>d101m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrvkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d102l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaakseldkaigrntngvit
kdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslr
mlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d102m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkagvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d103l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnsldaakseldkaigrntngv
itkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftns
lrmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d103m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkagvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d104la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaaeldkaigrntngvi
tkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnsl
rmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d104lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaaeldkaigrntngvi
tkdeaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnsl
rmlqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d104m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d105m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d106m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d107l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakgeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d107m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d108l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakieldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d108m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtfltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d109l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakkeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d109m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d10gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d10gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d10gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d10gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d10mha_ 3.56.1.5.1 DNA methylase HhaI, coenzyme-binding domain {Haemophilus haemolyticus}
mieikdkqltglrfidlfaglggfrlalescgaecvysnewdkyaqevyemnfgekpegd
itqvnektipdhdilcagfpcqafsisgkqkgfedsrgtlffdiarivrekkpkvvfmen
vknfashdngntlevvkntmneldysfhakvlnaldygipqkreriymicfrndlniqnf
qfpkpfelntfvkdlllpdsevehlvidrkdlvmtnqeieqttpktvrlgivgkggqger
iystrgiaitlsaygggifaktggylvngktrklhprecarvmgypdsykvhpstsqayk
qfgnsvvinvlqyiaynigsslnfkpy
>d110l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakleldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d110m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d111l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakneldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d111m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d112l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakpeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d112m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d113l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakreldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d114l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakteldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d115l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakveldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d117ea_ 2.35.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgapvsafhdiplyadkennifnmvveiprwtnakleit
keetlnpiiqdtkkgalrfvrncfphhgyihnygafpqtwedpnvshpetkavgdnepid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llaatnewfriykipdgkpenafafsgeaknkkyaldiikethdswkqliagkssdskgi
dltnvtlpdtptysaaasdaippaslkadapidksidkwffi
>d117eb_ 2.35.5.1.1 Inorganic pyrophosphatase {Baker's yeast (Saccharomyces cerevisiae)}
tyttrqigakntleykvyiekdgapvsafhdiplyadkannifnmvveiprwtnakleit
keetlnpiiqdtkkgalrfvrncfphhgyihnygafpqtwedpnvshpetkavgdnepid
vleigetiaytgqvkqvkalgimalldegetdwkviaidindplapklndiedvekyfpg
llratnewfriykipdgkpenafafsgeaknkkyaldiikathdswkqliagkssdskgi
dltnvtlpdtptyskaasdaippaslkadapidksidkwffi
>d118l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeasvnlaksrwynqtpnrakrvittfrtgtwdayk
>d119l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlsksrwynqtpnrakrvittfrtgtwdayk
>d11asa_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d11asb_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d11baa_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d11bab_ 4.5.1.1.5 Seminal ribonucleasease {Bovine (Bos taurus)}
kesaaakferqhmdsgnspssssnycnlmmccrkmtqgkckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqvekhiivacggkpsvpvhf
dasv
>d11gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d11gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d11gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d11gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d120l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnsakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d121p__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d122l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdsavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d123l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnsklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d125l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraslinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d126l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrtittfrtgtwdayk
>d127l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaatrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d128l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkptydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d129l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldtvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d12asa_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d12asb_ 4.82.1.1.12 Asparagine synthetase {Escherichia coli}
ayiakqrqisfvkshfsrqleerlglievqapilsrvgdgtqdnlsgaekavqvkvkalp
daqfevvhslakwkrqtlgqhdfsageglythmkalrpdedrlsplhsvyvdqwdwervm
gdgerqfstlkstveaiwagikateaavseefglapflpdqihfvhsqellsrypdldak
greraiakdlgavflvgiggklsdghrhdvrapdyddwstpselghaglngdilvwnpvl
edafelssmgirvdadtlkhqlaltgdedrlelewhqallrgempqtigggigqsrltml
llqlphigqvqagvwpaavresvpsll
>d12ca__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
wgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnngh
afnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlahwn
tkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgll
pesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdnw
rpaqplknrqikasf
>d12e8h1 2.1.1.1.110 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
evqlqqsgaevvrsgasvklsctasgfnikdyyihwvkqrpekglewigwidpeigdtey
vpkfqgkatmtadtssntaylqlssltsedtavyycnaghdydrgrfpywgqgtlvtvsa
a
>d12e8h2 2.1.1.2.109 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprd
>d12e8l1 2.1.1.1.110 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
divmtqsqkfmstsvgdrvsitckasqnvgtavawyqqkpgqspklmiysasnrytgvpd
rftgsgsgtdftltisnmqsedladyfcqqyssypltfgagtklelk
>d12e8l2 2.1.1.2.109 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnsatdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d12e8m1 2.1.1.1.110 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
divmtqsqkfmstsvgdrvsitckasqnvgtavawyqqkpgqspklmiysasnrytgvpd
rftgsgsgtdftltisnmqsedladyfcqqyssypltfgagtklelk
>d12e8m2 2.1.1.2.109 (108-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnsatdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d12e8p1 2.1.1.1.110 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
evqlqqsgaevvrsgasvklsctasgfnikdyyihwvkqrpekglewigwidpeigdtey
vpkfqgkatmtadtssntaylqlssltsedtavyycnaghdydrgrfpywgqgtlvtvsa
a
>d12e8p2 2.1.1.2.109 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 2E8 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkivprd
>d12gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d12gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d12gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d12gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d130l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvistfrtgtwdayk
>d131l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyysigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d132l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d133l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnhcqnrd
vrqyvqgcgv
>d134l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawvawrnecqnrd
vrqyvqgcgv
>d135l__ 4.2.1.2.2 Lysozyme {Turkey (Meleagris gallopavo)}
kvygrcelaaamkrlgldnyrgyslgnwvcaakfesnfnthatnrntdgstdygilqins
rwwcndgrtpgsknlcnipcsallssditasvncakkiasggngmnawvawrnrckgtdv
hawirgcrl
>d137la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakfeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d137lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakfeldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d138l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldcvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d139l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfcqdvdaavrgilrnaklkpvydsldcvrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d13gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d13gsa2 3.38.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgd
ltlyqsntilrhlgrtl
>d13gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d13gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d13pka_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkb_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkc_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d13pkd_ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d140l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakrvittlrtgtwdayk
>d141l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakriittfrtgtwdayk
>d142l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdevavnaaksrwynqtpnrakrvittlrtgtwdayk
>d143l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdevavnmaksrwynqtpnrakrvittlrtgtwdayk
>d144l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
iqqkrwdelavnmaksrwynqtpnrakrvittwrtgtwdayk
>d145l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
iqqkrwdewavnmaksrwynqtpnrakrvittfrtgtwdayk
>d146l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
mqqkrwdelavnmaksrwynqtpnrakriittwrtgtwdayk
>d147l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
mqqkrwdeaavnvaksrwynqtpnrakrvittlrtgtwdayk
>d148le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdaykn
>d149l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnlfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d14gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d14gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d14gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d14gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d150la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d150lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d150lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d150ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifeilrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d151l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaaslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d152l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdcegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqcpnrakrvittfrtgtwdayknc
>d153l__ 4.2.1.5.1 Lysozyme {Goose (Anser anser anser)}
rtdcygnvnridttgascktakpeglsycgvsaskkiaerdlqamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
infiktiqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d154l__ 4.2.1.5.1 Lysozyme {Goose (Anser anser anser)}
rtdcygnvnridttgascktakpeglsycgvsaskkiaerdlqamdryktiikkvgeklc
vepaviagiisreshagkvlkngwgdrgngfglmqvdkrshkpqgtwngevhitqgttil
infiktiqkkfpswtkdqqlkggisaynagagnvrsyarmdigtthddyandvvaraqyy
kqhgy
>d155c__ 1.3.1.1.17 Cytochrome c2 {Paracoccus denitrificans}
xnegdaakgekefnkckachmiqapdgtdikggktgpnlygvvgrkiaseegfkygegil
evaeknpdltwteanlieyvtdpkplvkkmtddkgaktkmtfkmgknqadvvaflaqddp
daxxxxxxxxxxxxx
>d155l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanalrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d156l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanslam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d157l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfaaalaa
laakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d158l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnalam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d159l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslam
lqakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d15c8h1 2.1.1.1.117 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
evqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqkpeqglewiaqidpangntky
dpkfqgkatitadtssntaylhlssltsedsavyycaadppyyghgdywgqgttltvss
>d15c8h2 2.1.1.2.115 (114-226) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkiv
>d15c8l1 2.1.1.1.117 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
divltqspaimsaslgervtmtctasssvsssnlhwyqqkpgsspklwiystsnlasgvp
arfsgsgsgtsysltissmeaedaatyychqyhrspytfgggtkleik
>d15c8l2 2.1.1.2.115 (108-212) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 5C8 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d160l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslra
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d161l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftaslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d162l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
laqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d163l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqakrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d164l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslam
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d165l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnalrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d166l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagfanslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d167la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknc
>d167lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrcdeglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknc
>d168la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d168le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawynqtpnrakrvittfrtgtwdayknl
>d169la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169lc_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169ld_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d169le_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaaaawaaatpnrakrvittfrtgtwdayk
>d16gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d16gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d16gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d16pk__ 3.75.1.1.4 Phosphoglycerate kinase {Trypanosoma brucei}
ekksinecdlkgkkvlirvdfnvpvkngkitndyrirsalptlkkvlteggscvlmshlg
rpkgipmaqagkirstggvpgfqqkatlkpvakrlselllrpvtfapdclnaadvvskms
pgdvvllenvrfykeegskkakdreamakilasygdvyisdafgtahrdsatmtgipkil
gngaagylmekeisyfakvlgnpprplvaivggakvsdkiqlldnmlqridylliggama
ytflkaqgysigkskceesklefarsllkkaedrkvqvilpidhvchtefkavdsplite
dqnipeghmaldigpktiekyvqtigkcksaiwngpmgvfemvpyskgtfaiakamgrgt
hehglmsiigggdsasaaelsgeakrmshvstgggaslellegktlpgvtvlddk
>d16vpa_ 4.149.1.1.1 Conserved core of transcriptional regulatory protein vp16 {Herpes simplex virus, type 1, HSV-1}
srmpsppmpvppaalfnrllddlgfsagpalctmldtwnedlfsalptnadlyreckfls
tlpsdvvewgdayvpertqidirahgdvafptlpatrdglglyyealsrffhaelraree
syrtvlanfcsalyrylrasvrqlhrqahmrgrdrdlgemlratiadryyretarlarvl
flhlylfltreilwaayaeqmmrpdlfdclccdleswrqlaglfqpfmfvngaltvrgvp
iearrlrelnhirehlnlplvrsaateepgaplttpptlhgnqarasgyfmvliraklds
yssfttspseavmrehaysraptknnygstieglldlpdddapeeaglaaprlsfl
>d170l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrnsngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrsalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrckrvittfrtgtwdayknl
>d171l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaaksaldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d172l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mncfemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d173l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrleiykdtegyytigighlltkspslnaakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslem
lqqkrwdeaavnlaesrwynqtpnraervittfrtgtwdayk
>d174la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaadlaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d174lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighllaaaadlaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d175la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavraaalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d175lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavraaalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d176la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigightlkvdgnsnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d176lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigightlkvdgnsnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d177l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d178l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d179l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwceaavnlaksrwynqtpnrakrvittfctgtwdayk
>d17gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d17gsa2 3.38.1.5.4 (0-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
mppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgd
ltlyqsntilrhlgrtl
>d17gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d17gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpafqdgdlt
lyqsntilrhlgrtl
>d180la_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d180lb_ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyyeigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayknl
>d181l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d182l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d183l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d184l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d185l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d186l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d187l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d188l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraaainmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d189l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnlfemlrideglrlkiykdtegyytigighlltkspdlnvakseldkaigrncngvitk
deaeklfnqdvdaavrgilrnpklkpvydsldavrrcalinmvfqmgetgvagftdslrm
lqqkrwdeaaanlaksrwynqtpdrakrvittfrtgtwdayknl
>d18gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d18gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d18gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d18gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d190l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigracagaitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdeaavnlaksrwynqtpnrakrvittfrtgtwdayk
>d1914__ 4.40.1.1.1 Signal recognition particle alu RNA binding heterodimer, SRP9/14 {Mouse (Mus musculus)}
mvlleseqflteltrlfqkcrssgsvfitlkkydgrtkpiprkssveglepaenkcllra
tdgkrkistvvsskevnkfqmaysnllranmdglkkrdkknkskkskpaqggeqklisee
ddsagspmpqfqtweefsraaeklyladpmkvrvvlkyrhvdgnlcikvtddlvclvyrt
dqaqdvkkiekfhsqlmrlmvakesrnv
>d191l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigracagaitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrrcalinmvfqmgetgvagftnslrm
lqqkrwdaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d192l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslaaakaalaaaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwaaaaaalaksrwynqtpnrakrvittfrtgtwdayk
>d193l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d194l__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d195l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdelavnlaksrwynqtpnrakrvittfrtgtwdayk
>d196l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdemavnlaksrwynqtpnrakrvittfrtgtwdayk
>d197l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
lqqkrwdemavnlaksrwynqtpnrakrvittartgtwdayk
>d198l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdelavnlaksrwynqtpnrakrvittfrtgtwdayk
>d199l__ 4.2.1.3.1 Phage T4 lysozyme {Escherichia coli infected with bacteriophage T4}
mnifemlrideglrlkiykdtegyytigighlltkspslnaakseldkaigrntngvitk
deaeklfnqdvdaavrgilrnaklkpvydsldavrraalinmvfqmgetgvagftnslrm
aqqkrwdemavnlaksrwynqtpnrakrvittfrtgtwdayk
>d19gsa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d19gsa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d19gsb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d19gsb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1a00a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a00b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a00c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a00d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a01a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a01b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a01c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a01d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a02n1 2.1.1.5.20 (577-678) Transcription factor NFATC, C-terminal domain {Human (Homo sapiens)}
lpmverqdtdsclvyggqqmiltgqnftseskvvftekttdgqqiwemeatvdkdksqpn
mlfveipeyrnkhirtpvkvnfyvingkrkrsqpqhftyhpv
>d1a02n2 2.2.5.1.2 (399-576) Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
wplssqsgsyelrievqpkphhrahyetegsrgavkaptgghpvvqlhgymenkplglqi
figtaderilkphafyqvhritgktvtttsyekivgntkvleiplepknnmratidcagi
lklrnadielrkgetdigrkntrvrlvfrvhipessgrivslqtasnpiecsqrsahe
>d1a03a_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1a03b_ 1.42.1.2.1 Calcyclin (S100) {Rabbit (Oryctolagus cuniculus)}
maspldqaiglligifhkysgkegdkhtlskkelkeliqkeltigsklqdaeivklmddl
drnkdqevnfqeyitflgalamiynealkg
>d1a04a1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1a04a2 3.16.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a04b1 1.37.1.2.1 (150-216) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
erdvnqltprerdilkliaqglpnkmiarrlditestvkvhvkhmlkkmklksrveaavw
vhqerif
>d1a04b2 3.16.2.1.4 (5-142) Nitrate/nitrite response regulator (NARL), receiver domain {Escherichia coli}
epatilliddhpmlrtgvkqlismapditvvgeasngeqgielaesldpdlilldlnmpg
mngletldklrekslsgrivvfsvsnheedvvtalkrgadgyllkdmepedllkalhqaa
agemvlsealtpvlaasl
>d1a05a_ 3.65.1.1.4 3-isopropylmalate dehydrogenase, IPMDH {Thiobacillus ferrooxidans}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a05b_ 3.65.1.1.4 3-isopropylmalate dehydrogenase, IPMDH {Thiobacillus ferrooxidans}
mkkiaifagdgigpeivaaarqvldavdqaahlglrcteglvggaaldasddplpaaslq
lamaadavilgavggprwdayppakrpeqgllrlrkgldlyanlrpaqifpqlldasplr
pelvrdvdilvvreltgdiyfgqprglevidgkrrgfntmvydedeirriahvafraaqg
rrkqlcsvdkanvlettrlwrevvtevardypdvrlshmyvdnaamqlirapaqfdvllt
gnmfgdilsdeasqltgsigmlpsaslgegramyepihgsapdiagqdkanplatilsva
mmlrhslnaepwaqrveaavqrvldqglrtadiaapgtpvigtkamgaavvnalnlk
>d1a06__ 4.117.1.1.6 Calmodulin-dependent protein kinase {Rat (Rattus norvegicus)}
wkqaedirdiydfrdvlgtgafsevilaedkrtqklvaikciakkalegkegsmeneiav
lhkikhpnivalddiyesgghlylimqlvsggelfdrivekgfyterdasrlifqvldav
kylhdlgivhrdlkpenllyysldedskimisdfglskmedpgsvlstacgtpgyvapev
laqkpyskavdcwsigviayillcgyppfydendaklfeqilkaeyefdspywddisdsa
kdfirhlmekdpekrftceqalqhpwiagdtaldknihqsvseqikknfakskwkqafna
tavvrhm
>d1a07a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a07b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a08b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09a_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a09b_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a0aa_ 1.41.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0ab_ 1.41.1.1.5 Pho4 B/HLH domain {Baker's yeast (Saccharomyces cerevisiae)}
mkreshkhaeqarrnrlavalhelaslipaewkqqnvsaapskattveaacryirhlqqn
gst
>d1a0b__ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
ksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghki
kgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1a0ca_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cb_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cc_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0cd_ 3.1.13.2.7 D-xylose isomerase {Clostridium Thermosulfurogenes, also known as Thermoanaerobacter thermosulfurigenes}
nkyfenvskikyegpksnnpysfkfynpeevidgktmeehlrfsiaywhtftadgtdqfg
katmqrpwnhytdpmdiakarveaafeffdkinapyfcfhdrdiapegdtlretnknldt
ivamikdylktsktkvlwgtanlfsnprfvhgastscnadvfaysaaqvkkaleitkelg
genyvfwggregyetllntdmefeldnfarflhmavdyakeigfegqfliepkpkeptkh
qydfdvanvlaflrkydldkyfkvnieanhatlafhdfqhelryaringvlgsidantgd
mllgwdtdqfptdirmttlamyevikmggfdkgglnfdakvrrasfepedlflghiagmd
afakgfkvayklvkdrvfdkfieeryasykdgigadivsgkadfrslekyalersqivnk
sgrqellesilnqylfa
>d1a0da_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0db_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dc_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0dd_ 3.1.13.2.8 D-xylose isomerase {Bacillus stearothermophilus}
pyfdnistiayegpasknplafkfynpeekvgdktmeehlrfsvaywhtftgdgsdpfga
gnmirpwnkysgmdlakarveaafeffeklnipffcfhdvdiapegetlketyknldiiv
dmieeymktsktkllwntanlfthprfvhgaatscnadvfayaaakvkkgleiakrlgae
nyvfwggregyetllntdmkleldnlarflhmavdyakeigfdgqfliepkpkeptkhqy
dfdvatalaflqtyglkdyfkfnieanhatlaghtfehelrvarihgmlgsvdanqgdml
lgwdtdefptdlysttlamyeilkngglgrgglnfdakvrrgsfepedlfyahiagmdsf
avglkvahrliedrvfdefieeryksytegigreivegtadfhkleahalqlgeiqnqsg
rqerlktllnqyllevc
>d1a0ea_ 3.1.13.2.9 D-xylose isomerase {Thermotoga neapolitana}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0ed_ 3.1.13.2.9 D-xylose isomerase {Thermotoga neapolitana}
aeffpeipkvqfegkestnplafkfydpeeiidgkplkdhlkfsvafwhtfvnegrdpfg
dptadrpwnrytdpmdkafarvdalfefceklnieyfcfhdrdiapegktlretnkildk
vverikermkdsnvkllwgtanlfshprymhgaattcsadvfayaaaqvkkaleitkelg
gegyvfwggregyetllntdlgfelenlarflrmavdyakrigftgqfliepkpkeptkh
qydfdvatayaflkshgldeyfkfnieanhatlaghtfqhelrmarilgklgsidanqgd
lllgwdtdqfptnvydttlamyevikaggftkgglnfdakvrrasykvedlfighiagmd
tfalgfkvayklvkdgvldkfieekyrsfregigrdivegkvdfekleeyiidketielp
sgkqeyleslinsyivktilelr
>d1a0fa1 1.48.1.1.19 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1a0fa2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1a0fb1 1.48.1.1.19 (81-201) Glutathione S-transferase {Escherichia coli}
qllapvnsisryktiewlnyiatelhkgftplfrpdtpeeykptvraqlekklqyvneal
kdehwicgqrftiadaylftvlrwayavklnleglehiaafmqrmaerpevqdalsaegl
k
>d1a0fb2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
mklfykpgacslashitlresgkdftlvsvdlmkkrlengddyfavnpkgqvpalllddg
tlltegvaimqyladsvpdr
>d1a0ga_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkpl
>d1a0gb_ 5.13.1.1.1 D-amino acid aminotransferase {Bacillus strain YM-1}
gytlwndqivkdeevkidkedrgyqfgdgvyevvkvyngemftvnehidrlyasaekiri
tipytkdkfhqllhelveknelntghiyfqvtrgtsprahqfpentvkpviigytkenpr
plenlekgvkatfvedirwlrcdikslnllgavlakqeahekgcyeailhrnntvtegss
snvfgikdgilythpannmiakgitrdvviacaneinmpvkeipftthealkmdelfvts
ttseitpvieidgklirdgkvgewtrklqkqfetkipkplhi
>e1a0h.1a 2.41.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.1b 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1a0h.2d 2.41.1.2.12 (271-320) Thrombin {Bovine (Bos taurus)}
rtsedhfqpffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>e1a0h.2e 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>d1a0ha1 7.14.1.1.5 (164-270) Meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0hd1 7.14.1.1.5 (164-270) Meizothrombin domain {Bovine (Bos taurus)}
splletcvpdrgreyrgrlavtthgsrclawsseqakalskdqdfnpavplaenfcrnpd
gdeegawcyvadqpgdfeycdlnyceepvdgdlgdrlgedpdpdaaieg
>d1a0i_1 2.35.4.6.2 (241-349) ATP-dependent DNA ligase {Bacteriophage T7}
peneadgiiqglvwgtkglanegkvigfevllesgrlvnatnisralmdeftetvkeatl
sqwgffspygigdndactinpydgwacqisymeetpdgslrhpsfvmfr
>d1a0i_2 4.115.2.1.1 (2-240) ATP-dependent DNA ligase, N-terminal domain {Bacteriophage T7}
vniktnpfkavsfvesaikkaldnagyliaeikydgvrgnicvdntansywlsrvsktip
alehlngfdvrwkrllnddrcfykdgfmldgelmvkgvdfntgsgllrtkwtdtknqefh
eelfvepirkkdkvpfklhtghlhiklyailplhivesgedcdvmtllmqehvknmlpll
qeyfpeiewqaaesyevydmvelqqlyeqkraegheglivkdpmciykrgkksgwwkmk
>d1a0ja_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jb_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jc_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0jd_ 2.41.1.2.5 Trypsin(ogen) {North atlantic salmon (Salmo salar)}
ivggyecrknsasyqaslqsgyhfcggslisstwvvsaahcyksriqvrlgehniavneg
teqfidsvkvimhpsynsrnldndimliklskpaslnsyvstvalpsscassgtrclvsg
wgnlsgsssnypdtlrcldlpilsssscnsaypgqitsnmfcagfmeggkdscqgdsggp
vvcngqlqgvvswgygcaqrnkpgvytkvcnyrswisstmssn
>d1a0k__ 4.86.1.1.6 Profilin (actin-binding protein) {Mouse-ear cress (Arabidopsis thaliana)}
swqsyvddhlmcdvegnhltaaailgqdgsvwaqsakfpqlkpqeidgikkdfeepgfla
ptglflggekymviqgeqgavirgkkgpggvtikktnqalvfgfydepmtggqcnlvver
lgdyliesel
>d1a0la_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0lb_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0lc_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0ld_ 2.41.1.2.19 beta-Tryptase {Human (Homo sapiens)}
ivggqeaprskwpwqvslrvhgpywmhfcggslihpqwvltaahcvgpdvkdlaalrvql
reqhlyyqdqllpvsriivhpqfytaqigadialleleepvkvsshvhtvtlppasetfp
pgmpcwvtgwgdvdnderlpppfplkqvkvpimenhicdakyhlgaytgddvrivrddml
cagntrrdscqgdsggplvckvngtwlqagvvswgegcaqpnrpgiytrvtyyldwihhy
vpkk
>d1a0nb_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1a0oa_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0ob_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetvev
>d1a0oc_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0od_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1a0oe_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0of_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
prriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviea
dqitfetve
>d1a0og_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1a0oh_ 4.47.21.1.1 CheY-binding domain of CheA {Escherichia coli}
rriilsrlkagevdlleeelghlttltdvvkgadslsailpgdiaedditavlcfviead
qitfetv
>d1a0p_1 1.61.2.1.2 (3-100) Recombinase XerD {Escherichia coli}
qdlarieqfldalwleknlaentlnayrrdlsmmvewlhhrgltlataqsddlqallaer
leggykatssarllsavrrlfqylyrekfreddpsahl
>d1a0p_2 4.133.1.1.4 (111-292) Recombinase XerD {Escherichia coli}
kdlseaqverllqaplidqplelrdkamlevlyatglrvselvgltmsdislrqgvvrvi
gkgnkerlvplgeeavywletylehgrpwllngvsidvlfpsqraqqmtrqtfwhrikhy
avlagidseklsphvlrhafathllnhgadlrvvqmllghsdlsttqiythvaterlrql
hq
>d1a0qh1 2.1.1.1.114 (2-114) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
vqlqesdaelvkpgasvkisckasgytftdhvihwvkqkpeqglewigyispgngdikyn
ekfkgkatltadkssstaymqlnsltsedsavylckrgyygrsnvdywgqgttltvssa
>d1a0qh2 2.1.1.2.112 (115-211) Immunoglobulin (constant domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpsstwpsetvtcnvahpasstkvdkkie
>d1a0ql1 2.1.1.1.114 (2-108) Immunoglobulin (variable domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
ieltqspsslsaslggkvtitckasqdikkyigwyqhkpgkqprllihytstllpgipsr
frgsgsgrdysfsisnlepediatyyclqyynlrtfgggtkleikr
>d1a0ql2 2.1.1.2.112 (109-213) Immunoglobulin (constant domains of L and H chains) {Fab 29G11 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfyskdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1a0rb_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
seldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiyam
hwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldnic
siynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttft
ghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngnaf
atgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdalk
adragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1a0rg_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
pviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgipedk
npfke
>d1a0rp_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
fegqashtgpkgvindwrkfklesedsdsvahskkeilrqmsspqsrddkdskerfsrkm
svqeyelihkdkedenclrkyrrqcmqdmhqklsfgprygfvyelesgeqfletiekeqk
ittivvhiyedgikgcdalnssliclaaeypmvkfckikasntgagdrfssdvlptllvy
kggellsnfisvteqlaeefftgdvesflneygllpek
>d1a0sp_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sq_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0sr_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tp_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tq_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0tr_ 6.4.3.2.3 Sucrose-specific porin {Enterobacterium (Salmonella typhimurium)}
sgfefhgyarsgvimndsgastksgayitpagetggaigrlgnqadtyvemnlehkqtld
ngattrfkvmvadgqtsyndwtastsdlnvrqafvelgnlptfagpfkgstlwagkrfdr
dnfdihwidsdvvflagtgggiydvkwndglrsnfslygrnfgdiddssnsvqnyiltmn
hfagplqmmvsglrakdnderkdsngnlakgdaantgvhallglhndsfyglrdgsskta
llyghglgaevkgigsdgalrpgadtwriasygttplsenwsvapamlaqrskdryadgd
syqwatfnlrliqainqnfalayegsyqymdlkpegyndrqavngsfykltfaptfkvgs
igdffsrpeirfytswmdwskklnnyasddalgsdgfnsggewsfgvqmetwf
>d1a0ua_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0ub_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0uc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0ud_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0va_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0vb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0vc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0vd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypytqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0wa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0wb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0wc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0wd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypatqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0xa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0xb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypgtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0xc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0xd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypgtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0ya_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0yb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypetqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0yc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0yd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypetqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0za_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0zb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a0zc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a0zd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1a10e_ 3.33.1.1.3 Subtilisin Carlsberg {Bacillus licheniformis, alcalase}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgssgntntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1a10i_ 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtpeyridrvrlfvdkldniaevp
rvg
>d1a12a_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a12b_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a12c_ 2.60.4.1.1 Regulator of chromosome condensation RCC1 {Human (Homo sapiens)}
kkvkvshrshstepglvltlgqgdvgqlglgenvmerkkpalvsipedvvqaeaggmhtv
clsksgqvysfgcndegalgrdtsvegsemvpgkvelqekvvqvsagdshtaaltddgrv
flwgsfrdnngvigllepmkksmvpvqvqldvpvvkvasgndhlvmltadgdlytlgcge
qgqlgrvpelfanrggrqglerllvpkcvmlksrgsrghvrfqdafcgayftfaishegh
vygfglsnyhqlgtpgtescfipqnltsfknstkswvgfsggqhhtvcmdsegkayslgr
aeygrlglgegaeeksiptlisrlpavssvacgasvgyavtkdgrvfawgmgtnyqlgtg
qdedawspvemmgkqlenrvvlsvssggqhtvllvkdkeqs
>d1a14h_ 2.1.1.1.62 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
qvqlqqsgaelvkpgasvrmsckasgytftnynmywvkqspgqglewigifypgngdtsy
nqkfkdkatltadkssntaymqlssltsedsavyycarsggsyrydggfdywgqgttvtv
>d1a14l_ 2.1.1.1.62 Immunoglobulin (variable domains of L and H chains) {Fab NC10 (mouse), kappa L chain}
dieltqttsslsaslgdrvtiscrasqdisnylnwyqqnpdgtvklliyytsnlhsevps
rfsgsgsgtdysltisnleqediatyfcqqdftlpftfgggtaa
>d1a14n_ 2.59.1.1.2 Influenza neuraminidase {Influenza virus A, different strains}
rdfnnltkglctinswhiygkdnavrigedsdvlvtrepyvscdpdecrfyalsqgttir
gkhsngtihdrsqyraliswplsspptvynsrvecigwsstschdgktrmsicisgpnnn
asaviwynrrpvteintwarnilrtqesecvchngvcpvvftdgsatgpaetriyyfkeg
kilkweplagtakhieecscygeraeitctcrdnwqgsnrpviridpvamthtsqyicsp
vltdnprpndptvgkcndpypgnnnngvkgfsyldgvntwlgrtisiasrsgyemlkvpn
altddkskptqgqtivlntdwsgysgsfmdywaegecyracfyvelirgrpkedkvwwts
nsivsmcssteflgqwdwpdgakieyfl
>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
>d1a16__ 4.101.1.1.5 Aminopeptidase P {Escherichia coli}
seisrqefqrrrqalveqmqpgsaalifaapevtrsadseypyrqnsdfwyftgfnepea
vlvliksddthnhsvlfnrvrdltaeiwfgrrlgqdaapeklgvdralafseinqqlyql
lngldvvyhaqgeyayadvivnsaleklrkgsrqnltapatmidwrpvvhemrlfkspee
iavlrrageitamahtramekcrpgmfeyhlegeihhefnrhgarypsyntivgsgengc
ilhytenecemrdgdlvlidagceykgyagditrtfpvngkftqaqreiydivleslets
lrlyrpgtsilevtgevvrimvsglvklgilkgdvdeliaqnahrpffmhglshwlgldv
hdvgvygqdrsrilepgmvltvepglyiapdaevpeqyrgigirieddivitetgnenlt
asvvkkpeeiealmvaarkq
>d1a17__ 1.110.8.1.1 Protein phosphatase 5 {Human (Homo sapiens)}
ppadgalkraeelktqandyfkakdyenaikfysqaielnpsnaiyygnrslaylrtecy
gyalgdatraieldkkyikgyyrraasnmalgkfraalrdyetvvkvkphdkdakmkyqe
cnkivkqkaferaiagdehkrsvvdsldiesmtiedeys
>d1a18__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>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
>d1a1aa_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
dsiqaeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvk
hykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ab_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
aeewyfgkitrreserlllnaenprgtflvresettkgayslsvsdfdnakglnvkhyki
rkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ba_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1bb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1ca_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
siqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkh
ykirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1cb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1d__ 2.35.4.9.1 RNA polymerase subunit RBP8 {Baker's yeast (Saccharomyces cerevisiae)}
msntlfddifqvsevdpgrynkvcrieaasttqdqckltldinvelfpvaaqdsltvtia
sslnledtpandssatrswrppqagdrsladdydyvmygtaykfeevskdliavyysfgg
llmrlegnyrnlnnlkqenayllirr
>d1a1ea_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1eb_ 4.72.1.1.3 c-src tyrosine kinase {Human (Homo sapiens)}
iqaeewyfgkitrreserlllnaenprgtflvresettkgayclsvsdfdnakglnvkhy
kirkldsggfyitsrtqfnslqqlvayyskhadglchrlttvcp
>d1a1fa1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1fa2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1fa3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ga1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsdssnltrhirihtg
>d1a1ga2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ga3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ha1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsqsgsltrhirihtg
>d1a1ha2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ha3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ia1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ia2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ia3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ja1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ja2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ja3 7.31.1.1.1 (160-186) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihl
>d1a1ka1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsadltrhirihtg
>d1a1ka2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1ka3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1la1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1a1la2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1a1la3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1a1ma1 2.1.1.2.9 (182-278) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwephh
>d1a1ma2 4.17.1.1.16 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B53}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1mb1 2.1.1.2.9 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1na1 2.1.1.2.10 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1na2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1nb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1oa1 2.1.1.2.9 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1a1oa2 4.17.1.1.16 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B53}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprppwieqegpeyw
drntqifktntqtyrenlrialryynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a1ob1 2.1.1.2.9 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B53}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a1qa_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettmrs
pvf
>d1a1qb_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>d1a1qc_ 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitaysqqtrgllgciitsltgrdknqvegevqvvstatqsflatcvngvcwtvyhgags
ktlagpkgpitqmytnvdqdlvgwqappgarsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpvsylkgssggpllcpsghavgifraavctrgvakavdfvpvesmettm
>e1a1r.1a 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
vegevqivstatqtflatcingvcwtvyhgagtrtiaspkgpviqmytnvdqdlvgwpap
qgsrsltpctcgssdlylvtrhadvipvrrrgdsrgsllsprpisylkgssggpllcptg
havglfraavctrgvakavdfipvenlettmr
>e1a1r.2b 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
pitayaqqtrgllgciitsltgrdknqvegevqivstatqtflatcingvcwtvyhgagt
rtiaspkgpviqmytnvdqdlvgwpapqgsrsltpctcgssdlylvtrhadvipvrrrgd
srgsllsprpisylkgssggpllcptghavglfraavctrgvakavdfipvenlettmr
>e1a1r.2d 2.41.1.3.3 NS3 protease {Human hepatitis C virus, Bk strain}
kgsvvivgrivlsgkpaiipk
>d1a1s_1 3.66.1.1.5 (1-150) Ornithine transcarbamoylase {Pyrococcus furiosus}
vvslagrdllclqdytaeeiwtiletakmfkiwqkigkphrllegktlamifqkpstrtr
vsfevamahlgghalylnaqdlqlrrgetiadtarvlsryvdaimarvydhkdvedlaky
atvpvinglsdfshpcqaladymtiwekkg
>d1a1s_2 3.66.1.1.5 (151-313) Ornithine transcarbamoylase {Pyrococcus furiosus}
tikgvkvvyvgdgnnvahslmiagtklgadvvvatpegyepdekvikwaeqnaaesggsf
ellhdpvkavkdadviytdvwasmgqeaeaeerrkifrpfqvnkdlvkhakpdymfmhcl
pahrgeevtddvidspnsvvwdqaenrlhaqkavlalvmggik
>d1a1ta_ 7.34.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqkgnfrnqrktvkcfncgkeghiakncraprkkgcwkcgkeghqmkdcterqan
>d1a1ua_ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1uc_ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfekireynealelkdaq
>d1a1va1 3.30.1.11.1 (190-325) HCV helicase domain {Hepatitis C virus, HCV}
ppavpqsfqvahlhaptgsgkstkvpaayaaqgykvlvlnpsvaatlgfgaymskahgvd
pnirtgvrtittgspitystygkfladggxsggaydiiicdechstdatsilgigtvldq
aetagarlvvlatatp
>d1a1va2 3.30.1.11.1 (326-624) HCV helicase domain {Hepatitis C virus, HCV}
pgsvtvphpnieevalsttgeipfygkaiplevikggrhlifchskkkcdelaaklvalg
inavayyrgldvsviptsgdvvvvatdalmtgftgdfdsvidcntxvtqtvdfsldptft
ietttlpqdavsrtqrrgrtgrgkpgiyrfvapgerpsgmfdssvlcecydagxawyelt
paettvrlraymntpglpvcqdhlefwegvftglthidahflsqtkqsgenfpylvayqa
tvcaraqapppswdqmwkclirlkptlhgptpllyrlgavqnevtlthpitkyimtcms
>d1a1w__ 1.76.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkylclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>d1a1x__ 2.56.1.1.2 MTCP-1 {Human (Homo sapiens)}
agedvgappdhlwvhqegiyrdeyqrtwvavveeetsflrarvqqiqvplgdaarpshll
tsqlplmwqlypeerymdnnsrlwqiqhhlmvrgvqelllkllpdd
>d1a1ye_ 3.33.1.1.3 Subtilisin Carlsberg {Bacillus licheniformis, alcalase}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgssgntntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1a1yi_ 4.33.1.1.2 Chymotrypsin inhibitor CI-2 {Barley (Hordeum vulgare)}
ktewpelvgksveeakkvilqdkpeaqiivlpvgtivtmeyridrvrlfvdkldniaevp
rvg
>d1a1z__ 1.76.1.1.3 FADD (Mort1) {Human (Homo sapiens)}
mdpflvllhsvssslssseltelkglclgrvgkrklervqsgldlfsmlleqndlepght
ellrellaslrrhdllrrvddfe
>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
>d1a21b1 2.1.2.1.2 (4-106) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
tgraynltwkstnfktilewepksidhvytvqistrlenwkskcfltaetecdltdevvk
dvgqtymarvlsyparngnttgfpeeppfrnspeftpyldtnl
>d1a21b2 2.1.2.1.2 (107-208) Extracellular region of human tissue factor {Rabbit (Oryctolagus cuniculus)}
gqptiqsfeqvgtklnvtvqdartlvrrngtflslravfgkdlnytlyywrasstgkkta
ttntneflidvdkgenycfsvqavipsrkrkqrspesltect
>d1a22a_ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
fptiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesipt
psnreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleer
iqtlmgrlegqifkqtyskfdtdallknygllycfrkdmdkvetflrivqcrsvegscgf
>d1a22b1 2.1.2.1.8 (233-328) Growth hormone receptor {Human (Homo sapiens)}
pkftkcrsperetfschwtdevhhgtknlgpiqlfytrrntqewtqewkecpdyvsagen
scyfnssftsiwipycikltsnggtvdekcfsvdei
>d1a22b2 2.1.2.1.8 (329-437) Growth hormone receptor {Human (Homo sapiens)}
vqpdppialnwtllnvsltgihadiqvrweaprnadiqkgwmvleyelqykevnetkwkm
mdpilttsvpvyslkvdkeyevrvrskqrnsgnygefsevlyvtlpqms
>d1a23_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a23_2 3.38.1.4.1 (1-64,129-189) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsekk
>d1a24_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a24_2 3.38.1.4.1 (1-64,129-189) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsekk
>d1a25a_ 2.6.1.2.2 C2 domain from protein kinase c (beta) {Rat (Rattus norvegicus)}
errgriyiqahidrevlivvvrdaknlvpmdpnglsdpyvklklipdpkseskqktktik
cslnpewnetfrfqlkesdkdrrlsveiwdwdltsrndfmgslsfgiselqkagvdgwfk
llsqeegeyfnv
>d1a25b_ 2.6.1.2.2 C2 domain from protein kinase c (beta) {Rat (Rattus norvegicus)}
errgriyiqahidrevlivvvrdaknlvpmdpnglsdpyvklklipdpkseskqktktik
cslnpewnetfrfqlkesdkdrrlsveiwdwdltsrndfmgslsfgiselqkagvdgwfk
llsqeegeyfnv
>d1a26_1 1.44.1.1.1 (662-796) Domain of poly(ADP-ribose) polymerase {Chicken (Gallus gallus)}
ksklakpiqdlikmifdvesmkkamvefeidlqkmplgklskrqiqsaysilnevqqavs
dggsesqildlsnrfytliphdfgmkkppllsnleyiqakvqmldnlldievaysllrgg
nedgdkdpidinyek
>d1a26_2 4.136.1.2.1 (797-1012) Poly(ADP-ribose) polymerase, C-terminal domain {Chicken (Gallus gallus)}
lrtdikvvdkdseeakiikqyvknthaathnaydlkvveifrieregesqrykpfkqlhn
rqllwhgsrttnfagilsqglriappeapvtgymfgkgiyfadmvsksanychtsqadpi
glillgevalgnmyelknashitklpkgkhsvkglgktapdptatttldgvevplgngis
tgindtcllyneyivydvaqvnlkyllklkfnykts
>d1a27__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevfg
>d1a28a_ 1.114.1.1.3 Progesterone receptor {Human (Homo sapiens)}
qlipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrn
lhiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltm
wqipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqk
gvvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkil
agmvkpllfhk
>d1a28b_ 1.114.1.1.3 Progesterone receptor {Human (Homo sapiens)}
lipplinllmsiepdviyaghdntkpdtssslltslnqlgerqllsvvkwskslpgfrnl
hiddqitliqyswmslmvfglgwrsykhvsgqmlyfapdlilneqrmkessfyslcltmw
qipqefvklqvsqeeflcmkvllllntipleglrsqtqfeemrssyirelikaiglrqkg
vvsssqrfyqltklldnlhdlvkqlhlyclntfiqsralsvefpemmseviaaqlpkila
gmvkpllfh
>d1a29__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
qlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgngt
idfpefltmmarkmkdtdseeeireafrvfdkdgngyisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvqmmt
>d1a2aa_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ab_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ac_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ad_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ae_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2af_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ag_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2ah_ 1.123.1.2.4 Snake phospholipase A2 {Chinese water moccasin (Agkistrodon halys pallas), different isoforms}
nllqfnkmikeetgknaipfyafygcycggggngkpkdgtdrccfvhdccygrlvncntk
sdiysyslkegyitcgkgtnceeqicecdrvaaecfrrnldtynngymfyrdskctetse
ec
>d1a2b__ 3.30.1.6.8 RhoA {Human (Homo sapiens)}
irkklvivgdvacgktcllivfskdqfpevyvptvfenyvadievdgkqvelalwdtagq
edydrlrplsypdtdvilmcfsidspdslenipekwtpevkhfcpnvpiilvgnkkdlrn
dehtrrelakmkqepvkpeegrdmanrigafgymecsaktkdgvrevfematraalqa
>e1a2c.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1a2c.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1a2da_ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2db_ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1a2f__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalkgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1a2g__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymhlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1a2i__ 1.126.1.1.2 Cytochrome c3 {Desulfovibrio vulgaris}
apkapadglkmeatkqpvvfnhsthksvkcgdchhpvngkedyrkcgtagchdsmdkkdk
