrwyn
tglervwgpdsrdwvrynqfrreltltvldivalfsnydsrry
>d1maz__ 6.1.4.1.1 Apoptosis regulator Bcl-xL {Human (Homo sapiens)}
msqsnrelvvdflsyklsqkgyswsqfsdveenrteapegtesemetpsaingnpswhla
dspavngatghsssldarevipmaavkqalreagdefelryrrafsdltsqlhitpgtay
qsfeqvvnelfrdgvnwgrivaffsfggalcvesvdkemqvlvsriaawmatylndhlep
wiqenggwdtfvelyg
>d1ddba_ 6.1.4.1.4 Proapoptotic molecule BID {Mouse (Mus musculus)}
mdsevsngsglgakhitdllvfgflqssgctrqelevlgrelpvqayweadledelqtdg
sqasrsfnqgriepdsesqeeiihniarhlaqigdemdhniqptlvrqlaaqfmngslse
edkrnclakaldevktafprdmendkamlimtmllakkvashapsllrdvfhttvnfinq
nlfsyvrnlvrnemd
>d1c3wa_ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
tgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgy
gltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglv
galtkvysyrfvwwaistaamlyilyvlffgfsmrpevastfkvlrnvtvvlwsaypvvw
ligsegagivplnietllfmvldvsakvgfglillrsraifg
>d1prch2 6.2.1.1.3 (1-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
myhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d2prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d3prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d4prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d5prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d6prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d7prch2 6.2.1.1.3 (2-36) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter viridis}
yhgalaqhldiaqlvwyaqwlviwtvvllylrred
>d1aigh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aigp2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aijh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aijt2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1mpsh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1pcrh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1pssh2 6.2.1.1.4 (12-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
laslaiysfwiflagliyylqten
>d1psth2 6.2.1.1.4 (12-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
laslaiysfwiflagliyylqten
>d1qovh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1qovl1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1qovm1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
aeyqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlsl
fsglmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasf
fmfvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygif
shldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiad
rgtaaeraalfwrwtmgfnwtmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqn
hg
>d1ysth2 6.2.1.1.4 (1-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
mvgvtafgnfdlaslaiysfwiflagliyylqten
>d2rcrh2 6.2.1.1.4 (1-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
mvgvtafgnfdlaslaiysfwiflagliyylqten
>d4rcrh2 6.2.1.1.4 (12-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
laslaiysfwiflagliyylqten
>d1occb2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1occg1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1occi1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1occj1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1occk1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1occl1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1occm1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1occo2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1occt1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1occv1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1occw1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1occx1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1occy1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1occz1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1ocob2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1ocog1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1ocoi1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1ocoj1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1ocok1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1ocol1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1ocom1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1ocoo2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1ocot1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1ocov1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1ocow1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1ocox1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1ocoy1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1ocoz1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1ocrb2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1ocrg1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1ocri1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1ocrj1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfphk
>d1ocrk1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1ocrl1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1ocrm1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1ocro2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1ocrt1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1ocrv1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1ocrw1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfphk
>d1ocrx1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1ocry1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1ocrz1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1oczb2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1oczg1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1oczi1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1oczj1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1oczk1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1oczl1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1oczm1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1oczo2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d1oczt1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d1oczv1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d1oczw1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfp
>d1oczx1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d1oczy1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d1oczz1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d2occa1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
mfinrwlfstnhkdigtlyllfgawagmvgtalslliraelgqpgtllgddqiynvvvta
hafvmiffmvmpimiggfgnwlvplmigapdmafprmnnmsfwllppsfllllassmvea
gagtgwtvypplagnlahagasvdltifslhlagvssilgainfittiinmkppamsqyq
tplfvwsvmitavllllslpvlaagitmlltdrnlnttffdpagggdpilyqhlfwffgh
pevyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwahhmftvgmdvd
trayftsatmiiaiptgvkvfswlatlhggnikwspammwalgfiflftvggltgivlan
ssldivlhdtyyvvahfhyvlsmgavfaimggfvhwfplfsgytlndtwakihfaimfvg
vnmtffpqhflglsgmprrysdypdaytmwntissmgsfisltavmlmvfiiweafaskr
evltvdltttnlewlngcpppyhtfeeptyvnlk
>d2occb2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d2occc1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
mthqthayhmvnpspwpltgalsallmtsgltmwfhfnsmtllmiglttnmltmyqwwrd
virestfqghhtpavqkglrygmilfiisevlfftgffwafyhsslaptpelggcwpptg
ihplnplevpllntsvllasgvsitwahhslmegdrkhmlqalfititlgvyftllqase
yyeapftisdgvygstffvatgfhglhviigstflivcffrqlkfhftsnhhfgfeagaw
ywhfvdvvwlflyvsiywwgs
>d2occd1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
svvksedyalpsyvdrrdyplpdvahvknlsasqkalkekekaswsslsidekvelyrlk
fkesfaemnrstnewktvvgaamffigftallliwekhyvygpiphtfeeewvakqtkrm
ldmkvapiqgfsakwdydknewkk
>d2occg1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d2occi1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d2occj1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfphk
>d2occk1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d2occl1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d2occm1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d2occo2 6.2.1.1.5 (1-90) Cytochrome c oxidase {Bovine (Bos taurus)}
maypmqlgfqdatspimeellhfhdhtlmivflisslvlyiislmlttklthtstmdaqe
vetiwtilpaiililialpslrilymmdei
>d2occt1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
asaakgdhggtgartwrfltfglalpsvalctlnswlhsghrerpafipyhhlrirtkpf
swgdgnhtffhnprvnplptgyek
>d2occv1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
stalakpqmrgllarrlrfhivgafmvslgfatfykfavaekrkkayadfyrnydsmkdf
eemrkagifqsak
>d2occw1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
fenrvaekqklfqednglpvhlkggatdnilyrvtmtlclggtlyslyclgwasfphk
>d2occx1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
apdfhdkygnavlasgatfcvavwvymatqigiewnpspvgrvtpkewr
>d2occy1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
shyeegpgknipfsvenkwrllammtlffgsgfaapffivrhqllkk
>d2occz1 6.2.1.1.5 Cytochrome c oxidase {Bovine (Bos taurus)}
itakpaktptspkeqaiglsvtflsfllpagwvlyhldnykks
>d1ar1b2 6.2.1.1.6 (1-107) Cytochrome c oxidase {Paracoccus denitrificans}
qdvlgdlpvigkpvnggmnfqpassplahdqqwldhfvlyiitavtifvcllllicivrf
nrranpvparfthntpieviwtlvpvlilvaigafslpilfrsqemp
>d1qled1 6.2.1.1.6 Cytochrome c oxidase {Paracoccus denitrificans}
tdhkhgemdirhqqatfagfikgatwvsilsiavlvflalans
>d1a91__ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c0va_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17a_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17b_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17c_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17d_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17e_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17f_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17g_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17h_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17i_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17j_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17k_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17l_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c99a_ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1c17m_ 6.2.1.1.8 Subunit A of the F1F0 ATP synthase {Escherichia coli}
hgkskliaplaltifvwvflmnlmdllpidllpyiaehvlglpalrvvpsadvnvtlsma
lgvfililfysikmkgiggftkeltlqpfnhwafipvnlilegvsllskpvslglrlfgn
myagelifiliagllpwwsqwilnvpwaifhiliitlqafifmvltivyls
>d1bl8a_ 6.2.1.1.9 Potassium chanel protein {Streptomyces lividans}
alhwraagaatvllvivllagsylavlaergapgaqlitypralwwsvetattvgygdly
pvtlwgrcvavvvmvagitsfglvtaalatwfvgreq
>d1be3e2 6.2.1.1.10 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1be3g1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1be3h1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1be3j1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1be3k1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bgye1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvlamskie
>d1bgyg1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyh1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyj1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyk1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bgyq2 6.2.1.1.10 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1bgys1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyt1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyv1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyw1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1qcrd1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
evlefddgtpatmsqvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhk
wsvlksrklayrppk
>d1qcre2 6.2.1.1.10 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1qcrg1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefeksk
>d1qcrh1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
ttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklfnsl
>d1qcrj1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
tltarlysllfrrtstfaltivvgalfferafdngadaiyehinegklwkhikhkyenk
>d1qcrk1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mltrflgpryrqlarnwvptaqlwgavgavglvsatdsrlildwv
>d1bccc1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
apnirkshpllkminnslidlpapsnisawwnfgsllavclmtqiltglllamhytadts
lafssvahtcrnvqygwlirnlhangasffficiflhigrglyygsylyketwntgvill
ltlmatafvgyvlpwgqmsfwgatvitnlfsaipyightlvewawggfsvdnptltrffa
lhfllpfaiagitiihltflhesgsnnplgissdsdkipfhpyysfkdilgltlmltpfl
tlalfspnllgdpenftpanplvtpphikpewyflfayailrsipnklggvlalaasvli
lflipflhkskqrtmtfrplsqtlfwllvanlliltwigsqpvehpfiiigqmaslsyft
illilfptigtlenkmlny
>d1bccd1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
sdlelhppsypwshrgplssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvsvreglyfnpyfpgqaigmappiyndvlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmgllvplvyymkrhkwsvlksrklayrpp
k
>d1bcce2 6.2.1.1.11 (1-69) Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
shtdikvpnfsdyrrppddystkssresdpsrkgfsylvtavttlgvayaaknvvtqfvs
smsasadvl
>d1bccf1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
srwlegirkwyynaagfnkyglmrddtiyenddvkeairrlpenlyddrmfrikraldln
mrqqilpkeqwtkyeedvpylepylkevirerkereewdk
>d1bccg1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
rqfghltrvrhlityslspfeqrpfphyfskgvpnvwrrlracilrvappflafyllytw
gtqefekskrknpaayvn
>d1bcch1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
lvdplttvreqceqlekcvkarerlelcdervssrsqteedcteelfdflhardhcvahk
lfnslk
>d1bccj1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
tltarlysllfrrtstfaltivvgallferafdqgadaiyehinegklwkhikhkyenk
>d2bcce2 6.2.1.1.11 (1-69) Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
shtdikvpnfsdyrrppddystkssresdpsrkgfsylvtavttlgvayaaknvvtqfvs
smsasadvl
>d2bccg1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
rqfghltrvrhlityslspfeqrpfphyfskgvpnvwrrlracilrvappflafyllytw
gtqefekskrknpaayvn
>d2bcch1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
lvdplttvreqceqlekcvkarerlelcdervssrsqteedcteelfdflhardhcvahk
lfnslk
>d2bccj1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
tltarlysllfrrtstfaltivvgallferafdqgadaiyehinegklwkhikhkyenk
>d3bcce2 6.2.1.1.11 (1-69) Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
shtdikvpnfsdyrrppddystkssresdpsrkgfsylvtavttlgvayaaknvvtqfvs
smsasadvl
>d3bccg1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
rqfghltrvrhlityslspfeqrpfphyfskgvpnvwrrlracilrvappflafyllytw
gtqefekskrknpaayvn
>d3bcch1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
lvdplttvreqceqlekcvkarerlelcdervssrsqteedcteelfdflhardhcvahk
lfnslk
>d3bccj1 6.2.1.1.11 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
tltarlysllfrrtstfaltivvgallferafdqgadaiyehinegklwkhikhkyenk
>d1fumc_ 6.2.1.1.12 Fumarate reductase respiratory complex transmembrane subunits {Escherichia coli}
ttkrkpyvrpmtstwwkklpfyrfymlregtavpavwfsielifglfalkngpeawagfv
dflqnpviviinlitlaaallhtktwfelapkaaniivkdekmgpepiikslwavtvvat
ivilfvalyw
>d1fumd_ 6.2.1.1.12 Fumarate reductase respiratory complex transmembrane subunits {Escherichia coli}
inpnpkrsdepvfwglfgaggmwsaiiapvmillvgillplglfpgdalsyervlafaqs
figrvflflmivlplwcglhrmhhamhdlkihvpagkwvfyglaailtvvtligvvti
>d1qlac_ 6.2.1.1.13 Fumarate reductase respiratory complex transmembrane subunits {Wolinella succinogenes}
mtnesilesysgvtperkksrmpakldwwqsatglflglfmighmffvstillgdnvmlw
vtkkfeldfifeggkpivvsflaafvfavfiahaflamrkfpinyrqyltfkthkdlmrh
gdttlwwiqamtgfamfflgsvhlyimmtqpqtigpvsssfrmvsewmwplylvllfave
lhgsvglyrlavkwgwfdgetpdktranlkklktlmsaflivlglltfgayvkkgleqtd
pnidykyfdykrth
>d1msla_ 6.2.1.1.14 Gated mechanosensitive channel {Mycobacterium tuberculosis}
argnivdlavavvigtaftalvtkftdsiitplinrigvnaqsdvgilrigigggqtidl
nvllsaainffliafavyflvvlpyntlrkkgeveqpgdtqvvllteir
>d1kzua_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzub_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1kzud_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzue_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1kzug_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
nqgkiwtvvnpaigipallgsvtviailvhlailshttwfpaywqggv
>d1kzuh_ 6.3.1.1.1 Light-harvesting complex LH2 {Purple bacterium (Rhodopseudomonas acidophila)}
atltaeqseelhkyvidgtrvflglalvahflafsatpwlh
>d1lgha_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghb_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghd_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghe_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghg_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghh_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1lghj_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
snpkddykiwlvinpstwlpviwivatvvaiavhaavlaapgfnwialgaaksaak
>d1lghk_ 6.3.1.1.2 Light-harvesting complex LH2 {Rhodospirillum molischianum}
rslsglteeeaiavhdqfkttfsafiilaavahvlvwvwkpwf
>d1bxwa_ 6.4.1.1.1 Outer membrane protein A (OMPA) transmembrane domain {Escherichia coli}
mapkdntwytgaklgwsqyhdtglinnngpthenklgagafggyqvnpyvgfemgydwlg
rmpykgsvengaykaqgvqltaklgypitddldiytrlggmvwradtysnvygknhdtgv
spvfaggveyaitpeiatrleyqwtnnigdahtigtrpdngmlslgvsyrfg
>d1qj8a_ 6.4.1.1.2 Outer membrane protein X (OMPX) {(Escherichia coli)}
atstvtggyaqsdaqgqmnkmggfnlkyryeednsplgvigsftyteksrtassgdynkn
qyygitagpayrindwasiygvvgvgygkfqtteyptykndtsdygfsygaglqfnpmen
valdfsyeqsrirsvdvgtwiagvgyrf
>e1qd6.1c 6.4.2.1.1 Outer membrane phospholipase A (OMPLA) {(Escherichia coli)}
ftlypydtnyliytqtsdlnkeaiasydwaenarkdevkfqlslafplwrgilgpnsvlg
asytqkswwqlsnseesspfretnyepqlflgfatdyrfagwtlrdvemgynhdsngrsd
ptsrswnrlytrlmaengnwlvevkpwyvvgntddnpditkymgyyqlkigyhlgdavls
akgqynwntgyggaelglsypitkhvrlytqvysgygeslidynfnqtrvgvgvmlndlf
>d2omf__ 6.4.3.1.1 Porin {Escherichia coli, different sequences}
aeiynkdgnkvdlygkavglhyfskgngensyggngdmtyarlgfkgetqinsdltgygq
weynfqgnnsegadaqtgnktrlafaglkyadvgsfdygrnygvvydalgytdmlpefgg
dtaysddffvgrvggvatyrnsnffglvdglnfavqylgknerdtarrsngdgvggsisy
eyegfgivgaygaadrtnlqeaqplgngkkaeqwatglkydanniylaanygetrnatpi
tnkftntsgfanktqdvllvaqyqfdfglrpsiaytkskakdvegigdvdlvnyfevgat
yyfnknmstyvdyiinqidsdnklgvgsddtvavgivyqf
>d2por__ 6.4.3.1.2 Porin {Rhodobacter capsulatus}
evklsgdarmgvmyngddwnfssrsrvlftmsgttdsglefgasfkahesvgaetgedgt
vflsgafgkiemgdalgasealfgdlyevgytdlddrggndipyltgderltaednpvll
ytysagafsvaasmsdgkvgetseddaqemavaaaytfgnytvglgyekidspdtalmad
meqlelaaiakfgatnvkayyadgeldrdfaravfdltpvaaaatavdhkayglsvdstf
gattvggyvqvldidtiddvtyyglgasydlgggasivggiadndlpnsdmvadlgvkfk
f
>d3prn__ 6.4.3.1.3 Porin {Rhodopseudomonas blastica, strain DSM2131}
mislngygrfglqyvedrgvgledtiissrlrinivgttetdqgvtfgaklrmqwddgda
fagtagnaaqfwtsyngvtvsvgnvdtafdsvaltydsemgyewssfgdaqssffaynsk