sakgyyhvmhdkntkfkscvgchvevagadaakkkdltgckkskche
>d1a2j_1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2j_2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2ka_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kb_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
hnfg
>d1a2kc_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlev
>d1a2kd_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqt
>d1a2ke_ 3.30.1.6.6 Ran {Dog (Canis familiaris)}
qvqfklvlvgdggtgkttfvkrhltgefekkyvatlgvevhplvfhtnrgpikfnvwdta
gqekfgglrdgyyiqaqcaiimfdvtsrvtyknvpnwhrdlvrvcenipivlcgnkvdik
drkvkaksivfhrkknlqyydisaksnynfekpflwlarkligdpnlefvampalappev
vmdpalaaqyehdlevaqttalpde
>d1a2la1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2la2 3.38.1.4.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2lb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2lb2 3.38.1.4.1 (3-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
yedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyhvn
fmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvkyl
sek
>d1a2ma1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2ma2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2mb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1a2mb2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcphcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1a2n__ 4.52.2.1.1 UDP-N-acetylglucosamine enolpyruvyl transferase (EPT, MurA, MurZ) {Escherichia coli}
mdkfrvqgptklqgevtisgaknaalpilfaallaeepveiqnvpklkdvdtsmkllsql
gakverngsvhidardvnvfcapydlvktmrasiwalgplvarfgqgqvslpggatigar
pvdlhisgleqlgatikleegyvkasvdgrlkgahivmdkvsvgatvtimcaatlaegtt
iienaarepeivdtanflitlgakisgqgtdriviegverlgggvyrvlpdrietgtflv
aaaisrgkiicrnaqpdtldavlaklrdagadievgedwisldmhgkrpkavnvrtaphp
afptdmqaqftllnlvaegtgfitetvfenrfmhvpelsrmgahaeiesntvichgvekl
sgaqvmatdlrasaslvlagciaegttvvdriyhidrgyeriedklralganiervkg
>d1a2oa1 3.16.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2oa2 3.32.1.1.1 (141-347) Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
maapttlkagpllssekliaigastggteairhvlqplplsspaviitqhmppgftrsfa
erlnklcqisvkeaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsv
dvlfhsvakhagrnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreain
mggvsevvdlsqvsqqmlakisagqai
>d1a2ob1 3.16.2.1.7 (1-140) Methylesterase CheB, N-terminal domain {Salmonella typhimurium}
mskirvlsvddsalmrqimteiinshsdmemvatapdplvardlikkfnpdvltldvemp
rmdgldfleklmrlrpmpvvmvssltgkgsevtlralelgaidfvtkpqlgiregmlays
emiaekvrtaarariaahkp
>d1a2ob2 3.32.1.1.1 (141-347) Methylesterase CheB, C-terminal domain {Salmonella typhimurium}
maapttlkagpllssekliaigastggteairhvlqplplsspaviitqhmppgftrsfa
erlnklcqisvkeaedgervlpghayiapgdkhmelarsganyqikihdgppvnrhrpsv
dvlfhsvakhagrnavgviltgmgndgaagmlamyqagawtiaqneascvvfgmpreain
mggvsevvdlsqvsqqmlakisagqai
>d1a2pa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2pb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2pc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1a2q__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasmvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsiqstlpgnkygaysgtxmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1a2s__ 1.3.1.1.1 Cytochrome c6 (synonym: cytochrome c553) {Monoraphidium braunii}
eadlalgkavfdgncaachagggnnvipdhtlqkaaieqfldggfnieaivyqiengkga
mpawdgrldedeiagvaayvydqaagnkw
>d1a2t__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2u__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a2va1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>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
>d1a2vb1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vb2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vb3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vc1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vc2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vc3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vd1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vd2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vd3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2ve1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2ve2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2ve3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2vf1 2.27.2.1.4 (237-672) Copper amine oxidase, domain 3 (catalytic) {Yeast (Hansenula polymorpha)}
peappinvtqpegvsfkmtgnvmewsnfkfhigfnyregivlsdvsyndhgnvrpifhri
slsemivpygspefphqrkhaldigeygagymtnplslgcdckgvihyldahfsdragdp
itvknavciheeddgllfkhsdfrdnfatslvtratklvvsqiftaanxeyclywvfmqd
gairldirltgilntyilgddeeagpwgtrvypnvnahnhqhlfslridpridgdgnsaa
acdaksspyplgspenmygnafysekttfktvkdsltnyesatgrswdifnpnkvnpysg
kppsyklvstqcppllakegslvakrapwashsvnvvpykdnrlypsgdhvpqwsgdgvr
gmrewigdgsenidntdilffhtfgithfpapedfplmpaepitlmlrprhfftenpgld
iqpsyamttseakrav
>d1a2vf2 4.15.2.1.4 (18-115) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
parpahpldplstaeikaatntvksyfagkkisfntvtlreparkayiqwkeqggplppr
layyvileagkpgvkeglvdlaslsvietraletvqpi
>d1a2vf3 4.15.2.1.4 (116-236) Copper amine oxidase, domains 1 and 2 {Yeast (Hansenula polymorpha)}
ltvedlcsteevirndpavieqcvlsgipanemhkvycdpwtigyderwgtgkrlqqalv
yyrsdeddsqyshpldfcpivdteekkvifidipnrrrkvskhkhanfypkhmiekvgam
r
>d1a2wa_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2wb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1a2xa_ 1.42.1.5.3 Troponin C {Rabbit (Oryctolagus cuniculus)}
dqqaearsylseemiaefkaafdmfdadgggdisvkelgtvmrmlgqtptkeeldaiiee
vdedgsgtidfeeflvmmvrqmkedakgkseeelaecfrifdrnadgyidaeelaeifra
sgehvtdeeieslmkdgdknndgridfdeflkmmegvq
>d1a2ya_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpedfgsyycqhfwstprtfgggtkleik
>d1a2yb_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a2yc_ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhglanyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1a2za_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zb_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zc_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a2zd_ 3.47.3.1.1 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Thermococcus litoralis}
mkkvlitgfepfggdsknpteqiakyfdrkqignamvygrvlpvsvkratielkryleei
kpeivinlglaptysnitveriavniidaripdndgyqpidekieedaplaymatlpvra
itktlrdngipatisysagtylcnyvmfktlhfskiegyplkagfihvpytpdqvvnkff
llgkntpsmcleaeikaielavkvsldylekdrddikipl
>d1a30a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a30b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a31a1 4.133.1.2.1 (431-626,720-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravXklnxldpritvawckkwgvpiekiynktqrekfawaidmaded
yef
>d1a31a2 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a32__ 1.16.1.2.1 Ribosomal protein S15 {Bacillus stearothermophilus}
ltqerkreiieqfkvhendtgspevqiailteqinnlnehlrvhkkdhhsrrgllkmvgk
rrrllaylrnkdvaryreiveklgl
>d1a33__ 2.55.1.1.4 Cyclophilin (eukaryotic) {Nematode (Brugia malayi)}
kdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhykgst
fhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntngsqf
fitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1a34a_ 2.9.1.2.2 STMV coat protein {Satellite tobacco mosaic virus}
tgdnsnvvtmiragsypkvnptptwvraipfevsvqsgiafkvpvgslfsanfrtdsfts
vtvmsvrawtqltppvneysfvrlkplfktgdsteefegrasnintrasvgyriptnlrq
ntvaadnvcevrsncrqvalvisccfn
>d1a35a1 4.133.1.2.1 (431-635,713-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravailcnhqrappktfeksmmnlqtkidakkeqlaXqialgtskln
fldpritvawckkwgvpiekiynktqrekfawaidmadedyef
>d1a35a2 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a36a1 1.2.5.1.1 (641-712) Eukaryotic DNA topoisomerase I, dispensable insert domain {Human (Homo sapiens)}
eksmmnlqtkidakkeqladarrdlksakadakvmkdaktkkvveskkkavqrleeqlmk
levqatdreenk
>d1a36a2 4.133.1.2.1 (431-633,713-765) Eukaryotic DNA topoisomerase I, catalytic core {Human (Homo sapiens)}
pssrikgekdwqkyetarrlkkcvdkirnqyredwkskemkvrqravalyfidklalrag
nekeegetadtvgccslrvehinlhpeldgqeyvvefdflgkdsiryynkvpvekrvfkn
lqlfmenkqpeddlfdrlntgilnkhlqdlmegltakvfrtynasitlqqqlkeltapde
nipakilsynranravailcnhqXqialgtsklnfldpritvawckkwgvpiekiynktq
rekfawaidmadedyef
>d1a36a3 5.12.1.1.1 (215-430) Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment {Human (Homo sapiens)}
ikwkflehkgpvfappyeplpenvkfyydgkvmklspkaeevatffakmldheyttkeif
rknffkdwrkemtneekniitnlskcdftqmsqyfkaqtearkqmskeeklkikeenekl
lkeygfcimdnhkerianfkieppglfrgrgnhpkmgmlkrrimpediiincskdakvps
pppghkwkevrhdnkvtwlvswteniqgsikyimln
>d1a37a_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a37b_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a38a_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a38b_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a39__ 2.26.1.9.4 Endoglucanase I {Humicola insolens}
kpgetkevhpqlttfrctkrggckpatnfivldslwhwihraeglgpggcgdwgnpppkd
vcpdvescakncimegipdysqygvttngtslrlqhilpdgrvpsprvylldktkrryem
lhltgfeftfdvdatklpcgmnsalylsemhptgakskynpggayygtgycdaqcfvtpf
inglgniegkgsccnemdiweansrashvaphtcnkkglylcegeecafegvcdkngcgw
nnyrvnvtdyygrgeefkvntlkpftvvtqflanrrgklekihrfyvqdgkviesfytnk
egvpytnmiddefceatgsrkymelgatqgmgealtrgmvlamsiwwdqggnmewldhge
agpcakgegapsnivqvepfpevtytnlrwgeigstyqelq
>d1a3aa_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
lfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiav
phgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnald
desvierlahttsvdevlellagrk
>d1a3ab_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
fklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiavp
hgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnaldd
esvierlahttsvdevlella
>d1a3ac_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
nlfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesia
vphgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnal
ddesvierlahttsvdevlellagrk
>d1a3ad_ 4.88.1.1.2 Phosphotransferase IIa-mannitol {Escherichia coli}
lfklgaeniflgrkaatkeeairfageqlvkggyvepeyvqamldrekltptylgesiav
phgtveakdrvlktgvvfcqypegvrfgeeeddiarlvigiaarnnehiqvitsltnald
desvierlahttsvdevlellagr
>e1a3b.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3b.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3c__ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
qkavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpv
tvgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalv
dvgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a3d__ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>e1a3e.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1a3e.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a3fa_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fb_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3fc_ 1.123.1.2.2 Snake phospholipase A2 {Indian cobra (Naja naja naja)}
nlyqfknmikctvpsrswwdfadygcycgrggsgtpvddldrccqvhdncyneaekisgc
wpyfktysyecsqgtltckgdnnacaasvcdcdrlaaicfagapyndnnynidlkarcq
>d1a3ga_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gb_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3gc_ 5.13.1.1.2 Branched-chain amino acid aminotransferase {Escherichia coli}
kadyiwfngemvrwedakvhvmshalhygtsvfegircydshkgpvvfrhrehmqrlhds
akiyrfpvsqsidelmeacrdvirknnltsayirplifvgdvgmgvnppagystdviiaa
fpwgaylgaealeqgidamvsswnraapntiptaakaggnylssllvgsearrhgyqegi
aldvngyisegagenlfevkdgvlftppftssalpgitrdaiiklakelgievreqvlsr
eslyladevfmsgtaaeitpvrsvdgiqvgegrcgpvtkriqqaffglftgetedkwgwl
dqvnq
>d1a3h__ 3.1.7.3.7 Endoglucanase Cel5a {Bacillus agaradherans}
svveehgqlsisngelvnergeqvqlkgmsshglqwygqfvnyesmkwlrddwginvfra
amytssggyiddpsvkekvkeaveaaidldiyviidwhilsdndpniykeeakdffdems
elygdypnviyeianepngsdvtwgnqikpyaeevipiirnndpnniiivgtgtwsqdvh
haadnqladpnvmyafhfyagthgqnlrdqvdyaldqgaaifvsewgtsaatgdggvfld
eaqvwidfmdernlswanwslthkdessaalmpganptggwteaelspsgtfvrekires
>d1a3k__ 2.26.1.3.5 Galectin-3 CRD {Human (Homo sapiens)}
livpynlplpggvvprmlitilgtvkpnanrialdfqrgndvafhfnprfnennrrvivc
ntkldnnwgreerqsvfpfesgkpfkiqvlvepdhfkvavndahllqynhrvkklneisk
lgisgdidltsasytmi
>d1a3lh1 2.1.1.1.104 (1-113) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
evqleesgpelvrpgtsvkisckasgytftnywlgwvkqrpghgfewigdiypggvyttn
nekfrgkailtadtssstaymqlssltsedsavyfcaraggyytggdywgqgtsvtvss
>d1a3lh2 2.1.1.2.105 (114-227) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivp
>d1a3ll1 2.1.1.1.104 (1-107) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
divltqaafsnpvtlgasasiscrssksllnsngiihmywylqkpgqspqlliyqmskla
sgapdrfsgsgsgtdftlrisrveaedvgvyycaqnlelpytfgggtkleik
>d1a3ll2 2.1.1.2.105 (108-212) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab 13G5 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
tkdstysmsstltltkdeyerhnsytceathktstspivksfnrn
>d1a3na_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3nb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3nc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3nd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3oa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttkthfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3ob_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3oc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttkthfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a3od_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
hltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkvk
ahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgke
ftppvqaayqkvvagvanalahkyh
>d1a3p__ 7.3.11.1.12 Epidermal growth factor, EGF {Mouse (Mus musculus)}
pgxpssydgyclnggvxmhiesldsytcncvigysgdrcqtrdlr
>d1a3qa1 2.1.1.5.22 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>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
>d1a3qb1 2.1.1.5.22 (227-327) p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
nlkisrmdktagsvrggdevyllcdkvqkddievrfyeddengwqafgdfsptdvhkqya
ivfrtppyhkmkierpvtvflqlkrkrggdvsdskqftyyp
>d1a3qb2 2.2.5.1.4 (37-226) p50 subunit of NF-kappa B (NFKB), N-terminal domain {Mouse (Mus musculus)}
gpylviveqpkqrgfrfrygcegpshgglpgassekgrktyptvkicnyegpakievdlv
thsdpprahahslvgkqcselgicavsvgpkdmtaqfnnlgvlhvtkknmmgtmiqklqr
qrlrsrpqglteaeqreleqeakelkkvmdlsivrlrfsaflrslplkpvisqpihdsks
pgas
>d1a3rh1 2.1.1.1.15 (2-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytkyd
pkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssakt
tap
>d1a3rh2 2.1.1.2.25 (120-228) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
svyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1a3rl1 2.1.1.1.15 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkradaapt
>d1a3rl2 2.1.1.2.25 (115-214) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
vsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqdskdstys
msstltltkdeyerhnsytceathktstspivksfnrnec
>d1a3s__ 4.18.1.1.5 Ubiquitin conjugating enzyme {Human/mouse (Homo sapiens/Mus musculus), ubc9}
msgialsrlaqerkawrkdhpfgfvavptknpdgtmnlmnwecaipgkkgtpwegglfkl
rmlfkddypssppkckfepplfhpnvypsgtvclsileedkdwrpaitikqillgiqell
nepniqdpaqaeaytiycqnrveyekrvraqakkfaps
>d1a3t__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3u__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3v__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1a3wa1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wa2 3.1.11.1.4 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wa3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3wb1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3wb2 3.1.11.1.4 (2-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
srlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyhk
svidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtandv
ltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavqk
kliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgnyp
inavttmaetaviaeqaiaylpnyd
>d1a3wb3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xa1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xa2 3.1.11.1.4 (1-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
msrlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyh
ksvidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtand
vltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavq
kkliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgny
pinavttmaetaviaeqaiaylpnyd
>d1a3xa3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3xb1 2.52.1.1.4 (88-188) Pyruvate kinase {Baker's yeast (Saccharomyces cerevisiae)}
peirtgtttndvdypippnhemifttddkyakacddkimyvdyknitkvisagriiyvdd
gvlsfqvlevvddktlkvkalnagkicshkgvnlpgtdvdl
>d1a3xb2 3.1.11.1.4 (1-87,189-366) Pyruvate kinase, N-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
msrlerltslnvvagsdlrrtsiigtigpktnnpetlvalrkaglnivrmnfshgsyeyh
ksvidnarkseelypgrplaialdtkgXpalsekdkedlrfgvkngvhmvfasfirtand
vltirevlgeqgkdvkiivkienqqgvnnfdeilkvtdgvmvargdlgieipapevlavq
kkliaksnlagkpvicatqmlesmtynprptraevsdvgnaildgadcvmlsgetakgny
pinavttmaetaviaeqaiaylpnyd
>d1a3xb3 3.40.1.1.4 (367-500) Pyruvate kinase, C-terminal domain {Baker's yeast (Saccharomyces cerevisiae)}
dmrnctpkptsttetvaasavaavfeqkakaiivlstsgttprlvskyrpncpiilvtrc
praarfshlyrgvfpfvfekepvsdwtddvearinfgiekakefgilkkgdtyvsiqgfk
agaghsntlqvstv
>d1a3ya_ 2.53.1.1.6 Odorant-binding protein {Pig (Sus scrofa)}
pfelsgkwitsyigssdlekigenapfqvfmrsiefddkeskvylnffskengiceefsl
igtkqegntydvnyagnnkfvvsyasetaliisninvdeegdktimtgllgkgtdiedqd
lekfkevtrengipeenivniierddcpa
>d1a3yb_ 2.53.1.1.6 Odorant-binding protein {Pig (Sus scrofa)}
elsgkwitsyigssdlekigenapfqvfmrsiefddkeskvylnffskengiceefslig
tkqegntydvnyagnnkfvvsyasetaliisninvdeegdktimtgllgkgtdiedqdle
kfkevtrengipeenivniierddcpa
>d1a3z__ 2.5.1.1.26 Rusticyanin {Thiobacillus ferrooxidans}
twkeatlpqvkamlekddgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknptle
ipagatvdvtfintnkgfghsfditkkgppyavmpvidpivagtgfspvpkdgkfgytdf
twhptagtyyyvcqipghaatgmfgkivvk
>d1a40__ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveywyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a41__ 4.133.1.2.2 Eukaryotic DNA topoisomerase I, catalytic core {Vaccinia virus}
nakrdrifvrvynvmkrincfinknikksstdsnyqlavfmlmetmffirfgkmkylken
etvglltlknkhieispdeivikfvgkdkvshefvvhksnrlykpllkltddsspeeflf
nklserkvyecikqfgirikdlrtygvnytflynfwtnvksisplpspkklialtikqta
evvghtpsiskraymattilemvkdknfldvvskttfdeflsivvdhvks
>d1a42__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasf
>d1a43__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtacq
>d1a44__ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsg
>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
>e1a46.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a46.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1a47_1 2.1.1.5.7 (496-578) Cyclodextrin glycosyltransferase, domain E {Thermoanaerobacterium thermosulfurigenes, EM1}
snsplighvgptmtkagqtitidgrgfgttsgqvlfgstagtivswddtevkvkvpsvtp
gkynislktssgatsntynnini
>d1a47_2 2.3.1.1.4 (579-683) Cyclodextrin glycosyltransferase, C-terminal domain {Thermoanaerobacterium thermosulfurigenes, EM1}
ltgnqicvrfvvnnastvygenvyltgnvaelgnwdtskaigpmfnqvvyqyptwyydvs
vpagttiqfkfikkngntitweggsnhtytvpssstgtvivnwqq
>d1a47_3 2.62.1.1.7 (407-495) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
gttqqrwinndvyiyerkfgnnvalvainrnlstsynitglytalpagtytdvlggllng
nsisvasdgsvtpftlsagevavwqyvss
>d1a47_4 3.1.7.1.7 (1-406) Cyclodextrin glycosyltransferase {Thermoanaerobacterium thermosulfurigenes, EM1}
asdtavsnvvnystdviyqivtdrfvdgntsnnptgdlydpthtslkkyfggdwqgiink
indgyltgmgvtaiwisqpveniyavlpdstfggstsyhgywardfkrtnpyfgsftdfq
nlintahahnikviidfapnhtspasetdptyaengrlydngtllggytndtngyfhhyg
gtdfssyedgiyrnlfdladlnqqnstidsylksaikvwldmgidgirldavkhmpfgwq
knfmdsilsyrpvftfgewflgtneidvnntyfanesgmslldfrfsqkvrqvfrdntdt
mygldsmiqstasdynfindmvtfidnhdmdrfynggstrpveqalaftltsrgvpaiyy
gteqymtgngdpynrammtsfntsttaynvikklaplrksnpaiay
>d1a48__ 4.116.1.1.1 SAICAR synthase {Baker's yeast (Saccharomyces cerevisiae)}
sitkteldgilplvargkvrdiyevdagtllfvatdrisaydvimensipekgilltkls
efwfkflsndvrnhlvdiapgktifdylpaklsepkyktqledrsllvhkhklipleviv
rgyitgsawkeyvktgtvhglkqpqglkesqefpepiftpstkaeqgehdenispaqaae
lvgedlsrrvaelavklyskckdyakekgiiiadtkfefgidektneiilvdevltpdss
rfwngasykvgesqdsydkqflrdwltanklngvngvkmpqdivdrtrakyieayetltg
skwsh
>d1a49a1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49a2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49a3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49b1 2.52.1.1.1 (716-817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49b2 3.1.11.1.2 (612-715,818-995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49b3 3.40.1.1.2 (996-1130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49c1 2.52.1.1.1 (1316-1417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49c2 3.1.11.1.2 (1212-1315,1418-1595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49c3 3.40.1.1.2 (1596-1730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49d1 2.52.1.1.1 (1916-2017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49d2 3.1.11.1.2 (1812-1915,2018-2195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49d3 3.40.1.1.2 (2196-2330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49e1 2.52.1.1.1 (3116-3217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49e2 3.1.11.1.2 (3012-3115,3218-3395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49e3 3.40.1.1.2 (3396-3530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49f1 2.52.1.1.1 (3716-3817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49f2 3.1.11.1.2 (3612-3715,3818-3995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49f3 3.40.1.1.2 (3996-4130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49g1 2.52.1.1.1 (4316-4417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49g2 3.1.11.1.2 (4212-4315,4418-4595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49g3 3.40.1.1.2 (4596-4730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a49h1 2.52.1.1.1 (4916-5017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a49h2 3.1.11.1.2 (4812-4915,5018-5195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a49h3 3.40.1.1.2 (5196-5330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a4aa_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ab_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ba_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4bb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ca_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cc_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4cd_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqydlkemvvdksckqftvhlkhvgkmaksamghnwvltkeadkegva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
hkgtlklsn
>d1a4ea_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4eb_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4ec_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4ed_ 5.5.1.1.3 Catalase I {Baker's yeast (Saccharomyces cerevisiae)}
dvredrvvtnstgnpinepfvtqrigehgplllqdynlidslahfnrenipqrnphahgs
gafgyfevtdditdicgsamfskigkrtkcltrfstvggdkgsadtvrdprgfatkfyte
egnldwvynntpvffirdpskfphfihtqkrnpqtnlrdadmfwdflttpenqvaihqvm
ilfsdrgtpanyrsmhgysghtykwsnkngdwhyvqvhiktdqgiknltieeatkiagsn
pdycqqdlfeaiqngnypswtvyiqtmterdakklpfsvfdltkvwpqgqfplrrvgkiv
lnenplnffaqveqaafapsttvpyqeasadpvlqarlfsyadahryrlgpnfhqipvnc
pyaskffnpairdgpmnvngnfgseptylandksytyiqqdrpiqqhqevwngpaipyhw
atspgdvdfvqarnlyrvlgkqpgqqknlaynigihvegacpqiqqrvydmfarvdkgls
eaikkvae
>d1a4fa_ 1.1.1.1.22 Hemoglobin D {Bar-headed goose (Anser indicus)}
vlsaadktnvkgvfskisghaeeygaetlermftaypqtktyfphfdlqhgsaqikahgk
kvvaalveavnhiddiagalsklsdlhaqklrvdpvnfkflghcflvvvaihhpsaltae
vhasldkflcavgtvltakyr
>d1a4fb_ 1.1.1.1.37 Hemoglobin D {Bar-headed goose (Anser indicus)}
vhwsaeekqlitglwgkvnvadcgaealarllivypwtqrffssfgnlssptailgnpmv
rahgkkvltsfgdavknldnikntfaqlselhcdklhvdpenfrllgdiliivlaahfak
eftpdcqaawqklvrvvahalarkyh
>d1a4ga_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4gb_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4h__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
masetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletep
dlfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqf
gvgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkdd
qleyleekrikevikrhsefvaypiqlvvtkeve
>d1a4ia1 3.2.1.7.7 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1a4ia2 3.48.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1a4ib1 3.2.1.7.7 (127-296) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll
wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk
pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1a4ib2 3.48.1.2.1 (2-126) Tetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)}
apaeilngkeisaqirarlknqvtqlkeqvpgftprlailqvgnrddsnlyinvklkaae
eigikathiklprtttesevmkyitslnedstvhgflvqlpldsensinteevinaiape
kdvdg
>d1a4ja1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4ja2 2.1.1.2.104 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4jb1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jb2 2.1.1.2.104 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jh1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvss
>d1a4jh2 2.1.1.2.104 (120-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4jl1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqsthvpptfgggtkleik
>d1a4jl2 2.1.1.2.104 (113-217) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4ka1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4ka2 2.1.1.2.104 (113-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1a4kb1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kb2 2.1.1.2.104 (120-213) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkvep
>d1a4kh1 2.1.1.1.103 (1-119) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
qvqllesgpelkkpgetvkisckasgytftnygmnwvkqapgkglkwmgwintytgepty
addfkgrfafsletsastaylqinnlknedtatyfcvqaerlrrtfdywgagttvtvssa
stkgp
>d1a4kh2 2.1.1.2.104 (120-211) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
svfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssglysls
svvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1a4kl1 2.1.1.1.103 (1-112) Immunoglobulin (variable domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqsllhsngntylhwylqkpgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqvthvpptfgggtkleikrtvaa
>d1a4kl2 2.1.1.2.104 (113-212) Immunoglobulin (constant domains of L and H chains) {Diels alder catalytic Fab (mouse), kappa L chain}
psvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdskdst
yslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1a4la_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4lb_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4lc_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4ld_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4ma_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4mb_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4mc_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4md_ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1a4oa_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4ob_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4oc_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4od_ 1.110.7.1.2 zeta isoform {Bovine (Bos taurus)}
mdknelvqkaklaeqaeryddmaacmksvteqgaelsneernllsvayknvvgarrsswr
vvssieqktegaekkqqmareyrekietelrdicndvlsllekflipnasqaeskvfylk
mkgdyyrylaevaagddkkgivdqsqqayqeafeiskkemqpthpirlglalnfsvfyye
ilnspekacslaktafdeaiaeldtlseesykdstlimqllrdnltlw
>d1a4pa_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmkq
>d1a4pb_ 1.42.1.2.5 Calcyclin (S100) {Human (Homo sapiens), P11 s100a10, calpactin}
psqmehametmmftfhkfagdkgyltkedlrvlmekefpgflenqkdplavdkimkdldq
crdgkvgfqsffsliagltiacndyfvvhmk
>d1a4qa_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4qb_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeargnsapliirepfiacgpkeckhfalthya
aqpggyyngtredrnklrhlisvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dsnalikikygeaytdtyhsyannilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeifptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctetyldtprpddgsitgpcesngdkgrggikggfvhqrmaskigrwysrtmsktermg
melyvrydgdpwtdsdalahsgvmvsmkepgwysfgfeikdkkcdvpcigiemvhdggkk
twhsaataiyclmgsgqllwdtvtgvdmal
>d1a4ra_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdvavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalepp
epkksrrcvl
>d1a4rb_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
mqtikcvvvgdvavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaalepp
epkksrrcvl
>d1a4sa_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sb_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sc_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4sd_ 3.71.1.1.6 Aldehyde reductase (dehydrogenase), ALDH {Baltic cod (Gadus callarias)}
aqlvdsmpsastgsvvvtddlnywggrrikskdgattepvfepatgrvlcqmvpcgaeev
dqavqsaqaaylkwskmagiersrvmleaariirerrdniaklevinngktiteaeydid
aawqcieyyaglaptlsgqhiqlpggafaytrreplgvcagilawnypfmiaawkcapal
acgnavvfkpspmtpvtgvilaeifheagvpvglvnvvqggaetgsllchhpnvakvsft
gsvptgkkvmemsaktvkhvtlelggkspllifkdcelenavrgalmanfltqgqvctng
trvfvqreimpqfleevvkrtkaivvgdplltetrmggliskpqldkvlgfvaqakkega
rvlcggepltpsdpklkngyfmspcvldncrddmtcvkeeifgpvmsvlpfdteeevlqr
annttfglasgvftrdisrahrvaanleagtcyintysispvevpfggykmsgfgrengq
atvdyysqlktvivemgdvdslf
>d1a4ua_ 3.2.1.2.12 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1a4ub_ 3.2.1.2.12 Drosophila alcohol dehydrogenase {Fruit fly (Drosophila lebanonensis)}
mdltnknvifvaalggigldtsrelvkrnlknfvildrvenptalaelkainpkvnitfh
tydvtvpvaeskkllkkifdqlktvdilingagilddhqiertiainftglvntttaild
fwdkrkggpggiianicsvtgfnaihqvpvysaskaavvsftnslaklapitgvtaysin
pgitrtplvhtfnswldveprvaelllshptqtseqcgqnfvkaieankngaiwkldlgt
leaiewtkhwdshi
>d1a4v__ 4.2.1.2.14 alpha-Lactalbumin {Human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivennesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>e1a4w.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidq
>e1a4w.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
dcglrplfekksledkterellesyi
>d1a4xa_ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
kavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpvt
vgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalvd
vgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a4xb_ 3.51.1.1.12 Uracil PRTase {Bacillus subtilis}
kavildeqairraltriahemiernkgmnncilvgiktrgiylakrlaerieqiegnpvt
vgeiditlyrddlskktsndeplvkgadipvditdqkvilvddvlytgrtvragmdalvd
vgrpssiqlavlvdrghrelpiradyigkniptsksekvmvqldevdqndlvaiyen
>d1a4ya_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1a4yb_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1a4yd_ 3.9.1.1.1 Ribonuclease inhibitor {Pig (Sus scrofa)}
sldiqsldiqceelsdarwaellpllqqcqvvrlddcgltearckdissalrvnpalael
nlrsnelgdvgvhcvlqglqtpsckiqklslqnccltgagcgvlsstlrtlptlqelhls
dnllgdaglqllceglldpqcrleklqleycslsaasceplasvlrakpdfkeltvsnnd
ineagvrvlcqglkdspcqlealklescgvtsdncrdlcgivaskaslrelalgsnklgd
vgmaelcpgllhpssrlrtlwiwecgitakgcgdlcrvlrakeslkelslagnelgdega
rllcetllepgcqleslwvkscsftaaccshfssvlaqnrfllelqisnnrledagvrel
cqglgqpgsvlrvlwladcdvsdsscsslaatllanhslreldlsnnclgdagilqlves
vrqpgclleqlvlydiywseemedrlqalekdkpslrvis
>d1a4ye_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1a4za_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zb_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zc_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a4zd_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1a50a_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
eryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdpladg
ptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceqv
gvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrsg
vtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivkii
eknlaspkqmlaelrsfvsamkaasr
>d1a50b_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
ttllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltk
cqnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasal
asallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsy
etahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmf
adfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysis
agldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkm
mreqpekeqllvvnlsgrgdkdiftvhdil
>d1a52a_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
lalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrvp
gfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmveif
dmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitdt
lihlmakagltlqqqherlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
>d1a52b_ 1.114.1.1.4 Estrogen receptor alpha {Human (Homo sapiens)}
slalsltadqmvsalldaeppilyseydptrpfseasmmglltnladrelvhminwakrv
pgfvdltlhdqvhllecawleilmiglvwrsmehpgkllfapnllldrnqgkcvegmvei
fdmllatssrfrmmnlqgeefvclksiillnsgvytflsstlksleekdhihrvldkitd
tlihlmakagltlqqqherlaqlllilshirhmsnkgmehlysmkcknvvplydllleml
>d1a53__ 3.1.2.2.4 Indole-3-glycerophosphate (IGP) synthase {Sulfolobus solfataricus}
prylkgwlkdvvqlslrrpsfrasrqrpiislnerilefnkrnitaiiaeykrkspsgld
verdpieyskfmeryavglsilteekyfngsyetlrkiassvsipilmkdfivkesqidd
aynlgadtvllivkiltereleslleyarsygmeplieindendldialrigarfigins
rdletleinkenqrklismipsnvvkvaesgiserneieelrklgvnafligsslmrnpe
kikefil
>d1a54a_ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveycyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a55a_ 3.84.1.1.5 Phosphate-binding protein {Escherichia coli}
easltgagatfpapvyakwadtyqketgnkvnyqgigssggvkqiiantvdfgasdapls
deklaqeglfqfptviggvvlavnipglksgelvldgktlgdiylgkikkwddeaiakln
pglklpsqniavvrradgsgtsfvftsylakvneewknnvgtgstvkwpiglggkgndgi
aafvqrlpgaigyveycyakqnnlaytklisadgkpvspteenfanaakgadwsktfaqd
ltnqkgedawpitsttfilihkdqkkpeqgtevlkffdwayktgakqandldyaslpdsv
veqvraawktnikdssgkply
>d1a56__ 1.3.1.1.24 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1a57__ 2.53.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenysgahdnlkltitqegnkftvkessnfrnidvvfelgvdfaysladg
teltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytyegveakrifkke
>d1a58__ 2.55.1.1.4 Cyclophilin (eukaryotic) {Nematode (Brugia malayi)}
mskkdrrrvfldvtidgnlagrivmelyndiaprtcnnflmlctgmagtgkisgkplhyk
gstfhrviknfmiqggdftkgdgtggesiyggmfddeefvmkhdepfvvsmankgpntng
sqffitttpaphlnnihvvfgkvvsgqevvtkieylktnsknrpladvvilncgelv
>d1a59__ 1.99.1.1.4 Citrate synthase {Antarctic bacterium, ds2-3r}
eptihkglagvtadvtaiskvnsdtnsllyrgypvqelaakcsfeqvayllwnselpnds
elkafvnfershrkldenvkgaidllstachpmdvartavsvlganharaqdsspeanle
kamsllatfpsvvaydqrrrrgeeliepredldysanflwmtfgeeaapevveafnvsmi
lyaehsfnastftarvitstladlhsavtgaigalkgplhgganeavmhtfeeigirkde
sldeaatrskawmvdalaqkkkvmgfghrvykngdsrvptmksaldamikhydrpemlgl
yngleaameeakqikpnldypagptynlmgfdtemftplfiaaritgwtahimeqvadna
lirplseyngpeqrqvp
>d1a5aa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1a5ab_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1a5ba_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1a5bb_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1a5ca_ 3.1.9.1.6 Fructose-1,6-bisphosphate aldolase {Plasmodium falciparum}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>d1a5cb_ 3.1.9.1.6 Fructose-1,6-bisphosphate aldolase {Plasmodium falciparum}
lpadvaeelattaqklvqagkgilaadestqtikkrfdniklentienrasyrdllfgtk
glgkfisgailfeetlfqkneagvpmvnllhneniipgikvdkglvnipctdeekstqgl
dglaerckeyykagarfakwrtvlvidtakgkptdlsihetawglaryasicqqnrlvpi
vepeiladgphsievcavvtqkvlscvfkalqengvllegallkpnmvtagyectakttt
qdvgfltvrtlrrtvppalpgvvflsggqseeeasvnlnsinalgphpwaltfsygralq
asvlntwqgkkenvakarevllqraeanslatygkykggagg
>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
>d1a5db2 2.10.1.1.6 (85-174) beta-Crystallin {Rat (Rattus norvegicus), isoform E}
sshririyeredyrgqmveitddcphlqdrfhfsdfhsfhvmegywvlyempnyrgrqyl
lrpgeyrryhdwgamnarvgslrrimdfy
>d1a5e__ 1.110.2.1.5 Cell cycle inhibitor p16ink4A {Human (Homo sapiens)}
mepaagssmepsadwlataaargrveevralleagalpnapnsygrrpiqvmmmgsarva
ellllhgaepncadpatltrpvhdaaregfldtlvvlhragarldvrdawgrlpvdlaee
lghrdvarylraaaggtrgsnharidaaegpsdipd
>d1a5fh1 2.1.1.1.118 (1-120) Immunoglobulin (variable domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
evalqqsgaelvkpgasvklscaasgftikdaymhwvkqkpeqglewigridsgssntny
dptfkgkatitaddssntaylqmssltsedtavyycarvglsywyamdywgqgtsvtvss
>d1a5fh2 2.1.1.2.116 (121-217) Immunoglobulin (constant domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvsvptstetvtcnvahapsstkvdkkivpr
>d1a5fl1 2.1.1.1.118 (1-113) Immunoglobulin (variable domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsgaqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelk
>d1a5fl2 2.1.1.2.116 (114-220) Immunoglobulin (constant domains of L and H chains) {Anti-E-selectin Fab (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>e1a5g.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a5g.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1a5h.1a 2.41.1.2.28 Two-chain tissue plasminogen activator (TC)-T-PA {Human (Homo sapiens)}
ikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaahcfqerfpphhltv
ilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdssrcaqessvvrtvc
lppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrctsqhllnrtvtdnm
lcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgcgqkdvpgvytkvt
nyldwirdnmrp
>e1a5h.2b 2.41.1.2.28 Two-chain tissue plasminogen activator (TC)-T-PA {Human (Homo sapiens)}
ikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaahcfqerfpphhltv
ilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdssrcaqessvvrtvc
lppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrctsqhllnrtvtdnm
lcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgcgqkdvpgvytkvt
nyldwirdnmrp
>d1a5ia_ 2.41.1.2.30 Single chain tissue plasminogen activator {Vampire bat (Desmodus rotundus)}
tcglrkykepqlhstgglftditshpwqaaifaqnrrssgerflcggilisscwvltaah
cfqesylpdqlkvvlgrtyrvkpgeeeqtfkvkkyivhkefdddtynndiallqlksdsp
qcaqesdsvraiclpeanlqlpdwtecelsgygkhkssspfyseqlkeghvrlypssrca
pkflfnktvtnnmlcagdtrsgeiypnvhdacqgdsggplvcmndnhmtllgiiswgvgc
gekdvpgvytkvtnylgwirdnmhl
>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
>d1a5ka_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5kb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5kc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5kc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagvigleihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5la_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5lb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5lc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5lc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvahhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5ma_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5mb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5mc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5mc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5na_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5nb_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5nc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5nc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglaihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5oa_ 4.7.1.1.1 Urease, gamma-subunit {Klebsiella aerogenes}
meltprekdklllftaalvaerrlarglklnypesvalisafimegardgksvaslmeeg
rhvltreqvmegvpemipdiqveatfpdgsklvtvhnpii
>d1a5ob_ 2.75.2.1.1 Urease, beta-subunit {Klebsiella aerogenes}
mipgeyhvkpgqialntgratcrvvvenhgdrpiqvgshyhfaevnpalkfdrqqaagyr
lnipagtavrfepgqkrevelvafaghravfgfrgevmgpl
>d1a5oc1 2.80.1.1.1 (2-129,423-475) alpha-Subunit of urease, composite domain {Klebsiella aerogenes}
snisrqayadmfgptvgdkvrladtelwieveddlttygeevkfgggkvirdgmgqgqml
aadcvdlvltnalivdhwgivkadigvkdgrifaigkagnpdiqpnvtipigaateviaa
egkivtagXsievgkladlvvwspaffgvkpatvikggmiaiapmgdinasiptpqpvhy
rp
>d1a5oc2 3.1.8.2.1 (130-422,476-567) alpha-subunit of urease, catalytic domain {Klebsiella aerogenes}
gidthihwicpqqaeealvsgvttmvgggtgpaagthattctpgpwyisrmlqaadslpv
nigllgkgnvsqpdalreqvaagviglcihedwgatpaaidcaltvademdiqvalhsdt
lnesgfvedtlaaiggrtihtfhtegaggghapdiitacahpnilpsstnptlpytlnti
dehldmlmvchhldpdiaedvafaesrirretiaaedvlhdlgafsltssdsqamgrvge
vilrtwqvahrmkvqrgalaeetgdndnfrvkryiakytinpalthgiahevgXmfgalg
sarhhcrltflsqaaaangvaerlnlrsaiavvkgcrtvqkadmvhnslqpnitvdaqty
evrvdgelitsepadvlpmaqryflf
>d1a5p__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrakpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypnaaykttqankhiivacegnpyvpvhf
dasv
>d1a5q__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskyancaykttqankhiivacegnpyvpvhf
dasv
>d1a5r__ 4.13.2.1.3 SUMO-1 {Human (Homo sapiens)}
gsmsdqeakpstedlgdkkegeyiklkvigqdsseihfkvkmtthlkklkesycqrqgvp
mnslrflfegqriadnhtpkelgmeeedvievyqeqtgghstv
>d1a5sa_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
eryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdpladg
ptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceqv
gvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrsg
vtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivkii
eknlaspkqmlaelrsfvsamkaasr
>d1a5sb_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhd
>d1a5t_1 1.112.1.1.1 (167-330) delta prime subunit of DNA polymerase III, C-terminal domain {Escherichia coli}
ppeqyavtwlsrevtmsqdallaalrlsagspgaalalfqgdnwqaretlcqalaysvps
gdwysllaalnheqaparlhwlatllmdalkrhhgaaqvtnvdvpglvaelanhlspsrl
qailgdvchireqlmsvtginrellitdlllriehylqpgvvlp
>d1a5t_2 3.30.1.10.3 (1-166) delta prime subunit of DNA polymerase III, N-terminal domain {Escherichia coli}
mrwypwlrpdfeklvasyqagrghhalliqalpgmgddaliyalsryllcqqpqghkscg
hcrgcqlmqagthpdyytlapekgkntlgvdavrevteklneharlggakvvwvtdaall
tdaaanallktleeppaetwfflatreperllatlrsrcrlhylap
>d1a5ua1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ua2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ua3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ub1 2.52.1.1.1 (716-817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ub2 3.1.11.1.2 (612-715,818-995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ub3 3.40.1.1.2 (996-1130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uc1 2.52.1.1.1 (1316-1417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uc2 3.1.11.1.2 (1212-1315,1418-1595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uc3 3.40.1.1.2 (1596-1730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ud1 2.52.1.1.1 (1916-2017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ud2 3.1.11.1.2 (1812-1915,2018-2195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ud3 3.40.1.1.2 (2196-2330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ue1 2.52.1.1.1 (3116-3217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ue2 3.1.11.1.2 (3012-3115,3218-3395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ue3 3.40.1.1.2 (3396-3530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uf1 2.52.1.1.1 (3716-3817) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uf2 3.1.11.1.2 (3612-3715,3818-3995) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uf3 3.40.1.1.2 (3996-4130) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5ug1 2.52.1.1.1 (4316-4417) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5ug2 3.1.11.1.2 (4212-4315,4418-4595) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5ug3 3.40.1.1.2 (4596-4730) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5uh1 2.52.1.1.1 (4916-5017) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1a5uh2 3.1.11.1.2 (4812-4915,5018-5195) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1a5uh3 3.40.1.1.2 (5196-5330) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1a5v__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5w__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5x__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1a5y__ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhxsagigrsgtfcladtclllmdkrkdp
ssvdikkvlldmrkfrmgliataeqlrfsylaviegakfimgds
>d1a5z_1 3.2.1.5.15 (22-163) Lactate dehydrogenase {Thermotoga maritima}
mkigivglgrvgsstafallmkgfaremvlidvdkkraegdaldlihgtpftrraniyag
dyadlkgsdvvivaagvpqkpgetrlqllgrnarvmkeiarnvskyapdsivivvtnpvd
vltyfflkesgmdprkvfgs
>d1a5z_2 4.132.1.1.15 (164-333) Lactate dehydrogenase {Thermotoga maritima}
gtvldtarlrtliaqhcgfsprsvhvyvigehgdsevpvwsgamiggiplqnmcqvcqkc
dskilenfaektkraayeiierkgathyaialavadivesiffdekrvltlsvyledylg
vkdlcisvpvtlgkhgverilelnlneeeleafrksasilknaineitaeen
>e1a61.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1a61.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1a62__ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
nltelkntpvselitlgenxglenlarxrkqdiifailkqhaksgedifgdgvleilqdg
fgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevnf
dkpe
>d1a63__ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
mnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleilqd
gfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvnevn
fdkpenarnk
>d1a64a_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a64b_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>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
>d1a66a_ 2.2.5.1.2 Transcription factor NFATC, DNA-binding domain {Human (Homo sapiens)}
mkdwqlpshsgpyelrievqpkshhraryetegsrgavkasagghpivqlhgyleneplm
lqlfigtaddrllrphafyqvhritgktvsttsheailsntkvleipllpensmravidc
agilklrnsdielrkgetdigrkntrvrlvfrvhvpqpsgrtlslqvasnpiecsqrs
>d1a67__ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfamaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepemakyttctfvvysipwlnqiklleskcq
>d1a68__ 4.35.1.2.1 Shaker potassium channel {California sea hare (Aplysia californica)}
ervvinvsglrfetqlktlnqfpdtllgnpqkrnryydplrneyffdrnrpsfdailyfy
qsggrlrrpvnvpldvfseeikfyelg
>d1a69a_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a69b_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a69c_ 3.47.1.1.3 Purine nucleoside phosphorylase, PNP {Escherichia coli}
atphinaemgdfadvvlmpgdplrakyiaetfledarevnnvrgmlgftgtykgrkisvm
ghgmgipscsiytkelitdfgvkkiirvgscgavlphvklrdvvigmgactdskvnrirf
kdhdfaaiadfdmvrnavdaakalgidarvgnlfsadlfyspdgemfdvmekygilgvem
eaagiygvaaefgakaltictvsdhirtheqttaaerqttfndmikialesvllgdk
>d1a6aa1 2.1.1.2.151 (82-180) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr3}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwef
>d1a6aa2 4.17.1.1.6 (5-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
hviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalania
vdkanleimtkrsnytp
>d1a6ab1 2.1.1.2.151 (93-191) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr3}
rrvhpkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeektgvvstglihngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrar
>d1a6ab2 4.17.1.1.6 (5-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr3}
prfleystsechffngtervryldryfhnqeenvrfdsdvgefravtelgrpdaeywnsq
kdlleqkrgrvdnycrhnygvvesftvq
>d1a6bb_ 7.34.1.1.5 Zinc finger protein ncp10 {Moloney murine leukemia virus, MMLV}
gerrrsqldrdqcayckekghwakdcpkkprgprgprpqt
>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
>d1a6da1 1.119.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1a6da2 3.7.5.2.1 (215-367) Thermosome {Thermoplasma acidophilum}
gividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetntfk
qmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtdld
dltpsvlgeaetveerkigddrmtfvmgcknpk
>d1a6da3 4.46.1.2.1 (146-214,368-403) Thermosome {Thermoplasma acidophilum}
tddatlrkialtalsgkntglsndfladlvvkavnavaevrdgktivdtanikvdkkngg
svndtqfisXavsilirggtdhvvseveralndairvvaitkedgk
>d1a6db1 1.119.1.2.1 (20-144,404-521) Thermosome {Thermoplasma acidophilum}
kdamkenieaaiaisnsvrsslgprgmdkmlvdslgdivitndgvtilkemdvehpaakm
mvevsktqdsfvgdgtttaviiaggllqqaqglinqnvhptvisegyrmaseeakrvide
istkiXayaagggataaeiafrlrsyaqkiggrqqlaiekfadaieeipralaenagldp
idillklraehakgnktyginvftgeiedmvkngviepirvgkqaiesateaaimilrid
dvia
>d1a6db2 3.7.5.2.1 (216-367) Thermosome {Thermoplasma acidophilum}
giivdkekvhpgmpdvvkdakialldapleikkpefdtnlriedpsmiqkflaqeenmlr
emvdkiksvganvvitqkgiddmaqhylsragiyavrrvkksdmdklakatgasivstid
eisssdlgtaerveqvkvgedymtfvtgcknp
>d1a6db3 4.46.1.2.1 (145-215,368-403) Thermosome {Thermoplasma acidophilum}
gadekalllkmaqtslnsksasvakdklaeisyeavksvaelrdgkyyvdfdniqvvkkq
ggaiddtqlinXkavsilvrgetehvvdemersitdslhvvasaledg
>d1a6ea1 1.119.1.2.1 (17-145,404-519) Thermosome {Thermoplasma acidophilum}
reqgknaqrnnieaakaiadavrttlgpkgmdkmlvdsigdiiisndgatilkemdvehp
takmivevskaqdtavgdgtttavvlsgellkqaetlldqgvhptvisngyrlavneark
iideiaeksXflwgggaveaelamrlakyansvggreqlaieafakaleiiprtlaenag
idpintliklkaddekgrisvgvdldnngvgdmkakgvvdplrvkthalesavevatmil
riddvi
>d1a6ea2 3.7.5.2.1 (215-367) Thermosome {Thermoplasma acidophilum}
gividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetntfk
qmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtdld
dltpsvlgeaetveerkigddrmtfvmgcknpk
>d1a6ea3 4.46.1.2.1 (146-214,368-403) Thermosome {Thermoplasma acidophilum}
tddatlrkialtalsgkntglsndfladlvvkavnavaevrdgktivdtanikvdkkngg
svndtqfisXavsilirggtdhvvseveralndairvvaitkedgk