ydasgaldnyngiavtysisgvnlylsyvdpdqtvdsslvteefgiaadwsndmislaaa
yttdaggivdndiafvgaaykfndagtvglnwydnglstagdqvtlygnyafgattvray
vsdidragadtaygigadyqfaegvkvsgsvqsgfanetvadvgvrfdf
>d2mpra_ 6.4.3.2.2 Maltoporin (also LamB protein) {Salmonella typhimurium}
vdfhgyarsgigwtgsggeqqcfqatgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvnqqndwestdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgagienidlgfgklslaatrsteaggsytfssqniydevkdtandvfdvrlaglq
tnpdgvlelgvdygranttdgykladgaskdgwmftaehtqsmlkgynkfvvqyatdamt
tqgkgqargsdgsssftekinyankvinnngnmwrildhgaislgdkwdlmyvgmyqnid
wdnnlgtewwtvgvrpmykwtpimstllevgydnvksqqtgdrnnqykitlaqqwqagds
iwsrpairifatyakwdekwgyikdgdnisryaaatnsgistnsrgdsdewtfgaqmeiw
w
>d1a0tp_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1by5a_ 6.4.3.3.1 Ferric hydroxamate uptake receptor FhuA {Escherichia coli}
qesawgpaatiaarqsatgtktdtpiqkvpqsisvvtaeemalhqpksvkealsytpgvs
vgtrgasntydhliirgfaaegqsqnnylnglklqgnfyndavidpymleraeimrgpvs
vlygksspggllnmvskrptteplkevqfkagtdslfqtgfdfsdsldddgvysyrltgl
arsanaqqkgseeqryaiapaftwrpddktnftflsyfqnepetgyygwlpkegtveplp
ngkrlptdfnegaknntysrnekmvgysfdhefndtftvrqnlrfaenktsqnsvygygv
csdpanayskqcaalapadkghylarkyvvddeklqnfsvdtqlqskfatgdidhtlltg
vdfmrmrndinawfgyddsvpllnlynpvntdfdfnakdpansgpyrilnkqkqtgvyvq
dqaqwdkvlvtlggrydwadqeslnrvagttdkrddkqftwrggvnylfdngvtpyfsys
esfepssqvgkdgnifapskgkqyevgvkyvpedrpivvtgavynltktnnlmadpegsf
fsveggeirargveieakrplsasvnvvgsytytdaeyttdttykgntpaqvpkhmaslw
adytffdgplsgltlgtggrytgssygdpansfkvgsytvvdalvrydlarvgmagsnva
lhvnnlfdreyvascfntygcfwgaerqvvatatfrf
>d1fepa_ 6.4.3.3.2 Ferric enterobactin receptor FepA {Escherichia coli}
ddtivvtaaeqnlqapgvstitadeirknpvardvskiirtxpgvnltgnstsgqrgnnr
qidirgxgpentlilidgkpvssrnsvrqgwrgerdtrgdtswvppexierievlrgpaa
arygngaaggvvniitkkgsgewhgswdayfnapehkeegatkrtnfsltgplgdefsfr
lygnldktqadawdinqghqsaragtyattlpagregvinkdingvvrwdfaplqslele
agysrqgnlyagdtqntnsdsytrskygdetnrlyrqnyaltwnggwdngvttsnwvqye
htrnsripeglaggtegkfnekatqdfvdidlddvxlhsevnlpidflvnqtltlgtewn
qqrxkdlssntqaltgtntggaidgvsttdrspyskaeifslfaennxeltdstivtpgl
rfdhhsivgnnwspalnisqglgddftlkxgiaraykapslyqtnpnyilyskgqgcyas
aggcylqgnddlkaetsinkeiglefkrdgwlagvtwfrndyrnkieagyvavgqnavgt
dlyqwdnvpkavveglegslnvpvsetvxwtnnityxlksenkttgdrlsiipeytlnst
lswqaredlsxqttftwygkqqpkkynykgqpavgpetkeispysivglsatwdvtknvs
ltggvdnlfdkrlwragnaqttgdlaganyiagagaytynepgrtwyxsvnthf
>d7ahla_ 6.5.1.1.1 Alpha-hemolysin {Staphylococcus aureus}
adsdiniktgttdigsnttvktgdlvtydkengmhkkvfysfiddknhnkkllvirtkgt
iagqyrvyseeganksglawpsafkvqlqlpdnevaqisdyyprnsidtkeymstltygf
ngnvtgddtgkiggliganvsightlkyvqpdfktilesptdkkvgwkvifnnmvnqnwg
pydrdswnpvygnqlfmktrngsmkaadnfldpnkassllssgfspdfatvitmdrkask
qqtnidviyervrddyqlhwtstnwkgtntkdkwtdrsserykidwekeemtn
>d3lkfa_ 6.5.1.1.3 Leukocidin F (HlgB) {Staphylococcus aureus}
egkitpvsvkkvddkvtlykttatadsdkfkisqiltfnfikdksydkdtlvlkatgnin
sgfvkpnpndydfsklywgakynvsissqsndsvnvvdyapknqneefqvqntlgytfgg
disisnglsgglngntafsetinykqesyrttlsrntnyknvgwgveahkimnngwgpyg
rdsfhptygnelflagrqssayagqnfiaqhqmpllsrsnfnpeflsvlshrqdgakksk
itvtyqremdlyqirwngfywaganyknfktrtfkstyeidwenhkvklldtketennk
>d1prea2 6.7.1.1.1 (85-470) (Pro)aerolysin, pore-forming lobe {Aeromonas hydrophila}
iptlsaldipdgdevdvqwrlvhdsanfikptsylahylgyawvggnhsqyvgedmdvtr
dgdgwvirgnndggcdgyrcgdktaikvsnfaynldpdsfkhgdvtqsdrqlvktvvgwa
vndsdtpqsgydvtlrydtatnwsktntyglsekvttknkfkwplvgetelsieiaanqs
wasqnggstttslsqsvrptvparskipvkielykadisypyefkadvsydltlsgflrw
ggnawythpdnrpnwnhtfvigpykdkassiryqwdkryipgevkwwdwnwtiqqnglst
mqnnlarvlrpvragitgdfsaesqfagnieigapvplaadskvrrarsvdgagqglrle
ipldaqelsglgfnnvslsvtpaanq
>d1pfo__ 6.8.1.1.1 Perfringolysin {Clostridium perfringens}
ditdknqsidsgisslsynrnevlasngdkiesfvpkegkkagnkfivverqkrslttsp
vdisiidsvndrtypgalqladkalvenrptilmvkrkpininidlpglkgensikvddp
tygkvsgaidelvskwnekyssthtlpartqysesmvysksqissalnvnakvlenslgv
dfnavannekkvmilaykqifytvsadlpknpsdlfddsvtfndlkqkgvsneapplmvs
nvaygrtiyvklettssskdvqaafkalikntdiknsqqykdiyenssftavvlggdaqe
hnkvvtkdfdeirkvikdnatfstknpaypisytsvflkdnsvaavhnktdyiettstey
skgkinldhsgayvaqfevawdevsydkegnevlthktwdgnyqdktahystvipleana
rnirikarectglawewwrdviseydvpltnninvsiwgttlypgssityn
>d1svb_2 6.9.1.1.1 (1-302) Envelope glycoprotein, central and dimerisation domains {Tick-borne encephalitis virus, TBE}
srcthlenrdfvtgtqgttrvtlvlelggcvtitaegkpsmdvwldaiyqenpaktreyc
lhaklsdtkvaarcptmgpatlaeehqggtvckrdqsdrgwgnhcglfgkgsivacvkaa
ceakkkatghvydankivytvkvephtgdyvaanethsgrktasftissektiltmgeyg
dvsllcrvasgvdlaqtvileldktvehlptawqvhrdwfndlalpwkhegaqnwnnaer
lvefgaphavkmdvynlgdqtgvllkalagvpvahiegtkyhlksghvtcevgleklkmk
gl
>d1acc__ 6.10.1.1.1 Anthrax protective antigen {Anthrax bacillus (Bacillus anthracis)}
sssqgllgyyfsdlnfqapmvvtssttgdlsipsselenipsenqyfqsaiwsgfikvkk
sdeytfatsadnhvtmwvddqevinkasnsnkirlekgrlyqikiqyqrenptekgldfk
lywtdsqnkkevissdnlqlpelkqkssnsrkkrstsagptvpdrdndgipdslevegyt
vdvknkrtflspwisnihekkgltkyksspekwstasdpysdfekvtgridknvspearh
plvaaypivhvdmeniilsknedqstqntdsetrtiskntstsrthtsevhgnaevhasf
fdiggsvsagfsnsnsstvaidhslslagertwaetmglntadtarlnaniryvntgtap
iynvlpttslvlgknqtlatikakenqlsqilapnnyypsknlapialnaqddfsstpit
mnynqflelektkqlrldtdqvygniatynfengrvrvdtgsnwsevlpqiqettariif
ngkdlnlverriaavnpsdplettkpdmtlkealkiafgfnepngnlqyqgkditefdfn
fdqqtsqniknqlaelnatniytvldkiklnakmnilirdkrfhydrnniavgadesvvk
eahrevinssteglllnidkdirkilsgyiveiedteglkevindrydmlnisslrqdgk
tfidfkkyndklplyisnpnykvnvyavtkentiinpsengdtstngikkilifskkgye
ig
>e1aph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1aph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>e1bph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1bph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>e1cph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1cph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>e1dph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1dph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>e1pid.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1pid.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergff
>e1pid.2c 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1pid.2d 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergff
>e2ins.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e2ins.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
vnqhlcgshlvealylvcgergffytpka
>e2ins.2c 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e2ins.2d 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
vnqhlcgshlvealylvcgergffytpka
>d1sju__ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgsdlvealylvcgergffytdkgiveqcctsicslyqlenycn
>d1zeia_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>d1zeib_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>d1zeic_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>d1zeid_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>d1zeie_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>d1zeif_ 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkaakgiveqcctsicslyqlenycn
>e1a7f.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1a7f.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealelvcgerggfytpk
>e1ai0.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ai0.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ai0.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1aiy.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1aiy.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1b9e.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1b9e.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgehlvealylvcgergffytpkt
>e1b9e.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1b9e.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgehlvealylvcgergffytpkt
>e1ben.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ben.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1ben.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1ben.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytp
>e1bzv.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1bzv.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergff
>e1hiq.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hiq.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergsfytpkt
>e1his.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1his.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergff
>e1hit.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hit.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgerggfytpkt
>e1hls.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hls.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealhlvcgergffytpkt
>e1hui.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1hui.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
evnqhlcgselvealelvcgergffyepk
>e1iog.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
gigeqcctsicslyqlenycn
>e1iog.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
evnqhlcgselvealelvcgergffyepk
>e1ioh.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcchsicslyqlenycn
>e1ioh.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
evnqhlcgselvealelvcgergffyepk
>e1lph.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1lph.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytkpt
>e1lph.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1lph.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytkpt
>e1mhi.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1mhi.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgdhlvealylvcgergffytpkt
>e1mhj.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1mhj.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergfytpkt
>e1qiy.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiy.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiy.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiy.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiy.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiy.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiy.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qiz.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qiz.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1qj0.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qj0.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
vnqylcgshlvealylvcgergffytpk
>e1qj0.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1qj0.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqylcgshlvealylvcgergffytpkt
>e1sjt.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1sjt.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgsdlvealylvcgergffytdk
>e1trz.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1trz.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1trz.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1trz.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1tyl.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1tyl.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1tyl.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1tyl.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
nqhlcgshlvealylvcgergffytpkt
>e1tym.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1tym.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1tym.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1tym.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
nqhlcgshlvealylvcgergffytpkt
>e1vks.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1vks.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgsdlvealylvcgergffytkpt
>e1vkt.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqsctsisslyqlenycn
>e1vkt.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgsdlvealylvcgergffytkpt
>e1xda.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1xda.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1xda.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1xda.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1xda.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1xda.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1xda.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1xda.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1xgl.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1xgl.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1zeg.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1zeg.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkt
>e1zeg.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1zeg.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkt
>e1zeh.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1zeh.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkt
>e1zeh.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1zeh.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytdkt
>e1znj.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1znj.2c 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.2d 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1znj.3e 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.3f 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1znj.4g 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.4h 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpk
>e1znj.5i 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.5j 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1znj.6k 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1znj.6l 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e2hiu.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e2hiu.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealylvcgergffytpkt
>e1dei.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1dei.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgerg
>e1dei.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1dei.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgerg
>e1iza.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1iza.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1iza.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1iza.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1izb.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1izb.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1izb.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1izb.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvqalylvcgergffytpkt
>e1mpj.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1mpj.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
vnqhlcgshlvealylvcgergffytpk
>e1mpj.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1mpj.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1sdb.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1sdb.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
nqhlcgshlvealylvcgergff
>e1wav.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1wav.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1wav.3e 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.3f 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1wav.4g 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.4h 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1wav.5i 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.5j 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1wav.6k 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1wav.6l 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1zni.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1zni.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e1zni.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e1zni.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e2tci.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e2tci.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
vnqhlcgshlvealylvcgergffytpk
>e2tci.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e2tci.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e3ins.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e3ins.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e3ins.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e3ins.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e3mth.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e3mth.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
vnqhlcgshlvealylvcgergffytpk
>e3mth.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e3mth.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e4ins.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e4ins.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e4ins.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e4ins.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e6ins.1e 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpkgiveqcctsicslyqlenycn
>e6ins.1f 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpkgiveqcctsicslyqlenycn
>e7ins.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e7ins.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e7ins.2c 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e7ins.2d 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e7ins.3e 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e7ins.3f 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e9ins.1a 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
giveqcctsicslyqlenycn
>e9ins.1b 7.1.1.1.3 Insulin {Pig (Sus scrofa)}
fvnqhlcgshlvealylvcgergffytpka
>e6rlx.1a 7.1.1.1.4 Relaxin {Human (Homo sapiens)}
xlysalankcchvgctkrslarfc
>e6rlx.1b 7.1.1.1.4 Relaxin {Human (Homo sapiens)}
swmeeviklcgrelvraqiaicgmstw
>e6rlx.2c 7.1.1.1.4 Relaxin {Human (Homo sapiens)}
xlysalankcchvgctkrslarfc
>e6rlx.2d 7.1.1.1.4 Relaxin {Human (Homo sapiens)}
swmeeviklcgrelvraqiaicgms
>d1b9ga_ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkpgivdeccfrscdlrrlemycaplkpaksa
>d1bqt__ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkptgygsssrrapqtgivdeccfrscdlrrlemy
caplkpaksa
>d1igl__ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
ayrpsetlcggelvdtlqfvcgdrgfyfsrpasrvsrrsrgiveeccfrscdlalletyc
atpakse
>d2gf1__ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkptgygsssrrapqtgivdeccfrscdlrrlemy
caplkpaksa
>d3gf1__ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkptgygsssrrapqtgivdeccfrscdlrrlemy
caplkpaksa
>e1bom.1a 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
givdecclrpcsvdvllsyc
>e1bom.1b 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
xqpqavhtycgrhlartladlcweagvd