>d1a6eb1 1.119.1.2.1 (20-144,404-521) Thermosome {Thermoplasma acidophilum}
kdamkenieaaiaisnsvrsslgprgmdkmlvdslgdivitndgvtilkemdvehpaakm
mvevsktqdsfvgdgtttaviiaggllqqaqglinqnvhptvisegyrmaseeakrvide
istkiXayaagggataaeiafrlrsyaqkiggrqqlaiekfadaieeipralaenagldp
idillklraehakgnktyginvftgeiedmvkngviepirvgkqaiesateaaimilrid
dvia
>d1a6eb2 3.7.5.2.1 (216-367) Thermosome {Thermoplasma acidophilum}
giivdkekvhpgmpdvvkdakialldapleikkpefdtnlriedpsmiqkflaqeenmlr
emvdkiksvganvvitqkgiddmaqhylsragiyavrrvkksdmdklakatgasivstid
eisssdlgtaerveqvkvgedymtfvtgcknp
>d1a6eb3 4.46.1.2.1 (145-215,368-403) Thermosome {Thermoplasma acidophilum}
gadekalllkmaqtslnsksasvakdklaeisyeavksvaelrdgkyyvdfdniqvvkkq
ggaiddtqlinXkavsilvrgetehvvdemersitdslhvvasaledg
>d1a6f__ 4.12.1.2.1 RNase P protein {Bacillus subtilis}
ahlkkrnrlkknedfqkvfkhgtsvanrqfvlytldqpendelrvglsvskkignavmrn
rikrlirqafleekerlkekdyiiiarkpasqltyeetkkslqhlfrksslyk
>d1a6g__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gnfgadaqgamnkalelfrkdiaakykelgy
>d1a6i_1 1.37.1.1.1 (2-67) Tetracyclin repressor (Tet-repressor, TetR), N-terminal domain {Escherichia coli}
srldkskvinsalellnevgieglttrklaqklgveqptlywhvknkralldalaveila
rhhdys
>d1a6i_2 1.113.1.1.1 (68-208) Tetracyclin repressor (Tet-repressor, TetR), C-terminal domain {Escherichia coli}
lpaageswqsflrnnamsfrrallryrdgakvhlgtrpdekqydtvetqlrfmtengfsl
rdglyaisavshftlgavleqqehtaaltdrpaapdenlppllrealqimdsddgeqafl
hgleslirgfevqltallqiv
>d1a6ja_ 4.88.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {Escherichia coli}
lqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekmgstgign
giaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkthlhtlslv
akrladkticrrlraaqsdeelyqiitdte
>d1a6jb_ 4.88.1.1.1 Nitrogen regulatory bacterial protein IIa-ntr {Escherichia coli}
mtnndttlqlssvlnrectrsrvhcqskkraleiiselaakqlslppqvvfeailtrekm
gstgigngiaiphgkleedtlravgvfvqletpiafdaidnqpvdllfallvpadqtkth
lhtlslvakrladkticrrlraaqsdeelyqiitdte
>d1a6k__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6l__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckycdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1a6m__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6n__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgy
>d1a6o__ 4.117.1.1.18 Protein kiase CK2, alpha subunit {Maize (Zea mays)}
skarvyadvnvlrpkeywdyealtvqwgeqddyevvrkvgrgkysevfeginvnnnekci
ikilkpvkkkkikreikilqnlcggpnivklldivrdqhsktpslifeyvnntdfkvlyp
tltdydiryyiyellkaldychsqgimhrdvkphnvmidhelrklrlidwglaefyhpgk
eynvrvasryfkgpellvdlqdydysldmwslgcmfagmifrkepffyghdnhdqlvkia
kvlgtdglnvylnkyrieldpqlealvgrhsrkpwlkfmnadnqhlvspeaidfldkllr
ydhqerltaleamthpyfqqvraaens
>d1a6pa_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6pb_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
gtvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlki
knltrddsgtynvtvystngtrildkaldlrile
>d1a6q__ 4.129.1.1.1 Protein serine/threonine phosphatase 2C {Human (Homo sapiens)}
gafldkpkmekhnaqgqgnglryglssmqgwrvemedahtaviglpsgleswsffavydg
hagsqvakyccehlldhitnnqdfkgsagapsvenvkngirtgfleidehmrvmsekkhg
adrsgstavgvlispqhtyfincgdsrgllcrnrkvhfftqdhkpsnplekeriqnaggs
vmiqrvngslavsralgdfdykcvhgkgpteqlvspepevhdierseeddqfiilacdgi
wdvmgneelcdfvrsrlevtddlekvcnevvdtclykgsrdnmsvilicfpnapkvspea
vkkeaeldkylecrveeiikkqgegvpdlvhvmrtlasenipslppggelaskrnvieav
ynrlnpy
>d1a6r__ 4.3.1.1.8 Bleomycin hydrolase, Gal6 {Baker's yeast (Saccharomyces cerevisiae)}
afqgamassidiskinswnkefqsdlthqlattvlknynaddallnktrlqkqdnrvfnt
vvstdstpvtnqkssgrawlfaatnqlrlnvlselnlkefelsqaylffydklekanyfl
dqivssadqdidsrlvqyllaaptedggqysmflnlvkkyglipkdlygdlpysttasrk
wnsllttklrefaetlrtalkersaddsiivtlreqmqreifrlmslfmdippvqpneqf
tweyvdkdkkihtikstplefaskyakldpstpvslindprhpygklikidrlgnvlggd
aviylnvdnetlsklvvkrlqnnkavffgshtpkfmdkktgvmdielwnypaigynlpqq
kasriryheslmthamlitgchvdetsklplryrvenswgkdsgkdglyvmtqkyfeeyc
fqivvdinelpkelaskftsgkeepivlpiwdpmgalak
>d1a6s__ 1.62.1.4.1 GAG polyprotein M-domain {Rous sarcoma virus, RSV}
geavikvissacktycgktspskkeigamlsllqkegllmspsdlyspgswdpitaalsq
ramilgksgelktwglvlgalkaaree
>d1a6ta1 2.1.1.1.107 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6ta2 2.1.1.2.107 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6tb1 2.1.1.1.107 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6tb2 2.1.1.2.107 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6tc1 2.1.1.1.107 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
qsvlsqspailsaspgekvimtcspsssvsymqwyqqkpgsspkpwiystsnlasgvpgr
fsgggsgtsfsltisgveaedaatyycqqysshpltfgggtklelk
>d1a6tc2 2.1.1.2.107 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1a6td1 2.1.1.1.107 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
evqlqqsgpdlvkpgasvkisckasgysfstyymhwvkqshgkslewigrvdpdnggtsf
nqkfkgkailtvdkssstaymelgsltsedsavyycarrddyyfdfwgqgtsltvss
>d1a6td2 2.1.1.2.107 (114-213) Immunoglobulin (constant domains of L and H chains) {Fab Mab1-IA (mouse), kappa L chain}
akttppsvyplapvcggttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsg
lytlsssvtvtsstwpsqtitcnvahpasstkvdkkiepr
>d1a6uh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6ul_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtv
>d1a6vi_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvs
>d1a6vj_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6vl_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a6vm_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6vn_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qavvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgv
parfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvl
>d1a6wh_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
qvqlqqpgaelvkpgasvklsckasgytftsywmhwvkqrpgrglewigridpnsggtky
nekfkskatltvdkpsstaymqlssltsedsavyycarydyygssyfdywgqgttvtvss
>d1a6wl_ 2.1.1.1.108 Immunoglobulin (variable domains of L and H chains) {Fv B1-8 (mouse), lambda L chain}
avvtqesalttspgetvtltcrsstgavttsnyanwvqekpdhlftgliggtnnrapgvp
arfsgslignkaaltitgaqtedeaiyfcalwysnhwvfgggtkltvle
>d1a6x__ 2.74.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
meapaaaeisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqiea
dksgtvkailvesgqpvefdeplvvie
>d1a6ya_ 7.33.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
llckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcqqcr
fkkclsvgmsrdavrfgr
>d1a6yb_ 7.33.1.2.7 Orphan nuclear receptor reverb {Human (Homo sapiens)}
gmvllckvcgdvasgfhygvhacegckgffrrsiqqniqykrclknencsivrinrnrcq
qcrfkkclsvgmsrdavrfgripk
>d1a6za1 2.1.1.2.12 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d1a6za2 4.17.1.1.19 (4-181) MHC class I, alpha-1 and alpha-2 domains {Human (Homo sapiens), hemochromatosis protein Hfe}
rshslhylfmgaseqdlglslfealgyvddqlfvfydhesrrveprtpwvssrissqmwl
qlsqslkgwdhmftvdfwtimenhnhskeshtlqvilgcemqednstegywkygydgqdh
lefcpdtldwraaeprawptklewerhkirarqnraylerdcpaqlqqllelgrgvld
>d1a6zb1 2.1.1.2.12 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a6zc1 2.1.1.2.12 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
qqvpplvkvthhvtssvttlrcralnyypqnitmkwlkdkqpmdakefepkdvlpngdgt
yqgwitlavppgeeqrytcqvehpgldqpliviw
>d1a6zc2 4.17.1.1.19 (4-181) MHC class I, alpha-1 and alpha-2 domains {Human (Homo sapiens), hemochromatosis protein Hfe}
rshslhylfmgaseqdlglslfealgyvddqlfvfydhesrrveprtpwvssrissqmwl
qlsqslkgwdhmftvdfwtimenhnhskeshtlqvilgcemqednstegywkygydgqdh
lefcpdtldwraaeprawptklewerhkirarqnraylerdcpaqlqqllelgrgvld
>d1a6zd1 2.1.1.2.12 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), hemochromatosis protein Hfe}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a70__ 4.13.6.1.10 2Fe-2S ferredoxin {Spinach (Spinacia oleracea)}
aaykvtlvtptgnvefqcpddvyildaaeeegidlpyscragscsscagklktgslnqdd
qsfldddqidegwvltcaaypvsdvtiethkkeelta
>d1a71a1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71a2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a71b1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a71b2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a72_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1a72_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1a73a_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a73b_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a74a_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a74b_ 4.4.1.3.1 Intron-encoded homing endonuclease I-PpoI {Slime mold (Physarum polycephalum)}
altnaqilavidsweetvgqfpvithhvplggglqgtlhcyeiplaapygvgfakngptr
wqykrtinqvvhrwgshtvpfllepdningktctashlchntrchnplhlcweslddnkg
rnwcpgpnggcvhavvclrqgplygpgatvagpqqrgshfvv
>d1a75a_ 1.42.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
agiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfieede
lklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a75b_ 1.42.1.4.5 Parvalbumin {Whiting (Merlangius merlangus)}
afagiladadcaaavkaceaadsfsykaffakcglsgksaddikkafvfidqdksgfiee
delklflqvfkagaraltdaetkaflkagdsdgdgaigveewvalvka
>d1a76_1 1.61.3.1.4 (209-316) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1a76_2 3.44.1.2.4 (2-208) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1a77_1 1.61.3.1.4 (209-316) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
islddlidiaifmgtdynpggvkgigfkrayelvrsgvakdvlkkeveyydeikrifkep
kvtdnyslslklpdkegiikflvdendfnydrvkkhvdklynliankt
>d1a77_2 3.44.1.2.4 (2-208) Flap endonuclease-1 from methanococcus jannaschii {Methanococcus jannaschii}
gvqfgdfipkniisfedlkgkkvaidgmnalyqfltsirlrdgsplrnrkgeitsayngv
fyktihllenditpiwvfdgeppklkektrkvrremkekaelkmkeaikkedfeeaakya
krvsyltpkmvenckyllslmgipyveapsegeaqasymakkgdvwavvsqdydallyga
prvvrnltttkempelielnevledlr
>d1a78a_ 2.26.1.3.3 S-lectin, different isoforms {Toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqreevfpfqqgaevmvcfeyqtqkiiikfssgdqfsfpvrkvlpsipf
lsleglafksitte
>d1a78b_ 2.26.1.3.3 S-lectin, different isoforms {Toad (Bufo arenarum)}
asagvavtnlnlkpghcveikgsippdckgfavnlgedasnfllhfnarfdlhgdvnkiv
cnskeadawgseqreevfpfqqgaevmvcfeyqtqkiiikfssgdqfsfpvrkvlpsipf
lsleglafksitte
>d1a79a1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79a2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79b1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79b2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79c1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79c2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a79d1 3.43.2.1.1 (83-179) tRNA splicing endonuclease, C-terminal domain {Methanococcus jannaschii}
erlclkylvykdlrtrgyivktglkygadfrlyerganidkehsvylvkvfpedssflls
eltgfvrvahsvrkklliaivdadgdivyynmtyvkp
>d1a79d2 4.57.1.1.1 (9-82) tRNA splicing endonuclease, N-terminal domain {Methanococcus jannaschii}
kitglldgdrvivfdkngisklsarhygnvegnflslslvealylinlgwlevkykdnkp
lsfeelyeyarnve
>d1a7aa1 3.2.1.4.8 (190-352) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dnlygcreslidgikratdvxiagkvavvagygdvgkgcaqalrgfgarviiteidpina
lqaaxegyevttxdeacqegnifvtttgcidiilgrhfeqxkddaivcnighfdveidvk
wlnenavekvnikpqvdryrlkngrriillaegrlvnlgcaxg
>d1a7aa2 3.16.9.3.1 (2-189,353-432) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
sdklpykvadiglaawgrkaldiaenexpglxrxrerysaskplkgariagclhxtveta
vlietlvtlgaevqwsscnifstqnhaaaaiakagipvyawkgetdeeylwcieqtlyfk
dgplnxilddggdltnlihtkypqllpgirgiseetttgvhnlykxxangilkvpainvn
dsvtkskfXhpsfvxsnsftnqvxaqielwthpdkypvgvhflpkkldeavaeahlgkln
vkltkltekqaqylgxscdgpfkpdhyry
>d1a7ab1 3.2.1.4.8 (190-352) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dnlygcreslidgikratdvxiagkvavvagygdvgkgcaqalrgfgarviiteidpina
lqaaxegyevttxdeacqegnifvtttgcidiilgrhfeqxkddaivcnighfdveidvk
wlnenavekvnikpqvdryrlkngrriillaegrlvnlgcaxg
>d1a7ab2 3.16.9.3.1 (3-189,353-432) S-adenosylhomocystein hydrolase {Human (Homo sapiens)}
dklpykvadiglaawgrkaldiaenexpglxrxrerysaskplkgariagclhxtvetav
lietlvtlgaevqwsscnifstqnhaaaaiakagipvyawkgetdeeylwcieqtlyfkd
gplnxilddggdltnlihtkypqllpgirgiseetttgvhnlykxxangilkvpainvnd
svtkskfXhpsfvxsnsftnqvxaqielwthpdkypvgvhflpkkldeavaeahlgklnv
kltkltekqaqylgxscdgpfkpdhyry
>d1a7ba_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bb_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bc_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7bd_ 2.1.1.1.8 CD2, first domain {Rat (Rattus rattus)}
tvwgalghginlnipnfqmtddidevrwergstlvaefkrkpflksgafeilangdlkik
nltrddsgtynvtvystngtrildkaldlrile
>d1a7ca_ 5.1.1.1.7 Plasminogen activator inhibitor-1 {Human (Homo sapiens)}
hhppsyvahlasdfgvrvfqqvaqaskdrnvvfspygvasvlamlqlttggetqqqiqaa
mgfkiddkgmapalrhlykelmgpwnkdeisttdaifvqrdlklvqgfmphffrlfrstv
kqvdfseverarfiindwvkthtkgmisnllgkgavdqltrlvlvnalyfngqwktpfpd
ssthrrlfhksdgstvsvpmmaqtnkfnytefttpdghyydilelpyhgdtlsmfiaapy
ekevplsaltnilsaqlishwkgnmtrlprllvlpkfsletevdlrkplenlgmtdmfrq
fqadftslsdqeplhvaqalqkvkievnesgtvessstavivsarmapeeiimdrpflfv
vrhnptgtvlfmgqvmep
>d1a7d__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewlvnhikgtdfkykgkl
>d1a7e__ 1.25.4.1.3 Myohemerythin {Sipunculan worm (Themiste zostericola)}
gweipepyvwdesfrvfyeqldeehkkifkgifdcirdnsapnlatlvkvttnhftheea
mmdaakysevvphkkmhkdflekigglsapvdaknvdyckewnvnhikgtdfkykgkl
>e1a7f.1a 7.1.1.1.2 Insulin {Human (Homo sapiens)}
giveqcctsicslyqlenycn
>e1a7f.1b 7.1.1.1.2 Insulin {Human (Homo sapiens)}
fvnqhlcgshlvealelvcgerggfytpk
>d1a7ge_ 4.47.8.1.2 Papillomavirus-1 E2 protein {Human papillomavirus-31}
attpiihlkgdanilkclryrlskykqlyeqvsstwhwtctdgkhknaivtltyistsqr
ddflntvvipntvsvstgymti
>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
>d1a7i_1 7.33.1.3.2 (8-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
nkcgacgrtvyhaeevqcdgrsfhrccf
>d1a7i_2 7.33.1.3.2 (36-67) Cysteine-rich (intestinal) protein, CRP, CRIP {Japanese quail (Coturnix coturnix japonica), CRP2}
lcmvcrknldsttvaihdaevyckscygkkyg
>d1a7j__ 3.30.1.4.1 Phosphoribulokinase {Rhodobacter sphaeroides}
skkhpiisvtgssgagtstvkhtfdqifrregvkavsiegdafhrfnradmkaeldrrya
agdatfshfsyeanelkelervfreygetgqgrtrtyvhddaeaartgvapgnftdwrdf
dsdshllfyeglhgavvnsevniagladlkigvvpvinlewiqkihrdratrgytteavt
dvilrrmhayvhcivpqfsqtdinfqrvpvvdtsnpfiarwiptadesvvvirfrnprgi
dfpyltsmihgswmsransivvpgnkldlamqliltplidrvvreskv
>d1a7ka1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7ka2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kb1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kb2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kc1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kc2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7kd1 3.2.1.3.7 (1-165,335-358) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
apikvgingfgrigrmvfqaicdqgligteidvvavvdmstnaeyfayqmkhdtvhgrpk
ytveavksspsvetadvlvvnghrikcvkaqrnpadlpwgklgvdyviestglftdklka
eghikggakkvvisapasggaktivmgvnqheyspashhvvsnasXnewayshrvvdlvr
ymaakdaass
>d1a7kd2 4.61.1.1.7 (166-334) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {Leishmania mexicana}
cttnclapivhvltkenfgietglmttihsytatqktvdgvslkdwrggraaavniipst
tgaakavgmvipstkgkltgmsfrvptpdvsvvdltfratrdtsiqeidkaikkaaqtym
kgilgftdeelvsadfindnrssvydskatlqnnlpgekrffkvvswyd
>d1a7la_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyfpaggsecc
>d1a7lb_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gsqdprvrglyf
>d1a7lc_ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
egklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdiifwa
hdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkdllp
nppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikdvgv
dnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskvnyg
vtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplgava
lksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdealkd
gs
>d1a7m__ 1.27.1.1.5 Leukemia inhibitory factor (LIF) {Mouse (Mus musculus)}
splpitpvnatcairhpchgnlmnqiknqlaqlngsanalfisyytaqgepfpnnldklc
gpnvtdfppfhangtekaklvelyrmvaylsasltnitrdqkvlnpsavslhsklnatid
vmrgllsnvlcrlcnkyrvghvdvppvpdhsdkevfqkkklgcqllgtykqvisvvvqaf
>d1a7nh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7nl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7oh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ol_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstptfgggtkleik
>d1a7ph_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttvtvss
>d1a7pl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstsrtfgggtkleik
>d1a7qh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqlpgkglewlgmiwgdgntayn
salksrlsiskdnsksqvflemdslhtddtaryycarerdyrldywgqgttvtvss
>d1a7ql_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcraggnthnylawyqqkqgkspqllvyytttlaagvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprsfgggtklei
>d1a7rh_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
qvqlqesgpglvapsqslsitctvsgfsltgygvnwvrqppgkglewlgmiwgdgntdyn
salksrlsiskdnsksqvflkmnslhtddtaryycarerdyrldywgqgttltvss
>d1a7rl_ 2.1.1.1.42 Immunoglobulin (variable domains of L and H chains) {Fab D1.3 (mouse), kappa L chain}
divltqspaslsasvgetvtitcrasgnihnylawyqqkqgkspqllvyytttladgvps
rfsgsgsgtqyslkinslqpddfgsyycqhfwstprtfgggtkleik
>d1a7s__ 2.41.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfpgvstvvlgaydlrrre
rqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveagtrcq
vagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplvcegl
ahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1a7ta_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7tb_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
svkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqteml
vnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehgf
tdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadvt
awpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a7ua_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7ub_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a7va_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7vb_ 1.25.3.2.7 Cytochrome c' {Rhodopseudomonas palustris}
qtdviaqrkailkqmgeatkpiaamlkgeakfdqavvqkslaaiaddskklpalfpadsk
tggdtaalpkiwedkakfddlfaklaaaataaqgtikdeaslkaniggvlgnckschddf
rakks
>d1a7w__ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfk
>d1a7xa_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a7xb_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1a80__ 3.1.6.1.6 2,5-diketo-D-gluconic acid reductase A {Corynebacterium}
tvpsivlndgnsipqlgygvfkvppadtqraveealevgyrhidtaaiygneegvgaaia
asgiarddlfittklwndrhdgdepaaaiaeslaklaldqvdlylvhwptpaadnyvhaw
ekmielraagltrsigvsnhlvphlerivaatgvvpavnqielhpayqqreitdwaaahd
vkieswgplgqgkydlfgaepvtaaaaahgktpaqavlrwhlqkgfvvfpksvrrerlee
nldvfdfdltdteiaaidamdpgdgsgrvsahpdevd
>d1a81a_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81c_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81e_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81g_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81i_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a81k_ 4.72.1.1.13 Syk tyrosine kinase {Human (Homo sapiens)}
sanhlpfffgnitreeaedylvqggmsdglyllrqsrnylggfalsvahgrkahhytier
elngtyaiaggrthaspadlchyhsqesdglvcllkkpfnrpqgvqpktgpfedlkenli
reyvkqtwnlqgqaleqaiisqkpqlekliattahekmpwfhgkisreeseqivligskt
ngkflirardnngsyalcllhegkvlhyridkdktgklsipegkkfdtlwqlvehysyka
dgllrvltvpcqki
>d1a82__ 3.30.1.8.1 Dethiobiotin synthetase {Escherichia coli}
skryfvtgtdtevgktvascallqaakaagyrtagykpvasgsektpeglrnsdalalqr
nsslqldyatvnpytfaeptsphiisaqegrpieslvmsaglraleqqadwvlvegaggw
ftplsdtftfadwvtqeqlpvilvvgvklgcinhamltaqviqhagltlagwvandvtpp
gkrhaeymttltrmipapllgeipwlaenpenaatgkyinlall
>d1a85a_ 4.71.1.9.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1a86a_ 4.71.1.9.2 Neutrophil collagenase (MMP-8) {Human (Homo sapiens)}
npkwertnltyrirnytpqlseaeveraikdafelwsvaspliftrisqgeadiniafyq
rdhgdnspfdgpngilahafqpgqgiggdahfdaeetwtntsanynlflvaahefghslg
lahssdpgalmypnyafretsnyslpqddidgiqaiyg
>d1a87__ 6.1.1.1.2 Colicin N {Escherichia coli}
sakvgeititpdnskpgryissnpeysllaklidaesikgtevytfhtrkgqyvkvtvpd
snidkmrvdyvnwkgpkynnklvkrfvsqfllfrkeekeknekeallkaselvsgmgdkl
geylgvkyknvakevandiknfhgrnirsyneamaslnkvlanpkmkvnksdkdaivnaw
kqvnakdmankignlgkafkvadlaikvekireksiegyntgnwgpllleveswiiggvv
agvaislfgavlsflpisglavtalgvigimtisylssfidanrvsninniissvir
>d1a88a_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a88b_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a88c_ 3.59.1.10.4 Chloroperoxidase L {Streptomyces lividans}
gtvttsdgtnifykdwgprdglpvvfhhgwplsaddwdnqmlfflshgyrviahdrrghg
rsdqpstghdmdtyaadvaaltealdlrgavhighstgggevaryvaraepgrvakavlv
savppvmvksdtnpdglplevfdefraalaanraqfyidvpsgpfygfnregatvsqgli
dhwwlqgmmgaanahyeciaafsetdftddlkridvpvlvahgtddqvvpyadaapksae
llanatlksyeglphgmlsthpevlnpdllafvks
>d1a8a__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8b__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1a8c__ 1.3.1.1.24 Cytochrome c552 {Nitrosomonas europaea}
dadlakknnciachqvetkvvgpalkdiaakyadkddaatylagkikggssgvwgqipmp
pnvnvsdadakaladwiltlk
>d1a8d_1 2.26.1.5.1 (1-247) Tetanus neurotoxin {Clostridium tetani}
mknldcwvdneedidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkai
hlvnnessevivhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkh
slsigsgwsvslkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlss
anlyingvlmgsaeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeiek
lytsyls
>d1a8d_2 2.37.4.2.1 (248-452) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d1a8e__ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8f__ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
dktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtl
daglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtgl
grsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstl
nqyfgysgafkclkdgagdvafvkhstifenlankadrdqyellcldntrkpvdeykdch
laqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgf
lkvpprmdakmylgyeyvtairnlregtc
>d1a8ga_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8gb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemnlpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8h_1 1.28.1.1.1 (349-500) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
laddlgnlvqrtramlfrfaegripepvageelaegtglagrlrplvrelkfhvaleeam
ayvkalnryinekkpwelfkkepeearavlyrvveglriasilltpampdkmaelrralg
lkeevrleeaerwglaeprpipeeapvlfpkk
>d1a8h_2 3.19.1.1.5 (1-348) Methionyl-tRNA synthetase (MetRS) {Thermus thermophilus}
mekvfyvttpiyyvnaephlghayttvvadflarwhrldgyrtffltgtdehgetvyraa
qaagedpkafvdrvsgrfkrawdllgiayddfirtteerhkkvvqlvlkkvyeagdiyyg
eyeglycvscerfytekelveglcpihgrpverrkegnyffrmekyrpwlqeyiqenpdl
irpegyrnevlamlaepigdlsisrpksrvpwgiplpwdenhvtyvwfdallnyvsaldy
pegeayrtfwphawhligkdilkphavfwptmlkaagipmyrhlnvggfllgpdgrkmsk
tlgnvvdpfallekygrdalryyllreipygqdtpvseealrtryead
>d1a8i__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
qekrkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgr
wirtqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeie
edaglgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlryg
npwekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsa
kapndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqd
iirrfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawe
vtvktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlr
rmslveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngi
tprrwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfa
aylereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmig
gkaapgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqi
stagteasgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgy
naqeyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqer
vsalyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1a8jh1 2.1.1.1.151 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jh2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8jl1 2.1.1.1.151 (2-111) Immunoglobulin (variable domains of L and H chains) {Lambda L chain dimer MCG (human)}
saltqppsasgslgqsvtisctgtssdvggynyvswyqqhagkapkviiyevnkrpsgvp
drfsgsksgntasltvsglqaedeadyycssyegsdnfvfgtgtkvtvlg
>d1a8jl2 2.1.1.2.136 (112-216) Immunoglobulin (constant domains of L and H chains) {Lambda L chain dimer MCG (human)}
qpkanptvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvettkpskq
snnkyaassylsltpeqwkshrsyscqvthegstvektvaptecs
>d1a8ka_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8kb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8kd_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8ke_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a8l_1 3.38.1.2.2 (1-119) Protein disulfide isomerase {Pyrococcus furiosus}
mglisdadkkvikeeffskmvnpvklivfvrkdhcqycdqlkqlvqelseltdklsyeiv
dfdtpegkelakryridrapattitqdgkdfgvryfglpaghefaafledivdvsreet
>d1a8l_2 3.38.1.2.2 (120-226) Protein disulfide isomerase {Pyrococcus furiosus}
nlmdetkqairnidqdvrilvfvtptcpycplavrmahkfaientkagkgkilgdmveai
eypewadqynvmavpkiviqvngedrvefegaypekmflekllsals
>d1a8ma_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mb_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8mc_ 2.20.1.1.3 Tumor necrosis factor (TNF) {Human (Homo sapiens)}
rtpsdkpvahvvanpqaegqlqwlndranallangvelrdnqlvvpseglyliysqvlfk
gqgcpsthvllthtisriavsyqtkvnllsaikspcqretpegaeakpwyepiylggvfq
lekgdrlsaeinrpdyldfaesgqvyfgiial
>d1a8o__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
dirqgpkepfrdyvdrfyktlraeqasqevknwxtetllvqnanpdcktilkalgpgatl
eexxtacqg
>d1a8p_1 2.38.1.1.5 (2-100) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
snlnvervlsvhhwndtlfsfkttrnpslrfengqfvmiglevdgrplmraysiaspnye
ehleffsikvqngpltsrlqhlkegdelmvsrkptgtlv
>d1a8p_2 3.18.1.1.5 (101-258) Ferredoxin reductase (flavodoxin reductase) {Azotobacter vinelandii}
tsdllpgkhlymlstgtglapfmsliqdpevyerfekvvlihgvrqvnelayqqfitehl
pqseyfgeavkekliyyptvtresfhnqgrltdlmrsgklfediglppinpqddramicg
spsmldescevldgfglkisprmgepgdylierafvek
>d1a8q__ 3.59.1.10.2 Bromoperoxidase A1 {Streptomyces aureofaciens}
picttrdgveifykdwgqgrpvvfihgwplngdawqdqlkavvdagyrgiahdrrghghs
tpvwdgydfdtfaddlndlltdldlrdvtlvahsmgggelaryvgrhgtgrlrsavllsa
ippvmiksdknpdgvpdevfdalkngvltersqfwkdtaegffsanrpgnkvtqgnkdaf
wymamaqtieggvrcvdafgytdftedlkkfdiptlvvhgdddqvvpidatgrksaqiip
naelkvyegsshgiamvpgdkekfnrdlleflnk
>d1a8ra_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rb_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rc_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rd_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8re_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rf_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rg_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rh_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8ri_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rj_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rk_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rl_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rm_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8rn_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8ro_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstceshfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a8s__ 3.59.1.10.5 Chloroperoxidase F {Pseudomonas fluorescens}
ttfttrdgtqiyykdwgsgqpivfshgwplnadswesqmiflaaqgyrviahdrrghgrs
sqpwsgndmdtyaddlaqliehldlrdavlfgfstgggevaryigrhgtarvakaglisa
vpplmlkteanpgglpmevfdgirqasladrsqlykdlasgpffgfnqpgakssagmvdw
fwlqgmaaghknaydcikafsetdftedlkkidvptlvvhgdadqvvpieasgiasaalv
kgstlkiysgaphgltdthkdqlnadllafikg
>d1a8ta_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
aqksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqt
emlvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpe
hgftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisda
dvtawpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a8tb_ 4.128.1.1.2 Zn metallo-beta-lactamase {Bacteroides fragilis}
ksvkisddisitqlsdkvytyvslaeiegwgmvpsngmivinnhqaalldtpindaqtem
lvnwvtdslhakvttfipnhwhgdcigglgylqrkgvqsyanqmtidlakekglpvpehg
ftdsltvsldgmplqcyylggghatdnivvwlptenilfggcmlkdnqttsignisdadv
tawpktldkvkakfpsaryvvpghgnyggteliehtkqivnqyiests
>d1a8ua_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8ub_ 3.59.1.10.3 Chloroperoxidase T {Streptomyces aureofaciens}
pfitvgqenstsidlyyedhgagqpvvlihgfplsghswerqsaalldagyrvitydrrg
fgqssqpttgydydtfaadlntvletldlqdavlvgfsmgtgevaryvssygtariakva
flaslepfllktddnpdgaapkeffdgivaavkadryafytgffndfynldenlgtrise
eavrnswntaasggffaaaaapttwytdfradipridvpalilhgtgdrtlpientarvf
hkalpsaeyvevegaphgllwthaeevntallaflak
>d1a8va_ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
ghmnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleil
qdgfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvne
>d1a8vb_ 2.35.4.5.5 Rho termination factor, N-terminal, RNA-binding domain {Escherichia coli}
ghmnltelkntpvselitlgenmglenlarmrkqdiifailkqhaksgedifgdgvleil
qdgfgflrsadssylagpddiyvspsqirrfnlrtgdtisgkirppkegeryfallkvne
>d1a8y_1 3.38.1.3.1 (3-126) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
gldfpeydgvdrvinvnaknyknvfkkyevlallyheppeddkasqrqfemeelilelaa
qvledkgvgfglvdsekdaavakklglteedsiyvfkedevieydgefsadtlveflldv
ledp
>d1a8y_2 3.38.1.3.1 (127-228) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
veliegerelqafeniedeikligyfknkdsehykafkeaaeefhpyipffatfdskvak
kltlklneidfyeafmeepvtipdkpnseeeivnfveehrrs
>d1a8y_3 3.38.1.3.1 (229-347) Calsequestrin {Rabbit (Oryctolagus cuniculus)}
tlrklkpesmyetweddmdgihivafaeeadpdgyefleilksvaqdntdnpdlsiiwid
pddfpllvpywektfdidlsapqigvvnvtdadsvwmemddeedlpsaeeledwledvl
>d1a8z__ 2.5.1.1.26 Rusticyanin {Thiobacillus ferrooxidans}
ldtswkeatlpqvkamlqkdtgkvsgdtvtysgktvhvvaaavlpgfpfpsfevhdkknp
tldipagatvdvtfintnkgfghsfditqktppfavmpvidpivagtgfspvpkdgkfgy
tnftwhptagtyyyvcqipghaatgmfgkivvk
>d1a90__ 4.15.1.2.1 Cystatin {Chicken (Gallus gallus)}
gapvpvdendeglqralqfaiaeynrasndkyssrvvrvisakrqlvsgikyilqveigr
ttcpkssgdlqscefhdepelakyttctfvvysipwlnqiklleskcq
>d1a91__ 6.2.1.1.7 Subunit C of the F1F0 ATP synthase {Escherichia coli}
menlnmdllymaaavmmglaaigaaigigilggkflegaarqpdlipllrtqffivmglv
daipmiavglglyvmfava
>d1a94a_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94b_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94d_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a94e_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwkrplvtikiggqlkealldtgaddtvieemslpgrwepkmiggiggfikvrqyd
qiiieiaghkaigtvlvgptpvniigrnlltqigatlnf
>d1a95a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a95b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a95c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a95d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
sekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvcis
sydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrpl
vddyvvdipqdtwieqpwdmgvvfvppisg
>d1a96a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a96b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a96c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a96d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvciss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a97a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97c_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a97d_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a98a_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppisgr
>d1a98b_ 3.51.1.1.1 Xantine-guanine PRTase (XPRTase) {Escherichia coli}
ekyivtwdmlqiharklasrlmpseqwkgiiavsrgglvpgallarelgirhvdtvaiss
ydhdnqrelkvlkraegdgegfividdlvdtggtavairemypkahfvtifakpagrplv
ddyvvdipqdtwieqpwdmgvvfvppis
>d1a99a_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99b_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99c_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a99d_ 3.84.1.1.13 Putrescine receptor (PotF) {Escherichia coli}
qktlhiynwsdyiapdtvanfeketgikvvydvfdsnevlegklmagstgfdlvvpsasf
lerqltagvfqpldksklpewknldpellklvakhdpdnkfampymwattgigynvdkvk
avlgenapvdswdlilkpenleklkscgvsfldapeevfatvlnylgkdpnstkaddytg
patdlllklrpniryfhssqyindlangdicvaigwagdvwqasnrakeakngvnvsfsi
pkegamaffdvfampadaknkdeayqflnyllrpdvvahisdhvfyanankaatplvsae
vrenpgiyppadvraklftlkvqdpkidrvrtrawtkvksg
>d1a9ba1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9ba2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9bb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9bd1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9bd2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9be1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9ca_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cb_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cc_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cd_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ce_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cf_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cg_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ch_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ci_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cj_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ck_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cl_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cm_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9cn_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9co_ 4.75.1.1.1 GTP cyclohydrolase I {Escherichia coli}
pslskeaalvhealvargletplrppvhemdnetrksliaghmteimqllnldladdslm
etphriakmyvdeifsgldyanfpkitlienkmkvdemvtvrditltstsehhfvtidgk
atvayipkdsviglskinrivqffaqrpqvqerltqqilialqtllgtnnvavsidavhy
cvkargirdatsattttslgglfkssqntrheflravrhhn
>d1a9ea1 2.1.1.2.10 (182-277) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
adppkthvthhpvsdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrweps
>d1a9ea2 4.17.1.1.17 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-B*3501}
gshsmryfytamsrpgrgeprfiavgyvddtqfvrfdsdaasprteprapwieqegpeyw
drntqifktntqtyreslrnlrgyynqseagshiiqrmygcdlgpdgrllrghdqsaydg
kdyialnedlsswtaadtaaqitqrkweaarvaeqlrayleglcvewlrrylengketlq
r
>d1a9eb1 2.1.1.2.10 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-B*3501}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1a9ma_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9mb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmihgiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1a9na_ 3.9.2.1.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfk
>d1a9nb_ 4.47.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmrg
>d1a9nc_ 3.9.2.1.1 Splicesomal U2A' protein {Human (Homo sapiens)}
vkltaelieqaaqytnavrdreldlrgykipvienlgatldqfdaidfsdneirkldgfp
llrrlktllvnnnricrigegldqalpdlteliltnnslvelgdldplaslksltylcil
rnpvtnkkhyrlyviykvpqvrvldfqkvklkerqeaekmfkgkrgaqlakdia
>d1a9nd_ 4.47.7.1.3 Splicing factor U2B'' {Human (Homo sapiens)}
irpnhtiyinnmndkikkeelkrslyalfsqfghvvdivalktmkmrgqafvifkelgss
tnalrqlqgfpfygkpmriqyaktdsdiiskmr
>d1a9o__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9p__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipvsghtg
>d1a9q__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9r__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9s__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mqngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasi
>d1a9t__ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
mangytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpest
vpghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggl
npnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkq
mgeqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsl
itnkvimdtesqgkanheevleagkqaaqkleqfvsllmasipv
>d1a9u__ 4.117.1.1.11 MAP kinase p38 {Human (Homo sapiens)}
erptfyrqelnktiwevperyqnlspvgsgaygsvcaafdtktglrvavkklsrpfqsii
hakrtyrelrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqklt
ddhvqfliyqilrglkyihsadiihrdlkpsnlavnedcelkildfglarhtddemtgyv
atrwyrapeimlnwmhynqtvdiwsvgcimaelltgrtlfpgtdhidqlklilrlvgtpg
aellkkissesarnyiqsltqmpkmnfanvfiganplavdllekmlvldsdkritaaqal
ahayfaqyhdpddepvadpydqsfesrdllidewksltydevisfvpppld
>d1a9v__ 2.1.1.5.26 Major mite allergen {House-dust mite (Dermatophagoides pteronyssinus), Der p 2}
sqvdvkdcanheikkvlvpgchgsepciihrgkpfqleavfeanqntktakieikasidg
levdvpgidpnachymkcplvkgqqydikytwnvpkiapksenvvvtvkvmgddgvlaca
iathakird
>d1a9wa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a9wc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1a9we_ 1.1.1.1.30 Hemoglobin, beta-chain {Human (Homo sapiens), embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1a9wf_ 1.1.1.1.30 Hemoglobin, beta-chain {Human (Homo sapiens), embryonic gower II}
vhftaeekaavtslwskmnveeaggealgrllvvypwtqrffdsfgnlsspsailgnpkv
kahgkkvltsfgdaiknmdnlkpafaklselhcdklhvdpenfkllgnvmviilathfgk
eftpevqaawqklvsavaialahky
>d1a9xa1 1.89.1.1.1 (403-555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xa2 3.17.1.1.1 (936-1073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xa3 3.24.1.1.3 (1-127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xa4 3.24.1.1.3 (556-676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xa5 4.115.1.2.3 (128-402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xa6 4.115.1.2.3 (677-935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xb1 3.7.3.1.1 (1502-1652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xb2 3.58.1.1.2 (1653-1880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xc1 1.89.1.1.1 (2403-2555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xc2 3.17.1.1.1 (2936-3073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xc3 3.24.1.1.3 (2001-2127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xc4 3.24.1.1.3 (2556-2676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xc5 4.115.1.2.3 (2128-2402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xc6 4.115.1.2.3 (2677-2935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xd1 3.7.3.1.1 (3502-3652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xd2 3.58.1.1.2 (3653-3880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xe1 1.89.1.1.1 (4403-4555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xe2 3.17.1.1.1 (4936-5073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xe3 3.24.1.1.3 (4001-4127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xe4 3.24.1.1.3 (4556-4676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xe5 4.115.1.2.3 (4128-4402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xe6 4.115.1.2.3 (4677-4935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xf1 3.7.3.1.1 (5502-5652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xf2 3.58.1.1.2 (5653-5880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9xg1 1.89.1.1.1 (6403-6555) Carbamoyl phosphate synthetase, large subunit connection domain {Escherichia coli}
evgatgfdpkvslddpealtkirrelkdagadriwyiadafraglsvdgvfnltnidrwf
lvqieelvrleekvaevgitglnadflrqlkrkgfadarlaklagvreaeirklrdqydl
hpvykrvdtcaaefatdtaymystyeeeceanp
>d1a9xg2 3.17.1.1.1 (6936-7073) Carbamoyl phosphate synthetase, large subunit allosteric, C-terminal domain {Escherichia coli}
nstmkkhgrallsvregdkervvdlaakllkqgfeldathgtaivlgeaginprlvnkvh
egrphiqdrikngeytyiinttsgrraiedsrvirrsalqykvhydttlnggfatamaln
adatekvisvqemhaqik
>d1a9xg3 3.24.1.1.3 (6001-6127) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
mpkrtdiksililgagpivigqacefdysgaqackalreegyrvinvnsnpatimtdpem
adatyiepihwevvrkiiekerpdavlptmggqtalncalelerqgvleefgvtmigata
daidkae
>d1a9xg4 3.24.1.1.3 (6556-6676) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
stdrekimvlgggpnrigqgiefdyccvhaslalredgyetimvncnpetvstdydtsdr
lyfepvtledvleivriekpkgvivqyggqtplklaraleaagvpvigtspdaidraedr
e
>d1a9xg5 4.115.1.2.3 (6128-6402) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
drrrfdvamkkigletarsgiahtmeealavaadvgfpciirpsftmggsgggiaynree
feeicargldlsptkellidesligwkeyemevvrdkndnciivcsienfdamgihtgds
itvapaqtltdkeyqimrnasmavlreigvetggsnvqfavnpkngrliviemnprvsrs
salaskatgfpiakvaaklavgytldelmnditggrtpasfepsidyvvtkiprfnfekf
agandrlttqmksvgevmaigrtqqeslqkalrgl
>d1a9xg6 4.115.1.2.3 (6677-6935) Carbamoyl phosphate synthetase (CPS), large subunit {Escherichia coli}
rfqhaverlklkqpanatvtaiemavekakeigyplvvraameivydeadlrryfqtavl
ldhflddavevdvdaicdgemvliggimehieqagvhsgdsacslpaytlsqeiqdvmrq
qvqklafelqvrglmnvqfavknnevylievnpraartvpfvskatgvplakvaarvmag
kslaeqgvtkevippyysvkevvlpfnkfpgvdpllgpemrstgevmgvgrtfaeafaka
qlgs
>d1a9xh1 3.7.3.1.1 (7502-7652) Carbamoyl phosphate synthetase, small subunit N-terminal domain {Escherichia coli}
iksallvledgtqfhgraigatgsavgevvfntsmtgyqeiltdpsysrqivtltyphig
nvgtndadeessqvhaqglvirdlpliasnfrntedlssylkrhnivaiadidtrkltrl
lrekgaqngciiagdnpdaalalekarafpg
>d1a9xh2 3.58.1.1.2 (7653-7880) Carbamoyl phosphate synthetase, small subunit C-terminal domain {Escherichia coli}
lngmdlakevttaeayswtqgswtltgglpqakkedelpfhvvaydfgakrnilrmlvdr
gcrltivpaqtsaedvlkmnpdgiflsngpgdpapcdyaitaiqkfletdipvfgixlgh
qllalasgaktvkmkfghhggnhpvkdveknvvmitaqnhgfavdeatlpanlrvthksl
fdgtlqgihrtdkpafsfqgnpeaspgphdaaplfdhfielieqyrkt
>d1a9y__ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdqpkipyvesfptgtpqspfgksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1a9z__ 3.2.1.2.1 Uridine diphosphogalactose-4-epimerase (UDP-galactose 4-epimerase) {Escherichia coli}
mrvlvtggsgyigshtcvqllqnghdviildnlcnskrsvlpvierlggkhptfvegdir
nealmteilhdhaidtvihfaglkavgesvqkpleyydnnvngtlrlisamraanvknfi
fssaatvygdnpkipyvesfptgtpqspfgksklmveqiltdlqkaqpdwsiallryfnp
vgahpsgdmgedpqgipnnlmpyiaqvavgrrdslaifgndyptedgtgvrdyihvmdla
dghvvameklankpgvhiynlgagvgnsvldvvnafskacgkpvnyhfaprregdlpayw
adaskadrelnwrvtrtldemaqdtwhwqsrhpqgypd
>d1aa1b1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1b2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1c_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1e1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1e2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1f_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1h1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1h2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1i_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa1l1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftxddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1aa1l2 4.47.9.1.2 (21-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
kltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldry
kgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlri
pvayvkt
>d1aa1s_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1aa2__ 1.43.1.1.1 beta-spectrin {Human (Homo sapiens)}
ksakdalllwcqmktagypnvnihnfttswrdgmafnalihkhrpdlidfdklkksnahy
nlqnafnlaeqhlgltklldpedisvdhpdeksiityvvtyyhyfskm
>d1aa3__ 4.39.1.1.1 RecA protein, C-terminal domain {Escherichia coli}
infygelvdlgvkekliekagawysykgekigqgkanatawlkdnpetakeiekkvrell
lsn
>d1aa4__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafekllengitfpkdapspfifktleeqgl
>d1aa6_1 2.46.2.2.3 (565-715) Formate dehydrogenase H {Escherichia coli}
pidkltdeypmvlstvrevghyscrsmtgncaalaaladepgyaqintedakrlgiedea
lvwvhsrkgkiitraqvsdrpnkgaiymtyqwwigacnelvtenlspitktpeykycavr
vepiadqraaeqyvideynklktrlreaala
>d1aa6_2 3.70.1.1.3 (1-564) Formate dehydrogenase H {Escherichia coli}
mkkvvtvcpycasgckinlvvdngkivraeaaqgktnqgtlclkgyygwdfindtqiltp
rlktpmirrqrggklepvswdealnyvaerlsaikekygpdaiqttgssrgtgnetnyvm
qkfaravigtnnvdccarvxhgpsvaglhqsvgngamsnaineidntdlvfvfgynpads
hpivanhvinakrngakiivcdprkietariadmhialkngsniallnamghviieenly
dkafvasrtegfeeyrkivegytpesveditgvsaseirqaarmyaqaksaailwgmgvt
qfyqgvetvrsltslamltgnlgkphagvnpvrgqnnvqgacdmgalpdtypgyqyvkdp
anrekfakawgveslpahtgyriselphraahgevraayimgedplqtdaelsavrkafe
dlelvivqdifmtktasaadvilpstswgehegvftaadrgfqrffkavepkwdlktdwq
iiseiatrmgypmhynntqeiwdelrhlcpdfygatyekmgelgfiqwpcrdtsdadqgt
sylfkekfdtpnglaqfftcdwva
>d1aa7a_ 1.91.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
mslltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgil
gfvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsys
agalascmgliynrmgavttevafglvcatceqiadsq
>d1aa7b_ 1.91.1.1.1 Influenza virus matrix protein M1 {Influenza virus}
slltevetyvlsiipsgplkaeiaqrledvfagkntdlevlmewlktrpilspltkgilg
fvftltvpserglqrrrfvqnalngngdpnnmdkavklyrklkreitfhgakeislsysa
galascmgliynrmgavttevafglvcatceqiadsq
>d1aa8a1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8a2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa8b1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1aa8b2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1aa9__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgaggvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqhklrkl
>d1aab__ 1.22.1.1.1 HMG1, domains A and B {Rat/Hamster (Rattus norvegicus/Cricetulus griseus)}
gkgdpkkprgkmssyaffvqtsreehkkkhpdasvnfsefskkcserwktmsakekgkfe
dmakadkaryeremktyippkge
>d1aac__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>d1aaf__ 7.34.1.1.2 HIV nucleocapsid {Human immunodeficiency virus, type 1, Mn isolate}
mqrgnfrnqrkiikcfncgkeghiakncraprkrgcwkcgkeghqmkdcterqan
>d1aaj__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>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
>d1aam__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaaidanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aan__ 2.5.1.1.1 Amicyanin {Paracoccus denitrificans}
dkatipsespfaaaevadgaivvdiakmkyetpelhvkvgdtvtwinreamphnvhfvag
vlgeaalkgpmmkkeqaysltfteagtydyhctphpfmrgkvvve
>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
>d1aaqa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aaqb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qiiieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aara_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aarb_ 4.13.2.1.1 Ubiquitin {Human (Homo sapiens)}
mqifvktltgktitlevepsdtienvkakiqdkegippdqqrlifagkqledgrtlsdyn
iqkestlhlvlrlrgg
>d1aat__ 3.57.1.1.2 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), cytosolic form}
aasifaavprappvavfkltadfredgdsrkvnlgvgayrtdegqpwvlpvvrkveqlia
gngslnheylpilglpefranasrialgddspaiaqkrvgsvqglggtgalrigaeflrr
wyngnnntatpvyvssptwenhnsvfmdagfkdirtyrywdaakrgldlqgllsdmekap
efsifilhacahnptgtdptpdewkqiaavmkrrclfpffdsayqgfasgnlekdawavr
yfvsegfelfcaqsfsknfglynervgnlsvvgkdednvqrvlsqmekivrttwsnppsq
garivattltspqlfaewkdnvktmadrvllmrselrsrleslgtpgtwnhitdqigmfs
ftglnpkqveymikekhiylmasgrinmcglttknldyvaksiheavtkiq
>d1aaw__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aax__ 3.37.1.3.1 Tyrosine phosphatase {Human (Homo sapiens), 1B}
emekefeqidksgswaaiyqdirheasdfpcrvaklpknknrnryrdvspfdhsriklhq
edndyinaslikmeeaqrsyiltqgplpntcghfwemvweqksrgvvmlnrvmekgslkc
aqywpqkeekemifedtnlkltlisediksyytvrqlelenlttqetreilhfhyttwpd
fgvpespasflnflfkvresgslspehgpvvvhssagigrsgtfcladtclllmdkrkdp
ssvdikkvllemrkfrmgliqtadqlrfsylaviegakfimgdssvqdqwkelshed
>d1aaya1 7.31.1.1.1 (103-131) ZIF268 {Mouse (Mus musculus)}
rpyacpvescdrrfsrsdeltrhirihtg
>d1aaya2 7.31.1.1.1 (132-159) ZIF268 {Mouse (Mus musculus)}
qkpfqcricmrnfsrsdhltthirthtg
>d1aaya3 7.31.1.1.1 (160-187) ZIF268 {Mouse (Mus musculus)}
ekpfacdicgrkfarsderkrhtkihlr
>d1aaza_ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1aazb_ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcvycdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1ab0__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1ab1__ 7.13.1.1.1 Crambin {Abyssinian cabbage (Crambe abyssinica)}
ttccpsivarsnfnvcrlpgtseaicatytgciiipgatcpgdyan
>d1ab2__ 4.72.1.1.12 Proto-oncogen tyrosine kinase {Human (Homo sapiens)}
gsgnslekhswyhgpvsrnaaeyllssgingsflvresesspgqrsislryegrvyhyri
ntasdgklyvssesrfntlaelvhhhstvadglittlhypapkrgihrd
>d1ab3__ 1.16.1.2.2 Ribosomal protein S15 {Thermus thermophilus}
pitkeekqkviqefarfpgdtgstevqvalltlrinrlsehlkvhkkdhhshrgllmmvg
qrrrllrylqredperyralieklgirg
>d1ab4__ 5.11.1.1.2 DNA Gyrase A {Escherichia coli}
vgralpdvrdglkpvhrrvlyamnvlgndwnkaykksarvvgdvigkyhphgdsavydti
vrmaqpfslrymlvdgqgnfgsidgdsaaamryteirlakiahelmadleketvdfvdny
dgtekipdvmptkipnllvngssgiavgmatnipphnltevingclayiddedisieglm
ehipgpdfptaaiingrrgieeayrtgrgkvyiraraevevetiivheipyqvnkarlie
kiaelvkekrvegisalrdesdkdgmriviegevvlnnlysqtqlqvsfginmvalhhgq
pkimnlkdiiaafvrhrrevvtrrtifelrkardrahilealavalanidpiielirhap
tpaeaktalvanpwqlgnvaamledaarpewlepefgvrdglyylteqqaqaildlrlqk
ltgleheklldeykelldqiaellrilgsadrlmevireelelvreqfgdkrrteit
>d1ab5a_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab5b_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrritrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6a_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab6b_ 3.16.2.1.1 CheY protein {Escherichia coli}
elkflvvddnstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmpnmd
glellktiradgamsalpvlmttaeakkeniiaaaqagasgyvvkpftaatleeklnkif
eklgm
>d1ab7__ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdaltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegaditiils
>d1ab8a_ 4.47.24.1.1 Type II adenylyl cyclase C2 domain {Rat (Rattus norvegicus)}
lyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvek
iktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfkl
rvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytc
tc
>d1ab8b_ 4.47.24.1.1 Type II adenylyl cyclase C2 domain {Rat (Rattus norvegicus)}
eelyhqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgv
ekiktigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndf
klrvginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgy
tctc
>e1ab9.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1ab9.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1aba__ 3.38.1.1.6 Glutaredoxin {Bacteriophage T4}
mfkvygydsnihkcgpcdnakrlltvkkqpfefinimpekgvfddekiaelltklgrdtq
igltmpqvfapdgshiggfdqlreyfk
>d1abba_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbb_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbc_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abbd_ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
rkqisvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwir
tqqhyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieeda
glgngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpw
ekarpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakap
ndfnlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiir
rfksskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtv
ktcaytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrms
lveegavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitpr
rwlvlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaayl
ereykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggka
apgyhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqista
gteasgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaq
eyydripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsa
lyknprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpap
>d1abe__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1abf__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllpspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>e1abi.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1abi.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyidgr
>e1abj.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1abj.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1abma1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abma2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abmb1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaayvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1abmb2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1abn__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvsall
sctshkdypfheef
>d1aboa_ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abob_ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1abq__ 2.30.2.1.4 Abl tyrosine kinase, SH3 domain {Mouse (Mus musculus)}
lfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvn
>d1abra_ 4.135.1.1.5 Abrin A-chain {Abrus precatorius}
edrpikfstegatsqsykqfiealrerlrgglihdipvlpdpttlqernryitvelsnsd
tesievgidvtnayvvayragtqsyflrdapssasdylftgtdqhslpfygtygdlerwa
hqsrqqiplglqalthgisffrsggndneekartliviiqmvaeaarfryisnrvrvsiq
tgtafqpdaamislennwdnlsrgvqesvqdtfpnqvtltnirnepvivdslshptvavl
almlfvcnppn
>d1abrb1 2.37.2.1.2 (1-140) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ivekskicssryeptvriggrdgmcvdvydngyhngnriimwkckdrleenqlwtlksdk
tirsngkclttygyapgsyvmiydctsavaeatyweiwdngtiinpksalvlsaesssmg
gtltvqtneylmrqgwrtgn
>d1abrb2 2.37.2.1.2 (141-267) Plant cytotoxin B-chain (lectin) {Abrus precatorius}
ntspfvtsisgysdlcmqaqgsnvwmadcdsnkkeqqwalytdgsirsvqntnncltskd
hkqgstillmgcsngwasqrwvfkndgsiyslyddmvmdvkgsdpslkqiilwpytgkpn
qiwltlf
>d1abs__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
mvlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkase
dlkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrh
pgnfgadaqgamnkalelfrkdiaakykelgyqg
>d1abta_ 7.7.1.1.10 Bungarotoxin {Alpha-bungarotoxin (Bungarus multicinctus)}
ivchttatspisavtcppgenlcyrkmwcdafcssrgkvvelgcaatcpskkpyeevtcc
stdkcnphpkqrpg
>d1abv__ 1.71.1.1.1 N-terminal domain of the delta subunit of the F1F0-ATP synthase {Escherichia coli}
sefitvarpyakaafdfavehqsverwqdmlafaaevtkneqmaellsgalapetlaesf
iavcgeqldengqnlirvmaengrlnalpdvleqfihlravseat
>d1abwa1 1.1.1.1.16 (1-142) Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyrg
>d1abwa2 1.1.1.1.16 (143-283) Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1abwb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abwd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abya1 1.1.1.1.16 (1-142) Hemoglobin, alpha-chain {Human (Homo sapiens)}
mlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyrg
>d1abya2 1.1.1.1.16 (143-283) Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1abyb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1abyd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
mhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgkvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1ac0__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1ac1a1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1a2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac1b1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1ac1b2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcplcyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1ac4__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ac5__ 3.59.1.4.3 Serine carboxypeptidase II {Baker's yeast (Saccharomyces cerevisiae), kex1(delta)p}
lpsseeykvayellpglsevpdpsnipqmhaghiplrsedadeqdssdleyffwkftnnd
sngnvdrpliiwlnggpgcssmdgalvesgpfrvnsdgklylnegswiskgdllfidqpt
gtgfsveqnkdegkidknkfdedledvtkhfmdflenyfkifpedltrkiilsgesyagq
yipffanailnhnkfskidgdtydlkalligngwidpntqslsylpfamekklidesnpn
fkhltnahencqnlinsastdeaahfsyqecenilnlllsytressqkgtadclnmynfn
lkdsypscgmnwpkdisfvskffstpgvidslhldsdkidhwkectnsvgtklsnpiskp
sihllpgllesgieivlfngdkdlicnnkgvldtidnlkwggikgfsddavsfdwihksk
stddseefsgyvkydrnltfvsvynashmvpfdkslvsrgivdiysndvmiidnngknvm
itt
>d1ac6a_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac6b_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
dsvtqtegqvalseedfltihcnysasgypalfwyvqypgegpqflfrasrdkekgssrg
featynkeatsfhlqkasvqesdsavyycalsggnnkltfgagtkltikp
>d1ac8__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aca__ 1.11.1.1.1 Acyl-CoA binding protein {Bovine (Bos taurus)}
sqaefdkaaeevkhlktkpadeemlfiyshykqatvgdinterpgmldfkgkakwdawne
lkgtskedamkayidkveelkkkygi
>d1acbe_ 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
cgvpaiqpvlsglsrivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgv
ttsdvvvagefdqgsssekiqklkiakvfknskynsltinnditllklstaasfsqtvsa
vclpsasddfaagttcvttgwgltrytnantpdrlqqaslpllsntnckkywgtkikdam
icagasgvsscmgdsggplvckkngawtlvgivswgsstcststpgvyarvtalvnwvqq
tlaan
>d1acbi_ 4.33.1.1.1 Eglin C {Leech (Hirudo medicinalis)}
ksfpevvgktvdqareyftlhypqydvyflpegspvtldlrynrvrvfynpgtnvvnhvp
hvg
>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
>d1acd__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
gdafvgtwklvssenfddymkevgvgfatrkdagmakpnmiisvngdlvtirsesthknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvexvmk
gvtstrvyera
>d1acf__ 4.86.1.1.3 Profilin (actin-binding protein) {Acanthamoeba castellanii}
swqtyvdtnlvgtgavtqaailgldgntwatsagfavtpaqgttlagafnnadairaggf
dlagvhyvtlraddrsiygkkgssgvitvktskailvgvynekiqpgtaanvvekladyl
igqgf
>d1aci__ 1.4.4.1.1 Ribosomal protein L11, C-terminal domain {Bacillus stearothermophilus}
mtfitktppaavllkkaagiesgsgepnrnkvatikrdkvreiaelkmpdlnaasieaam
rmiegtarsmgivved
>d1acj__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1acl__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1acma1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastatrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1acma2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1acmb1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1acmb2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1acmc1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastatrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1acmc2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1acmd1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1acmd2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1aco_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1aco_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1acp__ 1.29.1.1.1 Acyl carrier protein {Escherichia coli}
stieervkkiigeqlgvkqeevtnnasfvedlgadsldtvelvmaleeefdteipdeeae
kittvqaaidyinghqa
>d1acva1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acva2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acvb1 1.47.1.1.1 (65-128) Disulphide-bond formation facilitator (DSBA), insertion domain {Escherichia coli}
ggdlgkdltqawavamalgvedkvtvplfegvqktqtirsasdirdvfinagikgeeyda
awns
>d1acvb2 3.38.1.4.1 (1-64,129-188) Disulphide-bond formation facilitator (DSBA) {Escherichia coli}
aqyedgkqyttlekpvagapqvleffsffcpscyqfeevlhisdnvkkklpegvkmtkyh
vnfmXfvvkslvaqqekaaadvqlrgvpamfvngkyqlnpqgmdtsnmdvfvqqyadtvk
ylsek
>d1acw__ 7.3.7.2.14 Toxin analog P01 {Androctonus mauretanicus}
vscedcpehcstqkaqakcdndkcvcepi
>d1acx__ 2.1.7.1.3 Actinoxanthin {Actinomyces globisporus, number 1131}
apafsvspasgasdgqsvsvsvaaagetyyiaqcapvggqdacnpatatsfttdasgaas
fsftvrksyagqtpsgtpvgsvdcatdacnlgagnsglnlghvaltfg
>d1acyh1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1acyh2 2.1.1.2.40 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1acyl1 2.1.1.1.31 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1acyl2 2.1.1.2.40 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1acz__ 2.3.1.1.5 Glucoamilase, granular starch-binding domain {Aspergillus niger}
cttptavavtfdltatttygeniylvgsisqlgdwetsdgialsadkytssdplwyvtvt
lpagesfeykfiriesddsvewesdpnreytvpqacgtstatvtdtwr
>d1ad0a1 2.1.1.1.80 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0a2 2.1.1.2.84 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0b1 2.1.1.1.80 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0b2 2.1.1.2.84 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad0c1 2.1.1.1.80 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
qtvltqspsslsvsvgdrvtitcrasssvtyihwyqqkpglapksliyatsnlasgvpsr
fsgsgsgtdytftisslqpediatyycqhwsskpptfgqgtkvevkr
>d1ad0c2 2.1.1.2.84 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad0d1 2.1.1.1.80 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
evqllesggglvqpggslrlscatsgftftdyymnwvrqapgkglewlgfignkangytt
eysasvkgrftisrdkskstlylqmntlqaedsaiyyctrdrglrfyfdywgqgtlvtvs
s
>d1ad0d2 2.1.1.2.84 (114-211) Immunoglobulin (constant domains of L and H chains) {Fab A5B7 (engineered human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad1a_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhn
>d1ad1b_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhnfs
>d1ad2__ 5.20.1.1.1 Ribosomal protein L1 {Thermus thermophilus}
kryrallekvdpnkiytideaahlvkelatakfdetvevhaklgidprrsdqnvrgtvsl
phglgkqvrvlaiakgekikeaeeagadyvggeeiiqkildgwmdfdavvatpdvmgavg
sklgrilgprgllpnpkagtvgfnigeiireikagriefrndktgaihapvgkacfppek
ladnirafiraleahkpegakgtflrsvyvtttmgpsvrinphs
>d1ad3a_ 3.71.1.1.1 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1ad3b_ 3.71.1.1.1 Aldehyde reductase (dehydrogenase), ALDH {Rat (Rattus norvegicus)}
sisdtvkrareafnsgktrslqfriqqlealqrminenlksisgalasdlgknewtsyye
evahvleeldttikelpdwaedepvaktrqtqqddlyihseplgvvlvigawnypfnlti
qpmvgavaagnavilkpsevsghmadllatlipqymdqnlylvvkggvpettellkerfd
himytgstavgkivmaaaakhltpvtlelggkspcyvdkdcdldvacrriawgkfmnsgq
tcvapdyilcdpsiqnqiveklkkslkdfygedakqsrdygriindrhfqrvkglidnqk
vahggtwdqssryiaptilvdvdpqspvmqeeifgpvmpivcvrsleeaiqfinqrekpl
alyvfsnnekvikkmiaetssggvtandvivhitvptlpfggvgnsgmgayhgkksfetf
shrrsclvksllneeahkaryppspa
>d1ad4a_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarh
>d1ad4b_ 3.1.19.1.2 Dihydropteroate synthetase {Staphylococcus aureus}
tktkimgilnvtpdsfsdggkfnnvesavtrvkammdegadiidvggvstrpghemitve
eelnrvlpvveaivgfdvkisvdtfrsevaeaclklgvdiindqwaglydhrmfqvvaky
daeivlmhngngnrdepvveemltsllaqahqakiagipsnkiwldpgigfaktrneeae
vmarldelvateypvllatsrkrftkemmgydttpverdevtaattaygimkgvravrvh
nvelnaklakgidflkenenarhnfs
>d1ad5a1 2.30.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5a2 4.72.1.1.8 (146-248) Hemopoetic cell kinase Hck {Human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5a3 4.117.1.2.1 (249-531) Haemopoetic cell kinase Hck {Human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>d1ad5b1 2.30.2.1.10 (82-145) Hemapoetic cell kinase Hck {Human (Homo sapiens)}
ediivvalydyeaihhedlsfqkgdqmvvleesgewwkarslatrkegyipsnyvarvds
let
>d1ad5b2 4.72.1.1.8 (146-248) Hemopoetic cell kinase Hck {Human (Homo sapiens)}
eewffkgisrkdaerqllapgnmlgsfmirdsettkgsyslsvrdydprqgdtvkhykir
tldnggfyisprstfstlqelvdhykkgndglcqklsvpcmss
>d1ad5b3 4.117.1.2.1 (249-531) Haemopoetic cell kinase Hck {Human (Homo sapiens)}
kpqkpwekdaweipreslklekklgagqfgevwmatynkhtkvavktmkpgsmsveafla
eanvmktlqhdklvklhavvtkepiyiitefmakgslldflksdegskqplpklidfsaq
iaegmafieqrnyihrdlraanilvsaslvckiadfglarvgakfpikwtapeainfgsf
tiksdvwsfgillmeivtygripypgmsnpeviralergyrmprpencpeelynimmrcw
knrpeerptfeyiqsvlddfytatesqxqqqp
>d1ad6__ 1.73.1.3.1 Retinoblastoma tumor suppressor domains {Human (Homo sapiens)}
vmntiqqlmmilnsasdqpsenlisyfnnctvnpkesilkrvkdigyifkekfakavgqg
cveigsqryklgvrlyyrvmesmlkseeerlsiqnfskllndnifhmsllacalevvmat
ysrstsqnldsgtdlsfpwilnvlnlkafdfykviesfikaegnltremikhlercehri
mesla
>e1ad8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ad8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ad9a1 2.1.1.1.98 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9a2 2.1.1.2.99 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1ad9b1 2.1.1.1.98 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9b2 2.1.1.2.99 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9h1 2.1.1.1.98 (1-113) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
eiqlvqsgaevkkpgssvkvsckasgytftdyyinwmrqapgqglewigwidpgsgntky
nekfkgratltvdtstntaymelsslrsedtafyfcarekttyyyamdywgqgtlvtvss
>d1ad9h2 2.1.1.2.99 (114-212) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
astkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtktytcnvdhkpsntkvdkrve
>d1ad9l1 2.1.1.1.98 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (human consruct), kappa L chain}
diqmtqspstlsasvgdrvtitcrssksllhsngdtflywfqqkpgkapkllmyrmsnla
sgvpsrfsgsgsgteftltisslqpddfatyycmqhleypftfgqgtkvevkr
>d1ad9l2 2.1.1.2.99 (108-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (human construct), kappa L chain}
tvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqds
kdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1adba1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adba2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adbb1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adbb2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adca1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adca2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adcb1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adcb2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1add__ 3.1.8.1.1 Adenosine deaminase (ADA) {Mouse (Mus musculus)}
tpafnkpkvelhvhldgaikpetilyfgkkrgialpadtveelrniigmdkplslpgfla
kfdyympviagcreaikriayefvemkakegvvyvevrysphllanskvdpmpwnqtegd
vtpddvvdlvnqglqegeqafgikvrsilccmrhqpswslevlelckkynqktvvamdla
gdetiegsslfpghveayegavkngihrtvhagevgspevvreavdilktervghgyhti
edealynrllkenmhfevcpwssyltgawdpktthavvrfkndkanyslntddplifkst
ldtdyqmtkkdmgfteeefkrlninaakssflpeeekkellerlyreyq
>d1adea_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adeb_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adf_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adf_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adg_1 2.31.1.2.1 (1-174,325-374) Alcohol dehydrogenase {Horse (Equus caballus)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1adg_2 3.2.1.1.1 (175-324) Alcohol dehydrogenase {Horse (Equus caballus)}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1adia_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adib_ 3.30.1.8.2 Adenylosuccinate synthetase (gene purA product) {Escherichia coli}
gnnvvvlgtqwgdegkgkivdllterakyvvryqgghnaghtlvingektvlhlipsgil
renvtsiigngvvlspaalmkemkeledrgipvrerlllseacplildyhvaldnareka
rgakaigttgrgigpayedkvarrglrvgdlfdketfaeklkevmeyhnfqlvnyykaea
vdyqkvlddtmavadiltsmvvdvsdlldqarqrgdfvmfegaqgtlldidhgtypyvts
snttaggvatgsglgpryvdyvlgilkaystrvgagpfptelfdetgeflckqgnefgat
tgrrrrtgwldtvavrravqlnslsgfcltkldvldglkevklcvayrmpdgrevtttpl
aaddwkgvepiyetmpgwsestfgvkdrsglpqaalnyikrieeltgvpidiistgpdrt
etmilrdpfda
>d1adja1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adja2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjb1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjb2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjc1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjc2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adjd1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adjd2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adl__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1adn__ 7.40.1.1.1 Ada DNA repair protein, N-terminal domain (N-Ada 10) {Escherichia coli}
mkkatcltddqrwqsvlardpnadgefvfavrttgifcrpscrarhalrenvsfyanase
alaagfrpckrcqpdkanprqhrldkithacr
>d1adoa_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adob_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adoc_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adod_ 3.1.9.1.5 Fructose-1,6-bisphosphate aldolase {Rabbit (Oryctolagus cuniculus)}
phshpaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkysheeiamatvtalrrtvppavtgvtflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytssgqagaaaseslfisn
hay
>d1adqa1 2.1.1.2.139 (238-341) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
psvflfppkpkdtlmisrtpevtcvvvdvsqedpqvqfnwyvdgvqvhnaktkpreqqfn
styrvvsvltvlhqnwldgkeykckvsnkglpssiektiskakg
>d1adqa2 2.1.1.2.139 (342-443) Immunoglobulin (constant domains of L and H chains) {Fc (human) IgG1 class}
qprepqvytlppsqeemtknqvsltclvkgfypsdiavewesngqpennykttppvldsd
gsfflysrltvdksrwqegnvfscsvmhealhnhytqkslsl
>d1adqh1 2.1.1.1.111 (1-113) Immunoglobulin (variable domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
evqlvesggglvqpgrslrlscvtsgftfddyamhwvrqspgkglewvsgiswntgtiiy
adsvkgrfiisrdnaknslylqmnslrvedtalyycaktrsyvvaaeyyfhywgqgilvt
vss
>d1adqh2 2.1.1.2.110 (114-223b) Immunoglobulin (constant domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
gsasaptlfplvscensnpsstvavgclaqdflpdsitfswkyknnsdisstrgfpsvlr
ggkyaatsqvllpskdvmqgtnehvvckvqhpngnkekdvpl
>d1adql1 2.1.1.1.111 (2-107) Immunoglobulin (variable domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
yvltqppsvsvapgqtaritcggnnigsksvhwyqqkpgqapvlvvyddsdrppgiperf
sgsnsgntatltisrveagdeadyycqvwdsssdhavfgggtkltvlg
>d1adql2 2.1.1.2.110 (108-215) Immunoglobulin (constant domains of L and H chains) {IgM rheumatoid factor Fab (human), lambda L chain}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadgspvkagvetttpskq
snnkyaassylsltpeqwkshksyscqvthegstvektvaptecs
>d1adr__ 1.36.1.2.4 p22 C2 repressor, DNA-binding domain {Bacteriophage p22 (Salmonella)}
mntqlmgerirarrkklkirqaalgkmvgvsnvaisqwersetepngenllalskalqcs
pdyllkgdlsqtnvay
>d1ads__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
asrlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqe
klreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgke
ffpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpa
vnqiechpyltqekliqycqskgivvtaysplgspdrpwakpedpslledprikaiaakh
nkttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvcal
lsctshkdypfheef
>d1adt_1 1.56.1.1.1 (176-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
pivsawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltft
snktfvtmmgrflqaylqsfaevtykhhep
>d1adt_2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adt_3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpqfkws
tkhqyrnvslpvahsdarqnpfdf
>d1adua1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adua2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adua3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adub1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adub2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adub3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adva1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1adva2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1adva3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1advb1 1.56.1.1.1 (180-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
awekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnkt
fvtmmgrflqaylqsfaevtykhhep
>d1advb2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1advb3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1adwa_ 2.5.1.1.19 Pseudoazurin {Thiosphaera pantotropha}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adwb_ 2.5.1.1.19 Pseudoazurin {Thiosphaera pantotropha}
athevhmlnkgesgamvfepafvraepgdvinfvptdkshnveaikeilpegvesfkski
nesytltvtepglygvkctphfgmgmvglvqvgdapenldaaktakmpkkarermdaela
qvn
>d1adx__ 7.3.11.1.17 Thrombomodulin, different EGF-like domains {Human (Homo sapiens)}
qmfcnqtacpadcdpntqascecpegyilddgfictdide
>d1adya1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adya2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyb1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyb2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyc1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyc2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adyd1 3.42.1.1.2 (326-421) Histidyl-tRNA synthetase (HisRS), C-terminal domain {Thermus thermophilus}
ekgpdlyliplteeavaeafylaealrprlraeyalaprkpakgleealkrgaafagflg
edelragevtlkrlatgeqvrlsreevpgyllqalg
>d1adyd2 4.82.1.1.4 (2-325) Histidyl-tRNA synthetase (HisRS) {Thermus thermophilus}
taravrgtkdlfgkelrmhqrivatarkvleaagalelvtpifeetqvfekgvgaatdiv
rkemftfqdrggrsltlrpegtaamvraylehgmkvwpqpvrlwmagpmfraerpqkgry
rqfhqvnyealgsenpildaeavvllyeclkelglrrlkvklssvgdpedrarynaylre
vlsphrealsedskerleenpmrildskserdqallkelgvrpmldflgeearahlkeve
rhlerlsvpyelepalvrgldyyvrtafevhheeigaqsalggggrydglsellggprvp
gvgfafgvervalaleaegfglpe
>d1adz__ 7.8.1.1.3 Tissue factor pathway inhibitor {Human (Homo sapiens)}
dykddddklkpdfcfleedpgicrgyitryfynnqtkqcerfkyggclgnmnnfetleec
knicedgpngf
>d1ae1a_ 3.2.1.2.16 Tropinone reductase {Jimsonweed (Datura stramonium), I}
rwslkgttalvtggskgigyaiveelaglgarvytcsrnekeldecleiwrekglnvegs
vcdllsrterdklmqtvahvfdgklnilvnnagvvihkeakdftekdyniimgtnfeaay
hlsqiaypllkasqngnviflssiagfsalpsvslysaskgainqmtkslacewakdnir
vnsvapgviltplvetaikknphqkeeidnfivktpmgragkpqevsaliaflcfpaasy
itgqiiwadggftanggf
>d1ae1b_ 3.2.1.2.16 Tropinone reductase {Jimsonweed (Datura stramonium), I}
rwslkgttalvtggskgigyaiveelaglgarvytcsrnekeldecleiwrekglnvegs
vcdllsrterdklmqtvahvfdgklnilvnnagvvihkeakdftekdyniimgtnfeaay
hlsqiaypllkasqngnviflssiagfsalpsvslysaskgainqmtkslacewakdnir
vnsvapgviltplvetaikknphqkeeidnfivktpmgragkpqevsaliaflcfpaasy
itgqiiwadggftanggf
>d1ae2__ 2.35.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqrcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlrlvpa
>d1ae3__ 2.35.4.8.1 Gene V protein {Bacteriophage f1}
mikveikpsqaqfttrsgvsrqgkpyslneqlcyvdlgneypvlvkitldegqpayapgl
ytvhlssfkvgqfgslmidrlclvpa
>d1ae4__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
aascvllhtgqkmpliglgtwksepgqvkaaikyaltvgyrhidcaaiygneleigealt
etvgpgkavpreelfvtsklwntkhhpedvepalrktladlqleyldlylmhwpyaferg
dnpfpknadgtirydathykdtwkalealvakglvralglsnfssrqiddvlsvasvrpa
vlqvechpylaqneliahcqarglevtaysplgssdrawrdpnepvlleepvvqalaeky
nrspaqillrwqvqrkvicipksvtpsripqniqvfdftfspeemkqldalnknlrfivp
mltvdgkrvprdaghplypfndpy
>d1ae5__ 2.41.1.2.18 Heparin binding protein, HBP {Human (Homo sapiens)}
ivggrkarprqfpflasiqnqgrhfcggaliharfvmtaascfqsqnpgvstvvlgaydl
rrrerqsrqtfsissmsengydpqqnlndlmllqldreanltssvtilplplqnatveag
trcqvagwgsqrsggrlsrfprfvnvtvtpedqcrpnnvctgvltrrggicngdggtplv
ceglahgvasfslgpcgrgpdfftrvalfrdwidgvlnnpgpgpa
>d1ae6h1 2.1.1.1.97 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
qiqlqqsgpelvkpgasvkisckasgytftdyyinwmkqkpgqglewigwidpgsgntky
nekfkgkatltvdtssstaymqlssltsedtavyfcarekttyyyamdywgqgtsvtvsa
a
>d1ae6h2 2.1.1.2.98 (115-211) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
kttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsdl
ytlsssvtvpssprpsetvtcnvahpasstkvdkkiv
>d1ae6l1 2.1.1.1.97 (1-106a) Immunoglobulin (variable domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
divmtqaapsvpvtpgeslsiscrssksllhsngdtflywflqrpgqspqlliyrmsnla
sgvpdrfsgsgsgtaftlrvsrveaedvgvyycmqhleypftfgagtklelk
>d1ae6l2 2.1.1.2.98 (107-213) Immunoglobulin (constant domains of L and H chains) {Fab CTM01 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ae7__ 1.123.1.2.7 Snake phospholipase A2 {Mainland tiger snake (Notechis scutatus scutatus), notexin}
nlvqfsyliqcanhgkrptwhymdygcycgaggsgtpvdeldrcckihddcydeagkkgc
fpkmsaydyycgengpycrnikkkclrfvcdcdveaafcfakapynnanwnidtkkrcq
>e1ae8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ae8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1ae9a_ 4.133.1.1.2 Integrase (Int) {Bacteriophage lambda}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1ae9b_ 4.133.1.1.2 Integrase (Int) {Bacteriophage lambda}
rsrltadeylkiyqaaesspcwlrlamelavvtgqrvgdlcemkwsdivdgylyveqskt
gvkiaiptalhidalgismketldkckeilggetiiastrreplssgtvsryfmrarkas
glsfegdpptfhelrslsarlyekqisdkfaqhllghksdtmasqfrddrgrewdkiei
>d1aeb__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aec__ 4.3.1.1.1 Actinidin {Chinese gooseberry or kiwifruit (Actinidia chinensis)}
lpsyvdwrsagavvdiksqgecggcwafsaiatveginkivtgvlislseqelidcgrtq
ntrgcnggyitdgfqfiinngginteenypytaqdgecnvdlqnekyvtidtyenvpynn
ewalqtavtyqpvsvaldaagdafkqyssgiftgpcgtaidhavtivgygteggidywiv
knswdttwgeegymrilrnvggagtcgiatmpsypvky
>d1aed__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aee__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aef__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeg__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeh__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeia_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeib_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeic_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeid_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeie_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aeif_ 1.66.1.1.8 Annexin XII {Hydra (Hydra attenuata)}
vvqgtvkphasfnsredaetlrkamkgigtdeksithilatrsnaqrqqiktdyttlfgk
hledelkselsgnyeaaalallrkpdeflaeqlhaamkglgtdenalidilctqsnaqih
aikaafkllykedlekeiisetsgnfqrllvsmlqggrkedepvnaahaaedaaaiyqag
egqigtdesrfnavlatrsypqlhqifheyskisnktilqaienefsgdikngllaivks
venrfayfaerlhhamkglgtsdktlirilvsrseidlaniketfqamygkslyefiadd
csgdykdlllqitgh
>d1aej__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aek__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1ael__ 2.53.1.2.3 Intestinal fatty acid binding protein {Rat (Rattus rattus)}
afdgtwkvdrnenyekfmekmginvvkrklgahdnlkltitqegnkftvkessnfrnidv
vfelgvdfaysladgteltgtwtmegnklvgkfkrvdngkeliavreisgneliqtytye
gveakrifkke
>d1aem__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aen__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeo__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aep__ 1.64.1.1.1 Apolipophorin-III {African locust (Locusta migratoria)}
niaeavqqlnhtivnaahelhetlglptpdealnllteqanafktkiaevttslkqeaek
hqgsvaeqlnafarnlnnsihdaatslnlqdqlnslqsaltnvghqwqdiatktqasaqe
awapvqsalqeaaektkeaaanlqnsiqsavqk
>d1aeq__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aera_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
aflgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvraa
iwrgfyiagdpalaygyaqdqepdargrirngallrvyvprsslpgfyrtsltlaapeaa
geverlighplplrldaitgpeeeggrletilgwplaertvvipsaiptdprnvggdldp
ssipdkeqaisalpdyasqpgkppr
>d1aerb_ 4.136.1.1.4 Exotoxin A, C-terminal domain {Pseudomonas aeruginosa}
flgdggdvsfstrgtqnwtverllqahrqleergyvfvgyhgtfleaaqsivfggvrars
qdldaiwrgfyiagdpalaygyaqdqepdrgrirngallrvyvprsslpgfyrtsltlaa
peaageverlighplplrldaitgprletilgwplaertvvipsaiptdprnvggdldps
sipdkeqaisalpdy
>d1aes__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aet__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aeu__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aev__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1aew__ 1.26.1.1.5 (Apo)ferritin {Horse (Equus caballus), L chain}
sqirqnysteveaavnrlvnlylrasytylslgfyfdrddvalegvchffrelaeekreg
aerllkmqnqrggralfqdlqkpsqdewgttpdamkaaivlekslnqalldlhalgsaqa
dphlcdfleshfldeevklikkmgdhltniqrlvgsqaglgeylferltl
>d1aex__ 2.35.1.1.1 Staphylococcal nuclease {Staphylococcus aureus}
lhkepatlikaidgdtxklmykgqpmtfrlllvdtpetkhpkkgvekygpeasaftkkmv
enakkievefdkgqrtdkygrglayiyadgkmvnealvrqglakvayvykpnntheqhlr
kseaqakkeklniws
>d1aey__ 2.30.2.1.8 alpha-Spectrin, SH3 domain {Chicken (Gallus gallus)}
gkelvlalydyqeksprevtmkkgdiltllnstnkdwwkvevndrqgfvpaayvkkld
>d1af0a1 2.70.1.1.2 (247-471) Metalloprotease, C-terminal domain {Serratia marcescens}
ganlstrtgdtvygfnsntgrdflsttsnsqkvifaawdaggndtfdfsgytanqrinln
eksfsdvgglkgnvsiaagvtienaiggsgndvivgnaannvlkggagndvlfggggade
lwggagkdifvfsaasdsapgasdwirdfqkgidkidlsffdkeansssfihfvdhfsgt
ageallsynassnvtdlsvnigghqapdflvkivgqvdvatdfiv
>d1af0a2 4.71.1.4.2 (2-246) Metallo protease, catalytic (N-terminal) domain {Serratia marcescens}
attgydavddllhyhergngiqingkdsfsneqaglfitrenqtwngykvfgqpvkltfs
fpdykfsstnvagdtglskfsaeqqqqaklslqswadvanitftevaagqkanitfgnys
qdrpghydygtqayaflpntiwqgqdlggqtwynvnqsnvkhpatedygrqtftheigha
lglshpgdynagegdptyndvtyaedtrqfslmsywsetntggdngghyaaapllddiaa
iqhly
>d1af2a1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1af2a2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1af3__ 6.1.4.1.2 Apoptosis regulator Bcl-xL {Rat (Rattus norvegicus)}
sqsnrelvvdflsyklsqkgyswsqfsdveenrteapeeteperetpsaingnpswhlad
spavngatghsssldarevipmaavkqalreagdefelryrrafsdltsqlhitpgtayq
sfeqvvnelfrdgvnwgrivaffsfggalcvesvdkemqvlvsriaswmatylndhlepw
iqenggwdtfvdlyg
>d1af4__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1af5__ 4.74.2.1.1 DNA endonuclease I-CreI {Chlamydomonas reinhardtii}
kynkefllylagfvdgdgsiiaqikpnqsykfkhqlsltfqvtqktqrrwflgklvdeig
vgyvrdrgsvsdyilseikplhnfltqlqpflklkqkqanlvlkiieqlplevctwvdqi
aalnds
>d1af6a_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6b_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af6c_ 6.4.3.2.1 Maltoporin (also LamB protein) {Escherichia coli}
vdfhgyarsgigwtgsggeqqcfqttgaqskyrlgnecetyaelklgqevwkegdksfyf
dtnvaysvaqqndweatdpafreanvqgknliewlpgstiwagkrfyqrhdvhmidfyyw
disgpgaglenidvgfgklslaatrsseaggsssfasnniydytnetandvfdvrlaqme
inpggtlelgvdygranlrdnyrlvdgaskdgwlftaehtqsvlkgfnkfvvqyatdsmt
sqgkglsqgsgvafdnekfayninnnghmlrildhgaismgdnwdmmyvgmyqdinwdnd
ngtkwwtvgirpmykwtpimstvmeigydnvesqrtgdknnqykitlaqqwqagdsiwsr
pairvfatyakwdekwgydytgnadnnanfgkavpadfnggsfgrgdsdewtfgaqmeiw
w
>d1af7_1 1.60.1.1.1 (11-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
svllqmtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgryl
smleanqnsaewqafinaltt
>d1af7_2 3.56.1.3.1 (92-284) Chemotaxis receptor methyltransferase CheR, C-terminal domain {Salmonella typhimurium}
nltaffreahhfpilaeharrrhgeyrvwsaaastgeepysiaitladalgmapgrwkvf
asdidtevlekarsgiyrlselktlspqqlqryfmrgtgpheglvrvrqelanyvefssv
nllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvpllkpdgllfaghsenfsnlvr
efslrgqtvyals
>d1af8__ 1.29.1.1.2 Actinorhodin polyketide synthase acyl carrier protein, ACT ACP {Streptomyces coelicolor, A3(2)}
matllttddlrralvecagetdgtdlsgdfldlrfedigydslalmetaarlesrygvsi
pddvagrvdtprelldlingalaeaa
>d1af9_1 2.26.1.5.1 (875-1110) Tetanus neurotoxin {Clostridium tetani}
edidvilkkstilnldinndiisdisgfnssvitypdaqlvpgingkaihlvnnessevi
vhkamdieyndmfnnftvsfwlrvpkvsashleqygtneysiissmkkhslsigsgwsvs
lkgnnliwtlkdsagevrqitfrdlpdkfnaylankwvfititndrlssanlyingvlmg
saeitglgairednnitlkldrcnnnnqyvsidkfrifckalnpkeieklytsyls
>d1af9_2 2.37.4.2.1 (1111-1315) Tetanus neurotoxin {Clostridium tetani}
itflrdfwgnplrydteyylipvassskdvqlknitdymyltnapsytngklniyyrrly
nglkfiikrytpnneidsfvksgdfiklyvsynnnehivgypkdgnafnnldrilrvgyn
apgiplykkmeavklrdlktysvqlklyddknaslglvgthngqigndpnrdiliasnwy
fnhlkdkilgcdwyfvptdegwtnd
>d1afa11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afa31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afb31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afca_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcb_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcc_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcd_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afce_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcf_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afcg_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afch_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
kpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdt
dgllygsqtpneeclflerleenhyntyiskkhaekhwfvglkkngrsklgprthfgqka
ilflplp
>d1afd11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afd21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>d1afd31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvtivdnglwndiscqashtavcef
pa
>e1afe.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1afe.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>d1afh__ 1.54.1.1.4 Plant non-specific lipid-transfer protein (ns-LTP) {Maize (Zea mays)}
aiscgqvasaiapcisyargqgsgpsagccsgvrslnnaarttadrraacnclknaaagv
sglnagnaasipskcgvsipytiststdcsrvn
>d1afi__ 4.47.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afj__ 4.47.16.1.1 Mercuric ion binding protein MerP {Shigella flexneri}
atqtvtlavpgmtcaacpitvkkalskvegvskvdvgfekreavvtfddtkasvqkltka
tadagypssvkq
>d1afka_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afkb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afla_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1aflb_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afp__ 7.26.1.1.1 Antifungal protein (AGAFP) {Mold (Aspergillus giganteus)}
atyngkcykkdnickykaqsgktaickcyvkkcprdgakcefdsykgkcyc
>e1afq.1b 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ivngeeavpgswpwqvslqdktgfhfcggslinenwvvtaahcgvttsdvvvagefdqgs
ssekiqklkiakvfknskynsltinnditllklstaasfsqtvsavclpsasddfaagtt
cvttgwgltry
>e1afq.1c 2.41.1.2.7 (alpha,gamma)-chymotrypsin(ogen) {Bovine (Bos taurus)}
ntpdrlqqaslpllsntnckkywgtkikdamicagasgvsscmgdsggplvckkngawtl
vgivswgsstcststpgvyarvtalvnwvqqtlaan
>d1afra_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrb_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrc_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrd_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afre_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afrf_ 1.26.1.2.6 delta 9-stearoyl-acyl carrier protein desaturase {Castor bean (Ricinus communis)}
mpprevhvqvthsmppqkieifksldnwaeenilvhlkpvekcwqpqdflpdpasdgfde
qvrelrerakeipddyfvvlvgdmiteealptyqtmlntldgvrdetgasptswaiwtra
wtaeenrhgdllnkylylsgrvdmrqiektiqyligsgmdprtenspylgfiytsfqera
tfishgntarqakehgdiklaqicgtiaadekrhetaytkiveklfeidpdgtvlafadm
mrkkismpahlmydgrddnlfdhfsavaqrlgvytakdyadileflvgrwkvdkltglsa
egqkaqdyvcrlpprirrleeraqgrakeaptmpfswifdrqvkl
>d1afsa_ 3.1.6.1.7 3-alpha-hydroxysteroid dehydrogenase {Rat (Rattus norvegicus), sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afsb_ 3.1.6.1.7 3-alpha-hydroxysteroid dehydrogenase {Rat (Rattus norvegicus), sprague-dawley strain}
mdsislrvalndgnfipvlgfgttvpekvakdevikatkiaidngfrhfdsaylyeveee
vgqairskiedgtvkredifytsklwstfhrpelvrtclektlkstqldyvdlyiihfpm
alqpgdiffprdehgkllfetvdicdtweamekckdaglaksigvsnfncrqlerilnkp
glkykpvcnqvechlylnqskmldyckskdiilvsyctlgssrdktwvdqkspvllddpv
lcaiakkykqtpalvalryqlqrgvvplirsfnakrikeltqvfefqlasedmkaldgln
rnfrynnakyfddhpnhpf
>d1afua_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afub_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1afva_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvb_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmysptsil
>d1afvh1 2.1.1.1.82 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvh2 2.1.1.2.86 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvk1 2.1.1.1.82 (1-120) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
qvqlqqpgsvlvrpgasvklsckasgytftsswihwakqrpgqglewigeihpnsgntny
nekfkgkatltvdtssstayvdlssltsedsavyycarwrygspyyfdywgqgttltvss
>d1afvk2 2.1.1.2.86 (121-220) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkkivpk
>d1afvl1 2.1.1.1.82 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvl2 2.1.1.2.86 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afvm1 2.1.1.1.82 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
divltqspaslavslgqratiscrasesvdnygisfmnwfqqkpgqppklliyaasnlgs
gvparfsgsgsgtdfslnihpmeeedtamyfcqqskevpltfgagtkvelkr
>d1afvm2 2.1.1.2.86 (113-217) Immunoglobulin (constant domains of L and H chains) {Fab 25.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1afwa1 3.85.1.1.1 (25-293) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwa2 3.85.1.1.1 (294-417) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1afwb1 3.85.1.1.1 (25-293) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
knsllekrpedvvivaanrsaigkgfkgafkdvntdyllynflnefigrfpeplradlnl
ieevacgnvlnvgagatehraaclasgipystpfvalnrqcssgltavndiankikvgqi
diglalgvesmtnnyknvnplgmisseelqknreakkclipmgitnenvaanfkisrkdq
defaansyqkaykakneglfedeilpiklpdgsicqsdegprpnvtaeslssirpafikd
rgtttagnasqvsdgvagvllarrsvanq
>d1afwb2 3.85.1.1.1 (294-417) Thiolase {Baker's yeast (Saccharomyces cerevisiae)}
lnlpvlgryidfqtvgvppeimgvgpayaipkvleatglqvqdidifeineafaaqalyc
ihklgidlnkvnprggaialghplgctgarqvatilrelkkdqigvvsmcigtgmgaaai
fike
>d1ag0a_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag0b_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aaecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgv
vtdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffdtfpghsa
lmkgtltlk
>d1ag1o_ 3.1.1.1.4 Triosephosphate isomerase {Trypanosoma brucei brucei}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag1t_ 3.1.1.1.4 Triosephosphate isomerase {Trypanosoma brucei brucei}
skpqpiaaanwkcngsqqslselidlfnstsinhdvqcvvastfvhlamtkerlshpkfv
iaaqnaiaksgaftgevslpilkdfgvnwivlghserrayygetneivadkvaaavasgf
mviacigetlqeresgrtavvvltqiaaiakklkkadwakvviayepvwaigtgkvatpq
qaqeahalirswvsskigadvagelrilyggsvngknartlyqqrdvngflvggaslkpe
fvdiikatq
>d1ag2__ 4.6.1.1.1 Prion protein domain {Mouse (Mus musculus)}
glggymlgsamsrpmihfgndwedryyrenmyrypnqvyyrpvdqysnqnnfvhdcvnit
ikqhtvttttkgenftetdvkmmervveqmcvtqyqkesqayy
>d1ag4__ 2.10.1.2.2 Spherulin 3a (S3a) {Slime mold (Physarum polycephalum)}
msvckgvsgnpakgevflykhvnfqgdswkvtgnvydfrsvsglndvvssvkvgpntkaf
ifkddrfngnfirleessqvtdlttrnlndaissiivatfesa
>d1ag6__ 2.5.1.1.5 Plastocyanin {Spinach (Spinacia oleracea)}
vevllggddgslaflpgdfsvasgeeivfknnagfphnvvfdedeipsgvdaakismsee
dllnapgetykvtltekgtykfycsphqgagmvgkvtvn
>d1ag7__ 7.3.6.1.2 Conotoxin {Synthetic (Conus geographus), GS}
acsgrgsrcxxqccmglrcgrgnpqkcigahxdv
>d1ag8a_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8b_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8c_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag8d_ 3.71.1.1.3 Aldehyde reductase (dehydrogenase), ALDH {Bovine (Bos taurus), mitochondrial}
vptpnqqpevlynqifinnewhdavskktfptvnpstgdvichvaegdkadvdravkaar
aafqlgspwrrmdasergrllnrladlierdrtylaaletldngkpyiisylvdldmvlk
clryyagwadkyhgktipidgdyfsytrhepvgvcgqiipwnfpllmqawklgpalatgn
vvvmkvaeqtpltalyvanlikeagfppgvvnvipgfgptagaaiashedvdkvaftgst
evghliqvaagksnlkrvtleiggkspniimsdadmdwaveqahfalffnqgqcccagsr
tfvqediyaefversvaraksrvvgnpfdsrteqgpqvdetqfkkvlgyiksgkeeglkl
lcgggaaadrgyfiqptvfgdlqdgmtiakeeifgpvmqilkfksmeevvgrannskygl
aaavftkdldkanylsqalqagtvwvncydvfgaqspfggyklsgsgrelgeyglqayte
vktvtvrvpqkns
>d1ag9a_ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d1ag9b_ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhldeilna
>d1agba1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agba2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agbb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agca1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agca2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agcb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agda1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agda2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agdb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agea1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agea2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1ageb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agfa1 2.1.1.2.8 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
adppkthvthhpisdheatlrcwalgfypaeitltwqrdgedqtqdtelvetrpagdrtf
qkwaavvvpsgeeqrytchvqheglpkpltlrwep
>d1agfa2 4.17.1.1.15 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-b0801}
gshsmryfdtamsrpgrgeprfisvgyvddtqfvrfdsdaaspreeprapwieqegpeyw
drntqifktntqtdreslrnlrgyynqseagshtlqsmygcdvgpdgrllrghnqyaydg
kdyialnedlrswtaadtaaqitqrkweaarvaeqdraylegtcvewlrrylengkdtle
r
>d1agfb1 2.1.1.2.8 Class I MHC, beta2-microglobulin and alpha-3 domain {Human HLA-b0801}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1agg__ 7.3.6.2.1 omega-Agatoxin IV, IVa, IVb {Funnel web spider (Agelenopsis aperta)}
ednciaedygkctwggtkccrgrpcrcsmigtncectprlimeglsfa
>d1agi__ 4.5.1.1.8 Angiogenin {Bovine (Bos taurus)}
aqddyryihfltqhydakpkgrndeycfnmmknrrltrpckdrntfihgnkndikaiced
rngqpyrgdlrisksefqitickhkggssrppcrygatedsrvivvgcenglpvhfdesf
itprh
>d1agja_ 2.41.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agjb_ 2.41.1.1.8 Epidermolytic (exfoliative) toxin A {Staphylococcus aureus}
evsaeeikkheekwnkyygvnafnlpkelfskvdekdrqkypyntignvfvkgqtsatgv
ligkntvltnrhiakfangdpskvsfrpsintddngntetpygeyevkeilqepfgagvd
lalirlkpdqngvslgdkispakigtsndlkdgdkleligypfdhkvnqmhrseielttl
srglryygftvpgnsgsgifnsngelvgihsskvshldrehqinygvgignyvkriinek
ne
>d1agm__ 1.98.1.1.1 Glucoamylase {Aspergillus awamori, variant x100}
atldswlsneatvartailnnigadgawvsgadsgivvaspstdnpdyfytwtrdsglvi
ktlvdlfrngdtdllstiehyissqaiiqgvsnpsgdlssgglgepkfnvdetaytgswg
rpqrdgpalratamigfgqwlldngytsaateivwplvrndlsyvaqywnqtgydlweev
ngssfftiavqhralvegsafatavgsscswcdsqapqilcylqsfwtgsyilanfdssr
sgkdtntllgsihtfdpeagcddstfqpcspralanhkevvdsfrsiytlndglsdseav
avgrypedsyyngnpwflctlaaaeqlydalyqwdkqgsleitdvsldffkalysgaatg
tyssssstyssivsavktfadgfvsivethaasngslseqfdksdgdelsardltwsyaa
lltannrrnsvvppswgetsassvpgtcaatsasgtyssvtvtswpsiva
>d1agna1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agna2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agnd1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
gtagkvikckaavlweqkqpfsieeievappktkevrikilatgicrtddhvikgtmvsk
fpvivgheatgivesigegvttvkpgdkviplflpqcrecnacrnpdgnlcirsditgrg
vladgttrftckgkpvhhfmntstfteytvvdessvakiddaappekvcligcXrddvpk
lvteflakkfdldqlithvlpfkkisegfellnsgqsirtvltf
>d1agnd2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygaavktgkvkpgstcvvfglggvglsvimgcksagasriigidlnkdkfekama
vgatecispkdstkpisevlsemtgnnvgytfevighletmidalaschmnygtsvvvgv
ppsakmltydpmllftgrtwkgcvfgglks
>d1agp__ 3.30.1.6.1 cH-p21 Ras protein {Human (Homo sapiens)}
mteyklvvvgadgvgksaltiqliqnhfvdeydptiedsyrkqvvidgetclldildtag
qeeysamrdqymrtgegflcvfainntksfedihqyreqikrvkdsddvpmvlvgnkcdl
aartvesrqaqdlarsygipyietsaktrqgvedafytlvreirqh
>d1agqa_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
nrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkv
gqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqb_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
knrgcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdk
vgqaccrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqc_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agqd_ 7.17.1.2.6 Glial cell-derived neurotrophic factor, GDNF {Rat (Rattus norvegicus)}
gcvltaihlnvtdlglgyetkeelifrycsgsceaaetmydkilknlsrsrrltsdkvgq
accrpvafdddlsflddslvyhilrkhsakrcgci
>d1agra1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agra2 3.30.1.6.13 (5-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
lsaedkaaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgi
vethftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmh
esmklfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiq
cqfedlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agrd1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1agrd2 3.30.1.6.13 (11-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
aaverskmidrnlredgekaarevkllllgagesgkstivkqmkiiheagXtgivethft
fkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmklf
dsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfedl
nkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>d1agre_ 1.88.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
vsqeevkkwaeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspk
akkiynefisvqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflk
srfyldlt
>d1agrh_ 1.88.1.1.1 Regulator of G-protein signalling 4, RGS4 {Rat (Rattus norvegicus)}
aeslenlinhecglaafkaflkseyseenidfwisceeykkikspsklspkakkiynefi
svqatkevnldsctreetsrnmleptitcfdeaqkkifnlmekdsyrrflksrfyl
>d1agsa1 1.48.1.1.9 (80-221) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsa2 3.38.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agsb1 1.48.1.1.9 (80-221) Glutathione S-transferase {Human (Homo sapiens), class alpha}
lyrkdikekalidmyiegiadlgemilllpftqpeeqdaklalikekiknryfpafekvl
kshgqdylvgnklsradihlvellyyveeldsslissfpllkalktrisnlptvkkflqp
gsprkppmdeksleearkifrf
>d1agsb2 3.38.1.5.9 (1-79) Glutathione S-transferase {Human (Homo sapiens), class alpha}
aekpklhyfnargrmestrwllaaagvefeekfiksaedldklrndgylmfqqvpmveid
gmklvqtrailnyiaskyn
>d1agt__ 7.3.7.2.9 Agitoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
gvpinvsctgspqcikpckdagmrfgkcmnrkchctpk
>d1agwa_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
elpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksdatek
dlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppgley
synpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkiadfg
lardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggspypg
vpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrivalts
>d1agwb_ 4.117.1.2.5 Fibroblast growth factor receptor 1 {Human (Homo sapiens)}
seyelpedprwelprdrlvlgkplgegafgqvvlaeaigldkdkpnrvtkvavkmlksda
tekdlsdlisememmkmigkhkniinllgactqdgplyviveyaskgnlreylqarrppg
leysynpshnpeeqlsskdlvscayqvargmeylaskkcihrdlaarnvlvtednvmkia
dfglardihhidyykkttngrlpvkwmapealfdriythqsdvwsfgvllweiftlggsp
ypgvpveelfkllkeghrmdkpsnctnelymmmrdcwhavpsqrptfkqlvedldrival
t
>d1agx__ 3.78.1.1.3 Glutaminase-asparaginase {Acinetobacter glutaminasificans}
knnvvivatggtiagagasstnsatysaakvpvdalikavpqvndlanitgiqalqvase
sitdkellslarqvndlvkkpsvngvvithgtdtmeetafflnlvvhtdkpivlvgsmrp
stalsadgplnlysavalassneaknkgvmvlmndsifaardvtkginihthafvsqwga
lgtlvegkpywfrssvkkhtnnsefniekiqgdalpgvqivygsdnmmpdayqafakagv
kaiihagtgngsmanylvpevrklhdeqglqivrssrvaqgfvlrnaeqpddkygwiaah
dlnpqkarllmalaltktndakeiqnmfwny
>d1agy__ 3.16.7.1.1 Cutinase {Fungus (Fusarium solani), subsp. Pisi}
rttrddlingnsascrdvifiyargstetgnlgtlgpsiasnlesafgkdgvwiqgvgga
yratlgdnalprgtssaairemlglfqqantkcpdatliaggysqgaalaaasiedldsa
irdkiagtvlfgytknlqnrgripnypadrtkvfcntgdlvctgslivaaphlaygpdar
gpapefliekvravrgs
>d1ah0__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
ashlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqe
klqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkd
pfpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpa
vnqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaaky
nkttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcal
mscashkdypfheey
>d1ah1__ 2.1.1.1.159 Immunoreceptor CTLA-4 (CD152), N-terminal fragment {Human (Homo sapiens)}
amhvaqpavvlassrgiasfvceyaspgkatevrvtvlrqadsqvtevcaatymmgnelt
flddsictgtssgnqvnltiqglramdtglyickvelmypppyylgigngtqiyvidpep
cpdsdqepk
>d1ah2__ 3.33.1.1.11 Serine protease PB92 {Bacillus alcalophylus}
aqsvpwgisrvqapaahnrgltgsgvkvavldtgisthpdlnirggasfvpgepstqdgn
ghgthvagtiaalnnsigvlgvapnaelyavkvlgasgsgsvssiaqglewagnngmhva
nlslgspspsatleqavnsatsrgvlvvaasgnsgagsisyparyanamavgatdqnnnr
asfsqygagldivapgvnvqstypgstyaslngtsmatphvagaaalvkqknpswsnvqi
rnhlkntatslgstnlygsglvnaeaatr
>d1ah3__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah4__ 3.1.6.1.5 Aldose reductase (aldehyde reductase) {Porcine (Sus scrofa)}
shlvlytgakmpilglgtwksppgkvteavkvaidlgyrhidcahvyqnenevglglqek
lqgqvvkredlfivsklwctdheknlvkgacqttlrdlkldyldlylihwptgfkpgkdp
fpldgdgnvvpdesdfvetweameelvdeglvkaigvsnfnhlqvekilnkpglkykpav
nqievhpyltqeklieyckskgivvtaysplgspdrpwakpedpslledprikaiaakyn
kttaqvlirfpmqrnlivipksvtperiaenfqvfdfelspedmntllsynrnwrvcalm
scashkdypfheey
>d1ah5_1 3.84.1.1.2 (3-219) Porphobilinogen deaminase (hydroxymethylbilane synthase), N-terminal domain {Escherichia coli}
dnvlriatrqsplalwqahyvkdklxashpglvvelvpxvtrgdvildtplakvggkglf
vkelevallenradiavhsxkdvpvefpqglglvticeredprdafvsnnydsldalpag
sivgtsslrrqcqlaerrpdliirslrgnvgtrlskldngeydaiilavaglkrlglesr
iraalppeislpavgqgavgiecrlddsrtrellaal