>e1bon.1a 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
givdecclrpcsvdvllsyc
>e1bon.1b 7.1.1.1.6 Bombyxin-II {Silkmoth (Bombyx mori)}
xqpqavhtycgrhlartladlcweagvd
>d1ehs__ 7.2.1.1.1 Heat-stable enterotoxin B {Escherichia coli}
stqsnkkdlcehyrqiakesckkgflgvrdgtagacfgaqimvaakgc
>d1vib__ 7.2.2.1.1 Neurotoxin B-IV {Milky ribbon worm (Cerebratulus lacteus)}
asatwgaayxacenncrkkydlcircqgkwagkrgkcaahciiqknnckgkckke
>d1wgca1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d1wgca2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d1wgca3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d1wgca4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d1wgcb1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d1wgcb2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d1wgcb3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d1wgcb4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d1wgta1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsgmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d1wgta2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ktcpnnhccsqyghcgfgaeycgagcqggpcrad
>d1wgta3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgycglgsefcgegcqngacstd
>d1wgta4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d1wgtb1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsgmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d1wgtb2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ktcpnnhccsqyghcgfgaeycgagcqggpcrad
>d1wgtb3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgycglgsefcgegcqngacstd
>d1wgtb4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d2cwga1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d2cwga2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d2cwga3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d2cwga4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d2cwgb1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d2cwgb2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d2cwgb3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d2cwgb4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d2wgca1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d2wgca2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atcpnnhccsqyghcgfgaeycgagcqggpcrad
>d2wgca3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqsggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d2wgca4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcda
>d2wgcb1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d2wgcb2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atcpnnhccsqyghcgfgaeycgagcqggpcrad
>d2wgcb3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqsggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d2wgcb4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcda
>d7wgaa1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d7wgaa2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d7wgaa3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d7wgaa4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d7wgab1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d7wgab2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atctnnqccsqygycgfgaeycgagcqggpcrad
>d7wgab3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqaggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d7wgab4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcdg
>d9wgaa1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d9wgaa2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atcpnnhccsqyghcgfgaeycgagcqggpcrad
>d9wgaa3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqsggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d9wgaa4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcda
>d9wgab1 7.3.1.1.1 (1-52) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
xrcgeqgsnmecpnnlccsqygycgmggdycgkgcqngacwtskrcgsqagg
>d9wgab2 7.3.1.1.1 (53-86) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
atcpnnhccsqyghcgfgaeycgagcqggpcrad
>d9wgab3 7.3.1.1.1 (87-129) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
ikcgsqsggklcpnnlccsqwgfcglgsefcgggcqsgacstd
>d9wgab4 7.3.1.1.1 (130-171) Wheat germ agglutinin (WGA) {Wheat (Triticum vulgaris)}
kpcgkdaggrvctnnyccskwgscgigpgycgagcqsggcda
>d1hev__ 7.3.1.1.2 Hevein {Hevea brasiliensis}
eqcgrqaggklcpnnlccsqwgwcgstdeycspdhncqsnckd
>d1mmc__ 7.3.1.2.1 Antimicrobial peptide 2, AC-AMP2 {Tassel (Amaranthus caudatus)}
vgecvrgrcpsgmccsqfgycgkgpkycgr
>d1mcti_ 7.3.2.1.1 Trypsin inhibitor {Bitter gourd (Momordica charantia), linn. Cucurbitaceae, seed}
ricpriwmectrdsdcmakcicvaghcg
>d1mcui_ 7.3.2.1.1 Trypsin inhibitor {Bitter gourd (Momordica charantia), linn. Cucurbitaceae, seed}
ricpriwmeckrdsdcmaecicvmghcg
>d1bxj__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilleckkdsdclaecvclehgycg
>d1cti__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d1ppei_ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d2cti__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d2stai_ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d3cti__ 7.3.2.1.2 Trypsin inhibitor {Squash (Cucurbita maxima)}
rvcprilmeckkdsdclaecvclehgycg
>d2btci_ 7.3.2.1.3 Trypsin inhibitor {Vegetable marrow (Cucurbita pepo)}
rvcpkilmeckkdsdclaeciclehgycg
>d2stbi_ 7.3.2.1.3 Trypsin inhibitor {Vegetable marrow (Cucurbita pepo)}
rvcpkilmeckkdsdclaeciclehgycg
>d4cpai_ 7.3.2.1.4 Carboxypeptidase A inhibitor {Potato}
xhadpicnkpckthddcsgawfcqacwnsartcgpyv
>d2eti__ 7.3.2.1.5 Trypsin inhibitor II {Jumping cucumber (Ecballium elaterium)}
gcprilmrckqdsdclagcvcgpngfcg
>d2let__ 7.3.2.1.5 Trypsin inhibitor II {Jumping cucumber (Ecballium elaterium)}
gcprllmrckqdsdclagcvcgpngfcg
>d1qfda_ 7.3.2.1.6 alpha-amylase inhibitor (AAI) {Prince's feather (Amaranthus hypochondriacus)}
cipkwnrcgpkmdgvpccepytctsdyygncs
>d1kal__ 7.3.3.1.1 Kalata B1 {African plant (Oldenlandia affinis dc)}
swpvctrnglpvcgetcvggtcntpgctc
>d1c4ea_ 7.3.4.1.1 Gurmarin, a sweet taste-suppressing polypeptide {Gymnema sylveste}
qcvkkdelcipyyldccepleckkvnwwdhkcig
>d1gur__ 7.3.4.1.1 Gurmarin, a sweet taste-suppressing polypeptide {Gymnema sylveste}
qcvkkdelcipyyldccepleckkvnwwdhkcig
>d1bh4__ 7.3.5.1.1 Circulin A {Chassalia parviflora}
cgescvwipcisaalgcscknkvcyrngip
>d1omc__ 7.3.6.1.1 Conotoxin {Sea snail (Conus geographus), G IVa}
cksxgsscsxtsynccrscnxytkrcy
>d2cco__ 7.3.6.1.1 Conotoxin {Sea snail (Conus geographus), G IVa}
cksxgsscsxtsynccrscnxytkrcy
>d1ag7__ 7.3.6.1.2 Conotoxin {Synthetic (Conus geographus), GS}
acsgrgsrcxxqccmglrcgrgnpqkcigahxdv
>d1omn__ 7.3.6.1.3 Conotoxin {Sea snail (Conus magus), M VIIc}
ckgkgapcrktmydccsgscgrrgkc
>d1mvi__ 7.3.6.1.4 Conotoxin {Sea snail (Conus magus), M VIIa}
ckgkgakcsrlmydcctgscrsgkc
>d1omg__ 7.3.6.1.4 Conotoxin {Sea snail (Conus magus), M VIIa}
ckgkgakcsrlmydcctgscrsgkc
>d1mvj__ 7.3.6.1.5 Conotoxin {Conus striatus, S VIb}
cklkgqscrktsydccsgscgrsgkc
>d1av3__ 7.3.6.1.6 Conotoxin {Conus purpurascens, kappa-pVIIa}
crixnqkcfqhlddccsrkcnrfnkcv
>d1kcp__ 7.3.6.1.6 Conotoxin {Conus purpurascens, kappa-pVIIa}
crixnqkcfqhlddccsrkcnrfnkcv
>d1agg__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
ednciaedygkctwggtkccrgrpcrcsmigtncectprlimeglsfa
>d1iva__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
kkkciakdygrckwggtpccrgrgcicsimgtnceckprlimeglgla
>d1oav__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
kkkciakdygrckwggtpccrgrgcicsimgtnceckprlimeglgla
>d1oaw__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
kkkciakdygrckwggtpccrgrgcicsimgtnceckprlimeglgla
>d1oma__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
ednciaedygkctwggtkccrgrpcrcsmigtncectprlimeglsfa
>d1omb__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
ciaedygkctwggtkccrgrpcrcsmigtncectp
>d1eit__ 7.3.6.2.2 mu-Agatoxin-I {Funnel web spider (Agelenopsis aperta)}
ecvpenghcrdwydeccegfycscrqppkcicrnnn
>d1axh__ 7.3.6.2.3 Atracotoxin-hVI (versutoxin) {Australian funnel-web spider (Hadronyche versuta)}
sptcipsgqpcpynenccsqsctfkenengntvkrcd
>d1vtx__ 7.3.6.2.3 Atracotoxin-hVI (versutoxin) {Australian funnel-web spider (Hadronyche versuta)}
cakkrnwcgktedcccpmkcvyawyneqgscqstisalwkkc
>d1qdp__ 7.3.6.2.4 Robustoxin {Funnel-web spider (Atrax robustus)}
cakkrnwcgknedcccpmkciyawynqqgscqttitglfkkc
>d1qk6a_ 7.3.6.2.5 Huwentoxin-I {Chinese bird spider (Selenocosmia huwena)}
ackgvfdactpgkneccpnrvcsdkhkwckwkl
>d1qk7a_ 7.3.6.2.6 Lectin SHL-I {Chinese bird spider (Selenocosmia huwena)}
gclgdkcdynngccsgyvcsrtwkwcvlagpw
>d2sn3__ 7.3.7.1.1 Scorpion toxin {Centruroides sculpturatus ewing, variant 3}
kegylvkksdgckygclklgenegcdteckaknqggsygycyafacwceglpestptypl
pnksc
>d1b3ca_ 7.3.7.1.2 Scorpion toxin {Centruroides sculpturatus ewing, beta}
kdgylvektgckktcyklgendfcnreckwkhiggsygycygfgcyceglpdstqtwplp
nktc
>d2b3ca_ 7.3.7.1.2 Scorpion toxin {Centruroides sculpturatus ewing, beta}
kdgylvektgckktcyklgendfcnreckwkhiggsygycygfgcyceglpdstqtwplp
nktc
>d1vna__ 7.3.7.1.3 Scorpion toxin {Centruroides sculpturatus ewing, variant 1}
kegylvkksdgckydcfwlgknehcnteckaknqggsygycyafacwceglpestptypl
pnksc
>d1vnb__ 7.3.7.1.3 Scorpion toxin {Centruroides sculpturatus ewing, variant 1}
kegylvkksdgckydcfwlgknehcnteckaknqggsygycyafacwceglpestptypl
pnksc
>d1nra__ 7.3.7.1.4 Scorpion toxin {Centruroides sculpturatus ewing, variant V}
kkdgypvdsgnckyeclkddycndlclerkadkgycywgkvscycyglpdnsptktsgkc
npa
>d1nrb__ 7.3.7.1.4 Scorpion toxin {Centruroides sculpturatus ewing, variant V}
kkdgypvdsgnckyeclkddycndlclerkadkgycywgkvscycyglpdnsptktsgkc
npa
>d1aho__ 7.3.7.1.5 Scorpion toxin {Androctonus australius hector, Toxin II}
vkdgyivddvnctyfcgrnaycneectklkgesgycqwaspygnacycyklpdhvrtkgp
grch
>d1ptx__ 7.3.7.1.5 Scorpion toxin {Androctonus australius hector, Toxin II}
vkdgyivddvnctyfcgrnaycneectklkgesgycqwaspygnacycyklpdhvrtkgp
grch
>d1cn2__ 7.3.7.1.6 Scorpion toxin {Mexican scorpion (Centruroides noxius hoffmann), toxin II}
kegylvdkntgckyeclklgdndyclreckqqygkgaggycyafacwcthlyeqaivwpl
pnkrcs
>d1bcg__ 7.3.7.1.7 Scorpion toxin {Scorpion (Buthotus judaicus), BJXTR-IT}
mkkngypldrngkttecsgvnaiaphycnsectkvyyaesgyccwgacycfgleddkpig
pmkditkkycdvqi
>d1snb__ 7.3.7.1.8 Scorpion toxin {Scorpion (Buthus martensii karsch), toxin m8}
grdayiadsenctyfcgsnpycndvctengaksgycqwagrygnacycidlpaserikeg
grcg
>d1sn1a_ 7.3.7.1.9 Scorpion toxin {Chinese scorpion (Buthus martensii), toxin m1}
vrdayiakphncvyecarneycndlctkngaksgycqwvgkygngcwcielpdnvpirvp
gkch
>d1sn4a_ 7.3.7.1.10 Scorpion toxin {Chinese scorpion (Buthus martensii), toxin m4}
vrdayiakpencvyhcagnegcnklctdngaesgycqwggrygnacwciklpddvpirvp
gkch
>d1b7da_ 7.3.7.1.11 Scorpion toxin {Scorpion (Tityus serrulatus)}
kegylmdhegcklscfirpsgycgrecgikkgssgycawpacycyglpnwvkvwdratnk
c
>d1big__ 7.3.7.2.1 Bmtx1 {Buthus martensii karsch}
ftdvkctgskqcwpvckqmfgkpngkcmngkcrcys
>d1bkt__ 7.3.7.2.2 Bmktx {Buthus martensii}
vginvkckhsgqclkpckdagmrfgkcingkcdctpk
>d2bmt__ 7.3.7.2.3 Bmtx2 {Buthus martensii}
ftnvscsassqcwpvckklfgtyrgkcmnskcrcys
>d1du9a_ 7.3.7.2.4 Bmp02 neurotoxin {Chinese scorpion (Buthus martensii)}
vgceecpmhckgknakptcddgvcncnv
>d1mtx__ 7.3.7.2.5 Margatoxin {Scorpion (Centruroides margaritatus)}
tiinvkctspkqclppckaqfgqsagakcmngkckcyph
>d1sxm__ 7.3.7.2.6 Noxiustoxin {Scorpion (Centruroides noxius hoffmann)}
tiinvkctspkqcskpckelygssagakcmngkckcynn
>d1txm__ 7.3.7.2.7 Maurotoxin {Scorpion (Scorpio maurus)}
vsctgskdcyapcrkqtgcpnakcinksckcygc
>d1bah__ 7.3.7.2.8 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
ftnvscttskexwsvcqrlhntsrgkcmnkkxrcys
>d1cmr__ 7.3.7.2.8 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
cttskecwsvcqrlhntskgwcdhrgcices
>d2crd__ 7.3.7.2.8 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
xftnvscttskecwsvcqrlhntsrgkcmnkkcrcys
>d1scy__ 7.3.7.2.9 Scyllatoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
afcnlrmcqlscrslgllgkcigdkcecvkh
>d1agt__ 7.3.7.2.10 Agitoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
gvpinvsctgspqcikpckdagmrfgkcmnrkchctpk
>d1chl__ 7.3.7.2.11 Chlorootoxin {Scorpion (Leiurus quinquestriatus), venom}
mcmpcfttdhqmarkcddccggkgrgkcygpqclcr
>d1tsk__ 7.3.7.2.12 Toxin ts kappa {Scorpion (Tityus serrulatus)}
vvigqrcyrspdcysackklvgkatgkctngrcdc
>d1sis__ 7.3.7.2.13 Toxin I5a {Scorpion (Buthus eupeus)}
mcmpcfttdpnmakkcrdccggngkcfgpqclcnr
>d1pnh__ 7.3.7.2.14 Toxin analog {Androctonus mauretanicus}
tvcnlrrcqlscrslgllgkcigvkcecvkh
>d1acw__ 7.3.7.2.15 Toxin analog P01 {Androctonus mauretanicus}
vscedcpehcstqkaqakcdndkcvcepi
>d1sco__ 7.3.7.2.16 OSK1 TOXIN {Central asian scorpion (Orthochirus scrobiculosus)}
gviinvkckisrqclepckkagmrfgkcmngkchctpk
>d1ktx__ 7.3.7.2.17 Kaliotoxin (KTX) {Androctonus mauretanicus}
gveinvkcsgspqclkpckdagmrfgkcmnrkchctp
>d2ktx__ 7.3.7.2.17 Kaliotoxin (KTX) {Androctonus mauretanicus}
gveinvkcsgspqclkpckdagmrfgkcmnrkchctpk
>d1lqh__ 7.3.7.2.18 Alpha toxin {Scorpion (Leiurus quinquestriatus hebraeus)}
mvrdayiaknyncvyecfrdaycnelctkngassgycqwagkygnacwcyalpdnvpirv
pgkcr
>d1lqi__ 7.3.7.2.18 Alpha toxin {Scorpion (Leiurus quinquestriatus hebraeus)}
mvrdayiaknyncvyecfrdaycnelctkngassgycqwagkygnacwcyalpdnvpirv
pgkcr
>d1bmr__ 7.3.7.2.19 Alpha toxin {Hebraei scorpion (Leiurus quinquestriatus hebraeus), Lqh}
vrdgyiaqpencvyhcfpgssgcdtlckekggtsghcgfkvghglacwcnalpdnvgiiv
egekchs
>d1lir__ 7.3.7.2.20 LQ2 toxin {Scorpion (Leiurus quinquestriatus hebraeus)}
ftqesctasnqcwsickrlhntnrgkcmnkkcrcys
>d1lqq__ 7.3.7.2.21 LQQIII toxin {Egyptian scorpion (Leiurus quinquestriatus)}
vrdayiaknyncvyecfrdsycndlctkngassgycqwagkygnacwcyalpdnvpirvp
gkch
>d2pta__ 7.3.7.2.22 Pandinus toxin K-a (PITX-Ka) {Emperor scorpion (Pandinus imperator)}
tisctnpkqcyphckketgypnakcmnrkckcfgr
>d1qkya_ 7.3.7.2.23 PI7 {Scorpion (Pandinus imperator)}
deairctgtkdcyipcryitgcfnsrcinksckcygct
>d1myn__ 7.3.7.3.1 Drosomycin {Fruit fly (Drosophila melanogaster)}
dclsgrykgpcavwdnetcrrvckeegrssghcspslkcwcegc
>d1ica__ 7.3.7.3.2 Defensin A {Flesh fly (Phormia terranovae), larva}
atcdllsgtginhsacaahcllrgnrggycngkgvcvcrn
>d1gpt__ 7.3.7.4.1 gamma-Thionin {Barley (Hordeum vulgare)}
ricrrrsagfkgpcvsnkncaqvcmqegwgggncdgplrrckcmrrc
>d1gps__ 7.3.7.4.2 gamma-Thionin {Wheat (Triticum turgidum)}
kicrrrsagfkgpcmsnkncaqvcqqegwgggncdgpfrrckcirqc
>d1ayj__ 7.3.7.4.3 Antifungal protein 1 (RS-AFP1) {Radish (Raphanus sativus)}
klcerpsgtwsgvcgnnnacknqcinlekarhgscnyvfpahkcicyfpc
>d1bk8__ 7.3.7.4.4 Antimicrobial protein 1 (AH-AMP1) {Horse chestnut (Aesculus hippocastanum)}
lcnerpsqtwsgncgntahcdkqcqdwekashgachkrenhwkcfcyfnc
>d1brz__ 7.3.7.4.5 Brazzein {J'oublie (Pentadiplandra brazzeana)}
dkckkvyenypvskcqlanqcnydckldkharsgecfydekrnlqcicdycey
>d2brz__ 7.3.7.4.5 Brazzein {J'oublie (Pentadiplandra brazzeana)}
dkckkvyenypvskcqlanqcnydckldkharsgecfydekrnlqcicdycey
>d1az6__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azj__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpaysqcl
>d1azk__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpyasqcl
>d1cbh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpyysqcl
>d2cbh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshygqcggigysgptvcasgttcqvlnpyysqcl
>d1boea_ 7.3.9.1.1 Insulin-like growth factor-binding protein-5 (IGFBP-5) {Human (Homo sapiens)}
alaegqscgvytercaqglrclprqdeekplhallhgrgvclneks
>d1igra3 7.3.9.1.2 (150-299) Cys-rich domain of the type 1 insulin-like growth factor receptor {Human (Homo sapiens)}
dlcpgtmeekpmcekttinneynyrcwttnrcqkmcpstcgkractennecchpeclgsc
sapdndtacvacrhyyyagvcvpacppntyrfegwrcvdrdfcanilsaessdsegfvih
dgecmqecpsgfirngsqsmycipcegpcp
>d1ethb1 7.3.10.1.1 (4-44) (Pro)colipase {Pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethb2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1ethd1 7.3.10.1.1 (4-44) (Pro)colipase {Pig (Sus scrofa)}
prgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1ethd2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1lpaa1 7.3.10.1.1 (6-44) (Pro)colipase {Pig (Sus scrofa)}
giiinldegelclnsaqcksnccqhdtilsllrcalkar
>d1lpaa2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1lpba1 7.3.10.1.1 (6-44) (Pro)colipase {Pig (Sus scrofa)}
giiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1lpba2 7.3.10.1.1 (45-90) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnv
>d1pcn_1 7.3.10.1.1 (1-44) (Pro)colipase {Pig (Sus scrofa)}
vpdprgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1pcn_2 7.3.10.1.1 (45-93) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnvgrs
>d1pco_1 7.3.10.1.1 (1-44) (Pro)colipase {Pig (Sus scrofa)}
vpdprgiiinldegelclnsaqcksnccqhdtilslsrcalkar
>d1pco_2 7.3.10.1.1 (45-93) (Pro)colipase {Pig (Sus scrofa)}
ensecsaftlygvyykcpcergltcegdkslvgsitntnfgichnvgrs
>d1imt_1 7.3.10.1.2 (1-36) Intestinal toxin 1 {Black mamba (Dendroaspis polylepis polylepis)}
avitgacerdlqcgkgtccavslwiksvrvctpvgt
>d1imt_2 7.3.10.1.2 (37-80) Intestinal toxin 1 {Black mamba (Dendroaspis polylepis polylepis)}
sgedchpashkipfsgqrmhhtcpcapnlacvqtspkkfkclsk
>d1edmb_ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1edmc_ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1ixa__ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
vdgdqcesnpclnggsckddinsyecwcpfgfegkncel
>d1rfnb_ 7.3.11.1.1 Factor IX (IXa) {Human (Homo sapiens)}
mtcnikngrceqfcknsadnkvvcsctegyrlaenqkscepavpfpcgrvsvsqtsk
>d1pfxl1 7.3.11.1.2 (47-86) Factor IX (IXa) {Pig (Sus scrofa)}
dgdqcepnpclngglckxdinsyecwcqvgfegkncelda
>d1pfxl2 7.3.11.1.2 (87-146) Factor IX (IXa) {Pig (Sus scrofa)}
tcnikngrckqfcktgadskvlcscttgyrlapdqksckpavpfpcgrvsvshspttltr
>d1cvwl_ 7.3.11.1.3 Coagulation factor VIIa {Human (Homo sapiens)}
icvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipilekr
>d1danl1 7.3.11.1.3 (49-86) Coagulation factor VIIa {Human (Homo sapiens)}
qcasspcqnggsckdqlqsyicfclpafegrncethkd
>d1danl2 7.3.11.1.3 (87-142) Coagulation factor VIIa {Human (Homo sapiens)}
dqlicvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipile
>d1fakl1 7.3.11.1.3 (49-86) Coagulation factor VIIa {Human (Homo sapiens)}
qcasspcqnggsckdqlqsyicfclpafegrncethkd
>d1fakl2 7.3.11.1.3 (87-143) Coagulation factor VIIa {Human (Homo sapiens)}
dqlicvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipilek
>d1qfkl1 7.3.11.1.3 (49-86) Coagulation factor VIIa {Human (Homo sapiens)}
qcasspcqnggsckdqlqsyicfclpafegrncethkd
>d1qfkl2 7.3.11.1.3 (87-144) Coagulation factor VIIa {Human (Homo sapiens)}
dqlicvnenggceqycsdhtgtkrscrchegyslladgvsctptveypcgkipilekr
>d1esl_2 7.3.11.1.4 (119-157) E-selectin, EGF-domain {Human (Homo sapiens)}
taactntscsghgecvetinnytckcdpgfsglkceqiv
>d1faxl_ 7.3.11.1.5 Factor X, N-terminal module {Human (Homo sapiens)}
trklcsldngdcdqfcheeqasvvcscargytladngkaciptgpypcgkqtler
>d1hcgb_ 7.3.11.1.5 Factor X, N-terminal module {Human (Homo sapiens)}
csldngdcdqfcheeqnsvvcscargytladngkaciptgpypcgkqtler
>d1xkal1 7.3.11.1.5 (49-86) Factor X, N-terminal module {Human (Homo sapiens)}
qcetspcqnqgkckxglgeytctclegfegkncelftr
>d1xkal2 7.3.11.1.5 (87-139) Factor X, N-terminal module {Human (Homo sapiens)}
klcsldngdcdqfcheeqnsvvcscargytladngkaciptgpypcgkqtler
>d1xkba1 7.3.11.1.5 (48-86) Factor X, N-terminal module {Human (Homo sapiens)}
dqcetspcqnqgkckxglgeytctclegfegkncelftr
>d1xkba2 7.3.11.1.5 (87-138) Factor X, N-terminal module {Human (Homo sapiens)}
klcsldngdcdqfcheeqnsvvcscargytladngkaciptgpypcgkqtle
>d1xkbb1 7.3.11.1.5 (50-86) Factor X, N-terminal module {Human (Homo sapiens)}
cetspcqnqgkckxglgeytctclegfegkncelftr
>d1xkbb2 7.3.11.1.5 (87-139) Factor X, N-terminal module {Human (Homo sapiens)}
klcsldngdcdqfcheeqnsvvcscargytladngkaciptgpypcgkqtler
>d1apo__ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1ccf__ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1kigl_ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
csldnggcdqfcreersevrcscahgyvlgddskscvsterfpcgkftqgr
>d1whe_1 7.3.11.1.6 (47-86) Factor X, N-terminal module {Bovine (Bos taurus)}
gdqceghpclnqghckxgigdytctcaegfegkncefstr
>d1whf_1 7.3.11.1.6 (47-86) Factor X, N-terminal module {Bovine (Bos taurus)}
gdqceghpclnqghckxgigdytctcaegfegkncefstr
>d1autl1 7.3.11.1.7 (49-96) Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
qclvlplehpcaslccghgtcixgigsfscdcrsgwegrfcqrevsfl
>d1autl2 7.3.11.1.7 (97-146) Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
ncsldnggcthycleevgwrrcscapgyklgddllqchpavkfpcgrpwk
>d1bf9__ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethk
>d1f7ea_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1f7ma_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1ff7a_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1ffma_ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethkddgsa
>d1cqea2 7.3.11.1.9 (32-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
pvnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1cqeb2 7.3.11.1.9 (31-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
apvnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pgea2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pgeb2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pgfa2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pgfb2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pgga2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pggb2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1prha2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1prhb2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1pth_2 7.3.11.1.9 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Sheep (Ovis aries)}
vnpccyypcqhqgicvrfgldryqcdctrtgysgpnctipe
>d1cx2a2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2b2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2c2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1cx2d2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d3pgha2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d3pghb2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d3pghc2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d3pghd2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d4coxa2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d4coxb2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d4coxc2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d4coxd2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d5coxa2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d5coxb2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d5coxc2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d5coxd2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d6coxa2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d6coxb2 7.3.11.1.10 (33-73) Prostaglandin H2 synthase-1, EGF-like module {Mouse (Mus musculus)}
anpccsnpcqnrgecmstgfdqykcdctrtgfygencttpe
>d1fsb__ 7.3.11.1.11 P-selectin, EGF-domain {Human (Homo sapiens)}
tascqdmscskqgecletignytcscypgfygpeceyvre
>d1a3p__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
pgxpssydgyclnggvxmhiesldsytcncvigysgdrcqtrdlr
>d1egf__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epg__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1eph__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epi__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1epj__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d3egf__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
nsypgcpssydgyclnggvcmhiesldsytcncvigysgdrcqtrdlrwwelr
>d1yuf__ 7.3.11.1.13 Transforming growth factor alpha {Human (Homo sapiens)}
vvshfndcpdshtqfcfhgtcrflvqedkpacvchsgyvgarcehadlla
>d1yug__ 7.3.11.1.13 Transforming growth factor alpha {Human (Homo sapiens)}
vvshfndcpdshtqfcfhgtcrflvqedkpacvchsgyvgarcehadlla
>d2tgf__ 7.3.11.1.13 Transforming growth factor alpha {Human (Homo sapiens)}
vvshfndcpdshtqfcfhgtcrflvqedkpacvchsgyvgarcehadlla
>d3tgf__ 7.3.11.1.13 Transforming growth factor alpha {Human (Homo sapiens)}
vvshfndcpdshtqfcfhgtcrflvqedkpacvchsgyvgarcehadlla
>d4tgf__ 7.3.11.1.13 Transforming growth factor alpha {Human (Homo sapiens)}
vvshfndcpdshtqfcfhgtcrflvqedkpacvchsgyvgarcehadlla
>d1xdtr_ 7.3.11.1.14 Heparin-binding epidermal growth factor, HBEGF {Human (Homo sapiens)}
pclrkykdfcihgeckyvkelrapscichpgyhgerchgls
>d1urk_1 7.3.11.1.15 (6-49) Plasminogen activator (urokinase-type) {Human (Homo sapiens)}
qvpsncdclnggtcvsnkyfsnihwcncpkkfggqhceidkskt
>d1hae__ 7.3.11.1.16 Heregulin-alpha, EGF-like domain {Human (Homo sapiens)}
shlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqekae
ely
>d1haf__ 7.3.11.1.16 Heregulin-alpha, EGF-like domain {Human (Homo sapiens)}
shlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqekae
ely
>d1hre__ 7.3.11.1.16 Heregulin-alpha, EGF-like domain {Human (Homo sapiens)}
gtshlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqek
aeelyqk
>d1hrf__ 7.3.11.1.16 Heregulin-alpha, EGF-like domain {Human (Homo sapiens)}
gtshlvkcaekektfcvnggecfmvkdlsnpsrylckcqpgftgarctenvpmkvqnqek
aeelyqk
>d1adx__ 7.3.11.1.17 Thrombomodulin, different EGF-like domains {Human (Homo sapiens)}
qmfcnqtacpadcdpntqascecpegyilddgfictdide
>d1zaq__ 7.3.11.1.17 Thrombomodulin, different EGF-like domains {Human (Homo sapiens)}
epvdpcfranceyqcqplnqtsylcvcaegfapiphephrcqmf
>d2adx__ 7.3.11.1.17 Thrombomodulin, different EGF-like domains {Human (Homo sapiens)}
qmfcnqtacpadcdpntqascecpegyilddgfictdide
>d1emn_1 7.3.11.1.18 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emn_2 7.3.11.1.18 (2167-2205) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
tdecsvgnpcgngtcknviggfectceegfepgpmmtce
>d1emo_1 7.3.11.1.18 (2124-2166) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
savdmdeckepdvckhgqcintdgsyrcecpfgyilagnecvd
>d1emo_2 7.3.11.1.18 (2167-2205) Fibrillin-1 fragment (residues 2124-2205) {Human (Homo sapiens)}
tdecsvgnpcgngtcknviggfectceegfepgpmmtce
>d1apq__ 7.3.11.1.19 Complement protease C1R {Human (Homo sapiens)}
avdldecasrsksgeedpqpqcqhlchnyvggyfcscrpgyelqedrhscqae
>d1tpg_1 7.3.11.1.20 (51-91) Plasminogen activator (tissue-type) ,t-PA {Human (Homo sapiens)}
cseprcfnggtcqqalyfsdfvcqcpegfagksceidtrat
>d1klo_1 7.3.11.2.1 (11-65) Laminin gamma1 chain {Mouse (Mus musculus)}
cpcpggsscaivpktkevvcthcptgtagkrcelcddgyfgdplgsngpvrlcrp
>d1klo_2 7.3.11.2.1 (66-121) Laminin gamma1 chain {Mouse (Mus musculus)}
cqcndnidpnavgncnrltgeclkciyntagfycdrckegffgnplapnpadkcka
>d1klo_3 7.3.11.2.1 (122-172) Laminin gamma1 chain {Mouse (Mus musculus)}
cacnpygtvqqqsscnpvtgqcqclphvsgrdcgtcdpgyynlqsgqgcer
>d1tle__ 7.3.11.2.1 Laminin gamma1 chain {Mouse (Mus musculus)}
rpcqcndnidpnavgncnrltgeclkciyntagfycdrckegffgnplapnpadkcka
>d1bmoa2 7.3.11.3.1 (54-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1bmob2 7.3.11.3.1 (54-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
pcqnhhckhgkvceldenntpmcv
>d1nuba2 7.3.11.3.1 (53-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
apcqnhhckhgkvceldenntpmcv
>d1nubb2 7.3.11.3.1 (53-77) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
apcqnhhckhgkvceldenntpmcv
>d1b9wa1 7.3.11.4.1 (1-45) Merozoite surface protein 1 (MSP-1) {Plasmodium cynomolgi}
mssehrcidtnvpenaacyryldgteewrcllyfkedagkcvpap
>d1b9wa2 7.3.11.4.1 (46-89) Merozoite surface protein 1 (MSP-1) {Plasmodium cynomolgi}
nmtckdknggcapeaeckmndkneivckctkegseplfegvfcs
>d1ceja1 7.3.11.4.2 (1-45) Merozoite surface protein 1 (MSP-1) {Plasmodium falciparum}
nisqhqcvkkqcpqnsgcfrhldereeckcllnykqegdkcvenp
>d1ceja2 7.3.11.4.2 (46-96) Merozoite surface protein 1 (MSP-1) {Plasmodium falciparum}
nptcnennggcdadakcteedsgsngkkitcectkpdsyplfdgifcsssn
>d1bi6h1 7.3.12.1.1 (8-31) Bromelain inhibitor VI (cysteine protease inhibitor) {Pineapple (Ananas comosus)}
tdtysdcpgfcktckaefgkyicl
>d2bi6h1 7.3.12.1.1 (8-31) Bromelain inhibitor VI (cysteine protease inhibitor) {Pineapple (Ananas comosus)}
tdtysdcpgfcktckaefgkyicl
>d1bbi__ 7.3.13.1.1 Bowman-Birk inhibitor, BBI {Soybean (Glycine max)}
ddesskpccdqcactksnppqcrcsdmrlnschsackscicalsypaqcfcvditdfcye
pckpseddken
>d1pi2__ 7.3.13.1.1 Bowman-Birk inhibitor, BBI {Soybean (Glycine max)}
yskpccdlcmctrsmppqcscedrinschsdckscmctrsqpgqcrcldtndfcykpcks
r
>d1tabi_ 7.3.13.1.1 Bowman-Birk inhibitor, BBI {Soybean (Glycine max)}
sesskpccdqcsctksmppkcrcsdirlnschsackscactysipakcfctdindfcyep
ck
>d2bbi__ 7.3.13.1.1 Bowman-Birk inhibitor, BBI {Soybean (Glycine max)}
ddesskpccdqcactksnppqcrcsdmrlnschsackscicalsypaqcfcvditdfcye
pckpseddken
>d1pbia_ 7.3.13.1.2 Bowman-Birk inhibitor, BBI {Winter pea (Pisum sativum)}
ksaccdtclctksnpptcrcvdvgetchsaclscicaysnppkcqcfdtqkfcykqchns
eleevikn
>d1pbib_ 7.3.13.1.2 Bowman-Birk inhibitor, BBI {Winter pea (Pisum sativum)}
ksaccdtclctksnpptcrcvdvgetchsaclscicaysnppkcqcfdtqkfcykqchns
eleevikn
>d1c2aa1 7.3.13.1.3 (4-64) Bowman-Birk inhibitor, BBI {Barley (Hordeum vulgare)}
krpwkccdeavctrsippictcmdevfecpktckscgpsmgdpsrricqdqyvgdpgpic
r
>d1c2aa2 7.3.13.1.3 (65-123) Bowman-Birk inhibitor, BBI {Barley (Hordeum vulgare)}
pweccdkaictrsnpptcrcvdevkkcaptcktclpsrsrpsrrvcidsyfgpvpprct
>d1flei_ 7.3.14.1.1 Elafin, elastase-specific inhibitor {Human (Homo sapiens)}
tkpgscpiilircamlnppnrclkdtdcpgikkccegscgmacfvpq
>d2rel__ 7.3.14.1.1 Elafin, elastase-specific inhibitor {Human (Homo sapiens)}
aqepvkgpvstkpgscpiilircamlnppnrclkdtdcpgikkccegscgmacfvpq
>d1bx7__ 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
gntcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscaka
>d1bx8__ 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscaka
>e1hia.3i 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscak
>e1hia.3j 7.3.15.1.1 Hirustasin {Medicinal leech (Hirudo medicinalis)}
tcggetcsaaqvclkgkcvcnevhcrirckyglkkdengceypcscak
>d1skz_1 7.3.15.1.2 (7-58) Factor Xa inhibitor antistasin {Mexican leech (Haementeria officinalis)}
gceeagcpegsacniitdrctcsgvrcrvhcphgfqrsrygcefckcrlepm
>d1skz_2 7.3.15.1.2 (59-110) Factor Xa inhibitor antistasin {Mexican leech (Haementeria officinalis)}
katcdisecpegmmcsrltnkcdckidincrktcpnglkrdklgceycecrp
>d1hic__ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpqsh
>d1hrti_ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpqshndgdfeeip
eeylq
>d2hir__ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpq
>d3htci_ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
itytdctesgqnlclcegsnvcgkgnkcilgsngkgnqcvtgegtpkpeshnngdfeeip
eeylq
>d4hir__ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpepq
>d4htci_ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
itytdctesgqnlclcegsnvcgkgnkcilgsngkgnqcvtgegtpkpeshnngdfeeip
eeylq
>d5hir__ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpkpq
>d6hir__ 7.3.15.2.1 Hirudin {Leech (Hirudo medicinalis)}
vvytdctesgqnlclcegsnvcgqgnkcilgsdgeknqcvtgegtpepq
>d1dec__ 7.3.15.2.2 Decorsin {North american leech (Macrobdella decora)}
aprlpqcqgddqekclcnkdecppgqcrfprgdadpyce
>d1qgma_ 7.3.16.1.1 N-terminal domain of granulin-1 {Carp (Cyprinus carpio)}
vihcdaaticpdgttcslspygvwycspfs
>d1pmc__ 7.4.1.1.1 Proteinase inhibitor PMP-C {Migratory locust (Locusta migratoria)}
eiscepgktfkdkcntcrcgadgksaactlkacpnq
>d1mkna_ 7.5.1.1.1 Midkine, a heparin-binding growth factor, N-terminal domain {Synthetic}
kkkdkvkkggpgsecaewawgpctpsskdcgvgfregtcgaqtqrircrvpcnwkkefg
>d1mkca_ 7.5.1.2.1 Midkine, a heparin-binding growth factor, C-terminal domain {Synthetic}
ckykfenwgacdggtgtkvrqgtlkkarynaqcqetirvtkpc
>d1bbg__ 7.6.1.1.1 <i>Amb</i> V allergen {Giant ragweed (Ambrosia trifida), pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d2bbg__ 7.6.1.1.1 <i>Amb</i> V allergen {Giant ragweed (Ambrosia trifida), pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d3bbg__ 7.6.1.1.1 <i>Amb</i> V allergen {Giant ragweed (Ambrosia trifida), pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d1era__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1fra__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1nxb__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnqhssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1qkda_ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1qkdb_ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1qke__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d3ebx__ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d6ebxa_ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d6ebxb_ 7.7.1.1.1 Erabutoxin B (also neurotoxin B) {Sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscyhkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1cxn__ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1cxo__ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1tgxa_ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1tgxb_ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1tgxc_ 7.7.1.1.2 gamma-Cardiotoxin {Snake (Naja nigricollis)}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntdkcn
>d1fas__ 7.7.1.1.3 Fasciculin {Green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddylevkcctspdkcn
y
>d1fsc__ 7.7.1.1.3 Fasciculin {Green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d1fssb_ 7.7.1.1.3 Fasciculin {Green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d1mahf_ 7.7.1.1.3 Fasciculin {Green mamba (Dendroaspis angusticeps)}
tmcyshtttsrailtncgenscyrksrrhppkmvlgrgcgcppgddnlevkcctspdkcn
y
>d2era__ 7.7.1.1.4 Erabutoxin A {Broad-banded blue sea snake (Laticauda semifasciata)}
ricfnhqgsqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d3eraa_ 7.7.1.1.4 Erabutoxin A {Broad-banded blue sea snake (Laticauda semifasciata)}
ricfnhqtsqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d3erab_ 7.7.1.1.4 Erabutoxin A {Broad-banded blue sea snake (Laticauda semifasciata)}
ricfnhqtsqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d5ebx__ 7.7.1.1.4 Erabutoxin A {Broad-banded blue sea snake (Laticauda semifasciata)}
ricfnhqssqpqttktcspgesscynkqwsdfrgtiiergcgcptvkpgiklsccesevc
nn
>d1ntn__ 7.7.1.1.5 Neurotoxin I {Snake (Naja naja oxiana)}
itcyktpiitsetcapgqnlcytktwcdawcgsrgkvielgcaatcptvesyqdikccst
dncnphpkqkrp
>d1cdta_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cdtb_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkcnklipiayktcpegknlcykmmlaskkmvpvkrgcinvcpknsalvkyvccstdrcn
>d1cvo__ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1kxia_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1kxib_ 7.7.1.1.6 Cardiotoxin V {Taiwan cobra (Naja naja atra)}
lkchntqlpfiyktcpegknlcfkatlkkfplkfpvkrgcadncpknsallkyvccstdk
cn
>d1ctx__ 7.7.1.1.7 alpha-Cobratoxin {Cobra (Naja naja siamensis)}
ircfitpditskdcpnghvcytktwcdafcsirgkrvdlgcaatcptvktgvdiqccstd
ncnpfptrkrp
>d2ctx__ 7.7.1.1.7 alpha-Cobratoxin {Cobra (Naja naja siamensis)}
ircfitpditskdcpnghvcytktwcdafcsirgkrvdlgcaatcptvktgvdiqccstd
ncnpfptrkrp
>d1lsi__ 7.7.1.1.8 Long neurotoxin 1 (component LSIII) {Sea snake (Laticauda semifasciata)}
recylnphdtqtcpsgqeicyvkswcnawcssrgkvlefgcaatcpsvntgteikccsad
kcntyp
>d1tfs__ 7.7.1.1.9 FS2 toxin {Black mamba (Dendroaspis polylepis polylepis)}
ricyshkaslpratktcventcykmfirthreyisergcgcptamwpyqtecckgdrcnk
>d1abta_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1bxpa_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d2abxa_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatipssavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnhppkrqpg
>d2abxb_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatipssavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnhppkrqpg
>d2btxa_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1kbaa_ 7.7.1.1.11 Bungarotoxin {Kappa-bungarotoxin (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d1kbab_ 7.7.1.1.11 Bungarotoxin {Kappa-bungarotoxin (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d2nbta_ 7.7.1.1.12 Bungarotoxin {Neuronal bungarotoxin (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d2nbtb_ 7.7.1.1.12 Bungarotoxin {Neuronal bungarotoxin (Bungarus multicinctus)}
rtclispsstpqtcpngqdicflkaqcdkfcsirgpvieqgcvatcpqfrsnyrsllcct
tdncnh
>d2cdx__ 7.7.1.1.13 Cardiotoxin CTXI {Taiwan cobra (Naja naja atra)}
lkcnklipiasktcpagknlcykmfmmsdltipvkrgcidvcpknsllvkyvccntdrcn
>d2ccx__ 7.7.1.1.14 Cardiotoxin CTX IIB {Naja mossambica mossambica}
lkcnqlippfwktcpkgknlcykmtmraapmvpvkrgcidvcpkssllikymccntnkcn
>d1cre__ 7.7.1.1.15 Cardiotoxin II {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1crf__ 7.7.1.1.15 Cardiotoxin II {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1cb9a_ 7.7.1.1.16 Cardiotoxin II {Central asian cobra (Naja naja oxiana)}
lkckklvplfsktcpagknlcykmfmvaaphvpvkrgcidvcpkssllvkyvccntdkcn
>d1ccqa_ 7.7.1.1.16 Cardiotoxin II {Central asian cobra (Naja naja oxiana)}
lkckklvplfsktcpagknlcykmfmvaaphvpvkrgcidvcpkssllvkyvccntdkcn
>d2crs__ 7.7.1.1.17 Cardiotoxin III {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvatpkvpvkrgcidvcpkssllvkyvccntdrcn
>d2crt__ 7.7.1.1.17 Cardiotoxin III {Taiwan cobra (Naja naja atra)}
lkcnklvplfyktcpagknlcykmfmvatpkvpvkrgcidvcpkssllvkyvccntdrcn
>d1kbs__ 7.7.1.1.18 Cardiotoxin IV {Taiwan cobra (Naja naja atra)}
rkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1kbt__ 7.7.1.1.18 Cardiotoxin IV {Taiwan cobra (Naja naja atra)}
rkcnklvplfyktcpagknlcykmfmvsnltvpvkrgcidvcpknsalvkyvccntdrcn
>d1cod__ 7.7.1.1.19 Cobrotoxin II {Taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1coe__ 7.7.1.1.19 Cobrotoxin II {Taiwan cobra (Naja naja atra)}
lechnqqssqtptttgcsggetncykkrwrdhrgyrtergcgcpsvkngieinccttdrc
nn
>d1nea__ 7.7.1.1.20 alpha-Toxin {Snake (Naja nigricollis)}
lechnqqssqppttktcpgetncykkvwrdhrgtiiergcgcptvkpgiklnccttdkcn
n
>d1ntx__ 7.7.1.1.21 alpha-Toxin {Black mamba (Dendroaspis polylepis polylepis)}
ricynhqsttrattksceenscykkywrdhrgtiiergcgcpkvkpgvgihccqsdkcny
>d1nor__ 7.7.1.1.22 Neurotoxin II {Central asian cobra (Naja naja oxiana)}
lechnqqssqppttktcsgetncykkwwsdhrgtiiergcgcpkvkpgvnlnccrtdrcn
n
>d1txa__ 7.7.1.1.23 Toxin B (long neurotoxin) {King cobra (Ophiophagus hannah)}
tkcyvtpdatsqtcpdgqdicytktwcdgfcssrgkridlgcaatcpkvkpgvdikccst
dncnpfptwkrkh
>d1txb__ 7.7.1.1.23 Toxin B (long neurotoxin) {King cobra (Ophiophagus hannah)}
tkcyvtpdatsqtcpdgqdicytktwcdgfcssrgkridlgcaatcpkvkpgvdikccst
dncnpfptwkrkh
>d1drs__ 7.7.1.2.1 Dendroaspin {Dendroaspis jamesoni kaimose}
ricynhlgtkppttetcqedscykniwtfdniirrgcgcftprgdmpgpyccesdkcnl
>d1cdq__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cdr__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1cds__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcnfneqlen
>d1erg__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcn
>d1erh__ 7.7.1.3.1 CD59, extracellular domain {Human (Homo sapiens)}
lqcyncpnptadcktavncssdfdaclitkaglqvynkcwkfehcnfndvttrlrenelt
yycckkdlcn
>d1btea_ 7.7.1.4.1 Extracellular domain of the type II activin receptor {Mouse (Mus musculus)}
etqeclffnanwerdrtnqtgvepcygdkdkrrhcfatwknisgsieivkqgcwlddinc
ydrtdciekkdspevyfcccegnmcnekfsyfpeme
>d1aala_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgga
>d1aalb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglvqtfvyggcrakrnnfksaedamrtcgg
>d1b0ca_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cc_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0cd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1b0ce_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhca_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcc_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhce_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcf_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcg_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhch_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhci_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bhcj_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bpi__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bpt__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfanakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1brbi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
ageppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrta
>d1bthp_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bthq_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryaynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1bz5a_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5b_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5c_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5d_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bz5e_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d1bzxi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbwd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1cbwi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1faki_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
apdfcleppydgpcralhlryfynakaglcqtfyyggclakrnnfesaedcmrtc
>d1fan__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnaksaedcmrtcgga
>d1mtnd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1mtnh_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1nag__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrgnfksaedcmrtcg
>d1pit__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d1qlqa_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppyagacrariiryfynakaglcqtfvyggcrakrnnfksaedclrtcgga
>d1tpai_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d2hexa_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d2hexb_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d2hexc_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgg
>d2hexd_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d2hexe_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d2kaii_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
pdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d2ptci_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d2tgpi_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d2tpii_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
pdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d3tgii_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d3tgji_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcg
>d3tpii_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d4pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d4tpii_ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpcrariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d5pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgga
>d6pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcgg
>d7pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglaqtfvyggcrakrnnfksaedamrtcgga
>d8pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvgggcrakrnnfksaedcmrtcgga
>d9pti__ 7.8.1.1.1 Pancreatic trypsin inhibitor, BPTI {Bovine (Bos taurus)}
rpdfcleppytgpckariiryfynakaglcqtfvyggcrakrnnfksaedcmrtcga
>d1knt__ 7.8.1.1.2 Collagen type VI (domain C5 from alpha 3 chain) {Human (Homo sapiens)}
tdicklpkdegtcrdfilkwyydpntkscarfwyggcggnenkfgsqkecekvca
>d1kun__ 7.8.1.1.2 Collagen type VI (domain C5 from alpha 3 chain) {Human (Homo sapiens)}
etdicklpkdegtcrdfilkwyydpntkscarfwyggcggnenkfgsqkecekvcapv
>d2knt__ 7.8.1.1.2 Collagen type VI (domain C5 from alpha 3 chain) {Human (Homo sapiens)}
etdicklpkdegtcrdfilkwyydpntkscarfwyggcggnenkfgsqkecekvcapv
>d1adz__ 7.8.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
dykddddklkpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleec
knicedgpngf
>d1tfxc_ 7.8.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
kpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleecknicedg
>d1tfxd_ 7.8.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
kpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleecknicedg
>d1aapa_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1aapb_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1brci_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
vrevcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca0d_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1ca0i_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1tawb_ 7.8.1.1.4 Alzheimer's amyloid B-protein precursor, APPI {Human (Homo sapiens)}
evcseqaetgpcramisrwyfdvtegkcapffyggcggnrnnfdteeycmavcg
>d1bik_1 7.8.1.1.5 (25-78) Bikunin from inter-alpha-inhibitor complex {Human (Homo sapiens)}
scqlgysagpcmgmtsryfyngtsmacetfqyggcmgngnnfvtekeclqtcrt
>d1bik_2 7.8.1.1.5 (79-134) Bikunin from inter-alpha-inhibitor complex {Human (Homo sapiens)}
vaacnlpivrgpcrafiqlwafdavkgkcvlfpyggcqgngnkfysekecreycgv
>d1dtx__ 7.8.1.1.6 alpha-Dendrotoxin {Green mamba (Dendroaspis angusticeps)}
xprrklcilhrnpgrcydkipafyynqkkkqcerfdwsgcggnsnrfktieecrrtcig
>d1bunb_ 7.8.1.1.7 beta2-bungarotoxin, neurotoxin chain {Many-banded krait (elapid) (Bungarus multicinctus)}
rkrhpdcdkppdtkicqtvvrafyykpsakrcvqfryggcngngnhfksdhlcrcecley
r
>d1shp__ 7.8.1.1.8 Trypsin inhibitor {Sea anemone (Stichodactyla helianthus)}
sicsepkkvgrckgyfprfyfdsetgkctpfiyggcggngnnfetlhqcraicra
>d1dtk__ 7.8.1.1.9 Dendrotoxin K {Black mamba (Dendroaspis polylepis polylepis)}
aakycklplrigpckrkipsfyykwkakqclpfdysgcggnanrfktieecrrtcvg
>d1dem__ 7.8.1.1.10 Dendrotoxin I {African elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1den__ 7.8.1.1.10 Dendrotoxin I {African elapid snake (Dendroaspis polylepis polylepis)}
qplrklcilhrnpgrcyqkipafyynqkkkqcegftwsgcggnsnrfktieecrrtcirk
>d1bf0__ 7.8.1.1.11 Calcicludine (cac) {Green mamba (Dendroaspis angusticeps)}
wqppwyckepvrigsckkqfssfyfkwtakkclpflfsgcggnanrfqtigecrkkclgk
>d1tocr1 7.8.1.2.1 (1a-56) Ornithodorin {Soft tick (Ornithodoros moubata)}
slnvlcnnphtadcnndaqvdryfregttclmspactsegyasqhecqqacfvgged
>d1tocr2 7.8.1.2.1 (57-119) Ornithodorin {Soft tick (Ornithodoros moubata)}
hssemhssclgdpptscaegtdityydsdsktckvlaascpsgentfesevecqvacgap
ieg
>d1tocs1 7.8.1.2.1 (1a-56) Ornithodorin {Soft tick (Ornithodoros moubata)}
slnvlcnnphtadcnndaqvdryfregttclmspactsegyasqhecqqacfvgged
>d1tocs2 7.8.1.2.1 (57-119) Ornithodorin {Soft tick (Ornithodoros moubata)}
hssemhssclgdpptscaegtdityydsdsktckvlaascpsgentfesevecqvacgap
ieg
>d1toct1 7.8.1.2.1 (1a-56) Ornithodorin {Soft tick (Ornithodoros moubata)}
slnvlcnnphtadcnndaqvdryfregttclmspactsegyasqhecqqacfvgged
>d1toct2 7.8.1.2.1 (57-119) Ornithodorin {Soft tick (Ornithodoros moubata)}
hssemhssclgdpptscaegtdityydsdsktckvlaascpsgentfesevecqvacgap
ieg
>d1tocu1 7.8.1.2.1 (1a-56) Ornithodorin {Soft tick (Ornithodoros moubata)}
slnvlcnnphtadcnndaqvdryfregttclmspactsegyasqhecqqacfvgged
>d1tocu2 7.8.1.2.1 (57-119) Ornithodorin {Soft tick (Ornithodoros moubata)}
hssemhssclgdpptscaegtdityydsdsktckvlaascpsgentfesevecqvacgap
ieg
>d1kigi_ 7.8.1.2.2 Anticoagulant protein, factor Xa inhibitor {Soft tick (Ornithodoros moubata)}
ynrlcikprdwidecdsneggerayfrngkggcdsfwicpedhtgadyyssyrdcfnaci
>d1tap__ 7.8.1.2.2 Anticoagulant protein, factor Xa inhibitor {Soft tick (Ornithodoros moubata)}
ynrlcikprdwidecdsneggerayfrngkggcdsfwicpedhtgadyyssyrdcfnaci
>d1tcp__ 7.8.1.2.2 Anticoagulant protein, factor Xa inhibitor {Soft tick (Ornithodoros moubata)}
ynrlcikprdwidecdsneggerayfrngkggcdsfwicpedhtgadyyssyrdcfnaci
>d1dfna_ 7.9.1.1.1 Defensin HNP-3 {Human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1dfnb_ 7.9.1.1.1 Defensin HNP-3 {Human (Homo sapiens)}
dcycripaciagerrygtciyqgrlwafcc
>d1bnb__ 7.9.1.1.2 Beta-defensin 12 {Bovine (Bos taurus)}
aplscgrnggvcipircpvpmrqigtcfgrpvkccrsw
>d1b8wa_ 7.9.1.1.3 Defensin-like peptide 1 {Duckbilled platypus (Ornithorhynchus anatinus)}
fvqhrprdcesingvcrhkdtvncreifladcyndgqkccrk
>d1bds__ 7.9.1.1.4 BDs-I defensin {Sea anemone (Anemonia sulcata)}
aapcfcsgkpgrgdlwilrgtcpggygytsncykwpniccyph
>d2bds__ 7.9.1.1.4 BDs-I defensin {Sea anemone (Anemonia sulcata)}
aapcfcsgkpgrgdlwilrgtcpggygytsncykwpniccyph
>d1sh1__ 7.9.1.1.5 Sea anemone neurotoxin-1 {Sea anemone (Stichodactyla helianthus)}
aackcddegpdirtapltgtvdlgscnagwekcasyytiiadccrkkk
>d1shi__ 7.9.1.1.5 Sea anemone neurotoxin-1 {Sea anemone (Stichodactyla helianthus)}
aackcddegpdirtapltgtvdlgscnagwekcasyytiiadccrkkk
>d2sh1__ 7.9.1.1.5 Sea anemone neurotoxin-1 {Sea anemone (Stichodactyla helianthus)}
aackcddegpdirtapltgtvdlgscnagwekcasyytiiadccrkkk
>d1atx__ 7.9.1.1.6 Sea anemone toxin IA {Sea anemone (Anemonia sulcata)}
gaaclcksdgpntrgnsmsgtiwvfgcpsgwnncegraiigycckq
>d1ahl__ 7.9.1.1.7 Anthopleurin-A {Giant green sea anemone (Anthopleura xanthogrammica)}
gvsclcdsdgpsvrgntlsgtlwlypsgcpsgwhnckahgptigwcckq
>d1apf__ 7.9.1.1.8 Anthopleurin-B {Giant green sea anemone (Anthopleura xanthogrammica)}
gvpclcdsdgprprgntlsgilwfypsgcpsgwhnckahgpnigwcckk
>d1bhta1 7.10.1.1.1 (35-126) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rrntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkark
qclwfpfnsmssgvkkefghefdlyenkdyir
>d1bhtb1 7.10.1.1.1 (336-426) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkarkq
clwfpfnsmssgvkkefghefdlyenkdyir
>d1nk1a1 7.10.1.1.1 (38-125) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
tihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkarkqcl
wfpfnsmssgvkkefghefdlyenkdyi
>d1nk1b1 7.10.1.1.1 (38-125) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
tihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkarkqcl
wfpfnsmssgvkkefghefdlyenkdyi
>d2hgf__ 7.10.1.1.1 Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
gqrkrrntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfd
karkqclwfpfnsmssgvkkefghefdlyenkdyirn
>d1ans__ 7.11.1.1.1 Neurotoxin III (ATX III) {Sea anemone (Anemonia sulcata)}
rsccpcywggcpwgqncypegcsgpkv
>d1ajj__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
pcsafefhclsgecihsswrcdggpdckdksdeenca
>d1cr8a_ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
pggchtdefqcrldglciplrwrcdgdtdcmdssdekscegv
>d1d2la_ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
gsppqcqpgefacansrciqerwkcdgdndcldnsdeapalchqh
>d1ldl__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
avgdrcernefqcqdgkcisykwvcdgsaecqdgsdesqetclsvt
>d1ldr__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
lsvtcksgdfscggrvnrcipqfwrcdgqvdcdngsdeqgc
>d1ab1__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1cbn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccm__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1ccn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1cnr__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpealcatytgciiipgatcpgdyan
>d1crn__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtpeaicatytgciiipgatcpgdyan
>d1cxra_ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1bhp__ 7.13.1.1.2 beta-Purothionin {Wheat (Triticum aestivum)}
kscckstlgrncynlcrargaqklcanvcrckltsglscpkdfpk
>d2plh__ 7.13.1.1.3 alpha-1-Purothionin {Wheat (Triticum aestivum)}
ksccrstlgrncynlcrargaqklcagvcrckissglscpkgfpk
>d1ed0a_ 7.13.1.1.4 Viscotoxin a3 {European mistletoe (Viscum album)}
ksccpnttgrniynacrltgaprptcaklsgckiisgstcpsdypk
>d1krn__ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
dcyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkgp
wcfttdpsvrweycnlkkc
>d1pk4__ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
dcyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkgp
wcfttdpsvrweycnlkkc
>d1pmka_ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
cyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkgpw
cfttdpsvrweycnlkkc
>d1pmkb_ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
cyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkgpw
cfttdpsvrweycnlkkc
>d1pmla_ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
sdcyfgngsayrgthsltesgasclpwnsmiligkvytaqnpsaqalglgkhnycrnpdg
dakpwchvlknrrltweycdvpscst
>d1pmlb_ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
sdcyfgngsayrgthsltesgasclpwnsmiligkvytaqnpsaqalglgkhnycrnpdg
dakpwchvlknrrltweycdvpscst
>d1pmlc_ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
sdcyfgngsayrgthsltesgasclpwnsmiligkvytaqnpsaqalglgkhnycrnpdg
dakpwchvlknrrltweycdvpscs
>d2pk4__ 7.14.1.1.1 Plasminogen kringle 4 {Human (Homo sapiens)}
qdcyhgdgqsyrgtssttttgkkcqswssmtphrhqktpenypnagltmnycrnpdadkg
pwcfttdpsvrweycnlkkc
>d1b2ia_ 7.14.1.1.2 Plasminogen kringle 2 {Human (Homo sapiens)}
tseecmhgsgenydgkisktmsglecqawdsqsphahgyipskfpnknlkknycrnpdre
lrpwcfttdpnkrwelcdiprct
>d1tpka_ 7.14.1.1.2 Plasminogen kringle 2 {Human (Homo sapiens)}
gnsdcyfgngsayrgthsltesgasclpwnsmiligkvytaqnpsaqalglgkhnycrnp
dgdakpwchvlknrrltweycdvpscst
>d1ceaa_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceab_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1ceba_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1cebb_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d1hpj__ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
cktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqgp
wcyttdpekrydycdilec
>d1hpk__ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
cktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqgp
wcyttdpekrydycdilec
>d1pkr__ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
ecktgngknyrgtmsktkngitcqkwsstsphrprfspathpsegleenycrnpdndpqg
pwcyttdpekrydycdilec
>d5hpga_ 7.14.1.1.3 Plasminogen kringles {Human (Homo sapiens)}
dcmfgngkgyrgkrvttvtgtpcqdwaaqephrhsiftpetnpragleknycrnpdgdvg
gpwcyttnprklydycdvpqcaap
>d2pf1_1 7.14.1.1.4 (66-156) Prothrombin fragment 1 and 2 {Bovine (Bos taurus)}
caegvgmnyrgnvsvtrsgiecqlwrsryphkpeinstthpgadlrenfcrnpdgsitgp
wcyttsptlrreecsvpvcgqdrvtvevipr
>d2pf2_1 7.14.1.1.4 (66-146) Prothrombin fragment 1 and 2 {Bovine (Bos taurus)}
caegvgmnyrgnvsvtrsgiecqlwrsryphkpeinstthpgadlrenfcrnpdgsitgp
wcyttsptlrreecsvpvcgq
>d2spt_1 7.14.1.1.4 (66-145) Prothrombin fragment 1 and 2 {Bovine (Bos taurus)}
caegvgmnyrgnvsvtrsgiecqlwrsryphkpeinstthpgadlrenfcrnpdgsitgp
wcyttsptlrreecsvpvcg
>d1a0ha1 7.14.1.1.5 (164-270) Meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d2hppp_ 7.14.1.1.6 Meizothrombin domain {Human (Homo sapiens)}
cvpdrgreyrgrlavttsgsrclawsseqakalskdqdfnpavplaenfcrnpdgdeega
wcyvadqpgdfeycnlnyc
>d2hpqp_ 7.14.1.1.6 Meizothrombin domain {Human (Homo sapiens)}
cvpdrgqqyqgrlavtthglpclawasaqakalskhqdfnsavqlvenfcrnpdgdeegv
wcyvagkpgdfgycdlnyc
>d1kdu__ 7.14.1.1.7 Urokinase-type plasminogen activator {Human (Homo sapiens)}
tcyegnghfyrgkastdtmgrpclpwnsatvlqqtyhahrsdalqlglgkhnycrnpdnr
rrpwcyvqvglkplvqecmvhdcad
>d1urk_2 7.14.1.1.7 (50-135) Urokinase-type plasminogen activator {Human (Homo sapiens)}
cyegnghfyrgkastdtmgrpclpwnsatvlqqtyhahrsdalqlglgkhnycrnpdnrr
rpwcyvqvglkplvqecmvhdcadgk
>d1kiv__ 7.14.1.1.8 Apolipoprotein (A) IV-10/M66 variant {Human (Homo sapiens)}
cyhgngqsyrgtfsttvtgrtcqswssmtphrhqrtpenypndgltmnycrnpdadtgpw
cftmdpsirweycnltrc
>d3kiv__ 7.14.1.1.8 Apolipoprotein (A) IV-10/M66 variant {Human (Homo sapiens)}
qcyhgngqsyrgtfsttvtgrtcqswssmtphrhqrtpenypndgltmnycrnpdadtgp
wcfttdpsirweycnltrc
>d4kiv__ 7.14.1.1.8 Apolipoprotein (A) IV-10/M66 variant {Human (Homo sapiens)}
qcyhgngqsyrgtfsttvtgrtcqswssmtphrhqrtpenypndgltmnycrnpdadtgp
wcftmdpsirreycnltrc
>d1bhta2 7.14.1.1.9 (127-210) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcseve
>d1bhtb2 7.14.1.1.9 (427-509) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcsev
>d1nk1a2 7.14.1.1.9 (126-209) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
rnciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeeg
gpwcftsnpevryevcdipqcsev
>d1nk1b2 7.14.1.1.9 (126-209) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
rnciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeeg
gpwcftsnpevryevcdipqcsev