>d1ah5_2 4.41.2.1.1 (220-313) Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain {Escherichia coli}
nhhetalrvtaeraxntrleggcqvpigsyaelidgeiwlralvgapdgsqiirgerrga
pqdaeqxgislaeellnngareilaevyngdapa
>d1ah6__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1ah7__ 1.115.1.1.1 Bacterial phosholipase C {Bacillus cereus}
wsaedkhkegvnshlwivnraidimsrnttlvkqdrvaqlnewrtelengiyaadyenpy
ydnstfashfydpdngktyipfakqaketgakyfklagesyknkdmkqaffylglslhyl
gdvnqpmhaanftnlsypqgfhskyenfvdtikdnykvtdgngywnwkgtnpeewihgaa
vvakqdysgivndntkdwfvkaavsqeyadkwraevtpmtgkrlmdaqrvtagyiqlwfd
tygdr
>d1ah8a_ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeveke
>d1ah8b_ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkevekevpi
>d1ah9__ 2.35.4.5.4 Translational initiation factor 1, IF1 {Escherichia coli}
akedniemqgtvletlpntmfrvelenghvvtahisgkmrknyiriltgdkvtveltpyd
lskgrivfrsr
>d1aha__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahb__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahc__ 4.135.1.1.3 alpha-Momorcharin (momordin) {Bitter gourd (Momordica charantia)}
dvsfrlsgadprsygmfikdlrnalpfrekvyniplllpsvsgagryllmhlfnydgkti
tvavdvtnvyimgyladttsyffnepaaelasqyvfrdarrkitlpysgnyerlqiaagk
prekipiglpaldsaistllhydstaaagallvliqttaeaarfkyieqqiqerayrdev
pslatislenswsglskqiqlaqgnngifrtpivlvdnkgnrvqitnvtskvvtsniqll
lntrni
>d1ahdp_ 1.4.1.1.13 Antennapedia Homeodomain {Drosophila melanogaster}
mrkrgrqtytryqtlelekefhfnryltrrrrieiahalslterqikiwfqnrrmkwkke
nktkgepg
>d1ahea_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aheb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahfb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahga_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahgb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahha_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahhb_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqe
>d1ahia_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahib_ 3.2.1.2.9 7-alpha-hydroxysteroid dehydrogenase {Escherichia coli}
mfnsdnlrldgkcaiitgagagigkeiaitfatagasvvvsdinadaanhvvdeiqqlgg
qafacrcditseqelsaladfaisklgkvdilvnnaggggpkpfdmpmadfrrayelnvf
sffhlsqlvapemekngggviltitsmaaenkninmtsyasskaaashlvrnmafdlgek
nirvngiapgailtdalksvitpeieqkmlqhtpirrlgqpqdianaalflcspaaswvs
gqiltvsgggvqeln
>d1ahja_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjb_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjc_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjd_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahje_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjf_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahjg_ 4.121.1.1.1 Nitrile hydratase alpha chain {Rhodococcus sp. r312}
enaapaqaavsdrawalfraldgkglvpdgyvegwkktfeedfsprrgaelvarawtdpe
frqllltdgtaavaqygylgpqgeyivavedtptlknvivcslcsctawpilglpptwyk
sfeyrarvvreprkvlsemgteiasdieirvydttaetrymvlpqrpagtegwsqeqlqe
ivtkdcligvaipqvptv
>d1ahjh_ 2.30.6.1.1 Nitrile hydratase beta chain {Rhodococcus sp. r312}
mdgvhdlagvqgfgkvphtvdadigptfhaewehlpyslmfagvaelgafsvdevryvve
rmeprhymmtpyyeryvigvatlmvekgiltqdeleslaggpfplsrpsesegrpapvet
ttfevgqrvrvrdeyvpghirmpaycrgrvgtishrttekwpfpdaighgrndageepty
hvkfaaeelfgsdtdggsvvvdlfegylepaa
>d1ahk__ 2.1.1.5.25 Major mite allergen {House-dust mite (Dermatophagoides farinae), Der f 2}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahl__ 7.9.1.1.7 Anthopleurin-A {Giant green sea anemone (Anthopleura xanthogrammica)}
gvsclcdsdgpsvrgntlsgtlwlypsgcpsgwhnckahgptigwcckq
>d1ahm__ 2.1.1.5.25 Major mite allergen {House-dust mite (Dermatophagoides farinae), Der f 2}
dqvdvkdcanneikkvmvdgchgsdpciihrgkpftlealfdanqntktakieikasldg
leidvpgidtnachfvkcplvkgqqydikytwnvpkiapksenvvvtvkligdngvlaca
iathgkird
>d1ahn__ 3.16.4.1.4 Flavodoxin {Escherichia coli}
aitgiffgsdtgnteniakmiqkqlgkdvadvhdiaksskedleaydilllgiptwyyge
aqcdwddffptleeidfngklvalfgcgdqedyaeyfcdalgtirdiieprgativghwp
tagyhfeaskgladddhfvglaidedrqpeltaervekwvkqiseelhl
>d1aho__ 7.3.7.1.5 Scorpion toxin {Androctonus australius hector, Toxin II}
vkdgyivddvnctyfcgrnaycneectklkgesgycqwaspygnacycyklpdhvrtkgp
grch
>d1ahpa_ 3.77.1.2.3 Maltodextrin phosphorylase (MALP) {Escherichia coli}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahpb_ 3.77.1.2.3 Maltodextrin phosphorylase (MALP) {Escherichia coli}
sqpifndkqfqealsrqwqryglnsaaemtprqwwlavsealaemlraqpfakpvanqrh
vnyismefligrltgnnllnlgwyqdvqdslkaydinltdlleeeidpalgagglgrlaa
cfldsmatvgqsatgyglnyqyglfrqsfvdgkqveapddwhrsnypwfrhnealdvqvg
iggavtkdgrwepeftitgqawdlpvvgyrngvaqplrlwqathahpfdltkfndgdflr
aeqqginaekltkvlypndnhtagkklrlmqqyfqcacsvadilrrhhlagrelhelady
eviqlndthptiaipellrvlidehqmswddawaitsktfaytnhtlmpealerwdvklv
kgllprhmqiineintrfktlvektwpgdekvwaklavvhdkqvhmanlcvvggfavngv
aalhsdlvvkdlfpeyhqlwpnkfhnvtngitprrwikqcnpalaalldkslqkewandl
dqlinlvkladdakfrdlyrvikqankvrlaefvkvrtgidinpqaifdiqikrlheykr
qhlnllrilalykeirenpqadrvprvflfgakaapgyylakniifainkvadvinndpl
vgdklkvvflpdycvsaaeklipaadiseqistagkeasgtgnmklalngaltvgtldga
nveiaekvgeenififghtvkqvkailakgydpvkwrkkdkvldavlkelesgkysdgdk
hafdqmlhsigkqggdpylvmadfaayveaqkqvdvlyrdqeawtraailntarcgmfss
drsirdyqariwqaar
>d1ahq__ 4.85.1.2.2 Actophorin {Amoeba (Acanthamoeba castellanii)}
giavsddcvqkfnelklghqhryvtfkmnasntevvvehvggpnatyedfksqlperdcr
yaifdyefqvdggqrnkitfilwapdsapikskmmytstkdsikkklvgiqvevqatdaa
eisedavserakk
>d1ahr__ 1.42.1.5.10 Calmodulin {Chicken (Gallus gallus)}
adqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadgn
gtidfpefltmmarkmkdseeeireafrvfdkdgngfisaaelrhvmtnlgekltdeevd
emireadidgdgqvnyeefvtmmtsk
>d1ahsa_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsb_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>d1ahsc_ 2.17.1.1.2 Virus coat protein vp7 (BTV-10 vp7), central (top) domain {African horse sickness virus}
tgpyagavevqqsgryyvpqgrtrggyinsniaevcmdagaagqvnallaprrgdavmiy
fvwrplrifcdpqgaslesapgtfvtvdgvnvaagdvvawntiapvnvgnpgarrsilqf
evlwyt
>e1aht.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1aht.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyi
>d1ahua1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahua2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahub1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahub2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahva1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahva2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahvb1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahvb2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahwa1 2.1.1.1.99 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwa2 2.1.1.2.100 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwb1 2.1.1.1.99 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwb2 2.1.1.2.100 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1ahwc1 2.1.2.1.1 (4-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
tntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdei
vkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d1ahwc2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>d1ahwd1 2.1.1.1.99 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
dikmtqspssmyaslgervtitckasqdirkylnwyqqkpwkspktliyyatsladgvps
rfsgsgsgqdysltisslesddtatyyclqhgespytfgggtkleinr
>d1ahwd2 2.1.1.2.100 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1ahwe1 2.1.1.1.99 (1-117) Immunoglobulin (variable domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
eiqlqqsgaelvrpgalvklsckasgfnikdyymhwvkqrpeqglewiglidpengntiy
dpkfqgkasitadtssntaylqlssltsedtavyycardnsyyfdywgqgttltvss
>d1ahwe2 2.1.1.2.100 (118-214) Immunoglobulin (constant domains of L and H chains) {Fab 5G9 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpsstwpsetvtcnvahpasstkvdkki
>d1ahwf1 2.1.2.1.1 (4-106) Extracellular region of human tissue factor {Human (Homo sapiens)}
tntvaaynltwkstnfktilewepkpvnqvytvqistksgdwkskcfyttdtecdltdei
vkdvkqtylarvfsypagnvestgsageplyenspeftpylet
>d1ahwf2 2.1.2.1.1 (107-211) Extracellular region of human tissue factor {Human (Homo sapiens)}
nlgqptiqsfeqvgtkvnvtvedertlvrrnntflslrdvfgkdliytlyywkssssgkk
taktntneflidvdkgenycfsvqavipsrtvnrkstdspvecmg
>d1ahxa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahxb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahya_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahyb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgiglyydetgkipvltsvkkaeqyllene
ttklylgidgipefgrctqellfgkgsalindkrartaqtpggsgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanyssppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ahza1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahza2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>d1ahzb1 4.47.27.1.1 (274-560) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
rgyqsylitlpkdgdlkqavdiirplrlgmalqnvptirhilldaavlgdkrsyssrtep
lsdeeldkiakqlnlgrwnfygalygpepirrvlwetikdafsaipgvkfyfpedtpens
vlrvrdktmqgiptydelkwidwlpngahlffspiakvsgedammqyavtkkrcqeagld
figtftvgmremhhivcivfnkkdliqkrkvqwlmrtliddcaangwgeyrthlafmdqi
metynwnnssflrfnevlknavdpngiiapgksgvwpsqyshvtwkl
>d1ahzb2 4.118.1.1.1 (6-273) Vanillyl-alcohol oxidase {Fungus (Penicillium simplicissimum)}
efrpltlppklslsdfnefiqdiirivgsenvevisskdqivdgsymkpththdphhvmd
qdyflasaivaprnvadvqsivglankfsfplwpisigrnsgyggaaprvsgsvvldmgk
nmnrvlevnvegaycvvepgvtyhdlhnyleannlrdklwldvpdlgggsvlgnavergv
gytpygdhwmmhsgmevvlangellrtgmgalpdpkrpetmglkpedqpwskiahlfpyg
fgpyidglfsqsnmgivtkigiwlmpnp
>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
>d1ai1h1 2.1.1.1.31 (1-112) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
qvklqesgpavikpsqslsltcivsgfsitrtnycwhwirqapgkglewmgricyegsiy
yspsiksrstisrdtslnkffiqlisvtnedtamyycsrenhmyetyfdvwgqgttvtvs
>d1ai1h2 2.1.1.2.40 (113-226) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
sakttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqs
dlytlsssvtvpssprpsetvtcnvahpasstkvdkkivpr
>d1ai1l1 2.1.1.1.31 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
divmtqspaslvvslgqratiscrasesvdsygksfmhwyqqkpgqppkvliyiasnles
gvparfsgsgsrtdftltidpveaddaatyycqqnnedpptfgagtklemrr
>d1ai1l2 2.1.1.2.40 (109-211) Immunoglobulin (constant domains of L and H chains) {Fab 59.1 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ai2__ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>d1ai3__ 3.65.1.1.7 Isocitrate dehydrogenase, ICDH {Escherichia coli}
skvvvpaqgkkitlqngklnvpenpiipyiegdgigvdvtpamlkvvdaavekaykgerk
iswmeiytgekstqvygqdvwlpaetldlireyrvaikgplttpvgggirslnvalrqel
dlyiclrpvryyqgtpspvkhpeltdmvifrensediyagiewkadsadaekvikflree
mgvkkirfpehcgigikpcseegtkrlvraaieyaiandrdsvtlvhkgnimkftegafk
dwgyqlareefggelidggpwlkvknpntgkeivikdviadaflqqillrpaeydviacm
nlngdyisdalaaqvggigiapganigdecalfeathgtapkyagqdkvnpgsiilsaem
mlrhmgwteaadlivkgmegainaktvtydferlmdgakllkcsefgdaiienm
>e1ai4.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai4.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai5.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai5.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai6.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesny
>e1ai6.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai7.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ai7.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ai8.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1ai8.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>d1ai9a_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1ai9b_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aiaa_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiab_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aiba_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aibb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aica_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aicb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assyshnfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aida_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aidb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtiriggqlkealldtgaddtvleemnlpgkwkpkmiggiggfikvrqyd
qipveicghkaigtvlvgptpvniigrnlltqigctlnf
>d1aie__ 1.55.1.1.1 p53 tetramerization domain {Human (Homo sapiens)}
eyftlqirgrerfemfrelnealelkdaqag
>d1aifa1 2.1.1.1.66 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifa2 2.1.1.2.71 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aifb1 2.1.1.1.66 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifb2 2.1.1.2.71 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifh1 2.1.1.1.66 (1-121) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
evklqesggglvqpggsmklscvasgftfnnywmswvrqspekglewvaeirlnsdnfat
hyaesvkgkfiisrddsksrlylqmnslraedtgiyycvlrplfyyavdywgqgtsvtvs
s
>d1aifh2 2.1.1.2.71 (122-218) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpstwrpsetvtcnvahpasstkvdkki
>d1aifl1 2.1.1.1.66 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
diqltqspafmaaspgekvtitcsvsssisssnlhwyqqksetspkpwiygtsnlasgvp
vrfsgsgsgtsysltissmeaedaatyycqqwnsypytfgggtkleikr
>d1aifl2 2.1.1.2.71 (110-215) Immunoglobulin (constant domains of L and H chains) {Fab 409.5.3 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1aigh1 2.36.1.1.2 (36-258) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aigl1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aigm1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aign1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aigo1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aigp1 2.36.1.1.2 (36-258) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaamlae
>d1aigp2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aiha_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihb_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihc_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
elaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitftnt
kskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfash
fmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aihd_ 4.133.1.1.1 Integrase {Bacteriophage HP1}
etelaflyerdiyrllaecdnsrnpdlglivriclatgarwseaetltqsqvmpykitft
ntkskknrtvpisdelfdmlpkkrgrlfndayesfenavlraeielpkgqlthvlrhtfa
shfmmnggnilvlkeilghstiemtmryahfapshlesavkfnplsnpaq
>d1aii__ 1.66.1.1.2 Annexin III {Human (Homo sapiens)}
asiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkeyq
aaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttrt
srqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaqi
lykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedlll
aivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygyslys
aiksdtsgdyeitllkicggdd
>d1aijh1 2.36.1.1.2 (36-256) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijh2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1aijl1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aijm1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
aeyqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlsl
fsglmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasf
fmfvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygif
shldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiad
rgtaaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqn
h
>d1aijr1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
allsferkyrvpggtlvggnlfdfwvgpfyvgffgvatfffaalgiiliawsavlqgtwn
pqlisvyppaleyglggaplakgglwqiiticatgafvswalreveicrklgigyhipfa
fafailayltlvlfrpvmmgawgyafpygiwthldwvsntgytygnfhynpahmiaisff
ftnalalalhgalvlsaanpekgkemrtpdhedtffrdlvgysigtlgihrlglllslsa
vffsalcmiitgtiwfdqwvdwwqwwvklpwwanipgging
>d1aijs1 6.2.1.1.4 Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
yqnifsqvqvrgpadlgmtedvnlanrsgvgpfstllgwfgnaqlgpiylgslgvlslfs
glmwfftigiwfwyqagwnpavflrdlfffsleppapeyglsfaaplkegglwliasffm
fvavwswwgrtylraqalgmgkhtawaflsaiwlwmvlgfirpilmgswseavpygifsh
ldwtnnfslvhgnlfynpfhglsiaflygsallfamhgatilavsrfggereleqiadrg
taaeraalfwrwtmgfnatmegihrwaiwmavlvtltggigillsgtvvdnwyvwgqnh
>d1aijt1 2.36.1.1.2 (36-256) Photosynthetic reaction centre {Rhodobacter sphaeroides}
mregyplenedgtpaanqgpfplpkpktfilphgrgtltvpgpesedrpialartavseg
fphaptgdpmkdgvgpaswvarrdlpeldghghnkikpmkaaagfhvsagknpiglpvrg
cdleiagkvvdiwvdipeqmarflevelkdgstrllpmqmvkvqsnrvhvnalssdlfag
iptiksptevtlleedkicgyvagglmyaapkrksvvaaml
>d1aijt2 6.2.1.1.4 (11-35) Photosynthetic reaction centre, L-, M- and H-chains {Rhodobacter sphaeroides}
dlaslaiysfwiflagliyylqten
>d1ail__ 1.16.1.1.1 N-terminal, RNA-binding domain of nonstructural protein NS1 {Influenza virus A}
mdsntvssfqvdcflwhvrkqvvdqelgdapfldrlrrdqkslrgrgstlglnieaathv
gkqivekilk
>d1aim__ 4.3.1.1.9 Cruzain {Trypanosoma cruzi}
apaavdwrargavtavkdqgqcgscwafsaignvecqwflaghpltnlseqmlvscdktd
sgcsgglmnnafewivqenngavytedsypyasgegisppcttsghtvgatitghvelpq
deaqiaawlavngpvavavdasswmtytggvmtscvsealdhgvllvgyndsaavpywii
knswttqwgeegyiriakgsnqclvkeeassavvg
>d1ain__ 1.66.1.1.1 Annexin I {Human (Homo sapiens)}
gsavspyptfnpssdvaalhkaimvkgvdeatiidiltkrnnaqrqqikaaylqetgkpl
detlkkaltghleevvlallktpaqfdadelraamkglgtdedtlieilasrtnkeirdi
nrvyreelkrdlakditsdtsgdfrnallslakgdrsedfgvnedladsdaralyeager
rkgtdvnvfntilttrsypqlrrvfqkytkyskhdmnkvldlelkgdiekcltaivkcat
skpaffaeklhqamkgvgtrhkalirimvsrseidmndikafyqkmygislcqaildetk
gdyekilvalcggn
>d1aipa1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipa2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipa3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipb1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipb2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtk
>d1aipb3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipc_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipd_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aipe1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipe2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipe3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipf1 2.38.3.1.3 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus thermophilus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrrtvvtgvem
hrktlqegiagdnvgvllrgvsreevergqvlakpgsitp
>d1aipf2 2.39.1.1.3 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus thermophilus}
htkfeasvyvlkkeeggrhtgffsgyrpqfyfrttdvtgvvqlppgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1aipf3 3.30.1.6.16 (9-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus thermophilus}
kphvnvgtighvdhgkttltaaltyvtaaenpnvevkdygdidkapeerargitintahv
eyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehillarqvgv
pyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallaleqmhrnpkt
rrgenewvdkiwelldaideyipt
>d1aipg_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
sqmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiig
hyihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleke
rqiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakig
enivvrrfcrfelga
>d1aiph_ 4.36.1.1.2 Elongation factor Ts (EF-Ts), dimerisation domain {Thermus thermophilus}
qmelikklreatgagmmdvkraledagwdeekavqllrergamkaakkadrearegiigh
yihhnqrvgvlvelncetdfvarnelfqnlakdlamhiammnpryvsaeeipaeeleker
qiyiqaalnegkpqqiaekiaegrlkkyleevvlleqpfvkddkvkvkeliqqaiakige
nivvrrfcrfelga
>d1aiqa_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1aiqb_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>d1air__ 2.71.1.1.1 Pectate lyase {Erwinia chrysanthemi, type C}
atdtggyaataggnvtgavsktatsmqdivniidaarldangkkvkggayplvitytgne
dslinaaaanicgqwskdprgveikeftkgitiigangssanfgiwikkssdvvvqnmri
gylpggakdgdmirvddspnvwvdhnelfaanhecdgtpdndttfesavdikgasntvtv
synyihgvkkvgldgssssdtgrnityhhnyyndvnarlplqrgglvhaynnlytnitgs
glnvrqngqaliennwfekainpvtsrydgknfgtwvlkgnnitkpadfstysitwtadt
kpyvnadswtstgtfptvaynyspvsaqcvkdklpgyagvgknlatltstac
>d1aisa1 4.103.1.1.4 (1-92) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
mvdmskvklrienivasvdlfaqldlekvldlcpnskynpeefpgiichlddpkvallif
ssgklvvtgaksvqdieravaklaqklksigv
>d1aisa2 4.103.1.1.4 (93-181) TATA-box binding protein (TBP), C-terminal domain {Pyrococcus woesei}
kfkrapqidvqnmvfsgdigrefnldvvaltlpnceyepeqfpgviyrvkepksvillfs
sgkivcsgakseadaweavrkllreldky
>d1aisb1 1.73.1.2.2 (1108-1205) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
nlafalseldritaqlklprhveeeaarlyreavrkglirgrsiesvmaacvyaacrllk
vprtldeiadiarvdkkeigrsyrfiarnlnltpkklf
>d1aisb2 1.73.1.2.2 (1206-1300) Transcription factor IIB (TFIIB), core domain {Pyrococcus woesei}
vkptdyvnkfadelglsekvrrraieildeaykrgltsgkspaglvaaalyiasllegek
rtqrevaevarvtevtvrnrykelveklkikvpia
>d1aiu__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvn
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1aiv_1 3.84.1.2.6 (1-334) Ovotransferrin {Chicken (Gallus gallus)}
appksvirwctisspeekkcnnlrdltqqerisltcvqkatyldcikaianneadaisld
ggqafeaglapyklkpiaaevyehtegsttsyyavavvkkgteftvndlqgktschtglg
rsagwnipigtllhrgaiewegiesgsveqavakffsascvpgatieqklcrqckgdpkt
kcarnapysgysgafhclkdgkgdvafvkhttvnenapdqkdeyellcldgsrqpvdnyk
tcnwarvaahavvarddnkvediwsflskaqsdfgvdtksdfhlfgppgkkdpvlkdllf
kdsaimlkrvpslmdsqlylgfeyysaiqsmrkd
>d1aiv_2 3.84.1.2.6 (335-686) Ovotransferrin {Chicken (Gallus gallus)}
qltpsprenriqwcavgkdekskcdrwsvvsngdvectvvdetkdciikimkgeadaval
dgglvytagvcglvpvmaeryddesqcsktderpasyfavavarkdsnvnwnnlkgkksc
htavgrtagwvipmglihnrtgtcnfdeyfsegcapgsppnsrlcqlcqgsggippekcv
asshekyfgytgalrclvekgdvafiqhstveentggknkadwaknlqmddfellctdgr
ranvmdyrecnlaevpthavvvrpekankirdllerqekrfgvngsekskfmmfesqnkd
llfkdltkclfkvregttykeflgdkfytvisslktcnpsdilqmcsflegk
>d1aiw__ 2.63.1.1.1 Cellulose-binding domain of endoglucanase Z {Erwinia chrysanthemi}
mgdcananvypnwvskdwaggqpthneagqsivykgnlytanwytasvpgsdsswtqvgs
cn
>e1aix.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1aix.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>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
>d1aiza_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1aizb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1aj0__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1aj2__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1aj3__ 1.7.1.1.2 Spectrin {Chicken (Gallus gallus)}
hqffrdmddeeswikekkllvssedygrdltgvqnlrkkhkrleaelaahepaiqgvldt
gkklsddntigkeeiqqrlaqfvdhwkelkqlaaargq
>d1aj4__ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
adiykaaveqlteeqknefkaafdifvlgaedgsistkelgkvmrmlgqnptpeelqemi
devdedgsgtvdfdeflvmmvrsmkddskgkteeelsdlfrmfdknadgyidleelkiml
qatgetiteddieelmkdgdknndgridydeflefmkgve
>d1aj5a_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj5b_ 1.42.1.7.2 Calpain domain VI {Rat (Rattus norvegicus)}
eeerqfrklfvqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqgiykrfdtdrsgtigsnelpgafeaagfhlnqhiysmiir
rysdetgnmdfdnfisclvrldamfrafrsldkngtgqiqvniqewlqltmys
>d1aj6__ 4.96.1.2.1 DNA gyrase B {Escherichia coli}
vlkgldavrkrpgmyigdtddgtglhhmvfevvdnaidealaghckeiivtihadnsvsv
qddgrgiptgihpeegvsaaevimtvlhaggkfddnsykvsgglhgvgvsvvnalsqkle
lviqhegkihrqiyehgvpqaplavtgetektgtmvrfwpsletftnvtefeyeilakrl
relsflnsgvsirlrdkrdgkedhfh
>d1aj7h1 2.1.1.1.68 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
qvqlqqsgaelvkpgasvklsctasgfnikdtymhwvkqrpeqglewigridpangntky
dpkfqgkatitadtssntaylqlssltsedtavyycasyygiywgqgttltvssa
>d1aj7h2 2.1.1.2.73 (115-216) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
stkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aj7l1 2.1.1.1.68 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
diqmtqspsslsaslgervsltcrasqeisgylswlqqkpdgtikrliyaastldsgvpk
rfsgsrsgsdysltisslesedfadyyclqyasyprtfgggtkveikrt
>d1aj7l2 2.1.1.2.73 (110-214) Immunoglobulin (constant domains of L and H chains) {Fab 48G7 (mouse/human), kappa L chain}
vaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1aj8a_ 1.99.1.1.3 Citrate synthase {Pyrococcus furiosus}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielrr
>d1aj8b_ 1.99.1.1.3 Citrate synthase {Pyrococcus furiosus}
lakgledvyidqtnicyidgkegklyyrgysveelaelstfeevvyllwwgklpslsele
nfkkelaksrglpkevieimealpknthpmgalrtiisylgniddsgdipvtpeevyrig
isvtakiptivanwyrikngleyvppkeklshaanflymlhgeeppkewekamdvalily
aeheinastlavmtvgstlsdyysailagigalkgpihggaveeaikqfmeigspekvee
wffkalqqkrkimgaghrvyktydprarifkkyasklgdkklfeiaerlerlveeylskk
gisinvdywsglvfygmkipielyttifamgriagwtahlaeyvshnriirprlqyvgei
gkkylpielr
>d1aj9a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgssqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1aj9b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1ajaa_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajab_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajba_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajbb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajca_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajcb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajda_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1ajdb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqgatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1aje__ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
gskiisamqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytl
glfdtagqedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllv
gtqidlrddpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeai
laaleppepkksrr
>d1ajg__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1ajh__ 1.1.1.1.4 Myoglobin {Sperm whale (Physeter catodon)}
vlsegewqlvlhvwakveadvaghgqdilirlfkshpetlekfdrfkhlkteaemkased
lkkhgvtvltalgailkkkghheaelkplaqshatkhkipikylefiseaiihvlhsrhp
gdfgadaqgamnkalelfrkdiaakykelgyqg
>d1ajj__ 7.12.1.1.1 Ligand-binding domain of low-density lipoprotein receptor {Human (Homo sapiens)}
pcsafefhclsgecihsswrcdggpdckdksdeenca
>d1ajka_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajkb_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ntgivssfftytgpahgtqwdeidieflgkdttkvqfnyytngvgghekvislgfdaskg
fhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtgvddwlgsynganply
aeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctwrannvnftndgklkl
gltssaynkfdcaeyrstniygyglyevsmkpak
>d1ajm__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
kqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihellw
flqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlkn
dpdseriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfniasy
allvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesifd
yrfedfeiegydphpgikapvai
>e1ajn.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajn.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajoa_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
ghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwngtg
vddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnctw
rannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssffty
tgpahgtqwdeidieflgkdttkvqfnyytng
>d1ajob_ 2.26.1.2.3 Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
vgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgkimmnlwng
tgvddwlgsynganplyaeydwvkytsnqtggsffepfnsynsgtwekadgysnggvfnc
twrannvnftndgklklgltssaynkfdcaeyrstniygyglyevsmkpakntgivssff
tytgpahgtqwdeidieflgkdttkvqfnyytng
>e1ajp.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajp.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>e1ajq.1a 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
ssseikivrdeygmphiyandtwhlfygygyvvaqdrlfqmemarrstqgtvaevlgkdf
vkfdkdirrnywpdairaqiaalspedmsilqgyadgmnawidkvntnpetllpkqfntf
gftpkrwepfdvamifvgtmanrfsdstseidnlalltalkdkygvsqgmavfnqlkwlv
npsapttiavqesnyplkfnqqnsqt
>e1ajq.1b 4.124.1.2.1 Penicillin acylase, catalytic domain {Escherichia coli}
snmwvigkskaqdakaimvngpqfgwyapaytygiglhgagydvtgntpfaypglvfghn
gviswgstagfgddvdifaerlsaekpgyylhngkwvkmlsreetitvkngqaetftvwr
tvhgnilqtdqttqtayaksrawdgkevasllawthqmkaknwqqwtqqaakqaltinwy
yadvngnigyvhtgaypdrqsghdprlpvpgtgkwdwkgllpfemnpkvynpqsgyianw
nnspqkdypasdlfaflwggadrvteidrlleqkprltadqawdvirqtsrqdlnlrlfl
ptlqaatsgltqsdprrqlvetltrwdginllnddgktwqqpgsailnvwltsmlkrtvv
aavpmpfdkwysasgyettqdgptgslnisvgakilyeavqgdkspipqavdlfagkpqq
evvlaaledtwetlskrygnnvsnwktpamaltfrannffgvpqaaaeetrhqaeyqnrg
tendmivfspttsdrpvlawdvvapgqsgfiapdgtvdkhyedqlkmyenfgrkslwltk
qdveahkesqevlhvqr
>d1ajra_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajrb_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsa_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsknfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajsb_ 3.57.1.1.3 Aspartate aminotransferase, AAT {Pig (Sus scrofa), cytosolic form}
appsvfaevpqaqpvlvfkliadfredpdprkvnlgvgayrtddcqpwvlpvvrkveqri
annsslnheylpilglaefrtcasrlalgddspalqekrvggvqslggtgalrigaefla
rwyngtnnkdtpvyvssptwenhngvfttagfkdirsyrywdtekrgldlqgflsdlena
pefsifvlhacahnptgtdptpeqwkqiasvmkrrflfpffdsayqgfasgnlekdawai
ryfvsegfelfcaqsfsxnfglynervgnltvvakepdsilrvlsqmqkivrvtwsnppa
qgarivartlsdpelfhewtgnvktmadrilsmrselrarlealktpgtwnhitdqigmf
sftglnpkqveylinqkhiyllpsgrinmcglttknldyvatsiheavtkiq
>d1ajva_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajvb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajw__ 2.1.1.5.18 Rho GDP-dissociation inhibitor 1, RhoGDI {Bovine (Bos taurus)}
avsadpnvpnvvvtrltlvcstapgpleldltgdlesfkkqsfvlkegveyrikisfrvn
reivsgmkyiqhtyrkgvkidktdymvgsygpraeeyefltpmeeapkgmlargsyniks
rftdddrtdhlswewnltikkewkd
>d1ajxa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajxb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1ajya1 7.32.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajyb1 7.32.1.1.3 (30-66) PUT3 {Baker's yeast (Saccharomyces cerevisiae)}
msvaclscrkrhikcpggnpcqkcvtsnaiceyleps
>d1ajz__ 3.1.19.1.1 Dihydropteroate synthetase {Escherichia coli}
mklfaqgtsldlshphvmgilnvtpdsfsdggthnslidavkhanlminagatiidvgge
strpgaaevsveeelqrvipvveaiaqrfevwisvdtskpeviresakvgahiindirsl
sepgaleaaaetglpvclmhmqgnpktmqeapkyddvfaevnryfieqiarceqagiake
kllldpgfgfgknlshnysllarlaefhhfnlpllvgmsrksmigqllnvgpserlsgsl
acaviaamqgahiirvhdvketveamrvveatlsakenkrye
>d1ak0__ 1.115.1.2.1 P1 nuclease {Penicillium citrinum}
wgalghatvayvaqhyvspeaaswaqgilgsssssylasiaswadeyrltsagkwsaslh
fidaednpptncnvdyerdcgssgcsisaianytqrvsdsslssenhaealrflvhfigd
mtqplhdeayavggnkinvtfdgyhdnlhsdwdtympqkligghalsdaeswaktlvqni
esgnytaqaigwikgdnisepittatrwasdanalvctvvmphgaaalqtgdlyptyyds
vidtielqiakggyrlanwineih
>d1ak1__ 3.82.1.1.1 Ferrochelatase {Bacillus subtilis}
rkkmgllvmaygtpykeedieryythirrgrkpepemlqdlkdryeaiggisplaqiteq
qahnleqhlneiqdeitfkayiglkhiepfiedavaemhkdgiteavsivlaphfstfsv
qsynkrakeeaeklggltitsveswydepkfvtywvdrvketyasmpederenamlivsa
hslpekikefgdpypdqlhesakliaegagvseyavgwqsegntpdpwlgpdvqdltrdl
feqkgyqafvyvpvgfvadhlevlydndyeckvvtddigasyyrpempnakpefidalat
vvlkklgr
>d1ak2_1 3.30.1.1.10 (14-146,177-233) Adenylate kinase {Bovine (Bos taurus), mitochondrial izozyme-2}
pkgvravllgppgagkgtqapklaknfcvchlatgdmlramvasgselgkklkatmdagk
lvsdemvlelieknletppckngflldgfprtvrqaemlddlmekrkekldsviefsipd
sllirritgrlihXsddnkkalkirleayhtqttplveyyskrgihsaidasqtpdvvfa
silaafskats
>d1ak2_2 7.35.2.1.4 (147-176) Microbial and mitochondrial ADK, insert "zinc finger" domain {Bovine (Bos taurus), mitochondrial izozyme-2}
pqsgrsyheefnppkepmkdditgeplirr
>d1ak4a_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4b_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
nptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfmc
qggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktewl
dgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1ak4c_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak4d_ 1.72.1.1.1 HIV-1 capsid protein {Human immunodeficiency virus, type 1, HIV-1}
pivqnlqgqmvhqaisprtlnawvkvveekafspevipmfsalsegatpqdlntmlntvg
ghqaamqmlketineeaaewdrlhpvhagpiapgqmreprgsdiagttstlqeqigwmth
nppipvgeiykrwiilglnkivrmy
>d1ak5_1 3.1.6.2.1 (2-101,222-483) Inosine monophosphate dehydrogenase (IMPDH) {Tritrichomonas foetus}
akyynepchtfneyllipglstvdcipsnvnlstplvkfqkgqqseinlkiplvsaimqs
vsgekmaialareggisfifgsqsiesqaamvhavknfkaXhnelvdsqkrylvgagint
rdfrervpalveagadvlcidssdgfsewqkitigwirekygdkvkvgagnivdgegfry
ladagadfikigigggsicitreqkgigrgqatavidvvaernkyfeetgiyipvcsdgg
ivydyhmtlalamgadfimlgryfarfeesptrkvtingsvmkeywgegssrarnwqryd
lggkqklsfeegvdsyvpyagklkdnveaslnkvkstmcncgaltipqlqskakitlvss
vsi
>d1ak6__ 4.85.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak7__ 4.85.1.2.3 Destrin {Human (Homo sapiens)/pig (Sus scrofa)}
tmitpssgnsasgvqvadevcrifydmkvrkcstpeeikkrkkavifclsadkkciivee
gkeilvgdvgvtitdpfkhfvgmlpekdcryalydasfetkesrkeelmfflwapelapl
kskmiyasskdaikkkfqgikhecqangpedlnraciaeklggslivafegcpv
>d1ak8__ 1.42.1.5.8 Calmodulin {Bovine (Bos taurus)}
madqlteeqiaefkeafslfdkdgdgtittkelgtvmrslgqnpteaelqdminevdadg
ngtidfpefltmmark
>d1ak9__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsiqstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1akaa_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akab_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akba_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akca_ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyahnmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1akd__ 1.100.1.1.1 Cytochrome P450 {Pseudomonas putida}
nlaplpphvpehlvfdfdmynpsnlsagvqeawavlqesnvpdlvwtrcngghwiatrgq
lireayedyrhfssecpfipreageaydfiptsmdppeqrqfralanqvvgmpvvdklen
riqelacslieslrpqgqcnftedyaepfpirifmllaglpeediphlkyltdqmtrpdg
smtfaeakealydylipiieqrrqkpgtdaisivangqvngrpitsdeakrmcglllvgg
ldtvvnflsfsmeflakspehrqeliqrperipaaceellrrfslvadgriltsdyefhg
vqlkkgdqillpqmlsglderenacpmhvdfsrqkvshttfghgshlclgqhlarreiiv
tlkewltripdfsiapgaqiqhksgivsgvqalplvwdpattkav
>d1akea1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akea2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akeb1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1akeb2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1akha_ 1.4.1.1.2 Mating type protein A1 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
ispqarafleevfrrkqslnskekeevakkcgitplqvrvwfinkrmrs
>d1akhb_ 1.4.1.1.3 mat alpha2 Homeodomain {Baker's yeast (Saccharomyces cerevisiae)}
tkpyrghrftkenvrileswfaknienpyldtkglenlmkntslsriqiknwvsnrrrke
ktitiapeladllsgepl
>d1aki__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1akja1 2.1.1.2.4 (182-276) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwep
>d1akja2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1akjb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
qrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdws
fyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1akjd_ 2.1.1.1.3 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akje_ 2.1.1.1.3 CD8 {Human (Homo sapiens)}
sqfrvspldrtwnlgetvelkcqvllsnptsgcswlfqprgaaasptfllylsqnkpkaa
egldtqrfsgkrlgdtfvltlsdfrrenegyyfcsalsnsimyfshfvpvflpa
>d1akk__ 1.3.1.1.8 Mitochondrial cytochrome c {Horse (Equus caballus)}
gdvekgkkifvqkcaqchtvekggkhktgpnlhglfgrktgqapgftytdanknkgitwk
eetlmeylenpkkyipgtkmifagikkkteredliaylkkatne
>d1akl_1 2.70.1.1.1 (247-470) Metalloprotease, C-terminal domain {Pseudomonas aeruginosa, alkaline protease}
ganlttrtgdtvygfnsnterdfysatssssklvfsvwdaggndtldfsgfsqnqkinln
ekalsdvgglkgnvsiaagvtvenaiggsgsdlligndvanvlkggagndilygglgadq
lwggagadtfvygdiaessaaapdtlrdfvsgqdkidlsgldafvngglvlqyvdafagk
agqailsydaaskagslaidfsgdahadfainligqatqadivv
>d1akl_2 4.71.1.4.1 (1-246) Metallo protease, catalytic (N-terminal) domain {Pseudomonas aeruginosa, alkaline protease}
grsdaytqvdnflhayarggdelvnghpsytvdqaaeqilreqaswqkapgdsvltlsys
fltkpndffntpwkyvsdiyslgkfsafsaqqqaqaklslqswsdvtnihfvdagqgdqg
dltfgnfsssvggaafaflpdvpdalkgqswylinssysanvnpangnygrqtltheigh
tlglshpgdynagegdptyadatyaedtraysvmsyweeqntgqdfkgayssapllddia
aiqkly
>d1akma1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akma2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akmb1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akmb2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akmc1 3.66.1.1.4 (1-150) Ornithine transcarbamoylase {Escherichia coli}
sgfyhkhflklldftpaelnsllqlaaklkadkksgkeeakltgknialifekdstrtrc
sfevaaydqgarvtylgpsgsqighkesikdtarvlgrmydgiqyrgygqeivetlaeya
svpvwngltnefhptqlladlltmqehlpg
>d1akmc2 3.66.1.1.4 (151-333) Ornithine transcarbamoylase {Escherichia coli}
kafnemtlvyagdarnnmgnsmleaaaltgldlrlvapqacwpeaalvtecralaqqngg
nitltedvakgvegadfiytdvwvsmgeakekwaeriallreyqvnskmmqltgnpevkf
lhclpafhddqttlgkkmaeefglhggmevtdevfesaasivfdqaenrmhtikavmvat
lsk
>d1akn__ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptvtsagasll
ppednsq
>d1ako__ 4.122.1.1.1 DNA-repair enzyme exonuclease III {Escherichia coli}
mkfvsfninglrarphqleaivekhqpdviglqetkvhddmfpleevaklgynvfyhgqk
ghygvalltketpiavrrgfpgddeeaqrriimaeipsllgnvtvingyfpqgesrdhpi
kfpakaqfyqnlqnyletelkrdnpvlimgdmnisptdldigigeenrkrwlrtgkcsfl
peerewmdrlmswglvdtfrhanpqtadrfswfdyrskgfddnrglridlllasqplaec
cvetgidyeirsmekpsdhapvwatfrr
>d1akp__ 2.1.7.1.4 Kedarcidin (apo form) {Actimomycete strain L585-6}
asaavsvspatgladgatvtvsasgfatstsatalqcailadgrgacnvaefhdfslsgg
egttsvvvrrsftgyvmpdgpevgavdcdtapggceivvggntgeygnaaisfg
>d1akq__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akr__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwa
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>e1aks.1a 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntk
>e1aks.1b 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ssgssypsllqclkapvlsnssckssypgqitgnmicvgflqggkdscqgdsggpvvcng
qlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1akt__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwn
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1aku__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akv__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwg
ddsielqddfiplfdsleetgaqgrkvacfgcgassyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1akw__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwl
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1aky_1 3.30.1.1.11 (3-130,169-220) Adenylate kinase {Baker's yeast (Saccharomyces cerevisiae)}
esirmvligppgagkgtqapnlqerfhaahlatgdmlrsqiakgtqlgleakkimdqggl
vsddimvnmikdeltnnpackngfildgfprtipqaekldqmlkeqgtplekaielkvdd
ellvaritXnadalkkrlaayhaqtepivdfykktgiwagvdasqppatvwadilnklgk
n
>d1aky_2 7.35.2.1.5 (131-168) Microbial and mitochondrial ADK, insert "zinc finger" domain {Baker's yeast (Saccharomyces cerevisiae)}
grlihpasgrsyhkifnppkedmkddvtgealvqrsdd
>d1akz__ 3.14.1.1.1 Uracil-DNA glycosylase {Human (Homo sapiens)}
meffgeswkkhlsgefgkpyfiklmgfvaeerkhytvyppphqvftwtqmcdikdvkvvi
lgqdpyhgpnqahglcfsvqrpvppppsleniykelstdiedfvhpghgdlsgwakqgvl
llnavltvrahqanshkergweqftdavvswlnqnsnglvfllwgsyaqkkgsaidrkrh
hvlqtahpsplsvyrgffgcrhfsktnellqksgkkpidwkel
>d1al01_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltdaeenvrqklra
>d1al02_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
eqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldf
vgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftl
rvragntdvltda
>d1al03_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
teqsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtld
fvgyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaft
lrvragntdvltdaeenvrq
>d1al04_ 1.81.1.1.1 Scaffolding protein gpD of bacteriophage procapsid {Bacteriophage phi-x174}
qsvrfqtalasikliqasavldlteddfdfltsnkvwiatdrsrarrcveacvygtldfv
gyprfpapvefiaaviayyvhpvniqtaclimegaefteniingverpvkaaelfaftlr
vragntdvltdaeenvrqklraegvm
>d1al0f_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
qtgaermphdlshlgflagqigrlitisttpviagdsfemdavgalrlsplrrglaidst
vdiftfyvphrhvygeqwikfmkdgvnatplptvnttgyidhaaflgtinpdtnkipkhl
fqgylniynnyfkapwmpdrteanpnelnqddarygfrcchlkniwtaplppetelsrqm
ttsttsidimglqaayanlhtdqerdyfmqryrdvissfggktsydadnrpllvmrsnlw
asgydvdgtdqtslgqfsgrvqqtykhsvprffvpehgtmftlalvrfpptatkeiqyln
akgaltytdiagdpvlygnlppreismkdvfrsgdsskkfkiaegqwyryapsyvspayh
llegfpfiqeppsgdlqervlirhhdydqcfqsvqllqwnsqvkfnvtvyrnlpttrd
>d1al0g_ 2.9.1.1.1 Bacteriophage capsid proteins {Bacteriophage phiX174}
mfqtfisrhnsnffsdklvltsvtpassapvlqtpkatsstlyfdsltvnagnggflhci
qmdtsvnaanqvvsvgadiafdadpkffaclvrfesssvpttlptaydvyplngrhdggy
ytvkdcvtidvlprtpgnnvyvgfmvwsnftatkcrglvslnqvikeiiclqplk
>d1al21_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1al22_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1al23_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1al3__ 3.84.1.1.18 Cofactor-binding fragment of CysB {Klebsiella aerogenes}
twpdkgslyvatthtqaryalpgvikgfieryprvslhmhqgsptqiaeavskgnadfai
atealhlyddlvmlpcyhwnrsivvtpehplatkgsvsieelaqyplvtytfgftgrsel
dtafnragltprivftatdadviktyvrlglgvgviasmavdpvsdpdlvkldangifsh
sttkigfrrstflrsymydfiqrfaphltrdvvdtavalrsnedieamfkdiklpek
>d1al6__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1al7__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1al8__ 3.1.4.1.4 Glycolate oxidase {Spinach (Spinacia oleracea)}
meitnvneyeaiakqklpkmvydyyasgaedqwtlaenrnafsrilfrprilidvtnidm
tttilgfkismpimiaptamqkmahpegeyataraasaagtimtlsswatssveevastg
pgirffqlyvykdrnvvaqlvrraeragfkaialtvdtprlgrreadiknrfvlppfltl
knfegidlgkmdkandsglssyvagqidrslswkdvawlqtitslpilvkgvitaedarl
avqhgaagiivsnhgarqldyvpatimaleevvkaaqgripvfldggvrrgtdvfkalal
gaagvfigrpvvfslaaegeagvkkvlqmmrdefeltmalsgcrslkeisrshiaadwd
>d1ala__ 1.66.1.1.4 Annexin V {Chicken (Gallus gallus)}
kytrgtvtafspfdaradaealrkamkgmgtdeetilkiltsrnnaqrqeiasafktlfg
rdlvddlkseltgkfetlmvslmrparifdahalkhaikgagtnekvlteilasrtpaev
qnikqvymqeyeanledkitgetsghfqrllvvllqanrdpdgrveealvekdaqvlfra
gelkwgtdeetfitilgtrsvshlrrvfdkymtisgfqieetidretsgdleklllavvk
cirsvpayfaetlyysmkgagtdddtlirvmvsrseidlldirhefrknfakslyqmiqk
dtsgdyrkallllcgg
>d1alb__ 2.53.1.2.6 Adipocyte lipid-binding protein, ALBP {Mouse (Mus musculus)}
cdafvgtwklvssenfddymkevgvgfatrkvagmakpnmiisvngdlvtirsestfknt
eisfklgvefdeitaddrkvksiitldggalvqvqkwdgksttikrkrdgdklvvecvmk
gvtstrvyera
>d1alc__ 4.2.1.2.13 alpha-Lactalbumin {Baboon (Papio cynocephalus)}
kqftkcelsqnlydidgygrialpelictmfhtsgydtqaivendesteyglfqisnalw
ckssqspqsrnicditcdkflddditddimcakkildikgidywiahkalctekleqwlc
ek
>d1ald__ 3.1.9.1.3 Fructose-1,6-bisphosphate aldolase {Human (Homo sapiens)}
pyqypaltpeqkkelsdiahrivapgkgilaadestgsiakrlqsigtenteenrrfyrq
llltaddrvnpciggvilfhetlyqkaddgrpfpqvikskggvvgikvdkgvvplagtng
etttqgldglsercaqykkdgadfakwrcvlkigehtpsalaimenanvlaryasicqqn
givpivepeilpdgdhdlkrcqyvtekvlaavykalsdhhiylegtllkpnmvtpghact
qkfsheeiamatvtalrrtvppavtgitflsggqseeeasinlnainkcpllkpwaltfs
ygralqasalkawggkkenlkaaqeeyvkralanslacqgkytpsgqagaaaseslfvsn
hay
>d1alha_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtanhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alhb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaeargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtanhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alia_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alib_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1aljb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqentgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1alka_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgnitapggarrltgdqtaalrnslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsqkcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreeaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1alkb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgnitapggarrltgdqtaalrnslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsqkcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreeaeargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1alla_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
sivtksivnadaearylspgeldriksfvtsgerrvriaetmtgareriikqagdqlfgk
rpdvvspggnaygadmtatclrdldyylrlitygivagdvtpieeigvvgvremykslgt
pieaiaegvramksvatsllsgadaaeagsyfdyligams
>d1allb_ 1.1.1.2.3 Allophycocyanin {Spirulina platensis}
mqdaitsvinssdvqgkyldasaiqklkayfatgelrvraattisanaanivkeavaksl
lysdvtrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpigatvqaiqamkevtaglvgggagkemgiyfdyicsgls
>d1aln_1 3.87.1.1.1 (1-150) Cytidine deaminase {Escherichia coli}
mhprfqtafaqladnlqsalepiladkyfpalltgeqvsslksatgldedalafallpla
aacartplsnfnvgaiargvsgtwyfganmefigatmqqtvhaeqsaishawlsgekala
aitvnytpcghcrqfmnelnsgldlrihlp
>d1aln_2 3.87.1.1.1 (151-294) Cytidine deaminase {Escherichia coli}
greahalrdylpdafgpkdleiktllmdeqdhgyaltgdalsqaaiaaanrshmpysksp
sgvaleckdgrifsgsyaenaafnptlpplqgalillnlkgydypdiqravlaekadapl
iqwdatsatlkalgchsidrvlla
>d1alo_1 1.58.1.1.1 (81-193) Aldehyde oxidoreductase, domain 2 {Desulfovibrio gigas}
qpenlhplqkawvlhggaqcgfcspgfivsakglldtnadpsredvrdwfqkhrnacrct
gykplvdavmdaaavingkkpetdlefkmpadgriwgskyprptavakvtgtl
>d1alo_2 4.13.6.2.2 (1-80) Aldehyde oxidoreductase, N-terminal domain {Desulfovibrio gigas}
miqkvitvngieqnlfvdaeallsdvlrqqlgltgvkvgceqgqcgacsvildgkvvrac
vtkmkrvadgaqittiegvg
>d1alo_3 4.34.1.1.1 (194-310) Aldehyde oxidoreductase, domain 3 {Desulfovibrio gigas}
dygadlglkmpagtlhlamvqakvshanikgidtsealtmpgvhsvithkdvkgknritg
litfptnkgdgwdrpilcdekvfqygdcialvcadseanaraaaekvkvdleelpay
>d1alo_4 4.107.1.1.1 (311-907) Aldehyde oxidoreductase {Desulfovibrio gigas}
msgpaaaaedaieihpgtpnvyfeqpivkgedtgpifasadvtvegdfyvgrqphmpiep
dvafaymgddgkcyihsksigvhlhlymiapgvglepdqlvlvanpmggtfgykfsptse
alvavaamatgrpvhlrynyqqqqqytgkrspwemnvkfaakkdgtllamesdwlvdhgp
ysefgdlltlrgaqfigagynipnirglgrtvatnhvwgsafrgygapqsmfaseclmdm
laeklgmdplelryknayrpgdtnptgqepevfslpdmidqlrpkyqaalekaqkestat
hkkgvgisigvygsgldgpdaseawaelnadgtitvhtawedhgqgadigcvgtahealr
pmgvapekikftwpntattpnsgpsggsreqvmtgnairvacenllkacekpgggyytyd
elkaadkptkitgnwtasgathcdavtglgkpfvvymygvfmaevtvdvatgqttvdgmt
lmadlgslcnqlatdgqiygglaqgiglalsedfedikkhatlvgagfpfikqipdkldi
vyvnhprpdgpfgasgvgelpltsphaaiinaiksatgvriyrlpaypekvlealka
>d1alq__ 5.3.1.1.6 beta-Lactamase, class A {Staphylococcus aureus}
sepivlviftnkdnksdkpndklisetaksvmkefaagsknaakelndlekkynahigvy
aldtksgkevkfnsdkrfayastskainsailleqvpynklnkkvhinkddivayspile
kyvgkditlkalieasmtysdntannkiikeiggikkvkqrlkelgdkvtnpvryeieln
yyspkskkdtstpaafgktlnkliangklskenkkflldlmlnnksgdtlikdgvpkdyk
vadksgqaityasrndvafvypk
>d1alu__ 1.27.1.1.4 Interleukin-6 {Human (Homo sapiens)}
ltsseridkqiryildgisalrketcnksnmcesskealaennlnlpkmaekdgcfqsgf
neetclvkiitgllefevyleylqnrfesseeqaravqmstkvliqflqkkaknldaitt
pdpttnaslltklqaqnqwlqdmtthlilrsfkeflqsslralrqm
>d1alva_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alvb_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwa_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1alwb_ 1.42.1.7.3 Calpain domain VI {Pig (Sus scrofa)}
eevrqfrrlfaqlagddmevsatelmnilnkvvtrhpdlktdgfgidtcrsmvavmdsdt
tgklgfeefkylwnnikkwqaiykqfdvdrsgtigsselpgafeaagfhlnehlysmiir
rysdeggnmdfdnfisclvrldamfrafksldkdgtgqiqvniqewlqltmys
>d1aly__ 2.20.1.1.1 Extracellular domain of CD40 ligand {Human (Homo sapiens)}
gdqnpqiaahviseasskttsvlqwaekgyytmsnnlvtlengkqltvkrqglyyiyaqv
tfcsnreassqapfiaslclkspgrferillraanthssakpcgqqsihlggvfelqpga
svfvnvtdpsqvshgtgftsfgllkl
>d1am1__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1am2__ 2.76.1.2.2 GyrA intein {Mycobacterium xenopi}
asitgdalvalpegesvriadivpgarpnsdnaidlkvldrhgnpvladrlfhsgehpvy
avrtveglrvtgtanhpllclvdvagvptllwklideikpgdyaviqrsafsvdcagfar
gkpefapttytvgvpglvrfleahhrdpdakaiadeltdgrfyyakvasvtdagvqpvys
lrvdtadhafitngfvshn
>d1am4a_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4b_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4c_ 1.108.1.1.1 p50 RhoGAP domain {Human (Homo sapiens)}
prpplpnqqfgvslqhlqeknpeqepipivlretvaylqahalttegifrrsantqvvre
vqqkynmglpvdfdqynelhlpavilktflrelpeplltfdlyphvvgflnidesqrvpa
tlqvlqtlpeenyqvlrfltaflvqisahsdqnkmtntnlavvfgpnllwakdaaitlka
inpintftkflldhqgelf
>d1am4d_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4e_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am4f_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
pqtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvmiggepytlglfdtag
qedydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlr
ddpstieklaknkqkpitpetaeklardlkavkyvecsaltqrglknvfdeailaal
>d1am5__ 2.44.1.2.12 Pepsin(ogen) {Atlantic cod (Gadus morhua)}
rvteqmkneadteyygvisigtppesfkvifdtgssnlwvssshcsaqacsnhnkfkprq
sstyvetgktvdltygtggmrgilgqdtvsvgggsdpnqelgesqtepgpfqaaapfdgi
lglaypsiaaagavpvfdnmgsqslvekdlfsfylsgggangsevmlggvdnshytgsih
wipvtaekywqvaldgitvngqtaacegcqaivdtgtskivapvsalanimkdigasenq
gemmgncasvqslpditftingvkqplppsayiegdqafctsglgssgvpsntselwifg
dvflrnyytiydrtnnkvgfapaa
>d1am6__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1am7a_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am7b_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am7c_ 4.2.1.4.1 Lambda lysozyme {Bacteriophage lambda}
mveinnqrkafldmlaxsegtdngrqktrnhgydvivggelftdysdhprklvtlnpklk
stgagryqllsrxxdayrkqlglkdfspksqdavalqqikergalpmidrgdirqaidrc
snixaslpgagygqfehkadsliakfkeaggtvr
>d1am9a_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslk
>d1am9b_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
srgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnqk
lkqenlslrtavhks
>d1am9c_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhkskslkdl
>d1am9d_ 1.41.1.1.6 SREBP-1a {Human (Homo sapiens)}
qsrgekrtahnaiekryrssindkiielkdlvvgteaklnksavlrkaidyirflqhsnq
klkqenlslrtavhks
>d1ama__ 3.57.1.1.1 Aspartate aminotransferase, AAT {Chicken (Gallus gallus), mitochondria}