>d1pdc__ 7.14.1.2.1 PDC-109, collagen-binding type II domain {Bovine (Bos taurus)}
dyakcvfpfiyggkkyetctkigsmwmswcslspnydkdrawkyc
>d1qo6a1 7.14.1.2.2 (42-101) Fibronectin {Human (Homo sapiens)}
avtqtyggnsngepcvlpftyngrtfyscttegrqdghlwcsttsnyeqdqkysfctdht
>d2fn2__ 7.14.1.2.2 Fibronectin {Human (Homo sapiens)}
vlvqtrggnsngalchfpflynnhnytdctsegrrdnmkwcgttqnydadqkfgfcpma
>d1ck7a3 7.14.1.2.3 (217-277) Gelatinase A (MMP-2) type II modules {Human (Homo sapiens)}
egqvvrvkygnadgeyckfpflfngkeynsctdtgrsdgflwcsttynfekdgkygfcph
e
>d1ck7a4 7.14.1.2.3 (278-335) Gelatinase A (MMP-2) type II modules {Human (Homo sapiens)}
alftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpet
>d1ck7a5 7.14.1.2.3 (336-393) Gelatinase A (MMP-2) type II modules {Human (Homo sapiens)}
amstvggnsegapcvfpftflgnkyesctsagrsdgkmwcattanydddrkwgfcpdq
>d1cxwa_ 7.14.1.2.3 Gelatinase A (MMP-2) type II modules {Human (Homo sapiens)}
talftmggnaegqpckfpfrfqgtsydscttegrtdgyrwcgttedydrdkkygfcpeta
>d1choi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1csoi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactieyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1ct0i_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactseyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1ct2i_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactteyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1ct4i_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactveyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1hjai_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactkeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1omt__ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
laavsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1omu__ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
laavsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1ppfi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
laavsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1sgpi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactaeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1sgqi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactgeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1sgri_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
vdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1tur__ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
laavsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1tus__ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
laavsvdcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d3sgbi_ 7.15.1.1.1 Ovomucoid III domain {Turkey (Meleagris gallopavo)}
dcseypkpactleyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1ovoa_ 7.15.1.1.2 Ovomucoid III domain {Japanese quail (Coturnix coturnix japonica)}
laavsvdcseypkpacpkdyrpvcgsdnktysnkcnfcnavvesngtltlnhfgkc
>d1ovob_ 7.15.1.1.2 Ovomucoid III domain {Japanese quail (Coturnix coturnix japonica)}
laavsvdcseypkpacpkdyrpvcgsdnktysnkcnfcnavvesngtltlnhfgkc
>d1ovoc_ 7.15.1.1.2 Ovomucoid III domain {Japanese quail (Coturnix coturnix japonica)}
laavsvdcseypkpacpkdyrpvcgsdnktysnkcnfcnavvesngtltlnhfgkc
>d1ovod_ 7.15.1.1.2 Ovomucoid III domain {Japanese quail (Coturnix coturnix japonica)}
laavsvdcseypkpacpkdyrpvcgsdnktysnkcnfcnavvesngtltlnhfgkc
>d3ovo__ 7.15.1.1.2 Ovomucoid III domain {Japanese quail (Coturnix coturnix japonica)}
laavsvdcseypkpacpkdyrpvcgsdnktysnkcnfcnavvesngtltlnhfgkc
>d2ovo__ 7.15.1.1.3 Ovomucoid III domain {Silver pheasant (Lophura nycthemera)}
laavsvdcseypkpactmeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d4ovo__ 7.15.1.1.3 Ovomucoid III domain {Silver pheasant (Lophura nycthemera)}
laavsvdcseypkpactmeyrplcgsdnktygnkcnfcnavvesngtltlshfgkc
>d1cgii_ 7.15.1.1.4 Secretory trypsin inhibitor {Human (Homo sapiens)}
dslgreakcynelngctyeyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1cgji_ 7.15.1.1.4 Secretory trypsin inhibitor {Human (Homo sapiens)}
dslgreakcynelngctleyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1hpt__ 7.15.1.1.4 Secretory trypsin inhibitor {Human (Homo sapiens)}
dslgreakcynelngctyeyrpvcgtdgdtypnecvlcfenrkrqtsiliqksgpc
>d1tgsi_ 7.15.1.1.5 Secretory trypsin inhibitor {Porcine (Sus scrofa)}
tspqreatctsevsgcpkiynpvcgtdgitysnecvlcsenkkrqtpvliqksgpc
>d1tbqr1 7.15.1.1.6 (1-51) Rhodniin {Bug (Rhodnius prolixus)}
eggepcacphalhrvcgsdgetysnpctlncakfngkpelvkvhdgpcepd
>d1tbqr2 7.15.1.1.6 (52-103) Rhodniin {Bug (Rhodnius prolixus)}
ededvcqecdgdeykpvcgsdditydnncrlecasissspgvelkhegpcrt
>d1tbqs1 7.15.1.1.6 (1-51) Rhodniin {Bug (Rhodnius prolixus)}
eggepcacphalhrvcgsdgetysnpctlncakfngkpelvkvhdgpcepd
>d1tbqs2 7.15.1.1.6 (52-103) Rhodniin {Bug (Rhodnius prolixus)}
ededvcqecdgdeykpvcgsdditydnncrlecasissspgvelkhegpcrt
>d1tbrr1 7.15.1.1.6 (1-51) Rhodniin {Bug (Rhodnius prolixus)}
eggepcacphalhrvcgsdgetysnpctlncakfngkpelvkvhdgpcepd
>d1tbrr2 7.15.1.1.6 (52-103) Rhodniin {Bug (Rhodnius prolixus)}
ededvcqecdgdeykpvcgsdditydnncrlecasissspgvelkhegpcrt
>d1tbrs1 7.15.1.1.6 (1-51) Rhodniin {Bug (Rhodnius prolixus)}
eggepcacphalhrvcgsdgetysnpctlncakfngkpelvkvhdgpcepd
>d1tbrs2 7.15.1.1.6 (52-103) Rhodniin {Bug (Rhodnius prolixus)}
ededvcqecdgdeykpvcgsdditydnncrlecasissspgvelkhegpcrt
>d1bmoa3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bmob3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1nuba3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1nubb3 7.15.1.1.7 (78-135) Domain of BM-40/SPARC/osteonectin {Human (Homo sapiens)}
cqdptscpapigefekvcsndnktfdsschffatkctlegtkkghklhldyigpckyi
>d1bus__ 7.15.1.1.8 Seminal plasma inhibitor IIa {Bovine (Bos taurus)}
xgaqvdcaefkdpkvyctresnphcgsngetygnkcafckavmksggkinlkhrgkc
>d2bus__ 7.15.1.1.8 Seminal plasma inhibitor IIa {Bovine (Bos taurus)}
xgaqvdcaefkdpkvyctresnphcgsngetygnkcafckavmksggkinlkhrgkc
>d1pce__ 7.15.1.1.9 PEC-60 peptide {Pig (Sus scrofa)}
ekqvfsrmpicehmtespdcsriydpvcgtdgvtyesecklclarienkqdiqivkdgec
>d1an1i_ 7.15.1.1.10 Leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kvcacpkilkpvcgsdgrtyansciarcngvsiksegscp
>d1ldtl_ 7.15.1.1.10 Leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kkvcacpkilkpvcgsdgrtyansciarcngvsiksegscptgiln
>d4sgbi_ 7.15.1.2.1 Plant chymotrypsin inhibitor {Potato tuber (Solanum tuberosum)}
pictnccagykgcnyysangaficegqsdpkkpkacplncdphiayskcpr
>d1tih__ 7.15.1.2.2 Plant chymotrypsin inhibitor {Tobacco (Nicotiana alata)}
drictnccagtkgckyfsddgtfvcegesdprnpkacprncdpriaygicpla
>e1qh2.1b 7.15.1.2.3 Chymotrypsin inhibitor (c2) {Winged tobacco (Nicotiana alata)}
rictnccagkkgckyfsddgtficeges
>d1ce3a_ 7.15.1.2.4 Multidomain proteinase inhibitor {Winged tobacco (Nicotiana alata)}
mkactlncdpriaygvcprseekkndrictnccagtkgckyfsddgtfvceges
>d1pcp_1 7.16.1.1.1 (1-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
ekpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d1pcp_2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d1posa1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d1posa2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d1posb1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d1posb2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d1pspa1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d1pspa2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d1pspb1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d1pspb2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d2pspa1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d2pspa2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d2pspb1 7.16.1.1.1 (2-53) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
kpaacrcsrqdpknrvncgfpgitsdqcftsgccfdsqvpgvpwcfkplpaq
>d2pspb2 7.16.1.1.1 (54-106) Pancreatic spasmolytic polypeptide {Pig (Sus scrofa)}
eseecvmqvsarkncgypgispedcaarnccfsdtipevpwcffpmsvedchy
>d1ps2__ 7.16.1.1.2 PNR-2/PS2 {Human (Homo sapiens)}
eaqtetctvaprerqncgfpgvtpsqcankgccfddtvrgvpwcfypntidvppeeesef
>d1pdga_ 7.17.1.1.1 Platelet-derived growth factor BB {Human (Homo sapiens)}
epamiaecktrtevfeisrrlidrtnanflvwppcvevqrcsgccnnrnvqcrptqvqlr
pvqvrkieivrkkpifkkatvtledhlackcetvaa
>d1pdgb_ 7.17.1.1.1 Platelet-derived growth factor BB {Human (Homo sapiens)}
iaepamiaecktrtevfeisrrlidrtnanflvwppcvevqrcsgccnnrnvqcrptqvq
lrpvqvrkieivrkkpifkkatvtledhlackce
>d1fltv_ 7.17.1.1.2 Vascular endothelial growth factor, VEGF {Human (Homo sapiens)}
evvkfmdvyqrsychpietlvdifqeypdeieyifkpscvplmrcggccndeglecvpte
esnitmqimrikphqgqhigemsflqhnkcecrpk
>d2tgi__ 7.17.1.2.2 TGF-beta2 {Human (Homo sapiens)}
aldaaycfrnvqdncclrplyidfkrdlgwkwihepkgynanfcagacpylwssdtqhsr
vlslyntinpeasaspccvsqdlepltilyyigktpkieqlsnmivksckcs
>d1klaa_ 7.17.1.2.3 TGF-beta1 {Human (Homo sapiens)}
aldtnycfssteknccvrqlyidfrkdlgwkwihepkgyhanfclgpcpyiwsldtqysk
vlalynqhnpgasaapccvpqaleplpivyyvgrkpkveqlsnmivrsckcs
>d1bmp__ 7.17.1.2.4 Bone morphogenetic protein-7 (BMP-7) {Human (Homo sapiens)}
qackkhelyvsfrdlgwqdwiiapegyaayycegecafplnsymnatnhaivqtlvhfin
petvpkpccaptqlnaisvlyfddssnvilkkyrnmvvracgch
>d2bmpa_ 7.17.1.2.5 Bone morphogenetic protein-2 (BMP-2) {Human (Homo sapiens)}
lkssckrhplyvdfsdvgwndwivappgyhafychgecpfpladhlnstnhaivqtlvns
vnskipkaccvptelsaismlyldenekvvlknyqdmvvegcgcr
>d1agqa_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
nrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkv
gqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1bnda_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
gqlsvcdsisewvtaadkktavdmsggtvtvlekvpvskgqlkqyfyetkcnpmgytkeg
crgidkrhwnsqcrttqsyvraltmdskkrigwrfiridtscvctltik
>d1bndb_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
rgevsvcdseslwvtdkssaidirghqvtvlgeiktqnspvkqyfyetrckearpvkngc
rgiddkhwnsqcktsqtyvraltsennklvgwrwiridtscvcalsrk
>d1b8mb_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
gelavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadnaeeggp
gaggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsrtgra
>d1wwwv_ 7.17.1.3.4 beta-Nerve growth factor {Human (Homo sapiens)}
sshpifhrgefsvcdsvsvwvgdkttatdikgkevmvlgevninnsvfkqyffetkcrdp
npvdsgcrgidskhwnsycttthtfvkaltmdgkqaawrfiridtacvcvlsrk
>d1hcna_ 7.17.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
qdcpectlqenpffsqpgapilqcmgccfsrayptplrskktmlvqknvtsestccvaks
ynrvtvmggfkvenhtachcstcyy
>d1hcnb_ 7.17.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
keplrprcrpinatlavekegcpvcitvntticagycptmtrvlqgvlpalpqvvcnyrd
vrfesirlpgcprgvnpvvsyavalscqcalcrrsttdcggpkdhpltcd
>d1hrpa_ 7.17.1.4.1 Gonadotropin, A and B chains {Human (Homo sapiens)}
tqdcpectlqenpffsqpgapilqcmgccfsrayptplrskktmlvqknvtsestccvak
synrvtvmggfkvenhtachcstcyy
>d1aoca_ 7.17.1.5.1 Coagulogen {Japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1hcc__ 7.18.1.1.1 Factor H, 15th and 16th modules {Human (Homo sapiens)}
eglpcksppeishgvvahmsdsyqygeevtykcfegfgidgpaiakclgekwshppsci
>d1hfh_1 7.18.1.1.1 (1-63) Factor H, 15th and 16th modules {Human (Homo sapiens)}
ekipcsqppqiehgtinssrssqesyahgtklsytceggfriseenettcymgkwssppq
ceg
>d1hfh_2 7.18.1.1.1 (64-120) Factor H, 15th and 16th modules {Human (Homo sapiens)}
lpcksppeishgvvahmsdsyqygeevtykcfegfgidgpaiakclgekwshppsci
>d1hfi__ 7.18.1.1.1 Factor H, 15th and 16th modules {Human (Homo sapiens)}
ekipcsqppqiehgtinssrssqesyahgtklsytceggfriseenettcymgkwssppq
ce
>d1vvc_1 7.18.1.1.2 (1-58) Complement control protein {Vaccinia virus}
vkcqsppsisngrhngyedfytdgsvvtyscnsgyslignsgvlcsggewsdpptcqi
>d1vvc_2 7.18.1.1.2 (59-118) Complement control protein {Vaccinia virus}
vkcphptisngylssgfkrsysyndnvdfkckygyklsgsssstcspgntwkpelpkcvr
>d1vvd_1 7.18.1.1.2 (1-58) Complement control protein {Vaccinia virus}
vkcqsppsisngrhngyedfytdgsvvtyscnsgyslignsgvlcsggewsdpptcqi
>d1vvd_2 7.18.1.1.2 (59-118) Complement control protein {Vaccinia virus}
vkcphptisngylssgfkrsysyndnvdfkckygyklsgsssstcspgntwkpelpkcvr
>d1vve_1 7.18.1.1.2 (1-58) Complement control protein {Vaccinia virus}
vkcqsppsisngrhngyedfytdgsvvtyscnsgyslignsgvlcsggewsdpptcqi
>d1vve_2 7.18.1.1.2 (59-118) Complement control protein {Vaccinia virus}
vkcphptisngylssgfkrsysyndnvdfkckygyklsgsssstcspgntwkpelpkcvr
>d1ckla1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckla2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklb1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklb2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklc1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklc2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1ckld1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckld2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1ckle1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1ckle2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1cklf1 7.18.1.1.3 (1-62) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
ceepptfeameligkpkpyyeigervdykckkgyfyipplathticdrnhtwlpvsddac
yr
>d1cklf2 7.18.1.1.3 (63-126) CD46 (membrane cofactor protein, MCP) {Human (Homo sapiens)}
etcpyirdplngqavpangtyefgyqmhficnegyyligeeilycelkgsvaiwsgkppi
cekv
>d1c1za1 7.18.1.1.4 (1-62) beta2-glycoprotein I {Human (Homo sapiens)}
grtcpkpddlpfstvvplktfyepgeeitysckpgyvsrggmrkficpltglwpintlkc
tp
>d1c1za2 7.18.1.1.4 (63-120) beta2-glycoprotein I {Human (Homo sapiens)}
rvcpfagilengavryttfeypntisfscntgfylngadsakcteegkwspelpvcap
>d1c1za3 7.18.1.1.4 (121-183) beta2-glycoprotein I {Human (Homo sapiens)}
iicpppsiptfatlrvykpsagnnslyrdtavfeclpqhamfgndtitctthgnwtklpe
cre
>d1c1za4 7.18.1.1.4 (184-243) beta2-glycoprotein I {Human (Homo sapiens)}
vkcpfpsrpdngfvnypakptlyykdkatfgchdgysldgpeeiectklgnwsampscka
>d1c1za5 7.18.1.1.4 (244-326) beta2-glycoprotein I {Human (Homo sapiens)}
scklpvkkatvvyqgervkiqekfkngmlhgdkvsffcknkekkcsytedaqcidgtiev
pkcfkehsslafwktdasdvkpc
>d1quba1 7.18.1.1.4 (1-62) beta2-glycoprotein I {Human (Homo sapiens)}
grtcpkpddlpfstvvplktfyepgeeitysckpgyvsrggmrkficpltglwpintlkc
tp
>d1quba2 7.18.1.1.4 (63-120) beta2-glycoprotein I {Human (Homo sapiens)}
rvcpfagilengavryttfeypntisfscntgfylngadsakcteegkwspelpvcap
>d1quba3 7.18.1.1.4 (121-183) beta2-glycoprotein I {Human (Homo sapiens)}
iicpppsiptfatlrvykpsagnnslyrdtavfeclpqhamfgndtitctthgnwtklpe
cre
>d1quba4 7.18.1.1.4 (184-243) beta2-glycoprotein I {Human (Homo sapiens)}
vkcpfpsrpdngfvnypakptlyykdkatfgchdgysldgpeeiectklgnwsampscka
>d1quba5 7.18.1.1.4 (244-326) beta2-glycoprotein I {Human (Homo sapiens)}
sckvpvkkatvvyqgervkiqekfkngmlhgdkvsffcknkekkcsytedaqcidgtiev
pkcfkehtdasdvkpc
>d1bgk__ 7.19.1.1.1 Sea anemone toxin k {Sea anemone (Bunodosoma granulifera), BGK}
vcrdwfketacrhakslgncrtsqkyrancaktcelc
>d1bei__ 7.19.1.1.2 Sea anemone toxin k {Sun anemone (Stichodactyla helianthus), SHK}
rscidtipksrctafqckhsmxyrlsfcrktcgtc
>d1c2ua_ 7.19.1.1.2 Sea anemone toxin k {Sun anemone (Stichodactyla helianthus), SHK}
rsxidtipksrctafqckhsakyrlsfcrktcgt
>d1roo__ 7.19.1.1.2 Sea anemone toxin k {Sun anemone (Stichodactyla helianthus), SHK}
rscidtipksrctafqckhsmkyrlsfcrktcgtc
>d2ech__ 7.20.1.1.1 Echistatin {Echis carinatus}
ecesgpccrnckflkegtickrargddmddycngktcdcprnphkgpat
>d1fvl__ 7.20.1.1.2 Flavoridin {Snake (Trimeresurus flavoviridis)}
geecdcgspsnpccdaatcklrpgaqcadglccdqcrfkkkrticriargdfpddrctgl
sndcprwndl
>d1kst__ 7.20.1.1.3 Kistrin {Agkistrodon rhodostoma}
gkecdcsspenpccdaatcklrpgaqcgeglcceqckfsragkicriprgdmpddrctgq
sadcpryh
>d2bbkl_ 7.21.1.1.1 Methylamine dehydrogenase {Paracoccus denitrificans}
tdprakwvpqdndiqacdywrhcsidgnicdcsggsltncppgtklataswvascynptd
gqsyliayrdccgynvsgrcpclntegelpvyrpefandiiwcfgaeddamtyhctispi
vgkas
>d1ata__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1atb__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1atd__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1ate__ 7.22.1.1.1 Ascaris trypsin inhibitor {Pig roundworm (Ascaris Lumbricoides), var. Suum}
eaekctkpneqwtkcggcegtcaqkivpctreckpprceciasagfvrdaqgncikfedc
pk
>d1eaic_ 7.22.1.1.2 Ascaris elastase inhibitor {Pig roundworm (Ascaris suum)}
gqescgpnevwtectgcemkcgpdentpcplmcrrpscecspgrgmrrtndgkcipasqc
p
>d1eaid_ 7.22.1.1.2 Ascaris elastase inhibitor {Pig roundworm (Ascaris suum)}
gqescgpnevwtectgcemkcgpdentpcplmcrrpscecspgrgmrrtndgkcipasqc
p
>d1coua_ 7.22.1.1.3 Anticoagulant protein {Dog hookworm (Ancylostoma caninum)}
katmqcgenekydscgskecdkkckydgveeeddeepnvpclvrvchqdcvceegfyrnk
ddkcvsaedceldnmdfiypgtrnp
>d1ccva_ 7.22.1.1.4 Chymotrypsin inhibitor AMCI {Honeybee (Apis mellifera)}
eecgpnevfntcgsacaptcaqpktrictmqcrigcqcqegflrngegacvlpenc
>d1apj__ 7.23.1.1.1 Fibrillin {Human (Homo sapiens)}
saqdlrmsycyakfeggkcsspksrnhskqecccalkgegwgdpcelcptepdeafrqic
pygsgiivgpddsa
>d1exta1 7.24.1.1.1 (13-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
svcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhcl
>d1exta2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1exta3 7.24.1.1.1 (116-172) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclpqien
>d1extb1 7.24.1.1.1 (11-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
mdsvcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhc
l
>d1extb2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1extb3 7.24.1.1.1 (116-168) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvscsnckkslectklclp
>d1ncfa1 7.24.1.1.1 (11-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
mdsvcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhc
l
>d1ncfa2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1ncfa3 7.24.1.1.1 (116-150) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenec
>d1ncfb1 7.24.1.1.1 (14-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
vcpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhcl
>d1ncfb2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1ncfb3 7.24.1.1.1 (116-155) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvscsn
>d1tnrr1 7.24.1.1.1 (15-71) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
cpqgkyihpqnnsicctkchkgtylyndcpgpgqdtdcrecesgsftasenhlrhcl
>d1tnrr2 7.24.1.1.1 (72-115) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
scskcrkemgqveissctvdrdtvcgcrknqyrhywsenlfqcf
>d1tnrr3 7.24.1.1.1 (116-153) Tumor necrosis factor (TNF) receptor {Human (Homo sapiens)}
ncslclngtvhlscqekqntvctchagfflrenecvsc
>d1d0gr1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gr2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gr3 7.24.1.1.2 (102-128) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhk
>d1d0gs1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gs2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gs3 7.24.1.1.2 (102-130) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhkes
>d1d0gt1 7.24.1.1.2 (21-61) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
sspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d0gt2 7.24.1.1.2 (62-101) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d0gt3 7.24.1.1.2 (102-130) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhkes
>d1d4va1 7.24.1.1.2 (69-114) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
pqqkrsspseglcppghhisedgrdcisckygqdysthwndllfcl
>d1d4va2 7.24.1.1.2 (115-154) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
rctrcdsgevelspctttrntvcqceegtfreedspemcr
>d1d4va3 7.24.1.1.2 (155-185) Death receptor-5 (dr5) fragment {Human (Homo sapiens)}
kcrtgcprgmvkvgdctpwsdiecvhkesgd
>d1vgh__ 7.25.1.1.1 Heparin-binding domain from vascular endothelial growth factor {Human (Homo sapiens)}
arqenpcgpcserrkhlfvqdpqtckcsckntdsrckarqlelnertcrcdkprr
>d2vgh__ 7.25.1.1.1 Heparin-binding domain from vascular endothelial growth factor {Human (Homo sapiens)}
arqenpcgpcserrkhlfvqdpqtckcsckntdsrckarqlelnertcrcdkprr
>d1afp__ 7.26.1.1.1 Antifungal protein (AGAFP) {Mold (Aspergillus giganteus)}
atyngkcykkdnickykaqsgktaickcyvkkcprdgakcefdsykgkcyc
>d1fbr_1 7.27.1.1.1 (1-46) Fibronectin {Human (Homo sapiens)}
aekcfdhaagtsyvvgetwekpyqgwmmvdctclgegsgritctsr
>d1fbr_2 7.27.1.1.1 (47-93) Fibronectin {Human (Homo sapiens)}
nrcndqdtrtsyrigdtwskkdnrgnllqcictgngrgewkcerhts
>d1qgba1 7.27.1.1.1 (17-60) Fibronectin {Human (Homo sapiens)}
skpgcydngkhyqinqqwertylgnalvctcyggsrgfnceskp
>d1qgba2 7.27.1.1.1 (61-109) Fibronectin {Human (Homo sapiens)}
eaeetcfdkytgntyrvgdtyerpkdsmiwdctcigagrgrisctianr
>d1qo6a2 7.27.1.1.1 (1-41) Fibronectin {Human (Homo sapiens)}
yghcvtdsgvvysvgmqwlktqgnkqmlctclgngvscqet
>d1tpg_2 7.27.1.1.2 (1-50) Tissue-type plasminogen activator, t-PA {Human (Homo sapiens)}
syqvicrdektqmiyqqhqswlrpvlrsnrveycwcnsgraqchsvpvks
>d1tpm__ 7.27.1.1.2 Tissue-type plasminogen activator, t-PA {Human (Homo sapiens)}
syqvicrdektqmiyqqhqswlrpvlrsnrveycwcnsgraqchsvpvks
>d1tpn__ 7.27.1.1.2 Tissue-type plasminogen activator, t-PA {Human (Homo sapiens)}
syqvicrdektqmiyqqhqswlrpvlrsnrveycwcnsgraqchsvpvks
>d1icfi_ 7.28.1.1.1 MHC class II associated p41 invariant chain fragment {Human (Homo sapiens)}
ltkcqeevshipavhpgsfrpkcdengnylplqcygsigycwcvfpngtevpntrsrghh
ncses
>d1icfj_ 7.28.1.1.1 MHC class II associated p41 invariant chain fragment {Human (Homo sapiens)}
ltkcqeevshipavhpgsfrpkcdengnylplqcygsigycwcvfpngtevpntrsrghh
ncses
>d1ct7a_ 7.29.1.1.1 Endo-1;4-beta-xylanase A CBDX {Pseudomonas fluorescens, subsp. cellulosa}
mgnqqcnwygtlyplcvtttngwgwedqrsciarstcaaqpapfgivgsg
>d1qlda_ 7.29.1.1.1 Endo-1;4-beta-xylanase A CBDX {Pseudomonas fluorescens, subsp. cellulosa}
mgnqqcnwygtlyplcvtttngwgwedqrsciarstcaaqpapfgivgsg
>d2pf1_2 7.30.1.1.2 (36-65) Prothrombin {Bovine (Bos taurus)}
satdafwakytacesarnpreklneclegn
>d2pf2_2 7.30.1.1.2 (1-65) Prothrombin {Bovine (Bos taurus)}
ankgflxxvrkgnlrxxclxxpcsrxxafxalxslsatdafwakytacesarnpreklne
clegn
>d2spt_2 7.30.1.1.2 (1-65) Prothrombin {Bovine (Bos taurus)}
ankgflxxvrkgnlxrxclxxpcsrxxafxalxslsatdafwakytacesarnpreklne
clegn
>d1cfh__ 7.30.1.1.3 Coagulation factor IX (IXa) {Human (Homo sapiens)}
ynsgkleefvqgnlerecmeekcsfeearevfenterttefwkqyvd
>d1d6ga_ 7.31.1.1.1 Cholecystokinin A receptor, N-domain {Human (Homo sapiens)}
mdvvdsllvngsnitppcelglenetlfcldqprpskewqpaqvill
>d1vpu__ 7.32.1.1.1 HIV-1 VPU cytoplasmic domain {Human immunodeficiency virus, type 1}
lqidrlidriteraedsgnesegdqeelsalverghlapwdvddl
>d1isua_ 7.33.1.1.1 HIPIP (high potential iron protein) {Rodocyclus tenuis}
gtnaamrkafnyqdtakngkkcsgcaqfvpgasptaaggckvipgdnqiapggycdafiv
kk
>d1isub_ 7.33.1.1.1 HIPIP (high potential iron protein) {Rodocyclus tenuis}
gtnaamrkafnyqdtakngkkcsgcaqfvpgasptaaggckvipgdnqiapggycdafiv
kk
>d1b0ya_ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaadnataialkynqdatkservaaarpglppeeqqcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1ckua_ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1ckub_ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1hip__ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaadnataialkynqdatkservaaarpglppeeqhcadcqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1hrq__ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1hrr__ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1neh__ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1noe__ 7.33.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
asapanavaaddataialkynqdatkservaaarpglppeeqhcancqfmqadaagatde
wkgcqlfpgklinvngwsaswtlkag
>d3hipa_ 7.33.1.1.3 HIPIP (high potential iron protein) {Chromatium purpuratum}
vpanavtesdpaavalkyhrdaasservaaarpglppeeqhcencqfmnpdsaaadwkgc
qlfpgklinlsgwcaswtlrag
>d3hipb_ 7.33.1.1.3 HIPIP (high potential iron protein) {Chromatium purpuratum}
vpanavtesdpaavalkyhrdaasservaaarpglppeeqhcencqfmnpdsaaadwkgc
qlfpgklinlsgwcaswtlr
>d3hipc_ 7.33.1.1.3 HIPIP (high potential iron protein) {Chromatium purpuratum}
vpanavtesdpaavalkyhrdaasservaaarpglppeeqhcencqfmnpdsaaadwkgc
qlfpgklinlsgwcaswtlrag
>d1pih__ 7.33.1.1.4 HIPIP (high potential iron protein) {Ectothiorhodospira halophila}
asepraedghahdyvneaadasghpryqegqlcencafwgeavqdgwgrcthpdfdevlv
kaegwcsvyapas
>d1pij__ 7.33.1.1.4 HIPIP (high potential iron protein) {Ectothiorhodospira halophila}
asepraedghahdyvneaadasghpryqegqlcencafwgeavqdgwgrcthpdfdevlv
kaegwcsvyapas
>d2hipa_ 7.33.1.1.4 HIPIP (high potential iron protein) {Ectothiorhodospira halophila}
epraedghahdyvneaadasghpryqegqlcencafwgeavqdgwgrcthpdfdevlvka
egwcsvyapas
>d2hipb_ 7.33.1.1.4 HIPIP (high potential iron protein) {Ectothiorhodospira halophila}
epraedghahdyvneaadasghpryqegqlcencafwgeavqdgwgrcthpdfdevlvka
egwcsvyapas
>d1hpi__ 7.33.1.1.5 HIPIP (high potential iron protein) {Ectothiorhodospira vacuolata}
merlseddpaaqaleyrhdassvqhpayeegqtclncllytdasaqdwgpcsvfpgklvs
angwctawvar
>d1dj7a_ 7.34.1.1.1 Ferredoxin thioredoxin reductase (FTR), catalytic beta chain {Synechocystis sp.}
nnktlaamknfaeqyakrtdtyfcsdlsvtavvieglarhkeelgsplcpcrhyedkeae
vkntfwncpcvpmrerkechcmlfltpdndfagdaqdipmetleevkas
>d1a1fa1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1fa2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1fa3 7.35.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ga1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1ga2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ga3 7.35.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ha1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsqsgsltrhirihtg
>d1a1ha2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ha3 7.35.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ia1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ia2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ia3 7.35.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ja1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ja2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ja3 7.35.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ka1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ka2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ka3 7.35.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1la1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1a1la2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1la3 7.35.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1aaya1 7.35.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1aaya2 7.35.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1aaya3 7.35.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1zaac1 7.35.1.1.1 (3-31) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1zaac2 7.35.1.1.1 (32-59) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1zaac3 7.35.1.1.1 (60-87) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1rmd_1 7.35.1.1.2 (87-116) V(D)J recombination activating protein 1 (RAG1), dimerization domain {Mouse (Mus musculus)}
lmvkcpaqdcneevslekynhhvsshkesk
>d2drpa1 7.35.1.1.3 (103-139) Tramtrack protein (two zinc-finger peptide) {Drosophila melanogaster}
ftkegehtyrckvcsrvythisnfcrhyvtshkrnvk
>d2drpa2 7.35.1.1.3 (140-165) Tramtrack protein (two zinc-finger peptide) {Drosophila melanogaster}
vypcpfcfkeftrkdnmtahvkiihk
>d2drpd1 7.35.1.1.3 (102-139) Tramtrack protein (two zinc-finger peptide) {Drosophila melanogaster}
eftkegehtyrckvcsrvythisnfcrhyvtshkrnvk
>d2drpd2 7.35.1.1.3 (140-166) Tramtrack protein (two zinc-finger peptide) {Drosophila melanogaster}
vypcpfcfkeftrkdnmtahvkiihki
>d1ard__ 7.35.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqehlkrhyrshtnek
>d1are__ 7.35.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqealkrhyrshtnek
>d1arf__ 7.35.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqeylkrhyrshtnek
>d1paa__ 7.35.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
kayacglcnraftrrdllirhaqkihsgnl
>d2adr__ 7.35.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqehlkrhyrshtnekpypcglcnraftrrdllirhaqkihsgnlge
>d1znf__ 7.35.1.1.5 XFIN, third domain {Xenopus laevis}
xykcglcersfveksalsrhqrvhkn
>d5znf__ 7.35.1.1.6 ZFY {Human (Homo sapiens)}
ktyqcqyceyrsadssnlkthiktkhskek
>d7znf__ 7.35.1.1.6 ZFY {Human (Homo sapiens)}
ktyqcqycekrfadssnlkthiktkhskek
>d1ncs__ 7.35.1.1.7 SWI5 zinc-finger domains {Baker's yeast (Saccharomyces cerevisiae)}
tlprgsidkyvkempdktfeclfpgctktfkrrynirshiqthledr
>d1zfd__ 7.35.1.1.7 SWI5 zinc-finger domains {Baker's yeast (Saccharomyces cerevisiae)}
drpyscdhpgcdkafvrnhdlirhkkshqeka
>d2glia1 7.35.1.1.8 (103-134) Five-finger GLI1 {Human (Homo sapiens)}
etdcrwdgcsqefdsqeqlvhhinsehihger
>d2glia2 7.35.1.1.8 (135-167) Five-finger GLI1 {Human (Homo sapiens)}
kefvchwggcsrelrpfkaqymlvvhmrrhtge
>d2glia3 7.35.1.1.8 (168-197) Five-finger GLI1 {Human (Homo sapiens)}
kphkctfegcrksysrlenlkthlrshtge
>d2glia4 7.35.1.1.8 (198-228) Five-finger GLI1 {Human (Homo sapiens)}
kpymcehegcskafsnasdrakhqnrthsne
>d2glia5 7.35.1.1.8 (229-257) Five-finger GLI1 {Human (Homo sapiens)}
kpyvcklpgctkrytdpsslrkhvktvhg
>d1bbo_1 7.35.1.1.9 (1-28) Enhancer binding protein {Human (Homo sapiens)}
kyiceecgirxkkpsmlkkhirthtdvr
>d1bbo_2 7.35.1.1.9 (29-57) Enhancer binding protein {Human (Homo sapiens)}
pyhctycnfsfktkgnltkhmkskahskk
>d3znf__ 7.35.1.1.9 Enhancer binding protein {Human (Homo sapiens)}
rpyhcsycnfsfktkgnltkhmkskahskk
>d4znf__ 7.35.1.1.9 Enhancer binding protein {Human (Homo sapiens)}
rpyhcsycnfsfktkgnltkhmkskahskk
>d1sp1__ 7.35.1.1.10 Transcription factor sp1 {Human (Homo sapiens)}
kkfacpecpkrfmrsdhlskhikthqnkk
>d1sp2__ 7.35.1.1.10 Transcription factor sp1 {Human (Homo sapiens)}
rpfmctwsycgkrftrsdelqrhkrthtgek
>d1bhi__ 7.35.1.1.11 Transactivation domain of cre-bp1/atf-2 {Human (Homo sapiens)}
msddkpflctapgcgqrftnedhlavhkhkhemtlkfg
>d1ubdc1 7.35.1.1.12 (295-322) Ying-yang 1 (yy1, zinc finger domain) {Human (Homo sapiens)}
tiacphkgctkmfrdnsamrkhlhthgp
>d1ubdc2 7.35.1.1.12 (323-350) Ying-yang 1 (yy1, zinc finger domain) {Human (Homo sapiens)}
rvhvcaecgkafvessklkrhqlvhtge
>d1ubdc3 7.35.1.1.12 (351-380) Ying-yang 1 (yy1, zinc finger domain) {Human (Homo sapiens)}
kpfqctfegcgkrfsldfnlrthvrihtgd
>d1ubdc4 7.35.1.1.12 (381-408) Ying-yang 1 (yy1, zinc finger domain) {Human (Homo sapiens)}
rpyvcpfdgcnkkfaqstnlkshiltha
>d1tf3a1 7.35.1.1.13 (1-40) Transcription factor IIIA, TFIIIA {Xenopus laevis}
mkryicsfadcgaaynknwklqahlskhtge
>d1tf3a2 7.35.1.1.13 (41-70) Transcription factor IIIA, TFIIIA {Xenopus laevis}
kpfpckeegcekgftslhhltrhslthtge
>d1tf3a3 7.35.1.1.13 (71-101) Transcription factor IIIA, TFIIIA {Xenopus laevis}
knftcdsdgcdlrfttkanmkkhfnrfhnik
>d1tf6a1 7.35.1.1.13 (10-40) Transcription factor IIIA, TFIIIA {Xenopus laevis}
ykryicsfadcgaaynknwklqahlckhtge
>d1tf6a2 7.35.1.1.13 (41-70) Transcription factor IIIA, TFIIIA {Xenopus laevis}
kpfpckeegcekgftslhhltrhslthtge
>d1tf6a3 7.35.1.1.13 (71-100) Transcription factor IIIA, TFIIIA {Xenopus laevis}
knftcdsdgcdlrfttkanmkkhfnrfhni
>d1tf6a4 7.35.1.1.13 (101-131) Transcription factor IIIA, TFIIIA {Xenopus laevis}
kicvyvchfencgkafkkhnqlkvhqfshtq
>d1tf6a5 7.35.1.1.13 (132-160) Transcription factor IIIA, TFIIIA {Xenopus laevis}
qlpyecphegcdkrfslpsrlkrhekvha
>d1tf6a6 7.35.1.1.13 (161-188) Transcription factor IIIA, TFIIIA {Xenopus laevis}
gypckkddscsfvgktwtlylkhvaech
>d1tf6d1 7.35.1.1.13 (7-40) Transcription factor IIIA, TFIIIA {Xenopus laevis}
pvvykryicsfadcgaaynknwklqahlckhtge
>d1tf6d2 7.35.1.1.13 (41-70) Transcription factor IIIA, TFIIIA {Xenopus laevis}
kpfpckeegcekgftslhhltrhslthtge
>d1tf6d3 7.35.1.1.13 (71-100) Transcription factor IIIA, TFIIIA {Xenopus laevis}
knftcdsdgcdlrfttkanmkkhfnrfhni
>d1tf6d4 7.35.1.1.13 (101-131) Transcription factor IIIA, TFIIIA {Xenopus laevis}
kicvyvchfencgkafkkhnqlkvhqfshtq
>d1tf6d5 7.35.1.1.13 (132-160) Transcription factor IIIA, TFIIIA {Xenopus laevis}
qlpyecphegcdkrfslpsrlkrhekvha
>d1tf6d6 7.35.1.1.13 (161-188) Transcription factor IIIA, TFIIIA {Xenopus laevis}
gypckkddscsfvgktwtlylkhvaech
>d1yuia_ 7.35.1.1.14 GAGA factor {Drosophila melanogaster}
pkakrakhppgtekprsrsqseqpatcpicyavirqsrnlrrhlelrhfakpgv
>d1yuja_ 7.35.1.1.14 GAGA factor {Drosophila melanogaster}
pkakrakhppgtekprsrsqseqpatcpicyavirqsrnlrrhlelrhfakpgv
>d1aw6__ 7.36.1.1.1 Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
mkllssieqacdicrlkklkcskekpkcakclknnwecryspk
>d1d66a1 7.36.1.1.1 (8-48) Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1d66b1 7.36.1.1.1 (8-48) Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
eqacdicrlkklkcskekpkcakclknnwecryspktkrsp
>d1pyia1 7.36.1.1.2 (30-71) PPR1 {Baker's yeast (Saccharomyces cerevisiae)}
srtackrcrlkkikcdqefpsckrcaklevpcvsldpatgkd
>d1pyib1 7.36.1.1.2 (30-71) PPR1 {Baker's yeast (Saccharomyces cerevisiae)}
srtackrcrlkkikcdqefpsckrcaklevpcvsldpatgkd
>d1ajya1 7.36.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajyb1 7.36.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1zmec1 7.36.1.1.3 (31-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
svaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1zmed1 7.36.1.1.3 (31-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
svaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1pyc__ 7.36.1.1.4 CYP1 (HAP1) {Yeast (Kluyveromyces lactis)}
iplscticrkrkvkcdklrphcqqctktgvahlchymeqtw
>d1hwtc1 7.36.1.1.5 (59-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
riplscticrkrkvkcdklrphcqqctktgvahlchyme
>d1hwtd1 7.36.1.1.5 (55-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
rkrnriplscticrkrkvkcdklrphcqqctktgvahlchyme
>d1hwtg1 7.36.1.1.5 (59-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
riplscticrkrkvkcdklrphcqqctktgvahlchyme
>d1hwth1 7.36.1.1.5 (56-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
krnriplscticrkrkvkcdklrphcqqctktgvahlchyme
>d2hapc1 7.36.1.1.5 (55-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
rkrnriplrcticrkrkvkcdklrphcqqctktgvahlchyme
>d2hapd1 7.36.1.1.5 (56-97) CYP1 (HAP1) {Baker's yeast (Saccharomyces cerevisiae)}
krnriplrcticrkrkvkcdklrphcqqctktgvahlchyme
>d2alca_ 7.36.1.1.7 Ethanol regulon transcriptional activator ALCR DNA-binding domain {Aspergillus nidulans}
gsmadtrrrqnhscdpcrkgkrrcdapenrneanengwvscsnckrwnkdctfnwlssqr
sknss
>d1gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
>d1gaua_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
>d2gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
kgkkrr
>d3gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
kragtvcsncqtstttlwrrspmgdpvcnacglyyklhqvnrpltmrkdgiqtrnrkvss
kgkkrr
>d4gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
mkngeqngpttctncftqttplwrrnpegqplcnacglflklhgvvrplslktdvikkrn
rnsans
>d5gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
mkngeqngpttctncftqttplwrrnpegqplcnacglflklhgvvrplslktdvikkrn
rnsans
>d6gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
mkngeqngpttctncftqttpvwrrnpegqplcnacglflklhgvvrplslktdvikkrn
rnsans
>d7gata_ 7.37.1.1.1 Erythroid transcription factor GATA-1 {Chicken (Gallus gallus)}
mkngeqngpttctncftqttpvwrrnpegqplcnacglflklhgvvrplslktdvikkrn
rnsans
>d1gnf__ 7.37.1.1.2 Erythroid transcription factor GATA-1 {Mouse (Mus musculus)}
gsearecvncgatatplwrrdrtghylcnacglyhkmngqnrplir
>d1by4a_ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
tkhicaicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrcqyc
ryqkclamgmkreavqeer
>d1by4b_ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
gsftkhicaicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrc
qycryqkclamgmkreavqeer
>d1by4c_ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
khicaicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrcqycr
yqkclamgmkreavqeer
>d1by4d_ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
sftkhicaicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrcq
ycryqkclamgmkreavqee
>d1rxr__ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
ftkhicaicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrcqy
cryqkalamgmkreavqeerqrg
>d2nlla_ 7.37.1.2.1 Retinoid X receptor (RXR-alpha) DNA-binding domain {Human (Homo sapiens)}
caicgdrssgkhygvyscegckgffkrtvrkdltytcrdnkdclidkrqrnrcqycryqk
clamgm
>d2nllb_ 7.37.1.2.2 Thyroid hormone receptor (TR-beta) DNA-binding domain {Human (Homo sapiens)}
delcvvcgdkatgyhyrcitcegckgffrrtiqknlhpsysckyegkcvidkvtrnqcqe
crfkkciyvgmatdlvlddskrlakrklieenrekrrreelek
>d1cita_ 7.37.1.2.3 Orphan nuclear receptor NGFI-B {Rat (Rattus norvegicus)}
grcavcgdnascqhygvrtcegckgffkrtvqksakyiclankdcpvdkrrrnrcqfcrf
qkclavgmvkevvrtdslkgrrgrlpskp
>d1hcp__ 7.37.1.2.4 Estrogen receptor DNA-binding domain {Human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmkg
>d1hcqa_ 7.37.1.2.4 Estrogen receptor DNA-binding domain {Human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmk
>d1hcqb_ 7.37.1.2.4 Estrogen receptor DNA-binding domain {Human (Homo sapiens)/chicken (Gallus gallus)}
trycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscqacr
lrkcyevgmmk
>d1hcqe_ 7.37.1.2.4 Estrogen receptor DNA-binding domain {Human (Homo sapiens)/chicken (Gallus gallus)}
mketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscq
acrlrkcyevgmmk
>d1hcqf_ 7.37.1.2.4 Estrogen receptor DNA-binding domain {Human (Homo sapiens)/chicken (Gallus gallus)}
ketrycavcndyasgyhygvwscegckaffkrsiqghndymcpatnqctidknrrkscqa
crlrkcyevgmmk