sswwshvemgppdpilgvteafkrdtnskkmnlgvgayrddngkpyvlncvrkaeamiaa
kkmdkeylpiagladftrasaelalgenseafksgryvtvqgisgtgslrvganflqrff
kfsrdvylpkpswgnhtpifrdaglqlqayryydpktcsldftgamediskipeksiill
hacahnptgvdprqeqwkelasvvkkrnllayfdmayqgfasgdinrdawalrhfieqgi
dvvlsqsyaknmglygeragaftvicrdaeeakrvesqlkilirpmysnppmngariasl
ilntpelrkewlvevkgmadriismrtqlvsnlkkegsshnwqhitdqigmfcftglkpe
qverltkefsiymtkdgrisvagvassnvgylahaihqvtk
>d1ame__ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1amf__ 3.84.1.1.16 Molybdate-binding protein, ModA {Escherichia coli}
gkitvfaaasltnamqdiatqfkkekgvdvvssfassstlarqieagapadlfisadqkw
mdyavdkkaidtatrqtllgnslvvvapkasvqkdftidsktnwtsllnggrlavgdpeh
vpagiyakealqklgawdtlspklapaedvrgalalverneaplgivygsdavaskgvkv
vatfpedshkkveypvavveghnnatvkafydylkgpqaaeifkrygftik
>d1amha_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1amhb_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggksscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ami_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1ami_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amj_1 3.7.2.1.2 (529-754) Aconitase, C-terminal domain {Bovine (Bos taurus)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainsenrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehsa
leprflggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kpltciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1amj_2 3.72.1.1.2 (2-528) Aconitase, first 3 domains {Bovine (Bos taurus)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dsgchydqlieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1amk__ 3.1.1.1.7 Triosephosphate isomerase {Leishmania mexicana}
sakpqpiaaanwkcngttasieklvqvfnehtishdvqcvvaptfvhiplvqaklrnpky
visaenaiaksgaftgevsmpilkdigvhwvilghserrtyygetdeivaqkvseackqg
fmviacigetlqqreanqtakvvlsqtsaiaakltkdawnqvvlayepvwaigtgkvatp
eqaqevhlllrkwvsenigtdvaaklrilyggsvnaanaatlyakpdingflvggaslkp
efrdiidatr
>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
>d1amn__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
eskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllna
>d1amoa1 2.38.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amoa2 3.16.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amoa3 3.18.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amob1 2.38.1.4.1 (243-518) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rqyelvvhedmdvakvytgemgrlksyenqkppfdaknpflaavtanrklnqgterhlmh
leldisdskiryesgdhvavypandsalvnqigeilgadldvimslnnldeesnkkhpfp
cpttyrtaltyylditnpprtnvlyelaqyasepseqehlhkmasssgegkelylswvve
arrhilailqdypslrppidhlcellprlqaryysiassskvhpnsvhicavaveyeaks
grvnkgvatswlrakepagenggralvpmfvrksqf
>d1amob2 3.16.4.2.1 (64-235) NADPH-cytochrome p450 reductase, N-terminal domain {Rat (Rattus norvegicus)}
vkessfvekmkktgrniivfygsqtgtaeefanrlskdahrygmrgmsadpeeydladls
slpeidkslvvfcmatygegdptdnaqdfydwlqetdvdltgvkfavfglgnktyehfna
mgkyvdqrleqlgaqrifelglgdddgnleedfitwreqfwpavceffgvea
>d1amob3 3.18.1.3.1 (519-678) NADPH-cytochrome p450 reductase {Rat (Rattus norvegicus)}
rlpfksttpvimvgpgtgiapfmgfiqerawlreqgkevgetllyygcrrsdedylyree
larfhkdgaltqlnvafsreqahkvyvqhllkrdrehlwkliheggahiyvcgdarnmak
dvqntfydivaefgpmehtqavdyvkklmtkgrysldvws
>d1amp__ 3.47.4.4.1 Aminopeptidase {Aeromonas proteolytica}
mppitqqatvtawlpqvdasqitgtisslesftnrfytttsgaqasdwiasewqalsasl
pnasvkqvshsgynqksvvmtitgseapdewivigghldstigshtneqsvapgadddas
giaavtevirvlsennfqpkrsiafmayaaeevglrgsqdlanqyksegknvvsalqldm
tnykgsaqdvvfitdytdsnftqyltqlmdeylpsltygfdtcgyacsdhaswhnagypa
ampfeskfndynprihttqdtlansdptgshakkftqlglayaiemgsatg
>d1amq__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1amr__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ams__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1amua_ 5.19.1.1.2 Phenylalanine activating domain of gramicidin synthetase 1 {Bacillus brevis}
gtheeeqylfavnntkaeyprdktihqlfeeqvskrpnnvaivceneqltyhelnvkanq
larifiekgigkdtlvgimmeksidlfigilavlkaggayvpidieypkeriqyilddsq
armlltqkhlvhlihniqfngqveifeedtikiregtnlhvpskstdlayviytsgttgn
pkgtmlehkgisnlkvffenslnvtekdrigqfasisfdasvwemfmalltgaslyiilk
dtindfvkfeqyinqkeitvitlpptyvvhldperilsiqtlitagsatspslvnkwkek
vtyinaygptetticattwvatketighsvpigapiqntqiyivdenlqlksvgeagelc
iggeglargywkrpeltsqkfvdnpfvpgeklyktgdqarwlsdgnieylgridnqvkir
ghrveleevesillkhmyisetavsvhkdhqeqpylcayfvsekhipleqlrqfsseelp
tymipsyfiqldkmpltsngkidrkqlpepdltf
>d1amub_ 5.19.1.1.2 Phenylalanine activating domain of gramicidin synthetase 1 {Bacillus brevis}
gtheeeqylfavnntkaeyprdktihqlfeeqvskrpnnvaivceneqltyhelnvkanq
larifiekgigkdtlvgimmeksidlfigilavlkaggayvpidieypkeriqyilddsq
armlltqkhlvhlihniqfngqveifeedtikiregtnlhvpskstdlayviytsgttgn
pkgtmlehkgisnlkvffenslnvtekdrigqfasisfdasvwemfmalltgaslyiilk
dtindfvkfeqyinqkeitvitlpptyvvhldperilsiqtlitagsatspslvnkwkek
vtyinaygptetticattwvatketighsvpigapiqntqiyivdenlqlksvgeagelc
iggeglargywkrpeltsqkfvdnpfvpgeklyktgdqarwlsdgnieylgridnqvkir
ghrveleevesillkhmyisetavsvhkdhqeqpylcayfvsekhipleqlrqfsseelp
tymipsyfiqldkmpltsngkidrkqlpepdltf
>d1amw__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
asetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletepd
lfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqfg
vgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkddq
leyleekrikevikrhsefvaypiqlvvtkeve
>d1amx__ 2.2.3.1.1 Collagen-binding domain of adhesin {Staphylococcus aureus}
tssvfyyktgdmlpedtthvrwflninneksyvskditikdqiqggqqldlstlninvtg
thsnyysgqsaitdfekafpgskitvdntkntidvtipqgygsynsfsinyktkitneqq
kefvnnsqawyqehgkeevngksfnhtvhn
>d1amy_1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1amy_2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1amz__ 1.99.1.1.1 Citrate synthase {Chicken (Gallus gallus)}
stnlkdvlaslipkeqariktfrqqhgntavgqitvdmsyggmrgmkgliyetsvldpde
girfrgfsipecqkllpkagggeeplpeglfwllvtgqiptpeqvswvskewakraalps
hvvtmldnfptnlhpmsqlsaaitalnsesnfarayaeginrtkywefvyedamdliakl
pcvaakiyrnlyragssigaidskldwshnftnmlgytdpqftelmrlyltihsdheggn
vsahtshlvgsalsdpylsfaaamnglagplhglanqevllwlsqlqkdlgadasdeklr
dyiwntlnsgrvvpgyghavlrktdprytcqrefalkhlpsdpmfklvaqlykivpnvll
eqgkaknpwpnvdahsgvllqyygmtemnyytvlfgvsralgvlaqliwsralgfplerp
ksmstagleklsagg
>d1an0a_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
qtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvxiggepytlglfdtagq
edydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlrd
dpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaaleppe
pkksrrcv
>d1an0b_ 3.30.1.6.11 CDC42 {Human (Homo sapiens)}
qtikcvvvgdgavgktcllisyttnkfpseyvptvfdnyavtvxiggepytlglfdtagq
edydrlrplsypqtdvflvcfsvvspssfenvkekwvpeithhcpktpfllvgtqidlrd
dpstieklaknkqkpitpetaeklardlkavkyvecsaltqkglknvfdeailaaleppe
pkksrrcv
>d1an1e_ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlxsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1an1i_ 7.15.1.1.10 Leech derived tryptase inhibitor (LDTI-C) {Medicinal leech (Hirudo medicinalis)}
kvcacpkilkpvcgsdgrtyansciarcngvsiksegscp
>d1an2a_ 1.41.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an2c_ 1.41.1.1.2 Max protein {Mouse (Mus musculus)}
adkrahhnalerkrrdhikdsfhslrdsvpslqgekasraqildkateyiqymrrknhth
qqdiddlkrqnalleqqvralekars
>d1an4a_ 1.41.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an4b_ 1.41.1.1.4 Usf B/HLH domain {Human (Homo sapiens)}
mdekrraqhneverrrrdkinnwivqlskiipdssmestksgqskggilskasdyiqelr
qsnhr
>d1an5a_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an5b_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1an7a_ 4.113.1.1.2 Ribosomal protein S8 {Thermus thermophilus}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an7b_ 4.113.1.1.2 Ribosomal protein S8 {Thermus thermophilus}
tdpiadmltrirnatrvykestdvpasrfkeeilrilaregfikgyervdvdgkpylrvy
lkygprrqgpdprpeqvihhirriskpgrrvyvgvkeiprvrrglgiailstskgvltdr
earklgvggelicevw
>d1an8_1 2.35.2.2.6 (3-95) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
kkdisnvksdllyaytitpydykdcrvnfstthtlnidtqkyrgkdyyissemsyeasqk
fkrddhvdvfglfyilnshtgeyiyggitpaqn
>d1an8_2 4.13.7.1.6 (96-208) Streptococcal superantigen Spe-C {Streptococcus pyogenes}
nkvnhkllgnlfisgesqqnlnnkiilekdivtfqeidfkirkylmdnykiydatspyvs
grieigtkdgkheqidlfdspnegtrsdifakykdnriinmknfshfdiylek
>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
>d1an9a2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1an9b1 3.4.1.2.1 (1-194,288-340) D-amino acid oxidase, N-terminal domain {Pig (Sus scrofa)}
mrvvvigagviglstalciheryhsvlqpldvkvyadrftpftttdvaaglwqpytseps
npqeanwnqqtfnyllshigspnaanmgltpvsgynlfreavpdpywkdmvlgfrkltpr
eldmfpdyrygwfntslilegrkylqwlterltergvkfflrkvesfeevarggadviin
ctgvwagvlqpdplXqvrlereqlrfgssntevihnyghggygltihwgcalevaklfgk
vleernll
>d1an9b2 4.14.1.3.1 (195-287) D-amino acid oxidase {Pig (Sus scrofa)}
lqpgrgqiikvdapwlknfiithdlergiynspyiipglqavtlggtfqvgnwneinniq
dhntiwegccrleptlkdakivgeytgfrpvrp
>d1anb__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivewgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anc__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivkwgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1and__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdhktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1ane__ 2.41.1.2.3 Trypsin(ogen) {Rat (Rattus rattus)}
ivggytcqensvpyqvslnsgyhfcggslindqwvvsaahcyksriqvrlgehninvleg
neqfvnaakiikhpnfdrktlnndimliklsspvklnarvatvalpsscapagtqclisg
wgntlssgvnepdllqcldapllpqadceasypgkitdnmvcvgfleggkdscqgdsggp
vvcngelqgivswgygcalpdnpgvytkvcnyvdwiqdtiaan
>d1anf__ 3.84.1.1.6 D-maltodextrin-binding protein, MBP {Escherichia coli}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdea
lkdaqtritk
>d1ang__ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1ania_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqhatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anib_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqhatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anjb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
mpvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseitaarn
yaegaggffkgidalpltgqythyalnkktgkpdyvtdsaasatawstgvktyngalgvd
ihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpgnal
ekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsdaasl
nsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptlaqmt
dkaiellsknekgfflqvegasidhqdhaanpcgqigetvdldeavqralefakkegntl
vivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlriaayg
phaanvvgltdqtdlfytmkaalglk
>d1anka1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1anka2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ankb1 3.30.1.1.12 (1-121,157-214) Adenylate kinase {Escherichia coli}
mriillgapgagkgtqaqfimekygipqistgdmlraavksgselgkqakdimdagklvt
delvialvkeriaqedcrngflldgfprtipqadamkeaginvdyvlefdvpdelivdri
vXkddqeetvrkrlveyhqmtapligyyskeaeagntkyakvdgtkpvaevradlekilg
>d1ankb2 7.35.2.1.2 (122-156) Microbial and mitochondrial ADK, insert "zinc finger" domain {Escherichia coli}
grrvhapsgrvyhvkfnppkvegkddvtgeelttr
>d1ann__ 1.66.1.1.3 Annexin IV {Bovine (Bos taurus)}
ggtvkaasgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdl
mddlkselsgnfeqvilgmmtptvlydvqelrkamkgagtdegclieilasrtpeeirri
nqtyqlqygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagek
kwgtdevkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmr
nksayfaerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdts
gdyrkvllilcggdd
>d1ans__ 7.11.1.1.1 Neurotoxin III (ATX III) {Sea anemone (Anemonia sulcata)}
rsccpcywggcpwgqncypegcsgpkv
>d1anti_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
rdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladsknd
ndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyr
kankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsn
ktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmm
yqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldele
emmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkaf
levneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1antl_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
dipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyqhladskndn
dniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffaklncrlyrk
ankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsraainkwvsnk
tegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadgescsasmmy
qegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevlqewldelee
mmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyvsdafhkafl
evneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmgrvanpcvk
>d1anu__ 2.2.2.2.3 Cohesin-2 domain of cellulosome {Clostridium thermocellum}
vvveigkvtgsvgttveipvyfrgvpskgiancdfvfrydpnvleiigidpgdiivdpnp
tksfdtaiypdrkiivflfaedsgtgayaitkdgvfakiratvkssapgyitfdevggfa
dndlveqkvsfidggvnv
>d1anv_1 1.56.1.1.1 (179-265) Domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
sawekgmeaaralmdkyhvdndlkanfkllpdqvealaavcktwlneehrglqltftsnk
tfvtmmgrflqaylqsfaevtykhhep
>d1anv_2 7.43.1.1.1 (266-385) First Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
tgcalwlhrcaeiegelkclhgsiminkehviemdvtsengqralkeqsskakivknrwg
rnvvqisntdarccvhdaacpanqfsgkscgmffsegakaqvafkqikafmqalypnaqt
>d1anv_3 7.43.1.1.2 (386-529) Second Zn-domain of early E2A DNA-binding protein, ADDBP {Adenovirus type 5}
ghghllmplrcecnskpghapflgrqlpkltpfalsnaedldadlisdksvlasvhhpal
ivfqccnpvyrnsraqgggpncdfkisapdllnalvmvrslwsenftelprmvvpefkws
tkhqyrnvslpvahsdarqnpfdf
>d1anwa_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anwb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
aqvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlf
grdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpee
lraikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfq
agelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavv
ksirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmik
gdtsgdykkallllcgedd
>d1anxa_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1anxc_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcge
>d1ao0a1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0a2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0b1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0b2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0c1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0c2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao0d1 3.51.1.1.4 (235-459) Glutamine PRPP amidotransferase, C-terminal domain {Bacillus subtilis}
icsmeyiyfsrpdsnidginvhsarknlgkmlaqesaveadvvtgvpdssisaaigyaea
tgipyelgliknryvgrtfiqpsqalreqgvrmklsavrgvvegkrvvmvddsivrgtts
rrivtmlreagatevhvkissppiahpcfygidtstheeliasshsveeirqeigadtls
flsvegllkgigrkyddsncgqclacftgkypteiyqdtvlphvk
>d1ao0d2 4.124.1.1.2 (1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs
>d1ao3a_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao3b_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
csqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpw
nvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsv
dsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgn
sflhklc
>d1ao5a_ 2.41.1.2.32 Kallikrein-13 {Mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao5b_ 2.41.1.2.32 Kallikrein-13 {Mouse (Mus musculus)}
vvggfnceknsqpwqvavyyqkehicggvlldrnwvltaahcyvdqyevwlgknklfqee
psaqhrlvsksfphpgfnmsllmlqtippgadfsddlmllrlskpaditdvvkpialptk
epkpgskclasgwgsitptrwqkpddlqcvfitllpnencakvylqkvtdvmlcagemgg
gkdtcrddsggplicdgilqgttsygpvpcgkpgvpaiytnlikfnswikdtmmkna
>d1ao6a1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6a2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6a3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1ao6b1 1.116.1.1.1 (5-196) Serum albumin {Human (Homo sapiens)}
sevahrfkdlgeenfkalvliafaqylqqcpfedhvklvnevtefaktcvadesaencdk
slhtlfgdklctvatlretygemadccakqepernecflqhkddnpnlprlvrpevdvmc
tafhdneetflkkylyeiarrhpyfyapellffakrykaafteccqaadkaacllpklde
lrdegkassakq
>d1ao6b2 1.116.1.1.1 (197-388) Serum albumin {Human (Homo sapiens)}
rlkcaslqkfgerafkawavarlsqrfpkaefaevsklvtdltkvhtecchgdllecadd
radlakyicenqdsissklkeccekpllekshciaevendempadlpslaadfveskdvc
knyaeakdvflgmflyeyarrhpdysvvlllrlaktyettlekccaaadphecyakvfde
fkplveepqnli
>d1ao6b3 1.116.1.1.1 (389-582) Serum albumin {Human (Homo sapiens)}
kqncelfeqlgeykfqnallvrytkkvpqvstptlvevsrnlgkvgskcckhpeakrmpc
aedylsvvlnqlcvlhektpvsdrvtkccteslvnrrpcfsalevdetyvpkefnaetft
fhadictlsekerqikkqtalvelvkhkpkatkeqlkavmddfaafvekcckaddketcf
aeegkklvaasqaa
>d1ao7a1 2.1.1.2.4 (182-274) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrw
>d1ao7a2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1ao7b1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllycteftptekdeyacrvnhvtlsqpcivkwdrdm
>d1ao7d_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
keveqnsgplsvpegaiaslnctysdrgsqsffwyrqysgkspelimsiysngdkedgrf
taqlnkasqyvsllirdsqpsdsatylcavttdswgklqfgagtqvvvtpdiqnp
>d1ao7e1 2.1.1.1.157 (3-118) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcasrpglaggrpeqyfgpgtrltvted
>d1ao7e2 2.1.1.2.146 (119-246) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
lknvfppevavfepseaeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpqp
lkeqpalndsryalssrlrvsatfwqnprnhfrcqvqfyglsendewtqdrakpvtqivs
aeawgrad
>d1ao8__ 3.61.1.1.2 Dihydrofolate reductase, prokaryotic type {Lactobacillus casei}
taflwaqdrdgligkdghlpwhlpddlhyfraqtvgkimvvgrrtyesfpkrplpertnv
vlthqedyqaqgavvvhdvaavfayakqhpdqelviaggaqiftafkddvdtllvtrlag
sfegdtkmiplnwddftkvssrtvedtnpalthtyevwqkka
>d1aoa_1 1.43.1.1.2 (121-251) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
yseeekyafvnwinkalendpdcrhvipmnpntddlfkavgdgivlckminlsvpdtide
rainkkkltpfiiqenlnlalnsasaigchvvnigaedlragkphlvlgllwqiikiglf
adielsrneal
>d1aoa_2 1.43.1.1.2 (260-375) N-terminal actin-crosslinking domain from fimbrin {Human (Homo sapiens)}
tleelmklspeelllrwanfhlensgwqkinnfsadikdskayfhllnqiapkgqkegep
ridinmsgfnetddlkraesmlqqadklgcrqfvtpadvvsgnpklnlafvanlfn
>d1aob__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1aoca_ 7.17.1.5.1 Coagulogen {Japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aocb_ 7.17.1.5.1 Coagulogen {Japanese horseshoe crab (Tachypleus tridentatus)}
adtnapiclcdepgvlgrtqivtteikdkiekaveavaqesgvsgrgfsifshhpvfrec
gkyecrtvrpehsrcynfppfthfksecpvstrdcepvfgytvagefrvivqapragfrq
cvwqhkcrfgsnscgyngrctqqrsvvrlvtynlekdgflcesfrtccgcpcrsf
>d1aod__ 3.1.16.2.2 Phosphatidylinositol-specific phospholipase C {Listeria monocytogenes}
vttkqwmsalpdttnlaalsipgthdtmsyngditwtltkplaqtqtmslyqqleagiry
idirakdnlniyhgpiflnaslsgvletitqflkknpketiimrlkdeqnsndsfdyriq
pliniykdyfyttprtdtsnkiptlkdvrgkilllsenhtkkplvinsrkfgmqfgapnq
viqddyngpsvktkfkeivqtayqaskadnklflnhisatsltftprqyaaalnnkveqf
vlnltsekvrglgilimdfpekqtikniiknnkf
>d1aoea_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aoeb_ 3.61.1.1.7 Dihydrofolate reductases, eukaryotic type {Yeast (Candida albicans)}
mlkpnvaiivaalkpalgigykgkmpwrlrkeiryfkdvttrttkpntrnavimgrktwe
sipqkfrplpdrlniilsrsyeneiiddniihassiesslnlvsdvervfiiggaeiyne
linnslvshlliteiehpspesiemdtflkfpleswtkqpkselqkfvgdtvleddikeg
dftynytlwtrk
>d1aofa1 1.3.1.2.1 (36-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdltrdlgfdylq
sfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aofa2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aofb1 1.3.1.2.1 (26-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
epsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkgatgkaltpdl
trdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aofb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoga1 3.3.1.5.4 (3-169,287-357) Trypanothione reductase {Trypanosoma cruzi}
skifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkk
lmvtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegle
fflgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlq
nagvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aoga2 3.3.1.5.4 (170-286) Trypanothione reductase {Trypanosoma cruzi}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aoga3 4.67.1.1.4 (358-487) Trypanothione reductase {Trypanosoma cruzi}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aogb1 3.3.1.5.4 (5-169,287-357) Trypanothione reductase {Trypanosoma cruzi}
ifdlvvigagsggleaawnaatlykkrvavidvqmvhgppffsalggtcvnvgcvpkklm
vtgaqymehlresagfgwefdrttlraewknliavkdeavlninksydemfrdtegleff
lgwgslesknvvnvresadpasavkerletehillasgswphmpnXgrsprtkdlqlqna
gvmiknggvqvdeysrtnvsniyaigdvtnrvmltpvaineaaalvdtvfgttprkt
>d1aogb2 3.3.1.5.4 (170-286) Trypanothione reductase {Trypanosoma cruzi}
ipgiehcissneafylpepprrvltvgggfisvefagifnaykpkdgqvtlcyrgemilr
gfdhtlreeltkqltangiqiltkenpakvelnadgsksvtfesgkkmdfdlvmmai
>d1aogb3 4.67.1.1.4 (358-487) Trypanothione reductase {Trypanosoma cruzi}
dhtrvasavfsippigtcglieevaskryevvavylssftplmhkvsgskyktfvakiit
nhsdgtvlgvhllgdnapeiiqgigiclklnakisdfyntigvhptsaeelcsmrtpsyy
yvkgekmekp
>d1aoha_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
avrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgelivdpn
ptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvikfvev
ggfanndlveqktqffdggvnvg
>d1aohb_ 2.2.2.2.4 Cohesin domain from scaffolding protein CipA {Clostridium thermocellum}
tdldavrikvdtvnakpgdtvripvrfsgipskgiancdfvysydpnvleiieiepgeli
vdpnptksfdtavypdrkmivflfaedsgtgayaitedgvfativakvksgapnglsvik
fvevggfanndlveqktqffdggvnvg
>d1aoia_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
phryrpgtvalreirryqkstellirklpfqrlvreiaqdfktdlrfqssavmalqease
aylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoib_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
kvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtytehakrk
tvtamdvvyalkrqgrtlygfgg
>d1aoic_ 1.23.1.1.2 Histone H2A {African clawed frog (Xenopus laevis)}
gkqggktrakaktrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeil
elagnaardnkktriiprhlqlavrndeelnkllgrvtiaqggvlpniqsvllpk
>d1aoid_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1aoie_ 1.23.1.1.6 Histone H3 {African clawed frog (Xenopus laevis)}
latkaarksapatggvkkphryrpgtvalreirryqkstellirklpfqrlvreiaqdfk
tdlrfqssavmalqeaseaylvalfedtnlcaihakrvtimpkdiqlarrirgera
>d1aoif_ 1.23.1.1.8 Histone H4 {African clawed frog (Xenopus laevis)}
krhrkvlrdniqgitkpairrlarrggvkrisgliyeetrgvlkvflenvirdavtyteh
akrktvtamdvvyalkrqgrtlygfgg
>d1aoig_ 1.23.1.1.2 Histone H2A {African clawed frog (Xenopus laevis)}
akaktrssraglqfpvgrvhrllrkgnyaervgagapvylaavleyltaeilelagnaar
dnkktriiprhlqlavrndeelnkllgrvtiaqggvlpniqsvllpkk
>d1aoih_ 1.23.1.1.4 Histone H2B {African clawed frog (Xenopus laevis)}
kkrrktrkesyaiyvykvlkqvhpdtgisskamsimnsfvndvferiageasrlahynkr
stitsreiqtavrlllpgelakhavsegtkavtkytsak
>d1aoja_ 2.30.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aojb_ 2.30.2.1.24 EPS8 SH3 domain {Mouse (Mus musculus)}
kkyakskydfvarnsselsvmkddvleilddrrqwwkvrnasgdsgfvpnnildimrtpe
>d1aoka_ 1.123.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfgdmilqktgkeavhsyaiygcycgwggqgraqdatdrccfaqdccygrvndcnpk
tatytysrengdivcgdddlclravcecdraaaiclgenvntydknyeyysishcteese
qc
>d1aokb_ 1.123.1.2.10 Snake phospholipase A2 {Sand viper (Vipera ammodytes), vipoxin}
nlfqfakmingklgafsvwnyisygcycgwggqgtpkdatdrccfvhdccygrvrgcnpk
laiyyysfkkgnivcgknngclrdicecdrvaancfhqnkntynanykflsssrcrqtge
kc
>d1aol__ 2.18.1.1.1 F-MuLV receptor-binding domain {Friend murine leukemia virus, F-MuLV}
qvynitwevtngdretvwaisgnhplwtwwpvltpdlcmlalsgpphwgleyqapysspp
gppccsgssgssagcsrdcdepltsltprcntawnrlkldqvthkssegfyvcpgshrpr
eakscggpdsfycaswgcettgrvywkpssswdyitvdnnlttsqavqvckdnkwcnpla
iqftnagkqvtswttghywglrlyvsgrdpgltfgirlryqnlgprvp
>d1aoma1 2.61.2.1.1 (129-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ldpaappefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstye
iktvldtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsiets
kmegwedkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashy
rpefivnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvv
idtkegklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdna
wkildsfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefk
tlpiaewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikde
rlvtptgkfnvyntmtdty
>d1aomb1 1.3.1.2.1 (9-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaa
>d1aomb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aona1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aona2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aona3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonb1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonb2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonb3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonc1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonc2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonc3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aond1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aond2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aond3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aone1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aone2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aone3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonf1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonf2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonf3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aong1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aong2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aong3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonh1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonh2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonh3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aoni1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aoni2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aoni3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonj1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonj2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonj3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonk1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonk2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonk3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonl1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonl2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonl3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonm1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonm2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonm3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aonn1 1.119.1.1.1 (2-136,410-525) GroEL {Escherichia coli}
aakdvkfgndarvkmlrgvnvladavkvtlgpkgrnvvldksfgaptitkdgvsvareie
ledkfenmgaqmvkevaskandaagdgtttatvlaqaiiteglkavaagmnpmdlkrgid
kavtaaveelkalsvXgvvagggvalirvaskladlrgqnedqnvgikvalrameaplrq
ivlncgeepsvvantvkggdgnygynaateeygnmidmgildptkvtrsalqyaasvagl
mittecmvtdlp
>d1aonn2 3.7.5.1.1 (191-366) GroEL {Escherichia coli}
egmqfdrgylspyfinkpetgavelespfilladkkisniremlpvleavakagkpllii
aedvegealatlvvntmrgivkvaavkapgfgdrrkamlqdiatltggtviseeigmele
katledlgqakrvvinkdtttiidgvgeeaaiqgrvaqirqqieeatsdydreklq
>d1aonn3 4.46.1.1.1 (137-190,367-409) GroEL {Escherichia coli}
pcsdskaiaqvgtisansdetvgkliaeamdkvgkegvitvedgtglqdeldvvXervak
laggvavikvgaatevemkekkarvedalhatraavee
>d1aono_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonp_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonq_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonr_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aons_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aont_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aonu_ 2.31.1.1.1 Chaperonin-10 (GroES) {Escherichia coli}
mnirplhdrvivkrkevetksaggivltgsaaakstrgevlavgngrilengevkpldvk
vgdivifndgygvksekidneevlimsesdilaivea
>d1aoo__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aop_1 4.47.29.1.1 (81-145) Sulfite reductase, domains 1 and 3 {Escherichia coli}
llrcrlpggvittkqwqaidkfagentiygsirltnrqtfqfhgilkknvkpvhqmlhsv
gldal
>d1aop_2 4.47.29.1.1 (346-425) Sulfite reductase, domains 1 and 3 {Escherichia coli}
igwvkgiddnwhltlfiengrildyparplktglleiakihkgdfritanqnliiagvpe
sekakiekiakesglmnavt
>d1aop_3 4.108.1.1.1 (149-345) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
ndmnrnvlctsnpyesqlhaeayewakkisehllprtrayaeiwldqekvattdeepilg
qtylprkfkttvvippqndidlhandmnfvaiaengklvgfnllvggglsiehgnkktya
rtasefgylplehtlavaeavvttqrdwgnrtdrknaktkytlervgvetfkaeverrag
ikfepirpyeftgrgdr
>d1aop_4 4.108.1.1.1 (426-570) Sulfite reductase hemoprotein (SiRHP), domains 2 and 4 {Escherichia coli}
pqrensmacvsfptcplamaeaerflpsfidnidnlmakhgvsdehivmrvtgcpngcgr
amlaevglvgkapgrynlhlggnrigtriprmykenitepeilasldeligrwakereag
egfgdftvragiirpvldpardlwd
>d1aoqa1 1.3.1.2.1 (17-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
hktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagchgvlrkga
tgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyllldpaa
>d1aoqa2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aoqb1 1.3.1.2.1 (9-133) N-terminal (heme c) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
dpaaaledhktrtdnryepsldnlaqqdvaapgapegvtalsdaqyneankiyfercagc
hgvlrkgatgkaltpdltrdlgfdylqsfityaspagmpnwgtsgelsaeqvdlmanyll
ldpaa
>d1aoqb2 2.61.2.1.1 (134-567) C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase {Thiosphaera pantotropha}
ppefgmkemreswkvhvapedrptqqmndwdlenlfsvtlrdagqialidgstyeiktvl
dtgyavhisrlsasgrylfvigrdgkvnmidlwmkepttvaeikigsearsietskmegw
edkyaiagaywppqyvimdgetlepkkiqstrgmtydeqeyhpeprvaailashyrpefi
vnvketgkillvdytdlnnlktteisaerflhdggldgshryfitaanarnklvvidtke
gklvaiedtggqtphpgrganfvhptfgpvwatshmgddsvaligtdpeghpdnawkild
sfpalgggslfikthpnsqylyvdatlnpeaeisgsvavfdikamtgdgsdpefktlpia
ewagitegqprvvqgefnkdgtevwfsvwngkdqesalvvvddktlelkhvikderlvtp
tgkfnvyntmtdty
>d1aora1 1.104.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aora2 4.123.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aorb1 1.104.1.1.1 (211-605) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
iadkqkfmlvvrekvnklrndpvaggglpkygtavlvniinenglypvknfqtgvypyay
eqsgeamaakylvrnkpcyacpigcgrvnrlptvgetegpeyesvwalganlgindlasi
ieanhmcdelgldtistggtlatamelyekghikdeelgdappfrwgntevlhyyiekia
kregfgdklaegsyrlaesyghpelsmtvkklelpaydprgaeghglgyatnnrggchik
nymispeilgypykmdphdvsddkikmlilfqdltalidsaglclfttfglgaddyrdll
naalgwdfttedylkigeriwnaerlfnlkagldparddtlpkrfleepmpegpnkghtv
rlkemlpryyklrgwtedgkipkekleelgiaefy
>d1aorb2 4.123.1.1.1 (1-210) Aldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygnwgrfirvnlstgdikveeydeelakkwlgsrglaiylllkemdptvdplspenkli
iaagpltgtsaptggrynvvtkspltgfitmansggyfgaelkfagydaivvegkaekpv
yiyikdehieirdashiwgkkvseteatirkevgsekvkiasigpagenlvkfaaimndg
hraagrggvgavmgsknlkaiavegsktvp
>d1aosa_ 1.117.1.1.4 Argininosuccinate lyase/delta-crystallin {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aosb_ 1.117.1.1.4 Argininosuccinate lyase/delta-crystallin {Human (Homo sapiens)}
imekfnasiaydrhlwevdvqgskaysrglekaglltkaemdqilhgldkvaeewaqgtf
klnsndedihtanerrlkeligatagklhtgrsrndqvvtdlrlwmrqtcstlsgllwel
irtmvdraeaerdvlfpgythlqraqpirwshwilshavaltrdserllevrkrinvlpl
gsgaiagnplgvdrellraelnfgaitlnsmdatserdfvaeflfwrslcmthlsrmaed
lilyctkefsfvqlsdaystgsslmpqkknpdslelirskagrvfgrcagllmtlkglps
tynkdlqedkeavfevsdtmsavlqvatgvistlqihqenmgqalspdmlatdlayylvr
kgmpfrqaheasgkavfmaetkgvalnqlslqelqtisplfsgdvicvwdyrhsveqyga
lggtarssvdwqirqvrallqaq
>d1aotf_ 4.72.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aouf_ 4.72.1.1.5 Tyrosine kinase Fyn {Human (Homo sapiens)}
siqaeewyfgklgrkdaerqllsfgnprgtfliresettkgayslsirdwddmkgdhvkh
ykirkldnggyyittraqfetlqqlvqhyseraaglssrlvvpshk
>d1aov_1 3.84.1.2.5 (1-334) Ovotransferrin {Duck (Anas platyrhynchos)}
appkttvrwctissaeekkcnslkdhmqqervtlscvqkatyldcikaisnneadaisld
ggqvfeaglapyklkpiaaevyersggsttsyyavavvkkgtdfmikdlrgktschtglg
rsagwnipigtlihrediewegiesgiseqavakffsascvpgatieqklcrqckgdakt
kclrngpysgysgafqclkdgkgdvafvkhttvqenapeekdeyellcldgsrqpvdsyk
tcnwarvaahavvarddskiddiwsflgmqayslgvdttsdfhlfgppgkkdpvlkdllf
kdsaimlkrvpelmdsqlylgfeyysaiqslrkd
>d1aov_2 3.84.1.2.5 (335-686) Ovotransferrin {Duck (Anas platyrhynchos)}
qltvgprenkiqwcavgkdekskcdrwsvvsngevectilddnkdcivkitkgeadaisl
dggfvytagvcglvpvvgesyedetqcskdeeqpayyfavavvkkssaitwnnlqgkksc
htavgrtagwnipmglihnktgscdfddyfsegcapgsppnsrlcklcqgsgenllekcv
asshekyygytgalrclveqgdvafikhstvgenvsgsnkddwakgltrddfellctngk
raktmdyktchlakvpthavvarpekankirellegqeklfglhgtekerfmmfqsqtkd
llfkaltkclvklrqgitykeflgdeyyasvaslntcnpsdllqvctfledk
>d1aow__ 1.66.1.1.3 Annexin IV {Bovine (Bos taurus)}
asgfnaaedaqtlrkamkglgtdedaiinvlayrstaqrqeirtaykttigrdlmddlks
elsgnfeqvilgmmtptvlydvqevrkamkgagtdegclieilasrtpeeirrinqtyql
qygrsleddirsdtsfmfqrvlvslsaggrdesnylddalmrqdaqdlyeagekkwgtde
vkfltvlcsrnrnhllhvfdeykriaqkdieqsiksetsgsfedallaivkcmrnksayf
aerlyksmkglgtdddtlirvmvsraeidmldiranfkrlygkslysfikgdtsgdyrkv
llilcggdd
>d1aoxa_ 3.52.1.1.5 Integrin alpha2-beta1 {Human (Homo sapiens)}
scpslidvvvvcdesnsiypwdavknflekfvqgldigptktqvgliqyannprvvfnln
tyktkeemivatsqtsqyggdltntfgaiqyarkyaysaasggrrsatkvmvvvtdgesh
dgsmlkavidqcnhdnilrfgiavlgylnrnaldtknlikeikaiasipteryffnvsde
aallekagtlgeqifsieggt
>d1aoxb_ 3.52.1.1.5 Integrin alpha2-beta1 {Human (Homo sapiens)}
rsscpslidvvvvcdesnsiypwdavknflekfvqgldigptktqvgliqyannprvvfn
lntyktkeemivatsqtsqyggdltntfgaiqyarkyaysaasggrrsatkvmvvvtdge
shdgsmlkavidqcnhdnilrfgiavlgylnrnaldtknlikeikaiasipteryffnvs
deaallekagtlgeqifsieg
>d1aoy__ 1.4.3.3.1 Arginine repressor (ArgR), N-terminal DNA-binding domain {Escherichia coli}
mrssakqeelvkafkallkeekfssqgeivaalqeqgfdninqskvsrmltkfgavrtrn
akmemvyclpaelgvptt
>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
>d1aozb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aozb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aozb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1ap0__ 4.8.2.2.1 Modifier protein 1 (HP1 beta) {Mouse (Mus musculus)}
hmveevleeeeeeyvvekvldrrvvkgkveyllkwkgfsdedntwepeenldcpdliaef
lqsqktahetdks
>d1ap2a_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklep
>d1ap2b_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
>d1ap2c_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
divmtqspssltvtagekvtmsckssqsllnsgnqknyltwyqqkpgqppklliywastr
esgvpdrftgsgsgtdftltissvqaedlavyycqndysypltfgagtklepg
>d1ap2d_ 2.1.1.1.91 Immunoglobulin (variable domains of L and H chains) {scFv c219}
evqlqqsgaelvrpgasvklsctasgfnikddfmhwvkqrpeqglewigridpandntky
apkfqdkatiiadtssntaylqlssltsedtavyycarrevysyyspldvwgagttvtvp
sgs
>d1ap4__ 1.42.1.5.4 Troponin C {Human (Homo sapiens), cardiac isoform}
mddiykaaveqlteeqknefkaafdifvlgaedgcistkelgkvmrmlgqnptpeelqem
idevdedgsgtvdfdeflvmmvrcmkdds
>d1ap5a1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5a2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap5b1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap5b2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6a1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6a2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap6b1 1.2.7.1.6 (1-83) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
khslpdlpydygalephinaqimqlhhskhhaafvnnlnvteekyqealakgdvtaqial
qpalkfnggghinhsifwtnlsp
>d1ap6b2 4.37.1.1.3 (84-198) Mn superoxide dismutase (MnSOD) {Human (Homo sapiens)}
ngggepkgelleaikrdfgsfdkfkekltaasvgvqgsgwgwlgfnkerghlqiaacpnq
dplqgttglipllgidvwehayylqyknvrpdylkaiwnvinwenvterymackk
>d1ap7__ 1.110.2.1.6 Cell cycle inhibitor p16ink4A {Mouse (Mus musculus)}
gsmlleevcvgdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgspaval
ellkqgaspnvqdasgtspvhdaartgfldtlkvlvehgadvnaldstgslpihlaireg
hssvvsflapesdlhhrdasgltplelarqrgaqnlmdilqghmmipm
>d1ap8__ 4.66.1.1.1 Translation initiation factor eIF4e {Baker's yeast (Saccharomyces cerevisiae)}
msveevskkfeenvsvddttatpktvlsdsahfdvkhplntkwtlwytkpavdkseswsd
llrpvtsfqtveefwaiiqnipephelplksdyhvfrndvrpewedeanakggkwsfqlr
gkgadidelwlrtllavigetideddsqingvvlsirkggnkfalwtksedkepllrigg
kfkqvlkltddghleffphssangrhpqpsitl
>d1ap9__ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
rpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsmllgygl
tmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigtglvga
ltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvlwsayp
vvwligsegagivplnietllfmvldvsakvgfglillr
>d1apa__ 4.135.1.1.6 Pokeweed antiviral protein alpha {Pokeweed (Phytolacca americana)}
intitfdvgnatinkyatfmksihnqakdptlkcygipmlpntnltpkyllvtlqdsslk
titlmlkrnnlyvmgyadtyngkcryhifkdisntterndvmttlcpnpssrvgkninyd
ssypalekkvgrprsqvqlgiqilnsgigkiygvdsftekteaefllvaiqmvseaarfk
yienqvktnfnrafypnakvlnleeswgkistaihnakngaltsplelknangskwivlr
vddiepdvgllkyvngtcqat
>d1apb__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1apc__ 1.25.3.1.1 Cytochrome b562 {Escherichia coli}
adlednmetlndnlkviekadnaaqvkdaltkmraaaldaqkatppkledkspdspemkd
frhgfdilvgqiddalklanegkvkeaqaaaeqlkttrnayhqkyr
>d1apf__ 7.9.1.1.8 Anthopleurin-B {Giant green sea anemone (Anthopleura xanthogrammica)}
gvpclcdsdgprprgntlsgilwfypsgcpsgwhnckahgpnigwcckk
>d1apga_ 4.135.1.1.7 Ricin A-chain {Castor bean (Ricinus communis)}
ifpkqypiinfttagatvqsytnfiravrgrlttgadvrheipvlpnrvglpinqrfilv
elsnhaelsvtlaldvtnayvvgyragnsayffhpdnqedaeaithlftdvqnrytfafg
gnydrleqlagnlrenielgngpleeaisalyyystggtqlptlarsfiiciqmiseaar
fqyiegemrtrirynrrsapdpsvitlenswgrlstaiqesnqgafaspiqlqrrngskf
svydvsilipiialmvyrcapppssqf
>e1aph.1a 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
giveqccasvcslyqlenycn
>e1aph.1b 7.1.1.1.1 Insulin {Bovine (Bos taurus)}
fvnqhlcgshlvealylvcgergffytpka
>d1apj__ 7.23.1.1.1 Fibrillin {Human (Homo sapiens)}
saqdlrmsycyakfeggkcsspksrnhskqecccalkgegwgdpcelcptepdeafrqic
pygsgiivgpddsa
>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
>d1apme_ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
seqesvkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhy
amkildkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemf
shlrrigrfaepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfak
rvkgrtwtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyek
ivsgkvrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrk
veapfipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1apna_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apnb_ 2.26.1.1.1 Concanavalin A {Jack bean (Canavalia ensiformis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvdkr
lsavvsypnadsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtdgnleltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1apo__ 7.3.11.1.6 Factor X, N-terminal module {Bovine (Bos taurus)}
kdgdqceghpclnqghckdgigdytctcaegfegkncefstr
>d1apq__ 7.3.11.1.19 Complement protease C1R {Human (Homo sapiens)}
avdldecasrsksgeedpqpqcqhlchnyvggyfcscrpgyelqedrhscqae
>d1aps__ 4.47.10.1.2 Acylphosphatase {Horse (Equus caballus)}
starplksvdyevfgrvqgvcfrmyaedearkigvvgwvkntskgtvtgqvqgpeekvns
mkswlskvgspssridrtnfsnektiskleysnfsvry
>d1apte_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apue_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apve_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apwe_ 2.44.1.2.2 Acid protease {Fungus (Penicillium janthinellum), penicillopepsin}
aasgvatntptandeeyitpvtiggttlnlnfdtgsadlwvfstelpasqqsghsvynps
atgkelsgytwsisygdgssasgnvftdsvtvggvtahgqavqaaqqisaqfqqdtnndg
llglafssintvqpqsqttffdtvksslaqplfavalkhqqpgvydfgfidsskytgslt
ytgvdnsqgfwsfnvdsytagsqsgdgfsgiadtgttllllddsvvsqyysqvsgaqqds
naggyvfdcstnlpdfsvsisgytatvpgslinygpsgdgstclggiqsnsgigfsifgd
iflksqyvvfdsdgpqlgfapqa
>d1apxa_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxb_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxc_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>d1apxd_ 1.90.1.1.5 Ascorbate peroxidase {Pea (Pisum sativum)}
gksyptvspdyqkaiekakrklrgfiaekkcaplilrlawhsagtfdsktktggpfgtik
hqaelahganngldiavrllepikeqfpivsyadfyqlagvvaveitggpevpfhpgred
kpepppegrlpdatkgsdhlrdvfgkamglsdqdivalsgghtigaahkersgfegpwts
nplifdnsyftelltgekdgllqlpsdkalltdsvfrplvekyaadedvffadyaeahlk
lselgfaea
>e1apy.1a 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.1b 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apy.2c 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apy.2d 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.1a 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.1b 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>e1apz.2c 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
splplvvntwpfknateaawralasggsaldavesgcamcereqcdgsvgfggspdelge
ttldamimdgttmdvgavgdlrriknaigvarkvlehtthtllvgesattfaqsmgfine
dlstsasqalhsdwlarncqpnywrnvipdpskycgpykpp
>e1apz.2d 4.124.1.4.1 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Human (Homo sapiens)}
tigmvvihktghiaagtstngikfkihgrvgdspipgagayaddtagaaaatgngdilmr
flpsyqaveymrrgedptiacqkvisriqkhfpeffgavicanvtgsygaacnklstftq
fsfmvynseknqpteekvdci
>d1aq0a_ 3.1.7.3.11 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq0b_ 3.1.7.3.11 Plant beta-glucanases {Barley (Hordeum vulgare), 1,3-1,4-beta-glucanase}
igvcygmsannlpaastvvsmfksngiksmrlyapnqaalqavggtginvvvgapndvls
nlaaspaaaaswvksniqaypkvsfryvcvgnevaggatrnlvpamknvhgalvaaglgh
ikvttsvsqailgvfsppsagsftgeaaafmgpvvqflartnaplmaniypylawaynps
amdmgyalfnasgtvvrdgaygyqnlfdttvdafytamgkhggssvklvvsesgwpsggg
taatpanarfynqhlinhvgrgtprhpgaietyifamfnenqkdsgveqnwglfypnmqh
vypinf
>d1aq1__ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1aq2__ 3.81.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {Escherichia coli}
nngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtgift
grspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfvvda
fcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqwkeq
glnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgekgdv
avffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepeiyna
irrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifltad
afgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptqyae
vlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnlaip
telpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>d1aq3a_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3b_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq3c_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvtcsvrqssaqnrkysi
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4a_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4b_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq4c_ 4.65.1.1.1 MS2 virus coat protein {Bacteriophage MS2}
asnftqfvlvdnggtgdvtvapsnfangvaewissnsrsqaykvacsvrqssaqnrkyti
kvevpkvatqtvggvelpvaawrsylnmeltipifatnsdcelivkamqgllkdgnpips
aiaansgiy
>d1aq6a_ 5.17.1.1.2 L-2-Haloacid dehalogenase {Xanthobacter autotrophicus}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq6b_ 5.17.1.1.2 L-2-Haloacid dehalogenase {Xanthobacter autotrophicus}
mikavvfdaygtlfdvqsvadateraypgrgeyitqvwrqkqleyswlralmgryadfwg
vtrealaytlgtlglepdesfladmaqaynrltpypdaaqclaelaplkrailsngapdm
lqalvanagltdsfdavisvdakrvfkphpdsyalveevlgvtpaevlfvssngfdvgga
knfgfsvarvarlsqealarelvsgtiapltmfkalrmreetyaeapdfvvpalgdlprl
vrgma
>d1aq7__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1aq8a1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aq8b1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aq8c1 2.5.1.3.2 (9-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
iaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamafngtv
pgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrfkatk
pgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1aq8c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1aqa__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
kyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfedvghs
tdarelsktyiigelhpddrskia
>d1aqb__ 2.53.1.1.2 Retinol binding protein {Pig (Sus scrofa domestica)}
erdcrvssfrvkenfdkarfsgtwyamakkdpeglflqdnivaefsvdenghmsatakgr
vrllnnwdvcadmvgtftdtedpakfkmkywgvasflqkgnddhwiidtdydtyavqysc
rlqnldgtcadsysfvfardphgfspevqkivrqrqeelclarqyriithngycd
>d1aqca_ 2.49.1.2.1 X11 {Human (Homo sapiens)}
edlidgiifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesq
pxtevdlfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenv
eashpsqdgkrqykxichvfesedaqliaqsigqafsvayqeflr
>d1aqcb_ 2.49.1.2.1 X11 {Human (Homo sapiens)}
iifaanylgstqllsdktpsknvrxxqaqeavsrikxaqklaksrkkapegesqpxtevd
lfiltqrikvlnadtqetxxdhplrtisyiadignivvlxarrriprsnsqenveashps
qdgkrqykxichvfesedaqliaqsigqafsvayqeflranginp
>d1aqda1 2.1.1.2.149 (82-181) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwefd
>d1aqda2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdb1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdb2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdd1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdd2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqde1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqde2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdg1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdg2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdh1 2.1.1.2.149 (93-190) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewra
>d1aqdh2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqdj1 2.1.1.2.149 (82-179) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
itnvppevtvltnspvelrepnvlicfidkftppvvnvtwlrngkpvttgvsetvflpre
dhlfrkfhylpflpstedvydcrvehwgldepllkhwe
>d1aqdj2 4.17.1.1.4 (3-81) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
eehviiqaefylnpdqsgefmfdfdgdeifhvdmakketvwrleefgrfasfeaqgalan
iavdkanleimtkrsnytp
>d1aqdk1 2.1.1.2.149 (93-191) Class II MHC, C-terminal domains of alpha and beta chains {Human HLA-dr1}
rrvepkvtvypsktqplqhhnllvcsvsgfypgsievrwfrngqeekagvvstgliqngd
wtfqtlvmletvprsgevytcqvehpsvtspltvewrar
>d1aqdk2 4.17.1.1.4 (4-92) MHC class II, N-terminal domains of alpha and beta chains {Human HLA-dr1}
rprflwqlkfechffngtervrllerciynqeesvrfdsdvgeyravtelgrpdaeywns
qkdlleqrraavdtycrhnygvgesftvq
>d1aqe__ 1.126.1.1.1 Cytochrome c3 {Desulfovibrio desulfuricans, different strains}
tfeipesvtmspkqfegytpkkgdvtfnhashmdiacqqchhtvpdtytiescmtegchd
nikerteissvertfhttkdsekscvgchrelkrqgpsdaplacnschvq
>d1aqfa1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfa2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfa3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfb1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfb2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfb3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfc1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfc2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfc3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfd1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfd2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfd3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfe1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfe2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfe3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqff1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqff2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqff3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfg1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfg2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfg3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqfh1 2.52.1.1.1 (116-217) Pyruvate kinase {Rabbit (Oryctolagus cuniculus)}
peirtglikgsgtaevelkkgatlkitldnaymekcdenilwldyknickvvdvgskvyv
ddglislqvkqkgpdflvtevenggflgskkgvnlpgaavdl
>d1aqfh2 3.1.11.1.2 (12-115,218-395) Pyruvate kinase, N-terminal domain {Rabbit (Oryctolagus cuniculus)}
iqtqqlhaamadtflehmcrldidsapitarntgiictigpasrsvetlkemiksgmnva
rmnfshgtheyhaetiknvrtatesfasdpilyrpvavaldtkgXpavsekdiqdlkfgv
eqdvdmvfasfirkaadvhevrkilgekgknikiiskienhegvrrfdeileasdgimva
rgdlgieipaekvflaqkmiigrcnragkpvicatqmlesmikkprptraegsdvanavl
dgadcimlsgetakgdypleavrmqhliareaeaamfhrklfe
>d1aqfh3 3.40.1.1.2 (396-530) Pyruvate kinase, C-terminal domain {Rabbit (Oryctolagus cuniculus)}
elarssshstdlmeamamgsveasykclaaalivltesgrsahqvaryrprapiiavtrn
hqtarqahlyrgifpvvckdpvqeawaedvdlrvnlamnvgkargffkkgdvvivltgwr
pgsgftntmrvvpvp
>d1aqh_1 2.62.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1aqh_2 3.1.7.1.2 (1-354) Bacterial alpha-amylase (BLA) {Alteromonas haloplanctis}
tpttfvhlfewnwqdvaqeceqylgpkgyaavqvsppnehitgsqwwtryqpvsyelqsr
ggnraqfidmvnrcsaagvdiyvdtlinhmaagsgtgtagnsfgnksfpiyspqdfhesc
tinnsdygndryrvqncelvgladldtasnyvqntiaayindlqaigvkgfrfdaskhva
asdiqslmakvngspvvfqevidqggeavgaseylstglvtefkystelgntfrngslaw
lsnfgegwgfmpsssavvfvdnhdnqrghggagnvitfedgrlydlanvfmlaypygypk
vmssydfhgdtdaggpnvpvhnngnlecfasnwkcehrwsyiaggvdfrnntad
>d1aqia_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqib_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpstlvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqja_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqjb_ 3.56.1.5.2 DNA methylase TaqI, coenzyme-binding domain {Thermus aquaticus}
vetppevvdfmvslaeaprggrvlepacahgpflrafreahgtgyrfvgveidpkaldlp
pwaegiladfllwepgeafdlilgnppygivgeaskypihvfkavkdlykkafstwkgky
nlygaflekavrllkpggvlvfvvpatwlvledfallreflaregktsvyylgevfpqkk
vsavvirfqksgkglslwdtqesesgftpilwaeyphwegeiirfeteetrkleisgmpl
gdlfhirfaarspefkkhpavrkepgpglvpvltgrnlkpgwvdyeknhsglwmpkerak
elrdfyatphlvvahtkgtrvvaawderaypwreefhllpkegvrldpsslvqwlnseam
qkhvrtlyrdfvphltlrmlerlpvrreygfht
>d1aqkh1 2.1.1.1.94 (2-123) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
vqlvesgggvvqpgrslrlscaasgftfnnyaihwvrqapgkglewvafisydgsknyya
dsvkgrftisrdnskntlflqmnslrpedtaiyycarvlfqqlvlyapfdiwgqgtmvtv
ss
>d1aqkh2 2.1.1.2.96 (124-226) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpqpvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1aqkl1 2.1.1.1.94 (2-111) Immunoglobulin (variable domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
nvltqppsvsgapgqrvtisctgsnsnigagftvhwyqhlpgtapkllifantnrpsgvp
drfsgsksgtsaslaitglqaedeadyycqsydsslsarfgggtrltvlg
>d1aqkl2 2.1.1.2.96 (112-216) Immunoglobulin (constant domains of L and H chains) {Fab B7-15A2 (human), lambda L chain}
qpkaapsvtlfppsseelqankatlvclisdfypgavtvawkadsspvnagvettkpskq
snnkyaassylsltpeqwkshksyscqvthegstvektvapaecs
>d1aqla_ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptv
>d1aqlb_ 3.59.1.1.4 Bile-salt activated lipase (cholesterol esterase) {Bovine (Bos taurus)}
aklgsvyteggfvegvnkklslfgdsidifkgipfaaapkalekperhpgwqgtlkaksf
kkrclqatltqdstygnedclylniwvpqgrkevshdlpvmiwiyggaflmgasqganfl
snylydgeeiatrgnvivvtfnyrvgplgflstgdsnlpgnyglwdqhmaiawvkrniea
fggdpdnitlfgesaggasvslqtlspynkglikraisqsgvglcpwaiqqdplfwakri
aekvgcpvddtskmagclkitdpraltlayklplgsteypklhylsfvpvidgdfipddp
vnlyanaadvdyiagtndmdghlfvgmdvpainsnkqdvteedfyklvsgltvtkglrga
natyevytepwaqdssqetrkktmvdletdilfliptkiavaqhkshaksantytylfsq
psrmpiypkwmgadhaddlqyvfgkpfatplgyraqdrtvskamiaywtnfartgdpntg
hstvpanwdpytleddnyleinkqmdsnsmklhlrtnylqfwtqtyqalptv
>d1aqm_1 2.62.1.1.2 (355-448) Bacterial alpha-Amylase (BLA) {Alteromonas haloplanctis}
nwavtnwwdntnnqisfgrgssghmainkedstltatvqtdmasgqycnvlkgelsadak
scsgevitvnsdgtinlnigawdamaihknakln
>d1aqm_2 3.1.7.1.2 (1-354) Bacterial alpha-amylase (BLA) {Alteromonas haloplanctis}
tpttfvhlfewnwqdvaqeceqylgpkgyaavqvsppnehitgsqwwtryqpvsyelqsr
ggnraqfidmvnrcsaagvdiyvdtlinhmaagsgtgtagnsfgnksfpiyspqdfhesc
tinnsdygndryrvqncelvgladldtasnyvqntiaayindlqaigvkgfrfdaskhva
asdiqslmakvngspvvfqevidqggeavgaseylstglvtefkystelgntfrngslaw
lsnfgegwgfmpsssavvfvdnhdnqrghggagnvitfedgrlydlanvfmlaypygypk
vmssydfhgdtdaggpnvpvhnngnlecfasnwkcehrwsyiaggvdfrnntad
>d1aqn__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aqp__ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1aqq__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqr__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqs__ 7.38.1.1.5 Metallothionein {Baker's yeast (Saccharomyces cerevisiae)}
qneghecqcqcgscknneqcqkscscptgcnsddkcpcgn
>d1aqt_1 1.2.6.1.1 (87-136) Epsilon subunit of F1F0-ATP synthase C-terminal domain {Escherichia coli}
qdldearameakrkaeehissshgdvdyaqasaelakaiaqlrvieltkk
>d1aqt_2 2.81.1.1.1 (2-86) Epsilon subunit of F1F0-ATP synthase N-terminal domain {Escherichia coli}
styhldvvsaeqqmfsglvekiqvtgsegelgiypghaplltaikpgmirivkqhgheef
iylsggilevqpgnvtvladtairg
>d1aqua_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1aqub_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrm
>d1aqva1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqva2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqvb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqvb2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwa2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwb2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwc1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwc2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqwd1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqwd2 3.38.1.5.4 (1-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
ppytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdl
tlyqsntilrhlgrtl
>d1aqxa1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxa2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxb1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxb2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxc1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxc2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqxd1 1.48.1.1.4 (77-209) Glutathione S-transferase {Human (Homo sapiens), class pi}
glygkdqqeaalvdmvndgvedlrckyisliytnyeagkddyvkalpgqlkpfetllsqn
qggktfivgdqisfadynlldlllihevlapgcldafpllsayvgrlsarpklkaflasp
eyvnlpingngkq
>d1aqxd2 3.38.1.5.4 (2-76) Glutathione S-transferase {Human (Homo sapiens), class pi}
pytvvyfpvrgrcaalrmlladqgqswkeevvtvetwqegslkasclygqlpkfqdgdlt
lyqsntilrhlgrtl
>d1aqya_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrme
>d1aqyb_ 3.30.1.3.1 Estrogen sulfotransferase {Mouse (Mus musculus)}
eyyevfgefrgvlmdkrftkywedvemflarpddlviatypksgttwisevvymiykegd
vekckedaifnripylecrnedlingikqlkekesprivkthlppkllpasfweknckmi
ylcrnakdvavsyyyfllmitsypnpksfsefvekfmqgqvpygswydhvkawwekskns
rvlfmfyedmkedirrevvklieflerkpsaelvdriiqhtsfqemknnpstnytmmpee
mmnqkvspfmrkgiigdwknhfpealrerfdehykqqmkdctvkfrm
>d1aqza_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergillus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1aqzb_ 4.1.1.1.9 Ribotoxin restrictocin {Fungus (Aspergillus restrictus)}
atwtcinqqlnpktnkwedkrllysqakaesnshhaplsdgktgssyphwftngydgngk
likgrtpikfgkadcdrppkhsqngmgkddhyllefptfpdghdykfdskkpkenpgpar
viytypnkvfcgivahqrgnqgdlrlcsh
>d1ar0a_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpf
qkiqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1ar0b_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwkgqqfqgkaaiveklsslpfqk
iqhsitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
h
>d1ar1a1 6.2.1.1.6 Cytochrome c oxidase {Paracoccus denitrificans}
gfftrwfmstnhkdigilylftagivglisvcftvymrmelqhpgvqymclegarliada
saectpnghlwnvmityhgvlmmffvvipalfggfgnyfmplhigapdmafprlnnlsyw
myvcgvalgvasllapggndqmgsgvgwvlypplstteagysmdlaifavhvsgassilg
ainiittflnmrapgmtlfkvplfawsvfitawlillslpvlagaitmllmdrnfgtqff
dpagggdpvlyqhilwffghpevyiiilpgfgiishvistfakkpifgylpmvlamaaig
ilgfvvwahhmytagmsltqqayfmlatmtiavptgikvfswiatmwggsiefktpmlwa
fgflflftvggvtgvvlsqapldrvyhdtyyvvahfhyvmslgavfgifagvyywigkms
grqypewagqlhfwmmfigsnliffpqhflgrqgmprryidypvefaywnnissigayis
fasflffigivfytlfagkrvnvpnywnehadtlewtlpspppehtfet
>d1ar1b1 2.5.1.2.3 (108-252) Cytochrome c oxidase {Paracoccus denitrificans}
ndpdlvikaighqwywsyeypndgvafdalmlekealadagysedeyllatdnpvvvpvg
kkvlvqvtatdvihawtipafavkqdavpgriaqlwfsvdqegvyfgqcselcginhaym
pivvkavsqekyeawlagakeefaa
>d1ar1b2 6.2.1.1.6 (1-107) Cytochrome c oxidase {Paracoccus denitrificans}
qdvlgdlpvigkpvnggmnfqpassplahdqqwldhfvlyiitavtifvcllllicivrf
nrranpvparfthntpieviwtlvpvlilvaigafslpilfrsqemp
>d1ar1c_ 2.1.1.1.96 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
evklqesggdlvqpggslklscaasgftfssytmswvrqtpekrlewvasinngggrtyy
pdtvkgrftisrdnakntlylqmsslksedtamyycvrheyyyamdywgqgttvtvss
>d1ar1d_ 2.1.1.1.96 Immunoglobulin (variable domains of L and H chains) {Fv against Paracoccus denitrificans cytochrome c oxidase (mouse), kappa L chain}
dieltqtpvslsasvgetvtitcraseniysylawyqqkqgkspqflvynaktlgegvps
rfsgsgsgtqfslkinsllpedfgsyycqhhygtppltfgggtkleik
>d1ar2__ 2.1.1.1.143 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer REI (human)}
tpdiqmtqspsslsasvgdrvtitvqasqdiikhlnwyqqtpgkapklliyeasnlqagv
psrfsgsgsgtdytftisslqpediatyycqqyqslpytfgqgtklqit
>d1ar4a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar4b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar4b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5a1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5a2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar5b1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1ar5b2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1ar61_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyippgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar62_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar63_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar71_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar72_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar73_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar81_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnsasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar82_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar83_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1ar91_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1ar92_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmytsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1ar93_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1arb__ 2.41.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1arc__ 2.41.1.1.1 Achromobacter protease {Achromobacter lyticus, strain m497-1}
gvsgscnidvvcpegdgrrdiiravgaysksgtlactgslvnntandrkmyfltahhcgm
gtastaasivvywnyqnstcrapntpasgangdgsmsqtqsgstvkatyatsdftlleln
naanpafnlfwagwdrrdqnypgaiaihhpnvaekrisnstsptsfvawgggagtthlnv
qwqpsggvtepgssgspiyspekrvlgqlhggpsscsatgtnrsdqygrvftswtgggaa
asrlsdwldpastgaqfidglds
>d1ard__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqehlkrhyrshtnek
>d1are__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqealkrhyrshtnek
>d1arf__ 7.31.1.1.4 ADR1 {Synthetic, based on Saccharomyces cerevisiae sequence}
rsfvcevctrafarqeylkrhyrshtnek
>d1arga_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1argb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arha_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1arhb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfarqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgavnvagmtpdnmaplceaivavl
>d1aria_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1arib_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpshpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ark__ 2.30.2.1.3 SH3 domain from nebulin {Human (Homo sapiens)}
tagkiframydymaadadevsfkdgdaiinvqaidegwmygtvqrtgrtgmlpanyveai
>d1arl__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arm__ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaehpqlvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftedygqdpsftaildsmdifleivtnpdgfafth
sqnrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvkdhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1arn__ 2.5.1.1.22 Azurin {Alcaligenes xylosoxidans, NCIMB (11015), different isoforms}
aqceatvesndamqynvkeivvdksckqftmhlkhvgkmakvamghnlvltkdadkqava
tdgmgaglaqdyvkagdtrviahtkvigggesdsvtfdvskiaagenyayfcsfpghwam
mkgtlklgs
>d1arol_ 4.92.1.1.1 Bacteriophage T7 lysozyme (Zn amidase) {Bacteriophage T7}
rvqfkqrestdaifvhcsatkpsqnvgvreirqwhkeqgwldvgyhfiikrdgtveagrd
emavgshakgynhnsigvclvggiddkgkfdanftpaqmqslrsllvtllakyegavlra
hhevapkacpsfdlkrwweknelvtsdrg
>d1arop_ 5.8.1.3.1 T7 RNA polymerase {Bacteriophage T7}
kndfsdielaaipfntladhygerlareqlalehesyemgearfrkmferqlkagevadn
aaakplittllpkmiarindwfeevkakrgkrptafqflqeikpeavayitikttlaclt
sadnttvqavasaigraiedearfgrirdleakhfkknveeqlnkrvghvykkafmqvve
admlskgllggeawsswhkedsihvgvrciemliestgmvslhrqnagvvgqdsetiela
peyaeaiatragalagispmfqpcvvppkpwtgitgggywangrrplalvrthskkalmr
yedvympevykainiaqntawkinkkvlavanvitkwkhspvedipaiereelpmkpedi
dmnpealtawkraaaavyrkdkarksrrislefmleqankfanhkaiwfpynmdwrgrvy
avsmfnpqgndmtkglltlakgkpigkegyywlkihgancagvdkvpfperikfieenhe
nimacaksplentwwaeqdspfcflafcfeyagvqhhglsyncslplafdgscsgiqhfs
amlrdevggravnllpsetvqdiygivakkvneilqadaingtdnevvtvtdentgeise
kvklgtkalagqwlaygvtrsvtkrsvmtlaygskefgfrqqvledtiqpaidsgkglmf
tqpnqaagymakliwesvsvtvvaaveamnwlksaakllaaevkdkktgeilrkrsavhw
vtpdgfpvwqeykkpiqtrlnlmflgqfrlqptintnkdseidahkqesgiapnfvhsqd
gshlrktvvwahekygiesfalihdsfgtipadaanlfkavretmvdtyessdvladfyd
qfadqlhesqldkmpalpakgnlnlrdilesd
>d1arp__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arqa_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arqb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arra_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1arrb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1ars__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1art__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aru__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arv__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arw__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arx__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1ary__ 1.90.1.1.2 Peroxidase {Arthromyces ramous}
svtcpggqstsnsqccvwfdvlddlqtnfyqgskcespvrkilrivfhdaigfspaltaa
gqfggggadgsiiahsnielafpanggltdtiealravginhgvsfgdliqfatavgmsn
cpgsprlefltgrsnssqpsppslipgpgntvtaildrmgdagfspdevvdllaahslas
qeglnsaifrspldstpqvfdtqfyietllkgttqpgpslgfaeelspfpgefrmrsdal
lardsrtacrwqsmtssnevmgqryraamakmsvlgfdrnaltdcsdvipsavsnnaapv
ipggltvddievscpsepfpeiatasgplpslapap
>d1arza1 3.2.1.3.13 (4-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
anirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvq
ssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiai
vfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arza2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzb1 3.2.1.3.13 (5-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
nirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtvqs
sldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadiaiv
faanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzb2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzc1 3.2.1.3.13 (3-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
danirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtv
qssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadia
ivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzc2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1arzd1 3.2.1.3.13 (3-130,241-273) Dihydrodipicolinate reductase {Escherichia coli}
danirvaiagaggrmgrqliqaalalegvqlgaaleregssllgsdagelagagktgvtv
qssldavkddfdvfidftrpegtlnhlafcrqhgkgmvigttgfdeagkqairdaaadia
ivfaanfsXmtfangavrsalwlsgkesglfdmrdvldlnnl
>d1arzd2 4.61.1.2.2 (131-240) Dihydrodipicolinate reductase {Escherichia coli}
vgvnvmlkllekaakvmgdytdieiieahhrhkvdapsgtalamgeaiahaldkdlkdca
vysreghtgervpgtigfatvragdivgehtamfadigerleithkassr
>d1as0_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as0_2 3.30.1.6.13 (32-60,182-344) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdvii
>d1as2_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as2_2 3.30.1.6.13 (32-60,182-346) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgavesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcatdtkn
vqfvfdavtdviikn
>d1as3_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1as3_2 3.30.1.6.13 (9-60,182-354) Transducin (alpha subunit) {Rat (Rattus rattus)}
dkaaverskmidrnlredgekaarevkllllgavesgkstivkqmkiiheagXtgiveth
ftfkdlhfkmfdvggqrserkkwihcfegvtaiifcvalsdydlvlaedeemnrmhesmk
lfdsicnnkwftdtsiilflnkkdlfeekikksplticypeyagsntyeeaaayiqcqfe
dlnkrkdtkeiythftcatdtknvqfvfdavtdviiknnlkdcglf
>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
>d1as6a1 2.5.1.3.2 (5-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
taaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamaf
ngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrf
katkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as6b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as6c1 2.5.1.3.2 (5-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
taaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhamaf
ngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilrf
katkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as6c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as7a1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7a2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as7b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7b2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as7c1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as7c2 2.5.1.3.2 (167-340) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsgt
>d1as8a1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8a2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as8b1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8b2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1as8c1 2.5.1.3.2 (4-166) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
ataaeiaalprqkvelvdppfvhahsqvaeggpkvveftmvieekkividdagtevhama
fngtvpgplmvvhqddyleltlinpetntlmhnidfhaatgalgggglteinpgektilr
fkatkpgvfvyhcappgmvpwhvvsgmngaimvlpreglhdgk
>d1as8c2 2.5.1.3.2 (167-339) Nitrite reductase, NIR {Alcaligenes faecalis, strain s-6}
gkaltydkiyyvgeqdfyvprdengkykkyeapgdayedtvkvmrtltpthvvfngavga
ltgdkamtaavgekvlivhsqanrdtrphligghgdyvwatgkfntppdvdqetwfipgg
aagaafytfqqpgiyayvnhnlieafelgaaahfkvtgewnddlmtsvlapsg
>d1asa__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asb__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asc__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfafayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asd__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ase__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asf__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asg__ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfafqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1ash__ 1.1.1.1.44 Ascaris hemoglobin, domain 1 {Pig roundworm (Ascaris suum)}
anktrelcmkslehakvdtsnearqdgidlykhmfenypplrkyfksreeytaedvqndp
ffakqgqkillachvlcatyddretfnaytrelldrhardhvhmppevwtdfwklfeeyl
gkkttldeptkqawheigrefakeink
>d1asj1_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
aatsrdalpnteasgpthskeipaltavetgatnplvpsdtvqtrhvvqhrsrsessies
ffargacvtimtvdnpasttnkdklfavwkitykdtvqlrrklefftysrfdmeltfvvt
anftetnnghalnqvyqimyvppgapvpekwddytwqtssnpsifytygtaparisvpyv
gisnayshfydgfskvplkdqsaalgdslygaaslndfgilavrvvndhnptkvtskirv
ylkpkhirvwcprppravayygpgvdykdgtltplstkdltty
>d1asj2_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
eacgysdrvlqltlgnstittqeaansvvaygrwpeylrdseanpvdqptepdvaacrfy
tldtvswtkesrgwwwklpdalrdmglfgqnmyyhylgrsgytvhvqcnaskfhqgalgv
favpemclagdsntttmhtsyqnanpgekggtftgtftpdnnqtsparrfcpvdyllgng
tllgnafvfphqiinlrtnncatlvlpyvnslsidsmvkhnnwgiailplaplnfasess
peipitltiapmccefnglrnitlprlq
>d1asj3_ 2.9.1.4.5 Poliovirus {Poliovirus type 1, mahoney strain}
glpvmntpgsnqyltadnfqspcalpefdvtppidipgevknmmelaeidtmipfdlsat
kkntmemyrvrlsdkphtddpilclslspasdprlshtmlgeilnyythwagslkftflf
cgsmmatgkllvsyappgadppkkrkeamlgthviwdiglqssctmvvpwisnttyrqti
ddsfteggyisvfyqtrivvplstpremdilgfvsacndfsvrllrdtthieqka
>d1aska_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
gdkpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpf
qkiqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrl
alhnf
>d1askb_ 4.15.3.2.1 Nuclear transport factor-2 (NTF2) {Rat (Rattus norvegicus)}
kpiweqigssfiqhyyqlfdndrtqlgaiyidascltwegqqfqgkaaiveklsslpfqk
iqasitaqdhqptpdsciismvvgqlkadedpimgfhqmfllknindawvctndmfrlal
>d1asla_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1aslb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asma_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asmb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asna_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asnb_ 3.57.1.1.5 Aspartate aminotransferase, AAT {Escherichia coli}
mfenitaapadpilgladlfraderpgkinlgigvykdetgktpvltsvkkaeqyllene
ttknylgidgipefgrctqellfgkgsalindkrartaqtpggtgalrvaadflakntsv
krvwvsnpswpnhksvfnsaglevreyayydaenhtldfdalinslneaqagdvvlfhgc
chnptgidptleqwqtlaqlsvekgwlplfdfayqgfargleedaeglrafaamhkeliv
assysknfglynervgactlvaadsetvdrafsqmkaairanysnppahgasvvatilsn
dalraiweqeltdmrqriqrmrqlfvntlqekganrdfsfiikqngmfsfsgltkeqvlr
lreefgvyavasgrvnvagmtpdnmaplceaivavl
>d1asoa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asoa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asoa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asob1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asob2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asob3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1aspa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aspa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aspa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1aspb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1aspb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1aspb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asqa1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asqa2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asqa3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1asqb1 2.5.1.3.4 (1-129) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
sqirhykweveymfwapncnenivmgingqfpgptiranagdsvvveltnklhtegvvih
whgilqrgtpwadgtasisqcainpgetffynftvdnpgtffyhghlgmqrsaglygsli
vdppqgkke
>d1asqb2 2.5.1.3.4 (130-338) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
pfhydgeinlllsdwwhqsihkqevglsskpirwigepqtillngrgqfdcsiaakydsn
lepcklkgsescapyifhvspkktyririasttalaalnfaignhqllvveadgnyvqpf
ytsdidiysgesysvlittdqnpsenywvsvgtrarhpntppgltllnylpnsvsklpts
pppqtpawddfdrsknftyritaamgspk
>d1asqb3 2.5.1.3.4 (339-552) Ascorbate oxidase {Zucchini (Cucurbita pepo medullosa)}
ppvkfnrrifllntqnvingyvkwaindvslalpptpylgamkynllhafdqnpppevfp
edydidtpptnektrigngvyqfkigevvdvilqnanmmkenlsethpwhlhghdfwvlg
ygdgkfsaeeesslnlknpplrntvvifpygwtairfvadnpgvwafhchiephlhmgmg
vvfaegvekvgriptkalacggtakslinnpknp
>d1ass__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1ast__ 4.71.1.6.1 Astacin {European fresh water crayfish (Astacus astacus)}
aailgdeylwsggvipytfagvsgadqsailsgmqeleektcirfvprttesdyveifts
gsgcwsyvgrisgaqqvslqangcvyhgtiihelmhaigfyhehtrmdrdnyvtinyqnv
dpsmtsnfdidtysryvgedyqyysimhygkysfsiqwgvletivplqngidltdpydka
hmlqtdanqinnlytnecsl
>d1asu__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
plreprglgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwat
aiavlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdki
rvlaegdgfmkriptskqgellakamyalnhfergentktnl
>d1asv__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
glgplqiwqtdftleprmaprswlavtvdtassaivvtqhgrvtsvaaqhhwataiavlg
rpkaiktdngscftskstrewlarwgiahttgipgnsqgqamveranrllkdkirvlaeg
dgfmkriptskqgellakamyalnhf
>d1asw__ 3.46.3.2.1 ASV integrase, catalytic domain {Avian sarcoma virus, Rous sarcoma virus, Schmidt-Ruppin strain B}
reprglgplqiwqtdftleprxaprswlavtvdtassaivvtqhgrvtsvaaqhhwatai
avlgrpkaiktdngscftskstrewlarwgiahttgipgnsqgqaxveranrllkdkirv
laegdgfxkriptskqgellakaxyalnhfer
>d1asx__ 3.7.5.2.1 Thermosome {Thermoplasma acidophilum}
msgividkekvhskmpdvvknakialidsaleikkteieakvqisdpskiqdflnqetnt
fkqmvekikksganvvlcqkgiddvaqhylakegiyavrrvkksdmeklakatgakivtd
lddltpsvlgeaetveerkigddrmtfvmgck
>d1asya1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asya2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asyb1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asyb2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1asza1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1asza2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1aszb1 2.35.4.1.1 (68-204) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
edtakdnygklpliqsrdsdrtgqkrvkfvdldeakdsdkevlfrarvhntrqqgatlaf
ltlrqqasliqglvkankegtisknmvkwagslnlesivlvrgivkkvdepiksatvqnl
eihitkiytisetpeal
>d1aszb2 4.82.1.1.7 (205-557) Aspartyl-tRNA synthetase (AspRS) {Baker's yeast (Saccharomyces cerevisiae)}
pilledasrseaeaeaaglpvvnldtrldyrvidlrtvtnqaifriqagvcelfreylat
kkftevhtpkllgapseggssvfevtyfkgkaylaqspqfnkqqlivadfervyeigpvf
raensnthrhmteftgldmemafeehyhevldtlselfvfifselpkrfaheielvrkqy
pveefklpkdgkmvrltykegiemlraagkeigdfedlstenekflgklvrdkydtdfyi
ldkfpleirpfytmpdpanpkysnsydffmrgeeilsgaqrihdhallqermkahglspe
dpglkdycdgfsygcpphagggiglervvmfyldlknirraslfprdpkrlrp
>d1at0__ 2.76.1.1.1 Hedgehog {Fruit fly (Drosophila melanogaster)}
cftpestallesgvrkplgelsigdrvlsxtangqavysevilfxdrnleqxqnfvqlht
dggavltvtpahlvsvwqpesqkltfvfadrieeknqvlvrdvetgelrpqrvvkvgsvr
skgvvapltregtivvnsvaascya
>d1at1a1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastrtrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1at1a2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1at1b1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1b2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at1c1 3.66.1.1.1 (1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastrtrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg
>d1at1c2 3.66.1.1.1 (151-310) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
rldnlhvamvgdlkygrtvhsltqalakfdgnrfyfiapdalampeyildmldekgiaws
lhssieevmaevdilymtrvqkerldpseyanvkaqfvlrasdlhnakanmkvlhplprv
deiatdvdktphawyfqqagngifarqallalvlnrdlvl
>d1at1d1 4.47.2.1.1 (8-100) Aspartate carbamoyltransferase {Escherichia coli}
gveaikrgtvidhipaqigfkllslfkltetdqritiglnlpsgemgrkdlikientfls
edqvdqlalyapqatvnridnyevvgksrpslp
>d1at1d2 7.35.5.1.1 (101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan
>d1at3a_ 2.51.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1at3b_ 2.51.1.1.2 HSV-2 protease {Herpes simplex virus type II, HSV-2}
ravpiyvagflalydsgdpgelaldpdtvraalppenplpinvdhrarcevgrvlavvnd
prgpffvgliacvqlervletaasaaiferrgpalsreerllylitnylpsvslstkrrg
devppdrtlfahvalcaigrrlgtivtydtsldaaiapfrhldpatregvrreaaeaela
lagrtwapgvealthtllstavnnmmlrdrwslvaerrrqagiaghtylqa
>d1at5__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsxxngmnawvawrnrckgtdv
qawirgcrl
>d1at6__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsxgngmnawvawrnrckgtdv
qawirgcrl
>d1at9__ 6.2.1.1.2 Bacteriorhodopsin {Halobacterium salinarium}
aqitgrpewiwlalgtalmglgtlyflvkgmgvsdpdakkfyaittlvpaiaftmylsml
lgygltmvpfggeqnpiywaryadwlfttplllldlallvdadqgtilalvgadgimigt
glvgaltkvysyrfvwwaistaamlyilyvlffgftskaesmrpevastfkvlrnvtvvl
wsaypvvwligsegagivplnietllfmvldvsakvgfglillrsraifg
>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
>d1atg__ 3.84.1.1.17 Molybdate-binding protein, ModA {Azotobacter vinelandii}
elkvvtatnflgtleqlagqfakqtghavvissgssgpvyaqivngapynvffsadeksp
ekldnqgfalpgsrftyaigklvlwsakpglvdnqgkvlagngwrhiaisnpqiapygla
gtqvlthlglldkltaqeriveansvgqahsqtasgaadlgfvalaqiiqaaakipgshw
fppanyyepivqqavitkstaekanaeqfmswmkgpkavaiikaagyvlpq
>d1atha_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
rrvwelskansrfattfyqhladskndndniflsplsistafamtklgacndtlqqlmev
fkfdtisektsdqihfffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselv
ygaklqpldfkenaeqsraainkwvsnktegritdvipseaineltvlvlvntiyfkglw
kskfspentrkelfykadgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlil
pkpekslakvekeltpevlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfs
peksklpgivaegrddlyvsdafhkaflevneegseaaastavviagrslnpnrvtfkan
rpflvfirevplntiifmgrvanpcv
>d1athb_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
vwelskansrfattfyqhladskndndniflsplsistafamtklgacndtlqqlmevfk
fdtisektsdqihfffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselvyg
aklqpldfkenaeqsraainkwvsnktegritdvipseaineltvlvlvntiyfkglwks
kfspentrkelfykadgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpk
pekslakvekeltpevlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspe
ksklpgivaegrddlyvsdafhkaflevneegseaaastavviagrslnpnrvtfkanrp
flvfirevplntiifmgrvanpc
>d1atia1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1atia2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1atib1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1atib2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnritkkryrldhllkeqpeevlkrlyramev
eeenlhalvqammqaperaggamtaagvldpasgepgdwtppryfnmmfqdlrgprggrg
llaylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmei
eyfvrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfph
gslelegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviep
sagvdrgvlallaeaftreelpngeerivlklkp
>d1atja_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjb_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjc_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjd_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atje_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atjf_ 1.90.1.1.6 Peroxidase {Horseradish (Armoracia rusticana)}
qltptfydnscpnvsnivrdtivnelrsdpriaasilrlhfhdcfvngcdasilldntts
frtekdafgnansargfpvidrmkaavesacprtvscadlltiaaqqsvtlaggpswrvp
lgrrdslqafldlananlpapfftlpqlkdsfrnvglnrssdlvalsgghtfgknqcrfi
mdrlynfsntglpdptlnttylqtlrglcplngnlsalvdfdlrtptifdnkyyvnleeq
kgliqsdqelfsspnatdtiplvrsfanstqtffnafveamdrmgnitpltgtqgqirln
crvvns
>d1atk__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1atla_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atlb_ 4.71.1.7.2 Snake venom metalloprotease {Western diamonback rattlesnake (Crotalus atrox), atrolysin C}
lpqryielvvvadhrvfmkynsdlntirtrvheivnfingfyrslnihvsltdleiwsne
dqiniqsassdtlnafaewretdllnrkshdnaqlltaieldeetlglaplgtmcdpkls
igivqdhspinllmgvtmahelghnlgmehdgkdclrgaslcimrpgltkgrsyefsdds
mhyyerflkqykpqcilnkp
>d1atna1 3.46.1.1.4 (1-146) Actin {Bovine (Bos taurus), pancreas}
dedettalvcdngsglvkagfagddapravfpsivgrprhqgvmvgmgqkdsyvgdeaqs
krgiltlkypiehgiitnwddmekiwhhtfynelrvapeehptllteaplnpkanrekmt
qimfetfnvpamyvaiqavlslyasg
>d1atna2 3.46.1.1.4 (147-372) Actin {Bovine (Bos taurus), pancreas}
rttgivldsgdgvthnvpiyegyalphaimrldlagrdltdylmkiltergysfvttaer
eivrdikeklcyvaldfenemataassssleksyelpdgqvitignerfrcpetlfqpsf
igmesagihettynsimkcdidirkdlyannvmsggttmypgiadrmqkeitalapstmk
ikiiapperkysvwiggsilaslstfqqmwitkqeydeagpsivhr
>d1atnd_ 4.122.1.1.3 Deoxyribonuclease I {Bovine (Bos taurus)}
lkiaafnirtfgetkmsnatlasyivrivrrydivliqevrdshlvavgklldylnqddp
ntyhyvvseplgrnsykerylflfrpnkvsvldtyqyddgcgncgndsfsrepavvkfss
hstkvkefaivalhsapsdavaeinslydvyldvqqkwhlndvmlmgdfnadcsyvtssq
wssirlrtsstfqwlipdsadttatstncaydrivvagsllqssvvpgsaapfdfqaayg
lsnemalaisdhypvevtlt
>d1atpe_ 4.117.1.1.5 cAMP-dependent PK, catalytic subunit {Mouse (Mus musculus)}
vkeflakakedflkkwetpsqntaqldqfdriktlgtgsfgrvmlvkhkesgnhyamkil
dkqkvvklkqiehtlnekrilqavnfpflvklefsfkdnsnlymvmeyvaggemfshlrr
igrfsepharfyaaqivltfeylhsldliyrdlkpenllidqqgyiqvtdfgfakrvkgr
twtlcgtpeylapeiilskgynkavdwwalgvliyemaagyppffadqpiqiyekivsgk
vrfpshfssdlkdllrnllqvdltkrfgnlkngvndiknhkwfattdwiaiyqrkveapf
ipkfkgpgdtsnfddyeeeeirvsinekcgkeftef
>d1atr_1 3.46.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1atr_2 3.46.1.1.1 (189-384) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggvfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgdk
>d1ats_1 3.46.1.1.1 (2-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
skgpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvam
nptntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevss
mvltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaai
aygldkk
>d1ats_2 3.46.1.1.1 (189-383) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggefdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaailsgd
>d1atta_ 5.1.1.1.5 Antithrombin {Bovine (Bos taurus)}
vedvctakprdipvnpmciyrategqgseqkipgatnrrvwelskanshfatafyqhlad
sknnndniflsplsistafamtklgacnntltqlmevfkfdtisektsdqihfffaklnc
rlyrkanksselvsanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinq
wisnktegritdvippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescs
vlmmyqeskfryrrvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewl
deltetllvvhmprfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdaf
hkaflevneegseaaastvisiagrslrvtfkanrpflvlirevalntiifmgrvanpcv
d
>d1attb_ 5.1.1.1.5 Antithrombin {Bovine (Bos taurus)}
kprdipvnpmciyrssqkipgatnrrvwelskanshfatafyqhladsknnndniflspl
sistafamtklgacnntltqlmevfkfdtisektsdqihfffaklncrlyrkanksselv
sanrlfgdksitfnetyqdisevvygaklqpldfkgnaeqsrltinqwisnktegritdv
ippqaineftvlvlvntiyfkglwkskfspentrkelfykadgescsvlmmyqeskfryr
rvaestqvlelpfkgdditmvlilpklektlakveqeltpdmlqewldeltetllvvhmp
rfriedsfsvkeqlqdmgledlfspeksrlpgivaegrsdlyvsdafhkaflevneegse
aaastvisiagrslnsdrvtfkanrpflvlirevalntiifmgrvanpcvd
>d1atu__ 5.1.1.1.4 Antitrypsin, alpha-1 {Human (Homo sapiens)}
ptfnkitpnlaefafslyrqlahqsnstnilfspvsiaaafamlslgakgdthdeilegl
nfnlteipeaqihegfqellrtlnqpdsqlqlttgnglflseglklvdkfledvkklyhs
eaftvnfgdteeakkqindyvekgtqgkivdlvkeldrdtvfalvnyiffkgkwerpfev
kdteeedfhvdqvttvkvpmmkrlgmfniqhckklsswvllmkylgnataifflpdegkl
qhlenelthdiitkflenedrrsaslhlpklsitgtydlksvlgqlgitkvfsngadlsg
vteeaplklskavhkavltidekgteaagamfleaipmsippevkfnkpfvfliieqntk
aplfmgrvvnptqk
>d1atx__ 7.9.1.1.6 Sea anemone toxin IA {Sea anemone (Anemonia sulcata)}
gaaclcksdgpntrgnsmsgtiwvfgcpsgwnncegraiigycckq
>d1atza_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
qpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvpwnv
vpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvsvds
vdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlgnsf
lhkl
>d1atzb_ 3.52.1.1.2 von Willebrand factor A3 domain {Human (Homo sapiens)}
dcsqpldvillldgsssfpasyfdemksfakafiskanigprltqvsvlqygsittidvp
wnvvpekahllslvdvmqreggpsqigdalgfavryltsemhgarpgaskavvilvtdvs
vdsvdaaadaarsnrvtvfpigigdrydaaqlrilagpagdsnvvklqriedlptmvtlg
nsflhklcs
>d1au0__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au1a_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au1b_ 1.27.1.3.3 Interferon-beta {Human (Homo sapiens)}
msynllgflqrssnfqcqkllwqlngrleyclkdrmnfdipeeikqlqqfqkedaaltiy
emlqnifaifrqdssstgwnetivenllanvyhqinhlktvleeklekedftrgklmssl
hlkryygrilhylkakeyshcawtivrveilrnfyfinrltgylrn
>d1au2__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au3__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au4__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1au7a1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7a2 1.36.1.1.2 (5-76) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleeaeq
>d1au7b1 1.4.1.1.6 (103-160) Pit-1 POU homeodomain {Rat (Rattus norvegicus)}
krrttisiaakdalerhfgehskpssqeimrmaeelnlekevvrvwfcnrrqrekrvk
>d1au7b2 1.36.1.1.2 (5-74) Pit-1 {Rat (Rattus norvegicus)}
gmraleqfanefkvrriklgytqtnvgealaavhgsefsqtticrfenlqlsfknacklk
ailskwleea
>d1au8a_ 2.41.1.2.20 Cathepsin G {Human (Homo sapiens)}
iiggresrphsrpymaylqiqspagqsrcggflvredfvltaahcwgsninvtlgahniq
rrentqqhitarrairhpqynqrtiqndimllqlsrrvrrnrnvnpvalpraqeglrpgt
lctvagwgrvsmrrgtdtlrevqlrvqrdrqclrifgsydprrqicvgdrrerkaafkgd
sggpllcnnvahgivsygkssgvppevftrvssflpwirttmrs
>d1au9__ 3.33.1.1.7 Subtilisin Novo/BPN' {Bacillus amyloliquefaciens}
aqsvpygvsqikapalhsqgycgsnvkvavidsgidsshpdlkvaggasfvpsetnpfqd
nnshgthvagtvaalnnsigvlgvapcaslyavkvlgadgsgqyswiingiewaiannmd
vinmslggpsgsaalkaavdkavasgvvvvaaagnegtsgssstvgypakypsviavgav
dssnqrasfssvgpeldvmapgvsicstlpgnkygaksgtsmasphvagaaalilskhpn
wtntqvrsslentttklgdsfyygkglinvqaaaq
>d1aua_1 1.5.3.1.1 (4-96) N-terminal domain of phosphatidylinositol transfer protein sec14p {Baker's yeast (Saccharomyces cerevisiae)}
qqekeflesypqncppdalpgtpgnldsaqekalaelrklledagfierlddstllrflr
arkfdvqlakemfencekwrkdygtdtilqdfh
>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
>d1aub__ 1.4.5.1.2 N-terminal Zn binding domain of HIV integrase {Human immunodeficiency virus, type 2, HIV-2}
flekiepaqeehekyhsnvkelshkfgipnlvarqivnscaqcqqk
>d1auc__ 3.38.1.1.4 Thioredoxin {Human (Homo sapiens)}
mvkqiesktafqealdaagdklvvvdfsatwcgpckmikpffhslsekysnviflevdvd
dcqdvasecevkcmptfqffkkgqkvgefsgankekleatinelv
>d1auda_ 4.47.7.1.2 Splicesomal U1A protein {Human (Homo sapiens)}
avpetrpnhtiyinnlnekikkdelkkslhaifsrfgqildilvsrslkmrgqafvifke
vssatnalrsmqgfpfydkpmriqyaktdsdiiakmkgtfv
>d1auea_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
lwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdlmea
qewcrkymksgnvkdltqawdlyyhvfrrisk
>d1aueb_ 1.25.7.1.1 FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP) {Human (Homo sapiens)}
ilwhemwhegleeasrlyfgernvkgmfevleplhammergpqtlketsfnqaygrdlme
aqewcrkymksgnvkdltqawdlyyhvfrriskq
>d1auga_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augb_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augc_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1augd_ 3.47.3.1.2 Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase) {Bacillus amyloliquefaciens}
mekkvlltgfdpfggetvnpsweavkrlngaaegpasivseqvptvfykslavlreaikk
hqpdiiicvgqaggrmqitpervainlnearipdnegnqpvgedisqggpaaywtglpik
riveeikkegipaavsytagtfvcnhlfyglmdeisrhhphirggfihipyipeqtlqks
apslsldhitkalkiaavtaavheddietg
>d1auia_ 4.130.1.3.3 Protein phosphatase-2B (PP-2B, calcineurin A subunit) {Human (Homo sapiens)}
tdrvvkavpfppshrltakevfdndgkprvdilkahlmkegrleesvalriitegasilr
qeknlldidapvtvcgdihgqffdlmklfevggspantrylflgdyvdrgyfsiecvlyl
walkilypktlfllrgnhecrhlteyftfkqeckikyservydacmdafdclplaalmnq
qflcvhgglspeintlddirkldrfkeppaygpmcdilwsdpledfgnektqehfthntv
rgcsyfysypavceflqhnnllsilraheaqdagyrmyrksqttgfpslitifsapnyld
vynnkaavlkyennvmnirqfncsphpywlpnfmdvftwslpfvgekvtemlvnvlnics
ddelgseedgfdgataaarkevirnkiraigkmarvfsvlreesesvltlkgltptgmlp
sgvlsggkqtlqsatveaieadeaikgfspqhkitsfeeakgldrinermppr
>d1auib_ 1.42.1.5.20 Calcineurin regulatory subunit (B-chain) {Human (Homo sapiens)}
syplemcshfdadeikrlgkrfkkldldnsgslsveefmslpelqqnplvqrvidifdtd
gngevdfkefiegvsqfsvkgdkeqklrfafriydmdkdgyisngelfqvlkmmvgnnlk
dtqlqqivdktiinadkdgdgrisfeefcavvggldihkkmvvdv
>d1auj__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1auk__ 3.64.1.2.1 Arylsulfatase A {Human (Homo sapiens)}
rppnivlifaddlgygdlgcyghpssttpnldqlaagglrftdfyvpvslxtpsraallt
grlpvrmgmypgvlvpssrgglpleevtvaevlaargyltgmagkwhlgvgpegaflpph
qgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpipllanlsveaqppwlpgle
arymafahdlmadaqrqdrpfflyyashhthypqfsgqsfaersgrgpfgdslmeldaav
gtlmtaigdlglleetlviftadngpetmrmsrggcsgllrcgkgttyeggvrepalafw
pghiapgvthelassldllptlaalagaplpnvtldgfdlsplllgtgksprqslffyps
ypdevrgvfavrtgkykahfftqgsahsdttadpachasssltaheppllydlskdpgen
ynllggvagatpevlqalkqlqllkaqldaavtfgpsqvargedpalqicchpgctprpa
cchcp
>d1aum__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
ldirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgpgat
leemmtacqg
>d1aun__ 2.23.1.1.1 Pathogenesis-related protein 5d {Common tobacco (Nicotiana tabacum)}
sgvfevhnncpytvwaaatpvgggrrlergqswwfwappgtkmariwgrtncnfdgagrg
wcqtgdcggvleckgwgkppntlaeyalnqfsnldfwdisvidgfnipmsfgptkpgpgk
chgiqctaningecpgslrvpggcnnpcttfggqqycctqgpcgptelsrwfkqrcpday
sypqddptstftctswttdykvmfcpyg
>d1auoa_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1auob_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aup_1 3.2.1.7.1 (205-449) Glutamate dehydrogenase {Clostridium symbiosum}
rpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelgakavtlsgpdg
yiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkvdiimpcatqn
dvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavnaggvlvvgfem
sqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivgfqkiadamma
qgiaw
>d1aup_2 3.48.1.1.1 (1-192) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpylgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvl
>d1auq__ 3.52.1.1.3 von Willebrand factor A1 domain {Human (Homo sapiens)}
disepplhdfycsrlldlvflldgssrlseaefevlkafvvdmmerlrisqkwvrvavve
yhdgshayiglkdrkrpselrriasqvkyagsqvastsevlkytlfqifskidrpeasri
alllmasqepqrmsrnfvryvqglkkkkvivipvgigphanlkqirliekqapenkafvl
ssvdeleqqrdeivsylcdlapeapppt
>d1aura_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1aurb_ 3.59.1.12.1 Carboxylesterase {Pseudomonas fluorescens}
mteplilqpakpadacviwlhglgadrydfmpvaealqesllttrfvlpqaptrpvting
gyempswydikamsparsisleelevsakmvtdlieaqkrtgidasriflagfsqggavv
fhtafinwqgplggvialstyaptfgdelelsasqqripalclhgqyddvvqnamgrsaf
ehlksrgvtvtwqeypmghevlpqeihdigawlaarlg
>d1ausl1 3.1.12.1.2 (148-463) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
fqgpphgiqverdklnkygrpllgctikpklglsaknygravyeclrggldftkddenvn
sqpfmrwrdrflfcaealykaqaetgeikghylnatagtcedmmkravfarelgvpivmh
dyltggftanttlshycrdnglllhihramhavidrqknhgmhfrvlakalrlsggdhih
sgtvvgklegerditlgfvdllrddytekdrsrgiyftqswvstpgvlpvasggihvwhm
palteifgddsvlqfgggtlghpwgnapgavanrvaleacvqarnegrdlaregntiire
atkwspelaaacevwk
>d1ausl2 4.47.9.1.2 (20-147) Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
ykltyytpeyetldtdilaafrvspqpgvppeeagaavaaesstgtwttvwtdgltnldr
ykgrcyhiepvageenqyicyvaypldlfeegsvtnmftsivgnvfgfkalralrledlr
ipvayvkt
>d1auss_ 4.55.1.1.2 Ribulose 1,5-bisphosphate carboxylase-oxygenase {Spinach (Spinacia oleracea)}
mqvwpilnlkkyetlsylpplttdqlarqvdyllnnkwvpclefetdhgfvyrehhnspg
yydgrywtmwklpmfgctdpaqvlneleeckkeypnafiriigfdsnrevqcisfiaykp
agy
>d1autc_ 2.41.1.2.36 Activated protein c (autoprothrombin IIa) {Human (Homo sapiens)}
lidgkmtrrgdspwqvvlldskkklacgavlihpswvltaahcmdeskkllvrlgeydlr
rwekweldldikevfvhpnysksttdndiallhlaqpatlsqtivpiclpdsglaereln
qagqetlvtgwgyhssrekeakrnrtfvlnfikipvvphnecsevmsnmvsenmlcagil
gdrqdacegdsggpmvasfhgtwflvglvswgegcgllhnygvytkvsryldwihghird
>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
>d1auua_ 2.31.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auub_ 2.31.2.1.1 SacY {Bacillus subtilis}
mkikrilnhnaivvkdqneekillgagiafnkkkndivdpskiektfirkdtpdy
>d1auva1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlrng
vkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auva2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d1auvb1 3.24.1.5.1 (110-213) Synapsin Ia domain {Bovine (Bos taurus)}
gaaarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdxevlr
ngvkvvrslkpdfvlirqhafsxarngdyrslviglqyagipsi
>d1auvb2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqxvrlhkklgteefplinqtfypnhkexlssttypvvvkxgha
hsgxgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykayxrtsvsg
nwktntgsaxleqiaxsdryklwvdtcseifggldicavealhgkdgrdhiievvgssxp
ligdhqdedkqlivelvvnkxaqa
>d1auwa_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwb_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwc_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auwd_ 1.117.1.1.5 Argininosuccinate lyase/delta-crystallin {Domestic duck (Anas platyrhynchos), delta-crystallin}
tdpimeklnssiaydqrlsevdiqgsmayakalekagiltktelekilsglekiseewsk
gvfvvkqsdedintanerrlkeligdiagklhtgrsrndqvvtdlklfmknslsiisthl
lqliktlveraaieidvilpgythlqkaqpirwsqfllshavaltrdserlgevkkrinv
lplgsgalagnpldidremlrselefasislnsmdaiserdfvveflsfatllmihlskm
aedliiystsefgfltdsdafstgsslmpqkknpdslelirskagrvfgrlasilmvlkg
lpstynkdlqedkeavfdvvdtltavlqvatgvistlqiskenmekaltpemlatdlaly
lvrkgvpfrqahtasgkavhlaetkgitinklsledlksispqfssdvsqvfnfvnsveq
ytalggtakssvttqieqlrelmkkqk
>d1auxa1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxa2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auxb1 3.24.1.5.1 (112-213) Synapsin Ia domain {Bovine (Bos taurus)}
aarvllvidephtdwakyfkgkkihgeidikveqaefsdlnlvahanggfsvdmevlrng
vkvvrslkpdfvlirqhafsmarngdyrslviglqyagipsi
>d1auxb2 4.115.1.3.1 (214-417) Synapsin Ia, C-terminal domain {Bovine (Bos taurus)}
nslhsvynfcdkpwvfaqmvrlhkklgteefplinqtfypnhkemlssttypvvvkmgha
hsgmgkvkvdnqhdfqdiasvvaltktyattepfidakydvriqkigqnykaymrtsvsg
nwktntgsamleqiamsdryklwvdtcseifggldicavealhgkdgrdhiievvgssmp
ligdhqdedkqlivelvvnkmaqa
>d1auya_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
spltikqpfqsevlfagtkdaeasltianidsvstlttfyrhasleslwvtihptlqapt
fpttvgvcwvpaqspvtpaqitktyggqifciggaiqtlsplivkcplemmqprvkdsiq
yldspkllisitaqptappastciitvsgtlsmhsplitdtst
>d1auyb_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auyc_ 2.9.1.2.11 TYMV coat protein {Turnip yellow mosaic virus}
meidkelapqdrtvtvatvlpavpgpspltikqpfqsevlfagtkdaeasltianidsvs
tlttfyrhasleslwvtihptlqaptfpttvgvcwvpaqspvtpaqitktyggqifcigg
aiqtlsplivkcplemmqprvkdsiqyldspkllisitaqptappastciitvsgtlsmh
splitdtst
>d1auz__ 3.10.2.1.1 SpoIIaa {Bacillus subtilis}
slgidmnvkesvlcirltgeldhhtaetlkqkvtqslekddirhivlnledlsfmdssgl
gvilgrykqikqiggemvvcaispavkrlfdmsglfkiirfeqseqqalltlgvas
>d1av3__ 7.3.6.1.6 Conotoxin {Conus purpurascens, kappa-pVIIa}
crixnqkcfqhlddccsrkcnrfnkcv
>d1av4_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>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
>d1av5a_ 4.11.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {Human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av5b_ 4.11.1.1.3 Protein kinase C inhibitor-1, PKCI-1 {Human (Homo sapiens)}
ggdtifgkiirkeipakiifeddrclafhdispqapthflvipkkhisqisvaedddesl
lghlmivgkkcaadlglnkgyrmvvnegsdggqsvyhvhlhvlggrqmhwppg
>d1av6a_ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
vvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgildga
tvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeeylr
sikkqlhpskiilisdvrspstadllsnyalqnvmisilnpvasslkwrcpfpdqwikdf
yiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyylnkivrnkvv
vnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1av7__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtxmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1av8a_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1av8b_ 1.26.1.2.3 Ribonucleotide reductase R2 {Escherichia coli}
ayttfsqtkndqlkepmffgqpvnvarydqqkydifekliekqlsffwrpeevdvsrdri
dyqalpehekhifisnlkyqtlldsiqgrspnvallplisipeletwvetwafsetihsr
sythiirnivndpsvvfddivtneqiqkraegissyydeliemtsywhllgegthtvngk
tvtvslrelkkklylclmsvnaleairfyvsfacsfafaerelmegnakiirliardeal
hltgtqhmlnllrsgaddpemaeiaeeckqecydlfvqaaqqekdwadylfrdgsmigln
kdilcqyveyitnirmqavgldlpfqtrsnpipwintwlv
>d1avaa1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avaa2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1avab1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1avab2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1avac_ 2.37.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1avad_ 2.37.4.1.5 Amylase/subtilisin inhibitor {Barley (Hordeum vulgare), seed}
adpppvhdtdghelradanyyvlsanrahgggltmapghgrhcplfvsqdpngqhdgfpv
ritpygvapsdkiirlstdvrisfrayttclqstewhidselaagrrhvitgpvkdpsps
grenafriekysgaevheyklmscgdwcqdlgvfrdlkggawflgatepyhvvvfkkapp
a
>d1avba_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndasfnvetfnktnlilqgdatvsseghllltnvkgneedsmgrafysapiqindrtid
nlasfstnftfrinakniensayglafalvpvgsrpklkgrylglfnttnydrdahtvav
vfdtvsnrieidvnsirpiatescnfghnngekaevritydspkndlrvsllypsseekc
hvsatvplekevedwvsvgfsatsgskkettethnvlswsfssnfi
>d1avbb_ 2.26.1.1.15 Phytohemagglutinin-L, PHA-L, also arcelin {Kidney bean (Phaseolus vulgaris)}
sndasfnvetfnktnlilqgdatvsseghllltnvkgneedsmgrafysapiqindrtid
nlasfstnftfrinakniensayglafalvpvgsrpklkgrylglfnttnydrdahtvav
vfdtvsnrieidvnsirpiatescnfghnngekaevritydspkndlrvsllypsseekc
hvsatvplekevedwvsvgfsatsgskkettethnvlswsfssnfi
>d1avc__ 1.66.1.1.7 Annexin VI {Bovine (Bos taurus)}
yrgsirdfpdfnpsqdaetlynamkgfgsdkeaiinlitsrsnkqrqeicqnykslygkd
liadlkyeltgkferlivglmrppayadakeikdaisgigtdekclieilasrtneqihq
lvaaykdayerdleaditgdtsghfrkmlvvllqgtreeddvvsedlvqqdvqdlyeage
lkwgtdeaqfiyilgnrskqhlrlvfdeylkttgkpieasirgelsgdfeklmlavvkci
rstaeyfaerlfkamkglgtrdntlirimvsrseldmldireifrtkyekslysmikndt
sgeykktllklcggdddaagqffpeaaqvayqmwelsavarvelkgtvrpagdfnpdada
kalrkamkglgtdedtiidiithrsnaqrqqirqtfkshfgrdlmadlkselsgdlarli
lglmmppahydakqlkkamegagtdekalieilatrtnaeiqainkaykedyhktledal
ssdtsghfkrilislatgnreeggedreraredaqvaaeileiadttsgdkssletrfmm
ilctrsypdlrrvfqefvkmtnydvehtikkemsgdvrdvfvaivqsvknkplffadkly
ksmkgagteektltrimvsrseidllnirrefiekydkslhqaiegdtsghflkallaic
gg
>d1avda_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1avdb_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
rkcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtq
ptfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginift
rlrt
>d1avea_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>d1aveb_ 2.54.1.1.2 Avidin {Chicken (Gallus gallus)}
kcsltgkwtndlgsnmtigavnsrgeftgtyttavtatsneikesplhgtentinkrtqp
tfgftvnwkfsesttvftgqcfidrngkevlktmwllrssvndigddwkatrvginiftr
lrt
>e1avf.1a 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.1p 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekg
>e1avf.2j 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
vtyepmaymdaayfgeisigtppqnflvlfdtgssnlwvpsvycqsqactshsrfnpses
stystngqtfslqygsgsltgffgydtltvqsiqvpnqefglsenepgtnfvyaqfdgim
glaypalsvdeattamqgmvqegaltspvfsvylsnqqgssggavvfggvdsslytgqiy
wapvtqelywqigieefliggqasgwcsegcqaivdtgtslltvpqqymsallqatgaqe
deygqflvncnsiqnlpsltfiingvefplppssyilsnngyctvgveptylssqngqpl
wilgdvflrsyysvydlgnnrvgfataa
>e1avf.2q 2.44.1.2.11 Pepsin(ogen) {Human (Homo sapiens), progastricsin (pepsinogen C)}
avvkvplkkfksiretmkekgl
>e1avg.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1avg.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ffnektfgageadcglrplfekkqvqdqtekelfesyiegr
>d1avgi_ 2.53.1.3.1 Thrombin inhibitor {Triatomine bug (Triatoma pallidipennis)}
aegddcsiekamgdfkpeeffngtwylahgpgvtspavcqkfttsgskgftqiveigynk
fesnvkfqcnqvdnkngeqysfkckssdntefeadftfisvsydnfalvcrsitftsqpk
edrylvfertksdtdpdakeic
>d1avha_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avhb_ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcgedd
>d1avk_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignydygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avk_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avk_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avl_1 2.27.2.1.3 (212-628) Copper amine oxidase, domain 3 (catalytic) {Arthrobacter globiformis}
plrttqkpisitqpegpsftvtggnhiewekwsldvgfdvregvvlhniafrdgdrlrpi
inrasiaemvvpygdpspirswqnyfdtgeylvgqyanslelgcdclgditylspvisda