>d1gdc__ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
lclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncpacryr
kclqagmnlear
>d1glua_ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
mkparpclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncp
acryrkclqagmnlearktkk
>d1glub_ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
mkparpclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncp
acryrkclqagmnlearktkk
>d1lata_ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
rpclvcsdeasgchygvltcegckaffkravegqhnylckyegkciidkirrkncpacry
rkclqagmnle
>d1latb_ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
arpclvcsdeasgchygvltcegckaffkravegqhnylckyegkciidkirrkncpacr
yrkclqagmnlear
>d1rgd__ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
clvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncpacryrk
clqagmnlear
>d2gda__ 7.37.1.2.5 Glucocorticoid receptor DNA-binding domain {Rat (Rattus norvegicus)}
lclvcsdeasgchygvltcgsckvffkravegqhnylcagrndciidkirrkncpacryr
kclqagmnlear
>d1hra__ 7.37.1.2.6 Retinoic acid receptor DNA-binding domain {Human (Homo sapiens)}
prvykpcfvcqdkssgyhygvsacegckgffrrsiqknmiytchrdkncvinkvtrnrcq
ycrlqkcfevgmskesvrn
>d1a6ya_ 7.37.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
llckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcqqcr
fkkclsvgmsrdavrfgr
>d1a6yb_ 7.37.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
gmvllckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcq
qcrfkkclsvgmsrdavrfgripk
>d1b8ta1 7.37.1.3.1 (1-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
mpnwgggkkcgvcqkavyfaeevqcegssfhkscf
>d1b8ta2 7.37.1.3.1 (36-100) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
lcmvckknldsttvavhgdeiyckscygkkygpkgkgkgmgagtlstdkgeslgikyeeg
qshrp
>d1b8ta3 7.37.1.3.1 (101-143) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
tnpnasrmaqkvggsdgcprcgqavyaaekvigagkswhkscf
>d1b8ta4 7.37.1.3.1 (144-192) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
rcakcgkslesttladkdgeiyckgcyaknfgpkgfgfgqgagalihsq
>d1ctl_1 7.37.1.3.1 (1-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
maqkvggsdgcprcgqavyaaekvigagkswhksc
>d1ctl_2 7.37.1.3.1 (36-85) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
frcakcgkslesttladkdgeiyckgcyaknfgpkgfgfgqgagalihsq
>d1a7i_1 7.37.1.3.2 (8-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
nkcgacgrtvyhaeevqcdgrsfhrccf
>d1a7i_2 7.37.1.3.2 (36-67) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
lcmvcrknldsttvaihdaevyckscygkkyg
>d1cxxa1 7.37.1.3.2 (117-144) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
aekcsacgdsvyaaekvigagkpwhknc
>d1cxxa2 7.37.1.3.2 (145-175) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
frcakcgkslesttltekegeiyckgcyakn
>d1qli_1 7.37.1.3.2 (117-144) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
aekcsrcgdsvyaaekvigagkpwhknc
>d1qli_2 7.37.1.3.2 (145-175) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
frcakcgkslesttltekegeiyckgcyakn
>d1iml_1 7.37.1.3.3 (1-28) Cysteine-rich (intestinal) protein, CRP, CRIP {Rat (Rattus rattus)}
pkcpkcdkevyfaervtslgkdwhrpcl
>d1iml_2 7.37.1.3.3 (29-76) Cysteine-rich (intestinal) protein, CRP, CRIP {Rat (Rattus rattus)}
kcekcgktltsgghaehegkpycnhpcysamfgpkgfgrggaeshtfk
>d1zfo__ 7.37.1.4.1 LASP-1 {Pig (Sus scrofa)}
mnpncarcgkivyptekvncldkfwhkacf
>d1d4ua2 7.37.1.5.1 (1-36) DNA repair factor XPA DNA- and RPA-binding domain, N-terminal subdomain {Human (Homo sapiens)}
mefdyviceecgkefmdsylmdhfdlptcddcrdad
>d1xpa_2 7.37.1.5.1 (98-133) DNA repair factor XPA DNA- and RPA-binding domain, N-terminal subdomain {Human (Homo sapiens)}
mefdyviceecgkefmdsylmnhfdlptcdncrdad
>d1a1ta_ 7.38.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1aaf__ 7.38.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqrgnfrnqrkiikcfncgkeghiakncraprkrgcwkcgkeghqmkdcterqan
>d1bj6a_ 7.38.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
nvkcfncgkeghtarncraprkkgcwkcgkeghqmkdcterq
>d1mfs__ 7.38.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1nc8__ 7.38.1.1.3 HIV nucleocapsid {Human immunodeficiency virus, type 2}
aqqrkvircwncgkeghsarqcraprrqg
>d1cl4a_ 7.38.1.1.4 Nucleocapsid protein from mason-pfizer monkey virus (MPMV) {Mason-pfizer monkey virus}
vpglcprckrgkhwanecksktdnqgnpipph
>d1a6bb_ 7.38.1.1.5 Zinc finger protein ncp10 {Moloney murine leukemia virus, MMLV}
gerrrsqldrdqcayckekghwakdcpkkprgprgprpqt
>d1dsqa_ 7.38.1.1.6 Nucleic acid binding protein p14 {Mouse mammary tumor virus, MMTV}
kgpvcfscgktghikrdckee
>d1dsva_ 7.38.1.1.6 Nucleic acid binding protein p14 {Mouse mammary tumor virus, MMTV}
ppglcprckkgyhwkseckskfdkdgnplpp
>d1mea__ 7.39.1.1.1 Methionyl-tRNA synthetase (MetRS), Zn-domain {Escherichia coli}
gsdrfvkgtcpkckspdqygdncevcga
>d1med__ 7.39.1.1.1 Methionyl-tRNA synthetase (MetRS), Zn-domain {Escherichia coli}
gsdrfvkgtcpkckspdqygdncevcga
>d1qqta3 7.39.1.1.1 (141-175) Methionyl-tRNA synthetase (MetRS), Zn-domain {Escherichia coli}
vkgtcpkckspdqygdncevcgatyspteliepks
>d1zin_2 7.39.2.1.1 (126-160) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bacillus stearothermophilus}
grricrncgatyhlifhppakpgvcdkcggelyqr
>d1zio_2 7.39.2.1.1 (126-160) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bacillus stearothermophilus}
grricrncgatyhlifhppakpgvcdkcggelyqr
>d1zip_2 7.39.2.1.1 (126-160) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bacillus stearothermophilus}
grricrncgatyhlifhppakpgvcdkcggelyqr
>d1akea2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akeb2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1anka2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ankb2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d2ecka2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d2eckb2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d4akea2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d4akeb2 7.39.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d2ak3a2 7.39.2.1.3 (125-161) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-3}
arwihpgsgrvyniefnppktmgiddltgeplvqred
>d2ak3b2 7.39.2.1.3 (125-161) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-3}
arwihpgsgrvyniefnppktmgiddltgeplvqred
>d1ak2_2 7.39.2.1.4 (147-176) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-2}
pqsgrsyheefnppkepmkdditgeplirr
>d2ak2_2 7.39.2.1.4 (147-176) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-2}
pqsgrsyheefnppkepmkdditgeplirr
>d1aky_2 7.39.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqrsdd
>d1dvra2 7.39.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqisdd
>d1dvrb2 7.39.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqisdd
>d2aky_2 7.39.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqrsdd
>d3aky_2 7.39.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqrsdd
>d1zaka2 7.39.2.1.6 (128-158) Microbial and mitochondrial ADK, insert "zinc finger" domain {Maize (Zea mays)}
grrldpvtgkiyhlkysppeneeiasrltqr
>d1zakb2 7.39.2.1.6 (128-158) Microbial and mitochondrial ADK, insert "zinc finger" domain {Maize (Zea mays)}
grrldpvtgkiyhlkysppeneeiasrltqr
>d1tfi__ 7.39.3.1.1 Transcriptional factor SII {Human (Homo sapiens)}
ktggtqtdlftcgkckkknctytqvqtrsadepmttfvvcnecgnrwkfc
>d1qyp__ 7.39.3.1.2 Rbp9 subunit of RNA polymerase II, C-terminal domain {Thermococcus celer}
gshmeqdlktlpttkitcpkcgndtaywwemqtragdepstifykctkcghtwrsye
>d1pft__ 7.39.3.1.3 Transcription inititiation factor TFIIB, N-terminal domain {Pyrococcus furiosus}
mvnkqkvcpacesaeliydpergeivcakcgyvieeniidmgpewrafda
>d1yua_1 7.39.3.2.1 (1-65) Prokariotic DNA topoisomerase I, a C-terminal fragment {Escherichia coli}
mngevappkedpvplpelpceksdayfvlrdgaagvflaantfpksretraplveelyrf
rdrlp
>d1yua_2 7.39.3.2.1 (66-122) Prokariotic DNA topoisomerase I, a C-terminal fragment {Escherichia coli}
eklryladapqqdpegnktmvrfsrktkqqyvssekdgkatgwsafyvdgkwvegkk
>d1rb9__ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtsfddlpadwvcpvcgapksefeaa
>d1rdv__ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtafedvpadwvcpicgapksefepa
>d2rdva_ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtafedvpadwvcpicgapksefepa
>d2rdvb_ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtafedvpadwvcpicgapksefepa
>d2rdvc_ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtafedvpadwvcpicgapksefepa
>d7rxn__ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtsfddlpadwvcpvcgapksefeaa
>d8rxna_ 7.39.4.1.1 Rubredoxin {Desulfovibrio vulgaris}
mkkyvctvcgyeydpaegdpdngvkpgtsfddlpadwvcpvcgapksefeaa
>d1rdg__ 7.39.4.1.2 Rubredoxin {Desulfovibrio gigas}
xmdiyvctvcgyeydpakgdpdsgikpgtkfedlpddwacpvcgaskdafekq
>d6rxn__ 7.39.4.1.3 Rubredoxin {Desulfovibrio desulfuricans, strain 27774}
xmqkyvcnvcgyeydpaehdnvpfdqlpddwccpvcgvskdqfspa
>d1b13a_ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcayiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1b2ja_ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2oa_ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2ob_ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1be7__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplsgvgkdqfeevee
>d1bfy__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1irn__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeeve
>d1iro__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeeve
>d4rxn__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiydpedgdpddgvnpgtdfkdipddwvcplcgvgkdefeevee
>d5rxn__ 7.39.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiydpedgdpddgvnpgtdfkdipddwvcplcgvgkdefeevee
>d1bq8a_ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
makwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1bq9a_ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1brfa_ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1caa__ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1cad__ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1qcva_ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvlkitgyiydedagdpdngispgtkfeelpddwvapitgapksefekled
>d1zrp__ 7.39.4.1.5 Rubredoxin {Pyrococcus furiosus}
akwvckicgyiydedagdpdngispgtkfeelpddwvcpicgapksefekled
>d1b71a2 7.39.4.1.6 (148-191) Rubrerythrin, C-terminal domain {Desulfovibrio vulgaris}
flreqatkwrcrncgyvhegtgapelcpacahpkahfellginw
>d1ryt_2 7.39.4.1.6 (148-191) Rubrerythrin, C-terminal domain {Desulfovibrio vulgaris}
flreqatkwrcrncgyvhegtgapelcpacahpkahfellginw
>d1cfwa_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1cfwb_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dcda_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dcdb_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dhga_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dhgb_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dxga_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dxgb_ 7.39.4.2.1 Desulforedoxin {Desulfovibrio gigas}
anegdvykcelcgqvvkvleegggtlvccgedmvkq
>d1dfx_2 7.39.4.2.2 (1-36) Desulfoferrodoxin N-terminal domain {Desulfovibrio desulfuricans}
pkhlevykcthcgnivevlhgggaelvccgepmkhm
>d2occf_ 7.39.4.3.1 Cytochrome c oxidase Subunit F {Bovine (Bos taurus)}
asgggvptdeeqatglerevmlaarkgqdpynilapkatsgtkedpnlvpsitnkrivgc
iceednstviwfwlhkgeaqrcpscgthyklvphqlah
>d1acmb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1acmd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1d09b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1d09d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1nbeb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1nbed2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raab2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raad2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rabb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rabd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1racb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1racd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1radb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1radd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raeb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raed2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rafb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rafd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1ragb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1ragd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rahb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1rahd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raib2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1raid2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d2at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d2at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d2atcb2 7.39.5.1.1 (101-152) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
ernidvlvcpdsncishaepvsssfavrraddialkckycekefshnvvlan
>d3at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d3at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d4at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d4at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d5at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d5at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d6at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d6at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d7at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d7at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d8at1b2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d8at1d2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d8atcb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d8atcd2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
erinnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d9atcb2 7.39.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1dfea_ 7.40.1.1.1 Ribosomal protein L36 {Thermus thermophilus}
mkvrasvkricdkckvirrhgrvyvicenpkhkqrqg
>d1dgza_ 7.40.1.1.1 Ribosomal protein L36 {Thermus thermophilus}
mkvrasvkricdkckvirrhgrvyvicenpkhkqrqg
>d1fre__ 7.41.1.1.1 Nuclear factor XNF7 {African clawed frog (Xenopus laevis)}
ekcsehderlklyckddgtlscvicrdslkhashnflpi
>d1rmd_2 7.42.1.1.1 (1-86) V(D)J recombination activating protein 1 (RAG1), dimerization domain {Mouse (Mus musculus)}
ncskihlstkllavdfpahfvksiscqicehiladpvetsckhlfcricilrclkvmgsy
cpscrypcfptdlespvksflnilns
>d1chc__ 7.42.1.1.2 Immediate early protein, IEEHV {Equine herpes virus-1}
matvaercpicledpsnysmalpclhafcyvcitrwirqnptcplckvpvesvvhtiesd
sefgdqli
>d1bor__ 7.42.1.1.3 Acute promyelocytic leukaemia proto-onkoprotein PML {Human (Homo sapiens)}
eeefqflrcqqcqaeakcpkllpclhtlcsgcleasgmqcpicqapwplgadtpal
>d1dcqa2 7.43.1.1.1 (247-368) Pyk2-associated protein beta ARF-GAP domain {Mouse (Mus musculus)}
ltkeiisevqrmtgndvccdcgapdptwlstnlgiltciecsgihrelgvhysrmqsltl
dvlgtselllaknignagfneimecclpsedpvkpnpgsdmiarkdyitakymerryark
kh
>d1mhu__ 7.44.1.1.1 Metallothionein {Human (Homo sapiens)}
ksccsccpvgcakcaqgcickgasdkcscca
>d2mhu__ 7.44.1.1.1 Metallothionein {Human (Homo sapiens)}
mdpncscaagdsctcagsckckeckctsck
>d1mrb__ 7.44.1.1.2 Metallothionein {Rabbit}
ksccsccppgcakcaqgcickgasdkcscca
>d2mrb__ 7.44.1.1.2 Metallothionein {Rabbit}
mdpncscaaagdsctcansctckackctsck
>d1mrt__ 7.44.1.1.3 Metallothionein {Rat}
ksccsccpvgcakcsqgcickeasdkcscca
>d2mrt__ 7.44.1.1.3 Metallothionein {Rat}
mdpncscatdgscscagsckckqckctsck
>d4mt2__ 7.44.1.1.3 Metallothionein {Rat}
mdpncscatdgscscagsckckqckctsckksccsccpvgcakcsqgcickeasdkcscc
a
>d1dfsa_ 7.44.1.1.4 Metallothionein {Mouse (Mus musculus)}
ksccsccpvgcskcaqgcvckgaadkctcca
>d1dfta_ 7.44.1.1.4 Metallothionein {Mouse (Mus musculus)}
mdpncscstggsctctsscacknckctsck
>d1dmc__ 7.44.1.1.5 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
spcqkctsgckcatkeecsktctkpcsccpk
>d1dmd__ 7.44.1.1.5 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
spcqkctsgckcatkeecsktctkpcsccpk
>d1dme__ 7.44.1.1.5 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
pgpccndkcvcqeggckagcqctscrcs
>d1dmf__ 7.44.1.1.5 Metallothionein {Crab (Callinectes sapidus), alpha and beta domains}
pgpccndkcvcqeggckagcqctscrcs
>d1aoo__ 7.44.1.1.6 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqq__ 7.44.1.1.6 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqr__ 7.44.1.1.6 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqs__ 7.44.1.1.6 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1qjka_ 7.44.1.1.7 Metallothionein {Purple sea urchin (Strongylocentrotus purpuratus) |A|}
pdvkcvcctegkecacfgqdccvtgecckdgtccgi
>d1qjla_ 7.44.1.1.7 Metallothionein {Purple sea urchin (Strongylocentrotus purpuratus) |A|}
ictnaackcangckcgsgcsctegncac
>d1co4a_ 7.45.1.1.1 Zinc domain conserved in yeast copper-regulated transcription factors {Synthetic}
mvvingvkyacdscikshkaaqcehndrplkilkprgrpptt
>d1adn__ 7.46.1.1.1 Ada DNA repair protein, N-terminal domain (N-Ada 10) {Escherichia coli}
mkkatcltddqrwqsvlardpnadgefvfavrttgifcrpscrarhalrenvsfyanase
alaagfrpckrcqpdkanprqhrldkithacr
>d1ptq__ 7.47.1.1.1 Protein kinase C-delta (PKCdelta) {Murine (Mus musculus)}
hrfkvynymsptfcdhcgsllwglvkqglkcedcgmnvhhkcrekvanlc
>d1ptr__ 7.47.1.1.1 Protein kinase C-delta (PKCdelta) {Murine (Mus musculus)}
hrfkvynymsptfcdhcgsllwglvkqglkcedcgmnvhhkcrekvanlc
>d1faq__ 7.47.1.1.2 RAF-1 {Human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1far__ 7.47.1.1.2 RAF-1 {Human (Homo sapiens)}
ltthnfarktflklafcdicqkfllngfrcqtcgykfhehcstkvptmcvdw
>d1tbn__ 7.47.1.1.3 Protein kinase c-gamma {Rat (Rattus rattus)}
qtddprnkhkfrlhsyssptfcdhcgsllyglvhqgmkcsccemnvhrrcvrsvpslcgv
dhterr
>d1tbo__ 7.47.1.1.3 Protein kinase c-gamma {Rat (Rattus rattus)}
qtddprnkhkfrlhsyssptfcdhcgsllyglvhqgmkcsccemnvhrrcvrsvpslcgv
dhterr
>d1vfya_ 7.48.1.1.1 FYVE domain of vps27p protein {Baker's yeast (Saccharomyces cerevisiae)}
dwidsdacmicskkfsllnrkhhcrscggvfcqehssnsiplpdlgiyepvrvcdscfed
yefivtd
>d1zbdb_ 7.48.1.1.2 Effector domain of rabphilin-3a {Rat (Rattus norvegicus)}
eeltdeekeiinrviaraekxetxeqerigrlvdrletxrknvagdgvnrcilcgeqlgx
lgsasvvcedckknvctkcgvetsnnrphpvwlckicleqrevwkrsgawffkgfpkqvl
pqp
>d1adt_2 7.49.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adt_3 7.49.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpqfkws
tkhqyrnvslpvahsdarqnpfdf
>d1qbha_ 7.50.1.1.1 2MIHB/C-IAP-1 {Human (Homo sapiens)}
gshmqthaarmrtfmywpssvpvqpeqlasagfyyvgrnddvkcfccdgglrcwesgddp
wvehakwfprceflirmkgqefvdeiqgryphlleqllsts