fgnpreirngicmheedwgilakhsdlwsginytrrnrrmvisffttignxdygfywyly
ldgtiefeakatgvvftsafpeggsdnisqlapglgapfhqhifsarldmaidgftnrve
eedvvrqtmgpgnergnafsrkrtvltreseavreadartgrtwiisnpesknrlnepvg
yklhahnqptlladpgssiarraafatkdlwvtryadderyptgdfvnqhsggaglpsyi
aqdrdidgqdivvwhtfglthfprvedwpimpvdtvgfklrpegffdrspvldvpan
>d1avl_2 4.15.2.1.3 (9-96) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
aspfrlasageisevqgilrtagllgpekriaylgvldpargagseaedrrfrvfihdvs
garpqevtvsvtngtvisaveldtaatg
>d1avl_3 4.15.2.1.3 (97-211) Copper amine oxidase, domains 1 and 2 {Arthrobacter globiformis}
elpvleeefevveqllatderwlkalaarnldvskvrvaplsagvfeyaeergrrilrgl
afvqdfpedsawahpvdglvayvdvvskevtrvidtgvfpvpaehgnytdpeltg
>d1avma1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avma2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avmb1 1.2.7.1.9 (1-86) Cambialistic superoxide dismutase {Propionibacterium freudenreichii}
avytlpelpydysalepyisgeimelhhdkhhkayvdgantaldklaeardkadfgaink
lekdlafnlaghvnhsvfwknmapkg
>d1avmb2 4.37.1.1.9 (87-201) Cambialistic superoxide dismutase {Propionibacterium freudenreichii, shermani}
saperptdelgaaideffgsfdnmkaqftaaatgiqgsgwaslvwdplgkrintlqfydh
qnnlpagsipllqldmwehafylqyknvkgdyvkswwnvvnwddvalrfsearva
>d1avn__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnng
hafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvhw
ntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprgl
lpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvdn
wrpaqplknrqikasfk
>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.2d 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.3e 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.3f 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.4g 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.4h 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.5i 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.5j 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.6k 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.6l 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>e1avo.7m 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
lrvqpeaqakvdvfredlctktenllgsyfpkkiseldaflkepalneanlsnlkapldi
>e1avo.7n 1.25.8.1.1 Proteasome activator reg(alpha) {Human (Homo sapiens)}
avncnekivvllqrlkpeikdvieqlnlvttwlqlqipriedgnnfgvavqekvfelmts
lhtklegfhtqiskyfsergdavtkaakqphvgdyrqlvheldeaeyrdirlmvmeirna
yavlydiilknfeklkkprg
>d1avpa_ 4.3.1.4.1 Human adenovirus 2 proteinase {Mastadenovirus h2}
mgsseqelkaivkdlgcgpyflgtydkrfpgfvsphklacaivntagretggvhwmafaw
nprsktcylfepfgfsdqrlkqvyqfeyesllrrsaiasspdrcitlekstqsvqgpnsa
acglfccmflhafanwpqtpmdhnptmnlitgvpnsmlnspqvqptlrrnqeqlysfler
hspyfrshsaqirsatsfchlknm
>d1avqa_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqb_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
shmtpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyf
htllaevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacsp
dglcsdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydpr
mkreglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avqc_ 3.43.1.7.1 lambda exonuclease {Bacteriophage lambda}
tpdiilqrtgidvraveqgddawhklrlgvitasevhnviakprsgkkwpdmkmsyfhtl
laevctgvapevnakalawgkqyendartlfeftsgvnvtespiiyrdesmrtacspdgl
csdgnglelkcpftsrdfmkfrlggfeaiksaymaqvqysmwvtrknawyfanydprmkr
eglhyvvierdekymasfdeivpefiekmdealaeigfvfgeqwr
>d1avr__ 1.66.1.1.5 Annexin V {Human (Homo sapiens)}
qvlrgtvtdfpgfderadaetlrkamkglgtdeesiltlltsrsnaqrqeisaafktlfg
rdllddlkseltgkfeklivalmkpsrlydayelkhalkgagtnekvlteiiasrtpeel
raikqvyeeeygssleddvvgdtsgyyqrmlvvllqanrdpdagideaqveqdaqalfqa
gelkwgtdeekfitifgtrsvshlrkvfdkymtisgfqieetidretsgnleqlllavvk
sirsipaylaetlyyamkgagtddhtlirvmvsrseidlfnirkefrknfatslysmikg
dtsgdykkallllcged
>d1avsa_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
qaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieevd
edgsgtidfeeflvmmvrqmk
>d1avsb_ 1.42.1.5.1 Troponin C {Chicken (Gallus gallus)}
qqaearaflseemiaefkaafdmfdadgggdistkelgtvmrmlgqnptkeeldaiieev
dedgsgtidfeeflvmmvrqmk
>d1avt__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtxmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1avu__ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avv__ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avwa_ 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1avwb_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsefnnyklvfcpqdkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avxa_ 2.41.1.2.2 Trypsin(ogen) {Porcine (Sus scrofa)}
ivggytcaansipyqvslnsgshfcggslinsqwvvsaahcyksriqvrlgehnidvleg
neqfinaakiithpnfngntldndimliklsspatlnsrvatvslprscaaagteclisg
wgntkssgssypsllqclkapvlsdssckssypgqitgnmicvgfleggkdscqgdsggp
vvcngqlqgivswgygcaqknkpgvytkvcnyvnwiqqtiaan
>d1avxb_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqkcgdigisidhddgtrrlvvsknkplvvqfqkld
>d1avza_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
vplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpgpgv
rypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrlafhh
varelhpeyf
>d1avzb_ 4.80.1.1.1 Regulatory factor Nef {Human immunodeficiency virus, type 1, HIV-1}
tpqvplrpmtykaavdlshflkekggleglihsqrrqdildlwiyhtqgyfpdwqnytpg
pgvrypltfgwcyklvpvepdkveeankgentsllhpvslhgmddperevlewrfdsrla
fhhvarelhpeyf
>d1avzc_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
tlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1aw0__ 4.47.16.1.2 Menkes copper-transporting ATPase {Human (Homo sapiens)}
ltqetvinidgmtcnscvqsiegviskkpgvksirvslansngtveydplltspetlrga
iedmgfdatlsd
>d1aw1a_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1b_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1d_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1e_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1g_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1h_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw1j_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw1k_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2a_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2b_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2d_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2e_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2g_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2h_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw2j_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeaka
>d1aw2k_ 3.1.1.1.11 Triosephosphate isomerase {Vibrio marinus}
rhpvvmgnwklngskemvvdllnglnaelegvtgvdvavappalfvdlaertlteagsai
ilgaqntdlnnsgaftgdmspamlkefgathiiighserreyhaesdefvakkfaflken
gltpvlcigesdaqneagetmavcarqldavintqgvealegaiiayepiwaigtgkaat
aedaqrihaqirahiaekseavaknvviqyggsvkpenaaayfaqpdidgalvggaalda
ksfaaiakaaaeak
>d1aw3__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1aw5__ 3.1.9.3.1 5-aminolevulinate dehydratase (porphobilinogen synthase) {Baker's yeast (Saccharomyces cerevisiae)}
htaefletepteissvlaggynhpllrqwqserqltknxlifplfisdnpddfteidsap
ninrigvnrlkdylkplvakglrsvilfgvplipgtkdpvgtaaddpagpviqgirfire
kfpelyiicdvclceytshghcgvlyddgtinrersvsrlaavavnyakagahcvapsdx
idgrirdikrglinanlahktfvlsyaakfsgnlygpacyqlppagrglarralerdxse
gadgiivkpstfyldivrdaseickdlpicayhvsgeyaxlhaaaekgvvdlktiafesh
qgflragarliitylapefldwlde
>d1aw6__ 7.32.1.1.1 Gal4 {Baker's yeast (Saccharomyces cerevisiae)}
mkllssieqacdicrlkklkcskekpkcakclknnwecryspk
>d1aw7a1 2.35.2.2.3 (1-93) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7a2 4.13.7.1.3 (94-194) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7b1 2.35.2.2.3 (201-293) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7b2 4.13.7.1.3 (294-394) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7c1 2.35.2.2.3 (401-493) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7c2 4.13.7.1.3 (494-594) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>d1aw7d1 2.35.2.2.3 (601-693) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
stndnikdlldwyssgsdtftnsevldnslgsmrikntdgsisliifpspyyspaftkge
kvdlntkrtkksqhtsegtyihfqisgvtntek
>d1aw7d2 4.13.7.1.3 (694-794) Toxic shock syndrome toxin-1 (TSST-1) {Staphylococcus aureus}
lptpielplkvkvhgkdsplkywpkfdkkqlaistldfeirhaltqihglyrssdktggy
wkitmndgstyqsdlskkfeyntekppinideiktieaein
>e1aw8.1a 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.1b 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>e1aw8.2d 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
mirtmlqgklhrvkvthadlhyeg
>e1aw8.2e 2.46.2.1.1 Pyruvoyl dependent aspartate decarboxylase, ADC {Escherichia coli}
caidqdfldaagileneaidiwnvtngkrfstyaiaaergsriisvngaaahcasvgdiv
iiasfvtmpdeeartwrpnvayfegdnemk
>d1aw9_1 1.48.1.1.18 (83-217) Glutathione S-transferase {Maize (Zea mays), type III}
gtdllpatasaaklevwleveshhfypnasplvfqllvrpllggapdaavvdkhaeqlak
vldvyeahlarnkylagdeftladanhasyllylsktpkaglvaarphvkawweaivarp
afqktvaaiplpppp
>d1aw9_2 3.38.1.5.18 (2-82) Glutathione S-transferase {Maize (Zea mays), type III}
aplklygmplspnvvrvatvlnekgldfeivpvdlttgahkqpdflalnpfgqipalvdg
devlfesrainryiaskyase
>d1awba_ 5.7.1.2.1 Inositol monophosphatase {Human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awbb_ 5.7.1.2.1 Inositol monophosphatase {Human (Homo sapiens)}
wqecmdyavtlarqagevvceaiknemnvmlksspvdlvtatdqkvekmlissikekyps
hsfigeesvaageksiltdnptwiidpidgttnfvhrfpfvavsigfavnkkiefgvvys
cvegkmytarkgkgafcngqklqvsqqeditksllvtelgssrtpetvrmvlsnmeklfc
ipvhgirsvgtaavnmclvatggadayyemgihcwdvagagiivteaggvlmdvtggpfd
lmsrrviaannrilaeriakeiqviplqrdde
>d1awca_ 1.4.3.16.5 GA binding protein (GABP) alpha {Mouse (Mus musculus)}
iqlwqfllelltdkdardciswvgdegefklnqpelvaqkwgqrknkptmnyeklsralr
yyydgdmickvqgkrfvykfvcdlktligysaaelnrlvieceqkklarm
>d1awcb_ 1.110.2.1.2 GA bindinig protein (GABP) beta 1 {Mouse (Mus musculus)}
dlgkklleaaragqddevrilmangapfttdwlgtsplhlaaqyghfsttevllragvsr
dartkvdrtplhmaaseghanivevllkhgadvnakdmlkmtalhwatehnhqevvelli
kygadvhtqskfcktafdisidngnedlaeilq
>d1awd__ 4.13.6.1.6 2Fe-2S ferredoxin {Chlorella fusca}
ykvtlktpsgeetiecpedtyildaaeeagldlpyscragacsscagkvesgevdqsdqs
flddaqmgkgfvltcvayptsdvtilthqeaaly
>d1awe__ 2.49.1.1.8 Son of sevenless-1 (sos-1) {Human (Homo sapiens)}
mneiqknidgwegkdigqccnefimegtltrvgakherhiflfdglmiccksnhgqprlp
gasnaeyrlkekffmrkvqindkddtneykhafeiilkdensvifsaksaeeknnwmaal
islqyrstle
>e1awf.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1awf.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesyi
>e1awh.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1awh.2c 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
tfgsgeadcglrplfekksledkterellesyidgr
>e1awh.2d 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>d1awia_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1awib_ 4.86.1.1.2 Profilin (actin-binding protein) {Human (Homo sapiens)}
gwnayidnlmadgtcqdaaivgykdspsvwaavpgktfvnitpaevgvlvgkdrssfyvn
gltlggqkcsvirdsllqdgefsmdlrtkstggaptfnvtvtktdktlvllmgkegvhgg
linkkcyemashlrrsqy
>d1awj__ 2.30.2.1.9 IL-2 inducible T-cell (Itc) kinase {Mouse (Mus musculus)}
kkplpptpednrrsfqepeetlvialydyqtndpqelalrcdeeyylldsseihwwrvqd
knghegyapssylveks
>d1awo__ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
slfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvs
>d1awpa_ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1awpb_ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dpavtyyrleevakrntaeetwmvihgrvyditrflsehpggeellleqagadatesfed
lghspdaremlkqyyigdvhpndlkp
>d1awqa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awra_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awre_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awrf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awsa_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awta_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awte_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awtf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfx
cqggdftrhngtggksiygekfedenfilkhtgpgilsxanagpntngsqffictaktew
ldgkhvvfgkvkegxniveaxerfgsrngktskkitiadcgqle
>d1awua_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awva_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvb_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvc_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvd_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awve_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1awvf_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
vnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgfm
cqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictaktew
ldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1aww__ 2.30.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awx__ 2.30.2.1.13 Bruton's tyrosine kinase {Human (Homo sapiens)}
gsmstselkkvvalydympmnandlqlrkgdeyfileesnlpwwrardkngqegyipsny
vteaeds
>d1awz__ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1ax0__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax1__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax2__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ax3__ 2.74.3.1.1 Glucose permease IIa domain, IIa-glc {Bacillus subtilis}
miaeplqneigeevfvspitgeihpitdvpdqvfsgkmmgdgfailpsegivvspvrgki
lnvfptkhaiglqsdggreilihfgidtvslkgegftsfvsegdrvepgqkllevdldav
kpnvpslmtpivftnlaegetvsikasgsvnreqedivkiek
>d1ax4a_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4b_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4c_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax4d_ 3.57.1.2.2 Tryptophan indol-lyase (tryptophanase) {Proteus vulgaris}
akrivepfrikmvekirvpsreereaalkeagynpfllpssavyidlltdsgtnamsdhq
waamitgdeayagsrnyydlkdkakelfnydyiipahqgrgaenilfpvllkykqkegka
knpvfisnfhfdttaahvelngckainivtekafdsetyddwkgdfdikklkeniaqhga
dnivaivstvtcnsaggqpvsmsnlkevyeiakqhgifvvmdsarfcenayfikardpky
knatikevifdmykyadaltmsakxdpllnigglvairdneeiftlarqrcvpmegfvty
gglagrdmaamvqgleegteeeylhyrigqvkylgdrlreagipiqyptgghavfvdckk
lvpqipgdqfpaqavinalylesgvraveigsfllgrdpatgeqkhadmefmrltiarrv
ytndhmdyiadaliglkekfatlkglefeyeppvlrhftarlkpi
>d1ax8__ 1.27.1.1.8 Leptin (obesity protein) {Human (Homo sapiens)}
iqkvqddtktliktivtrindishtqsvsskqkvtgldfipglhpiltlskmdqtlavyq
qiltsmpsrnviqisndlenlrdllhvlafskschlpeasgletldslggvleasgyste
vvalsrlqgslqdmlwqldlspgc
>d1ax9__ 3.59.1.1.1 Acetylcholinesterase {Electric ray (Torpedo californica)}
sellvntksgkvmgtrvpvlsshisaflgipfaeppvgnmrfrrpepkkpwsgvwnasty
pnncqqyvdeqfpgfsgsemwnpnremsedclylniwvpsprpksttvmvwiygggfysg
sstldvyngkylayteevvlvslsyrvgafgflalhgsqeapgnvglldqrmalqwvhdn
iqffggdpktvtifgesaggasvgmhilspgsrdlfrrailqsgspncpwasvsvaegrr
ravelgrnlncnlnsdeelihclrekkpqelidvewnvlpfdsifrfsfvpvidgeffpt
slesmlnsgnfkktqillgvnkdegsffllygapgfskdseskisredfmsgvklsvpha
ndlgldavtlqytdwmddnngiknrdglddivgdhnvicplmhfvnkytkfgngtylyff
nhrasnlvwpewmgvihgyeiefvfglplvkelnytaeeealsrrimhywatfaktgnpn
ephsqeskwplfttkeqkfidlntepmkvhqrlrvqmcvfwnqflpkllnat
>d1axaa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axab_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgsddtvleemslpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1axb__ 5.3.1.1.3 beta-Lactamase, class A {Escherichia coli, TEM-1}
hpetlvkvkdaedqlgarvgyieldlnsgkilesfrpeerfpmmstfkvllcgavlsrid
agqeqlgrrihysqndlveyspvtekhltdgmtvrelcsaaitmsdntaanlllttiggp
keltaflhnmgdhvtrldrwepelneaipnderdttmpvamattlrklltgelltlasrq
qlidwmeadkvagpllrsalpagwfiadksgagergsrgiiaalgpdgkpsrivviyttg
sqatmdernrqiaeigaslikhw
>d1axca1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axca2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axcc1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axcc2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axce1 4.105.1.2.3 (1-126) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
mfearlvqgsilkkvlealkdlineacwdisssgvnlqsmdsshvslvqltlrsegfdty
rcdrnlamgvnltsmskilkcagnediitlraednadtlalvfeapnqekvsdyemklmd
ldveql
>d1axce2 4.105.1.2.3 (127-255) Prolifirating cell nuclear antigen (PCNA) {Human (Homo sapiens)}
gipeqeyscvvkmpsgefaricrdlshigdavviscakdgvkfsasgelgngniklsqts
nvdkeeeavtiemnepvqltfalrylnfftkatplsstvtlsmsadvplvveykiadmgh
lkyylapki
>d1axda1 1.48.1.1.17 (81-210) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalm
>d1axda2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1axdb1 1.48.1.1.17 (81-210) Glutathione S-transferase {Maize (Zea mays), type I}
ellregnleeaamvdvwieveanqytaalnpilfqvlispmlggttdqkvvdenleklkk
vlevyearltkckylagdflsladlnhvsvtlclfatpyasvldayphvkawwsglmerp
svqkvaalm
>d1axdb2 3.38.1.5.17 (1-80) Glutathione S-transferase {Maize (Zea mays), type I}
apmklygavmswnltrcataleeagsdyeivpinfataehkspehlvrnpfgqvpalqdg
dlylfesraickyaarknkp
>d1axea1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axea2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axeb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplwtpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axeb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggvglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axfa_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1axfb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahky
>d1axfc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1axfd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahky
>d1axga1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axga2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgb1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgb2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgc1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgc2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axgd1 2.31.1.2.2 (1-174,325-374) Alcohol dehydrogenase {Human (Homo sapiens)}
stagkvikckaavlweekkpfsieevevappkahevrikmvatgicrsddhvvsgtlvtp
lpviagheaagivesigegvttvrpgdkviplftpqcgkcrvckhpegnfclkndlsmpr
gtmqdgtsrftcrgkpihhflgtstfsqytvvdeisvakidaasplekvcligcXkdsvp
klvadfmakkfaldplithvlpfekinegfdllrsgesirtiltf
>d1axgd2 3.2.1.1.2 (175-324) Alcohol dehydrogenase {Human (Homo sapiens), different isozymes}
gfstgygsavkvakvtqgstcavfglggaglsvimgckaagaariigvdinkdkfakake
vgatecvnpqdykkpiqevltemsnggvdfsfevigrldtmvtalsccqeaygvsvivgv
ppdsqnlsmnpmlllsgrtwkgaifggfks
>d1axh__ 7.3.6.2.3 Atracotoxin-hVI (versutoxin) {Australian funnel-web spider (Hadronyche versuta)}
sptcipsgqpcpynenccsqsctfkenengntvkrcd
>d1axia_ 1.27.1.1.6 Growth hormone, somatotropin {Human (Homo sapiens)}
tiplsrlfdnamlrahrlhqlafdtyqefeeayipkeqkysflqnpqtslcfsesiptps
nreetqqksnlellrisllliqswlepvqflrsvfanslvygasdsnvydllkdleeriq
tlmgrltdgsprtgqifkqtyskfdtnshnddallknygllycfrrdmtyvatylrivqc
rsvegscgf
>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
>d1axj__ 2.38.1.5.1 FMN-binding protein {Desulfovibrio vulgaris, strain Miyazaki F}
mlpgtffevlknegvvaiatqgedgphlvntwnsylkvldgnrivvpvggmhkteanvar
dervlmtlgsrkvagrngpgtgflirgsaafrtdgpefeaiarfkwaraalvitvvsaeq
tl
>d1axka1 2.26.1.2.3 (1-156,342-393) Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnXgsvfwepksyfnpstwekadgys
nggvfnctwrannvnftndgklklgltss
>d1axka2 2.26.1.10.2 (157-341) Xylanase II {Bacillus subtilis}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitfsnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1axkb1 2.26.1.2.3 (1-156,342-394) Bacillus 1-3,1-4-beta-glucanase {Bacillus macerans}
fdcaeyrstniygyglyevsmkpakntgivssfftytgpahgtqwdeidieflgkdttkv
qfnyytngvgghekvislgfdaskgfhtyafdwqpgyikwyvdgvlkhtatanipstpgk
immnlwngtgvddwlgsynganplyaeydwvkytsnXgsvfwepksyfnpstwekadgys
nggvfnctwrannvnftndgklklgltssa
>d1axkb2 2.26.1.10.2 (157-341) Xylanase II {Bacillus subtilis}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitfsnhvnawkshgmnlgsnwayqvmategyqssgss
nvtvw
>d1axma_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kkpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxd
tdgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqk
ailflplpvs
>d1axmb_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axmc_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpv
>d1axmd_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
pkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdtd
gllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqkai
lflplpv
>d1axme_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axmf_ 2.37.1.1.3 Acidic FGF {Human (Homo sapiens)}
kpkllycsngghflrilpdgtvdgtrdrsdqhiqlqlsaesvgevyikstetgqylaxdt
dgllygsqtpneeclflerleenhyntyiskkhaeknwfvglkkngsckrgprthygqka
ilflplpvs
>d1axn__ 1.66.1.1.2 Annexin III {Human (Homo sapiens)}
sasiwvghrgtvrdypdfspsvdaeaiqkairgigtdekmlisiltersnaqrqlivkey
qaaygkelkddlkgdlsghfehlmvalvtppavfdakqlkksmkgagtnedalieilttr
tsrqmkdisqayytvykkslgddissetsgdfrkalltladgrrdeslkvdehlakqdaq
ilykagenrwgtdedkfteilclrsfpqlkltfdeyrnisqkdivdsikgelsghfedll
laivncvrntpaflaerlhralkgigtdeftlnrimvsrseidlldirtefkkhygysly
saiksdtsgdyeitllkicggdd
>d1axq__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckytdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1axr__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
svrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqqh
yyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglgn
gglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpwekar
peftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndfn
lkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfks
skfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktca
ytnhtvlpealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslvee
gavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwlv
lcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylerey
kvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapgy
hmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagtea
sgtgnmkfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyyd
ripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalykn
prewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlpapdekip
>d1axsa1 2.1.1.1.95 (1-107) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsa2 2.1.1.2.97 (108-211) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axsb1 2.1.1.1.95 (1-113) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsb2 2.1.1.2.97 (114-214) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsh1 2.1.1.1.95 (1-113) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
qvqllesgaelmkpgasvkisckatgytfssfwiewvkqrpghglewigeilpgsggthy
nekfkgkatftadkssntaymqlssltsedsavyycarghsyyfydgdywgqgtsvtvss
>d1axsh2 2.1.1.2.97 (114-214) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepk
>d1axsl1 2.1.1.1.95 (1-107) Immunoglobulin (variable domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
elvltqspssmyaslgervtitckasqdinsylnwfqqkpgkspktliyrtnrlvdgvps
rfsgsgsgqdysltissleyedmgiyyclqydefpytfgsgtkleik
>d1axsl2 2.1.1.2.97 (108-211) Immunoglobulin (constant domains of L and H chains) {Oxy-cope catalytic Fab, chimeric (mouse V domains/human C1 domains)}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1axth1 2.1.1.1.119 (1-113) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
evkleesggglvqpggsmklscvvsgltfsrfwmswvrqspekglewvaeirlksdnyat
hyaesvkgkftisrddsksrlylqmnslrtedtgiyyckiyfysfsywgqgtlvtvsa
>d1axth2 2.1.1.2.117 (114-228) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
akttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsd
lytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1axtl1 2.1.1.1.119 (1-107) Immunoglobulin (variable domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
elvmtqtplslpvslgdqasiscrssqslvhsygntflnwylqksgqspklliykvsnrf
sgvpdrfsgsgsgtdftlkisrveaedlgvyfcsqgthvpytfgggtkleik
>d1axtl2 2.1.1.2.117 (108-211) Immunoglobulin (constant domains of L and H chains) {Catalytic Fab 33F12 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1axwa_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1axwb_ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1axx__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1axy__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1axz__ 2.26.1.1.6 Lectin {Coral tree (Erythrina corallodendron)}
vetisfsfsefepgndnltlqgaalitqsgvlqltkinqngmpawdstgrtlyakpvhiw
dmttgtvasfetrfsfsieqpytrplpadglvffmgptkskpaqgygylgifnnskqdns
yqtlgvefdtfsnpwdppqvphigidvnsirsiktqpfqldngqvanvvikydasskilh
avlvypssgaiytiaeivdvkqvlpewvdvglsgatgaqrdaaethdvyswsfqaslpe
>d1ay0a1 3.29.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0a2 3.29.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0a3 3.39.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay0b1 3.29.1.2.1 (3-337) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
qftdidklavstirilavdtvskansghpgaplgmapaahvlwsqmrmnptnpdwinrdr
fvlsnghavallysmlhltgydlsiedlkqfrqlgsrtpghpefelpgvevttgplgqgi
snavgmamaqanlaatynkpgftlsdnytyvflgdgclqegisseasslaghlklgnlia
iyddnkitidgatsisfdedvakryeaygwevlyvengnedlagiakaiaqaklskdkpt
likmtttigygslhagshsvagaplkaddvkqlkskfgfnpdksfvvpqevydhyqktil
kpgveannkwnklfseyqkkfpelgaelarrlsgq
>d1ay0b2 3.29.1.2.1 (338-534) Transketolase, TK {Baker's yeast (Saccharomyces cerevisiae)}
lpanwesklptytakdsavatrklsetvledvynqlpeliggsadltpsnltrwkealdf
qppssgsgnysgryirygirehamgaimngisafganykpyggtflnfvsyaagavrlsa
lsghpviwvathdsigvgedgpthqpietlahfrslpniqvwrpadgnevsaayknsles
khtpsiialsrqnlpql
>d1ay0b3 3.39.1.1.1 (535-680) Transketolase {Baker's yeast (Saccharomyces cerevisiae)}
egssiesaskggyvlqdvanpdiilvatgsevslsveaaktlaaknikarvvslpdfftf
dkqpleyrlsvlpdnvpimsvevlattcwgkyahqsfgidrfgasgkapevfkffgftpe
gvaeraqktiafykgdklisplkkaf
>d1ay1h1 2.1.1.1.105 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
evqlqesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdy
npslksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1ay1h2 2.1.1.2.106 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1ay1l1 2.1.1.1.105 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1ay1l2 2.1.1.2.106 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1ay2__ 4.21.1.1.1 Pilin {Gc (Neisseria gonorrhoeae)}
ftlielmiviaivgilaavalpayqdytaraqvseaillaegqksavteyylnhgkwpen
ntsagvasppsdikgkyvkevevkngvvtatmlssgvnneikgkklslwarrengsvkwf
cgqpvtrtdddtvadakdgkeidtkhlpstcrdnfdak
>d1ay4a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay4b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay5a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay5b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>e1ay6.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>e1ay6.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
geadcglrplfekksledkterellesyi
>d1ay7a_ 4.1.1.1.1 RNase Sa {Streptomyces aureofaciens}
dvsgtvclsalppeatdtlnliasdgpfpysqdgvvfqnresvlptqsygyyheytvitp
gartrgtrriitgeatqedyytgdhyatfslidqtc
>d1ay7b_ 3.8.1.1.1 Barstar (barnase inhibitor) {Bacillus amyloliquefaciens}
kkavingeqirsisdlhqtlkkelalpeyygenldalwdcltgwveyplvlewrqfeqsk
qltengaesvlqvfreakaegcditiils
>d1ay8a_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay8b_ 3.57.1.1.7 Aromatic aminoacid aminotransferase, AroAT {Paracoccus denitrificans}
mlgnlkpqapdkilalmgefradprqgkidlgvgvykdatghtpimravhaaeqrmlete
ttktyaglsgepefqkamgelilgdglksettatlatvggtgalrqalelarmanpdlrv
fvsdptwpnhvsimnfmglpvqtyryfdaetrgvdfegmkadlaaakkgdmvllhgcchn
ptganltldqwaeiasilektgalplidlayqgfgdgleedaagtrliasripevliaas
csknfgiyrertgcllalcadaatrelaqgamaflnrqtysfppfhgakivstvlttpel
radwmaeleavrsgmlrlreqlagelrdlsgsdrfgfvaehrgmfsrlgatpeqvkrike
efgiymvgdsriniaglndntipilaraiievgv
>d1ay9a_ 2.30.1.2.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ay9b_ 2.30.1.2.1 UmuD' {Escherichia coli}
dyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavd
geftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr
>d1ayaa_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayab_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayba_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayca_ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
rrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdyy
dlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1ayd__ 4.72.1.1.6 Tyrosine phosphatase Syp {Mouse (Mus musculus)}
mrrwfhpnitgveaenllltrgvdgsflarpsksnpgdftlsvrrngavthikiqntgdy
ydlyggekfatlaelvqyymehhgqlkekngdvielkypln
>d1aye_1 3.47.4.1.3 (1-309) Carboxypeptidase A {Human (Homo sapiens)}
ersgnfnfgayhtleeisqemdnlvaehpglvskvnigssfenrpmnvlkfstggdkpai
wldagiharewvtqatalwtankivsdygkdpsitsildaldifllpvtnpdgyvfsqtk
nrmwrktrskvsgslcvgvdpnrnwdagfggpgassnpcsdsyhgpsansevevksivdf
ikshgkvkafiilhsysqllmfpygykctklddfdelsevaqkaaqslrslhgtkykvgp
icsviyqasggsidwsydygikysfafelrdtgrygfllparqilptaeetwlglkaime
hvrdhpy
>d1aye_2 4.47.3.1.3 (4a-99a) Procarboxypeptidase A {Human (Homo sapiens)}
letfvgdqvleivpsneeqiknllqleaqehlqldfwkspttpgetahvrvpfvnvqavk
vflesqgiaysimiedvqvlldkeneemlfnrrr
>d1ayfa_ 4.13.6.1.13 Adrenodoxin {Bovine (Bos taurus)}
kitvhfinrdgetlttkgkigdslldvvvqnnldidgfgacegtlacstchlifeqhife
kleaitdeendmldlaygltdrsrlgcqicltkamdnmtvrvp
>d1ayfb_ 4.13.6.1.13 Adrenodoxin {Bovine (Bos taurus)}
dkitvhfinrdgetlttkgkigdslldvvvqnnldidgfgacegtlacstchlifeqhif
ekleaitdeendmldlaygltdrsrlgcqicltkamdnmtvrvp
>d1ayg__ 1.3.1.1.23 Cytochrome c552 {Hydrogenobacter thermophilus}
neqlakqkgcmachdlkakkvgpayadvakkyagrkdavdylagkikkggsgvwgsvpmp
pqnvtdaeakqlaqwilsik
>d1ayi__ 1.29.2.1.1 ImmE7 protein {Escherichia coli}
melknsisdyteaefvqllkeiekenvaatddvldvllehfvkitehpdgtdliyypsdn
rddspegivkeikewraangkpgfkq
>d1ayj__ 7.3.7.4.3 Antifungal protein 1 (RS-AFP1) {Radish (Raphanus sativus)}
klcerpsgtwsgvcgnnnacknqcinlekarhgscnyvfpahkcicyfpc
>d1ayk__ 4.71.1.9.1 Fibroblast collagenase (MMP-1) {Human (Homo sapiens)}
vltegnprweqthltyrienytpdlpradvdhaiekafqlwsnvtpltftkvsegqadim
isfvrgdhrdnspfdgpggnlahafqpgpgiggdahfdederwtnnfreynlhrvaahel
ghslglshstdigalmypsytfsgdvqlaqddidgiqaiygrsqnpvqp
>d1ayl__ 3.81.1.1.1 Phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-liase) {Escherichia coli}
mrvnngltpqeleaygisdvhdivynpsydllyqeeldpsltgyergvltnlgavavdtg
iftgrspkdkyivrddttrdtfwwadkgkgkndnkplspetwqhlkglvtrqlsgkrlfv
vdafcganpdtrlsvrfitevawqahfvknmfirpsdeelagfkpdfivmngakctnpqw
keqglnsenfvafnltermqliggtwyggemkkgmfsmmnyllplkgiasmhcsanvgek
gdvavffglsgtgkttlstdpkrrligddehgwdddgvfnfeggcyaktiklskeaepei
ynairrdallenvtvredgtidfddgsktentrvsypiyhidnivkpvskaghatkvifl
tadafgvlppvsrltadqtqyhflsgftaklagtergiteptptfsacfgaaflslhptq
yaevlvkrmqaagaqaylvntgwngtgkrisikdtraiidailngsldnaetftlpmfnl
aiptelpgvdtkildprntyaspeqwqekaetlaklfidnfdkytdtpagaalvaagpkl
>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
>d1ayn1_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
npveryvdevlnevlvvpninqshpttsnaapvldaaetghtnkiqpedtietryvqssq
tldemsvesflgrsgcihesvldivdnyndqsftkwninlqemaqirrkfemftyarfds
eitmvpsvaakdghighivmqymyvppgapipttrddyawqsgtnasvfwqhgqpfprfs
lpflsiasayymfydgydgdtyksrygtvvtndmgtlcsrivtseqlhkvkvvtriyhka
khtkawcprppravqyshthttnyklssevhndvairprtnlttv
>d1ayn2_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
sdriiqitrgdstitsqdvanavvgygvwphyltpqdataidkptqpdtssnrfytldsk
mwnstskgwwwklpdalkdmgifgenmfyhflgrsgytvhvqcnaskfhqgtllvvmipe
hqlatvnkgnvnagykythpgeagrevgtqvenekqpsddnwlnfdgtllgnllifphqf
inlrsnnsatlivpyvnavpmdsmvrhnnwslviipvcqlqsnnisnivpitvsispmca
efsgaraktvvq
>d1ayn3_ 2.9.1.4.9 Rhinovirus coat protein {Human (Homo sapiens), rhinovirus 16}
glpvyvtpgsgqfmttddmqspcalpwyhptkeifipgevknliemcqvdtlipinstqs
nignvsmytvtlspqtklaeeifaikvdiashplattligeiasyfthwtgslrfsfmfc
gtanttlkvllaytppgigkprsrkeamlgthvvwdvglqstvslvvpwisasqyrfttp
dtyssagyitcwyqtnfvvppntpntaemlcfvsgckdfclrmardtdlhkqtgpitq
>d1ayoa_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1ayob_ 2.2.4.1.2 Receptor domain from alpha-2-macroglobulin {Bovine (Bos taurus)}
efpfalevqtlpqtcdgpkahtsfqislsvsyigsrpasnmaivdvkmvsgfiplkptvk
mlersnvsrtevsnnhvliyldkvtnetltltftvlqdipvrdlkpaivkvydyyetdef
avaeysapcs
>d1aypa_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypb_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypc_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypd_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aype_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1aypf_ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1ayra1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayra2 2.1.1.5.19 (183-368) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtaka
>d1ayrb1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrb2 2.1.1.5.19 (183-363) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
p
>d1ayrc1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrc2 2.1.1.5.19 (183-368) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
pdtaka
>d1ayrd1 2.1.1.5.19 (1-182) Arrestin {Bovine (Bos taurus)}
mkankpapnhvifkkisrdksvtiylgkrdyidhvervepvdgvvlvdpelvkgkrvyvs
ltcafrygqedidvmglsfrrdlyfsqvqvfppvgasgattrlqeslikklgantypfll
tfpdylpcsvmlqpapqdvgkscgvdfeikafathstdveedkipkkssvrllirkvqha
pr
>d1ayrd2 2.1.1.5.19 (183-363) Arrestin {Bovine (Bos taurus)}
dmgpqpraeaswqffmsdkplrlavslskeiyyhgepipvtvavtnstektvkkikvlve
qvtnvvlyssdyyiktvaaeeaqekvppnssltktltlvpllannrerrgialdgkikhe
dtnlasstiikegidktvmgilvsyqikvkltvsgllgeltssevatevpfrlmhpqped
p
>d1ayu__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayv__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayw__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1ayx__ 1.98.1.1.2 Glucoamylase {Yeast (Saccharomycopsis fibuligera)}
aypsfeaysnykvdrtdletfldkqkevslyyllqniaypegqfnngvpgtviaspstsn
pdyyyqwtrdsaitfltvlselednnfnttlakaveyyintsynlqrtsnpsgsfddenh
kglgepkfntdgsaytgawgrpqndgpalrayaisrylndvnslnegklvltdsgdinfs
stediykniikpdleyvigywdstgfdlweenqgrhfftslvqqkalayavdiaksfddg
dfantlsstastlesylsgsdggfvntdvnhivenpdllqqnsrqgldsatyigpllthd
igessstpfdvdneyvlqsyylllednkdrysvnsaysagaaigrypedvyngdgssegn
pwflatayaaqvpyklaydaksasnditinkinydffnkyivdlstinsayqssdsvtik
sgsdefntvadnlvtfgdsflqvildhinddgslneqlnrytgystgaysltwssgalle
airlrnkvkala
>e1ayy.1a 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlkts
>e1ayy.1b 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfal
>e1ayy.2c 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tnkpivlstwnfglhanveawkvlskggkaldavekgvrlveddptersvgyggrpdrdg
rvtldacimdenynigsvacmehiknpisvaravmektphvmlvgdgalefalsqgfkke
nlltaesekewkewlktsqy
>e1ayy.2d 4.124.1.4.2 Glycosylasparaginase (aspartylglucosaminidase, AGA) {Flavobacterium meningosepticum}
tigmialdaqgnlsgacttsgmaykmhgrvgdspiigaglfvdneigaatatghgeevir
tvgthlvvelmnqgrtpqqackeaverivkivnrrgknlkdiqvgfialnkkgeygayci
qdgfnfavhdqkgnrletpgfalk
>d1ayza_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1ayzb_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1ayzc_ 4.18.1.1.2 Ubiquitin conjugating enzyme {Baker's yeast (Saccharomyces cerevisiae), ubc2 (RAD6)}
stparrrlmrdfkrmkedappgvsasplpdnvmvwnamiigpadtpyedgtfrlllefde
eypnkpphvkflsemfhpnvyangeicldilqnrwtptydvasiltsiqslfndpnpasp
anveaatlfkdhksqyvkrvketveksweddmd
>d1az0a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1az0b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1az1__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpyakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvaall
sctshkdypfheef
>d1az2__ 3.1.6.1.3 Aldose reductase (aldehyde reductase) {Human (Homo sapiens)}
srlllnngakmpilglgtwksppgqvteavkvaidvgyrhidcahvyqnenevgvaiqek
lreqvvkreelfivsklwctyhekglvkgacqktlsdlkldyldlylihwptgfkpgkef
fpldesgnvvpsdtnildtwaameelvdeglvkaigisnfnhlqvemilnkpglkykpav
nqiechpyltqekliqycqskgivvtaysplgspdrpyakpedpslledprikaiaakhn
kttaqvlirfpmqrnlvvipksvtperiaenfkvfdfelssqdmttllsynrnwrvaall
sctshkdypfheef
>d1az3a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywr
>d1az3b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
>d1az4a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywr
>d1az4b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikatytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
>d1az5__ 2.44.1.1.6 Simian immunodeficiency virus (SIV) protease {Simian immunodeficiency virus, Mac251 isolate}
pqfhlwkrpvvtahiegqpvevlldtgaddsivtgielgphytpkivggiggfintkeyk
nvevevlgkrikgtimtgdtpinifgrnlltalgmslnf
>d1az6__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1az8__ 2.41.1.2.1 Trypsin(ogen) {Bovine (Bos taurus)}
ivggytcgantvpyqvslnsgyhfcggslinsqwvvsaahcyksgiqvrlgedninvveg
neqfisasksivhpsynsntlnndimliklksaaslnsrvasislptscasagtqclisg
wgntkssgtsypdvlkclkapilsdsscksaypgqitsnmfcagyleggkdscqgdsggp
vvcsgklqgivswgsgcaqknkpgvytkvcnyvswikqtiasn
>d1az9__ 4.101.1.1.5 Aminopeptidase P {Escherichia coli}
seisrqefqrrrqalveqmqpgsaalifaapevtrsadseypyrqnsdfwyftgfnepea
vlvliksddthnhsvlfnrvrdltaeiwfgrrlgqdaapeklgvdralafseinqqlyql
lngldvvyhaqgeyayadvivnsaleklrkgsrqnltapatmidwrpvvhemrlfkspee
iavlrrageitamahtramekcrpgmfeyhlegeihhefnrhgarypsyntivgsgengc
ilhytenecemrdgdlvlidagceykgyagditrtfpvngkftqaqreiydivleslets
lrlyrpgtsilevtgevvrimvsglvklgilkgdvdeliaqnahrpffmhglshwlgldv
hdvgvygqdrsrilepgmvltvepglyiapdaevpeqyrgigirieddivitetgnenlt
asvvkkpeeiealmvaarkq
>d1azba_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azbb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azca_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azcb_ 2.5.1.1.21 Azurin {Alcaligenes denitrificans}
aqceatiesndamqynlkemvvdksckqftvhlkhvgkmakvamghnwvltkeadkqgva
tdgmnaglaqdyvkagdtrviahtkvigggesdsvtfdvskltpgeayayfcsfpghwam
mkgtlklsn
>d1azda_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdb_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdc_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azdd_ 2.26.1.1.2 Concanavalin A {Brazilian jackbean (Canavalia brasiliensis)}
adtivaveldtypntdigdpsyphigidiksvrskktakwnmqngkvgtahiiynsvgkr
lsavvsypngdsatvsydvdldnvlpewvrvglsastglyketntilswsftsklksnst
hetnalhfmfnqfskdqkdlilqgdattgtegnlrltrvssngspqgssvgralfyapvh
iwessavvasfeatftflikspdshpadgiaffisnidssipsgstgrllglfpdan
>d1azea_ 2.30.2.1.15 Growth factor receptor-bound protein 2 (GRB2), N- and C-terminal domains {Mouse (Mus musculus)}
meaiakvdfkataddelsfkrgdilkvlneesdqnwykaelngkdgfipknyiemk
>d1azf__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1azgb_ 2.30.2.1.2 Fyn proto-oncogene tyrosine kinase, SH3 domain {Human (Homo sapiens)}
vtlfvalydyearteddlsfhkgekfqilnssegdwwearslttgetgyipsnyvapv
>d1azh__ 7.3.8.1.1 Cellobiohydrolase I {Trichoderma reesei, ct-cbh I}
tqshagqcggigysgptvcasgttcqvlnpyysqcl
>d1azi__ 1.1.1.1.8 Myoglobin {Horse (Equus caballus)}
glsdgewqqvlnvwgkveadiaghgqevlirlftghpetlekfdkfkhlkteaemkased
lkkhgtvvltalggilkkkghheaelkplaqshatkhkipikylefisdaiihvlhskhp
gdfgadaqgamtkalelfrndiaakykelgfqg
>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
>d1azl__ 3.16.4.1.2 Flavodoxin {Desulfovibrio vulgaris}
pkalivygsttgnteytaetiareladagyevdsrdaasveagglfegfdlvllgcstwv
ddsielqddfiplfdsleetgaqgrkvacfgcgdssyeyfcgavdaieeklknlgaeivq
dglridgdpraarddivgwahdvrgai
>d1azm__ 2.65.1.1.1 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme I}
pdwgyddkngpeqwsklypiangnnqspvdiktsetkhdtslkpisvsynpatakeiinv
ghsfhvnfedndnrsvlkggpfsdsyrlfqfhfhwgstnehgsehtvdgvkysaelhvah
wnsakysslaeaaskadglavigvlmkvgeanpklqkvldalqaiktkgkrapftnfdps
tllpssldfwtypgslthpplyesvtwiickesisvsseqlaqfrsllsnvegdnavpmq
hnnrptqplkgrtvrasf
>d1azna_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznc_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1aznd_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctapghsal
mkgtltlk
>d1azo__ 3.43.1.8.1 DNA mismatch repair protein MutH from {Escherichia coli}
prpllsppeteeqllaqaqqlsgytlgelaalvglvtpenlkrdkgwigvlleiwlgasa
gskpeqdfaalgvelktipvdslgrplettfvcvapltgnsgvtwetshvrhklkrvlwi
pvegeasiplaqrrvgspllwspneeedrqlredweelxdxivlgqveritarhgeylqi
rpkaanakalteaigargeriltlprgfylkknftsallarhfliq
>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
>d1azra_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrc_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azrd_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aqcsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghdwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1azsa_ 4.47.24.1.2 Adenylyl cyclase VC1, domain C1a {Dog (Canis familiaris)}
dmmfhkiyiqkhdnvsilfadiegftslasqctaqelvmtlnelfarfdklaaenhclri
kilgdcyycvsglpearadhahccvemgmdmieaislvremtgvnvnmrvgihsgrvhcg
vlglrkwqfdvwsndvtlanhmeaggkagrihitkatlsylngdyevepgcggernaylk
ehsietflil
>d1azsb_ 4.47.24.1.3 Adenylyl cyclase IIC1, domain C2a {Rat (Rattus norvegicus)}
hqsydcvcvmfasipdfkefytesdvnkegleclrllneiiadfddllskpkfsgvekik
tigstymaatglsaipsqehaqeperqymhigtmvefayalvgkldainkhsfndfklrv
ginhgpviagvigaqkpqydiwgntvnvasrmdstgvldkiqvteetslilqtlgytctc
rgiinvkgkgdlktyfvnt
>d1azsc1 1.67.1.1.1 (86-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
gfngdgekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdf
dfppefyehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrc
r
>d1azsc2 3.30.1.6.12 (36-66,202-393) Transducin (alpha subunit) {Bovine (Bos taurus)}
vyrathrllllgagesgkstivkqmrilhvnXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqyel
>d1azta1 1.67.1.1.1 (88-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
katkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppefy
ehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1azta2 3.30.1.6.12 (35-65,202-391) Transducin (alpha subunit) {Bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvXvltsgifetkfqvdkvnfhmfdvggqrd
errkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrtisvil
flnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdeflris
tasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1aztb1 1.67.1.1.1 (87-201) Transducin (alpha subunit), insertion domain {Bovine (Bos taurus)}
ekatkvqdiknnlkeaietivaamsnlvppvelanpenqfrvdyilsvmnvpdfdfppef
yehakalwedegvracyersneyqlidcaqyfldkidvikqddyvpsdqdllrcr
>d1aztb2 3.30.1.6.12 (35-69,202-391) Transducin (alpha subunit) {Bovine (Bos taurus)}
qvyrathrllllgagesgkstivkqmrilhvngfnXvltsgifetkfqvdkvnfhmfdvg
gqrderrkwiqcfndvtaiifvvasssynmvirednqtnrlqealnlfksiwnnrwlrti
svilflnkqdllaekvlagkskiedyfpefaryttpedatpepgedprvtrakyfirdef
lristasgdgrhycyphftcavdtenirrvfndcrdiiqrmhlrqy
>d1azu__ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
csvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvvtd
gmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsalmk
gtltlk
>d1azva_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azvb_ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavcvlkgdgpvqgiinfeqkesngpvkvwgsikrlteglhgfhvhefgdntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhciigrtlvvh
ekaddlgkggneestktgnagsrlacgvigiaq
>d1azwa_ 3.59.1.5.1 Proline iminopeptidase {Xanthomonas campestris, pv. citri}
mrtlypeitpyqqgslkvddrhtlyfeqcgnphgkpvvmlhggpgggcndkmrrfhdpak
yrivlfdqrgsgrstphadlvdnttwdlvadierlrthlgvdrwqvfggswgstlalaya
qthpqqvtelvlrgifllrrfelewfyqegasrlfpdawehylnaippveradlmsafhr
rltsddeatrlaaakawsvwegatsflhvdedfvtghedahfalafarienhyfvnggff
evedqllrdahriadipgvivhgrydvvcplqsawdlhkawpkaqlqispasghsafepe
nvdalvratdgfa
>d1azwb_ 3.59.1.5.1 Proline iminopeptidase {Xanthomonas campestris, pv. citri}
mrtlypeitpyqqgslkvddrhtlyfeqcgnphgkpvvmlhggpgggcndkmrrfhdpak
yrivlfdqrgsgrstphadlvdnttwdlvadierlrthlgvdrwqvfggswgstlalaya
qthpqqvtelvlrgifllrrfelewfyqegasrlfpdawehylnaippveradlmsafhr
rltsddeatrlaaakawsvwegatsflhvdedfvtghedahfalafarienhyfvnggff
evedqllrdahriadipgvivhgrydvvcplqsawdlhkawpkaqlqispasghsafepe
nvdalvratdgfa
>d1azxi_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
gspvdictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfatt
fyqhladskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihf
ffaklncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeq
sraainkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfyk
adgescsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltp
evlqewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrdd
lyvsdafhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntii
fmgrvanpcv
>d1azxl_ 5.1.1.1.6 Antithrombin {Human (Homo sapiens)}
vdictakprdipmnpmciyrspekkatedegseqkipeatnrrvwelskansrfattfyq
hladskndndniflsplsistafamtklgacndtlqqlmevfkfdtisektsdqihfffa
klncrlyrkankssklvsanrlfgdksltfnetyqdiselvygaklqpldfkenaeqsra
ainkwvsnktegritdvipseaineltvlvlvntiyfkglwkskfspentrkelfykadg
escsasmmyqegkfryrrvaegtqvlelpfkgdditmvlilpkpekslakvekeltpevl
qewldeleemmlvvhmprfriedgfslkeqlqdmglvdlfspeksklpgivaegrddlyv
sdafhkaflevneegseaaastavviagrslnpnrvtfkanrpflvfirevplntiifmg
rvanpcv
>d1azya1 1.49.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1azya2 3.20.1.1.1 (71-335) Thymidine phosphorylase {Escherichia coli}
dwkslhlngpivdkhstggvgdvtslmlgpmvaacggyipmisgrglghtggtldklesi
pgfdifpddnrfreiikdvgvaiigqtsslapadkrfyatrditatvdsiplitasilak
klaegldalvmdvkvgsgafmptyelsealaeaivgvangagvrttalltdmnqvlassa
gnavevreavqfltgeyrnprlfdvtmalcvemlisgklakddaearaklqavldngkaa
evfgrmvaaqkgptdfvenyakylp
>d1azya3 4.34.3.1.1 (336-440) Thymidine phosphorylase {Escherichia coli}
tamltkavyadtegfvsemdtralgmavvamgggrrqasdtidysvgftdmarlgdqvdg
qrplavihakdennwqeaakavkaaikladkapestptvyrrise
>d1azyb1 1.49.2.1.1 (1-70) Thymidine phosphorylase {Escherichia coli}
lflaqeiirkkrdghalsdeeirffingirdntisegqiaalamtiffhdmtmpervslt
mamrdsgtvl
>d1azyb2 3.20.1.1.1 (71-335) Thymidine phosphorylase {Escherichia coli}
dwkslhlngpivdkhstggvgdvtslmlgpmvaacggyipmisgrglghtggtldklesi
pgfdifpddnrfreiikdvgvaiigqtsslapadkrfyatrditatvdsiplitasilak
klaegldalvmdvkvgsgafmptyelsealaeaivgvangagvrttalltdmnqvlassa
gnavevreavqfltgeyrnprlfdvtmalcvemlisgklakddaearaklqavldngkaa
evfgrmvaaqkgptdfvenyakylp
>d1azyb3 4.34.3.1.1 (336-440) Thymidine phosphorylase {Escherichia coli}
tamltkavyadtegfvsemdtralgmavvamgggrrqasdtidysvgftdmarlgdqvdg
qrplavihakdennwqeaakavkaaikladkapestptvyrrise
>d1azza_ 2.41.1.2.9 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzb_ 2.41.1.2.9 Crab collagenase {Atlantic sand fiddler crab (Uca pugilator)}
ivggveavpnswphqaalfiddmyfcggslispewiltaahcmdgagfvdvvlgahnire
deatqvtiqstdftvhenynsfvisndiavirlpvpvtltaaiatvglpstdvgvgtvvt
ptgwglpsdsalgisdvlrqvdvpimsnadcdavygivtdgnicidstggkgtcngdsgg
plnyngltygitsfgaaagceagypdaftrvtyfldwiqtqtgitp
>d1azzc_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
plekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktle
gwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvdv
kyrvwkaeekidnavvr
>d1azzd_ 2.14.1.1.1 Ecotin, trypsin inhibitor {Escherichia coli}
qplekiapypqaekgmkrqviqltpqedestlkvelligqtlevdcnlhrlggklenktl
egwgydyyvfdkvsspvstmmacpdgkkekkfvtaylgdagmlrynsklpivvytpdnvd
vkyrvwkaeekidnavvr
>d1b02a_ 4.91.1.1.3 Thymidylate synthase {Bacillus subtilis}
mtqfdkqynsiikdiinngisdeefdvrtkwdsdgtpahtlsviskqmrfdnsevpiltt
kkvawktaikellwiwqlksndvndlnmmgvhiwdqwkqedgtighaygfqlgkknrsln
gekvdqvdyllhqlknnpssrrhitmlwnpdeldamaltpcvyetqwyvkhgklhlevra
rsndmalgnpfnvfqynvlqrmiaqvtgyelgeyifnigdchvytrhidnlkiqmereqf
eapelwinpevkdfydftiddfklinykhgdkllfevav
>d1b05a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b07a_ 2.30.2.1.1 C-Crk, N-terminal SH3 domain {Mouse (Mus musculus)}
saeyvralfdfngndeedlpfkkgdilrirdkpeeqwwnaedsegkrgmipvpyvekyh
>d1b0aa1 3.2.1.7.8 (123-288) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
fhpynvgrlcqraprlrpctprgivtllerynidtfglnavvigasnivgrpmsmellla
gctttvthrftknlrhhvenadllivavgkpgfipgdwikegaividvginrlengkvvg
dvvfedaakrasyitpvpggvgpmtvatlientlqacveyhdpqde
>d1b0aa2 3.48.1.2.2 (2-122) Tetrahydrofolate dehydrogenase/cyclohydrolase {Escherichia coli}
aakiidgktiaqqvrsevaqkvqariaaglrapglavvlvgsnpasqiyvaskrkaceev
gfvsrsydlpettseaellelidtlnadntidgilvqlplpagidnvkvlerihpdkdvd
g
>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
>d1b0d__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1b0e__ 2.41.1.2.15 Elastase {Porcine (Sus scrofa)}
vvggteaqrnswpsqislqyrsgsswahtcggtlirqnwvmtaahcvdreltfrvvvgeh
nlnqnngteqyvgvqkivvhpywntddvaagydiallrlaqsvtlnsyvqlgvlpragti
lannspcyitgwgltrtngqlaqtlqqaylptvdyaicssssywgstvknsmvcaggdgv
rsgcqgdsggplhclvngqyavhgvtsfvsrlgcnvtrkptvftrvsayiswinnviasn
>d1b0f__ 2.41.1.2.14 Elastase {Human (Homo sapiens)}
ivggrrarphawpfmvslqlagghfcgatliapnfvmsaahcvanvnvravrvvlgahnl
srreptrqvfavqrifedgydpvnllndivilqlngsatinanvqvaqlpaqgrrlgngv
qclamgwgllgrnrgiasvlqelnvtvvtslcrrsnvctlvrgrqagvcfgdsgsplvcn
glihgiasfvrggcasglypdafapvaqfvnwidsiiq
>d1b0ga1 2.1.1.2.5 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1b0ga2 4.17.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a2.1}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0gb1 2.1.1.2.5 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0gd1 2.1.1.2.5 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1b0gd2 4.17.1.1.12 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a2.1}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0ge1 2.1.1.2.5 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a2.1}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b0j_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegasrehsa
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0j_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0k_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehra
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0k_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0l_1 3.84.1.2.1 (1-334) Lactoferrin {Human (Homo sapiens)}
grrrsvqwctvsqpeatkcfqwqrnmrkvrgppvscikrdspiqciqaiaenradavtld
ggfiyeaglapyklrpvaaevygterqprthyyavavvkkggsfqlnelqglkschtglr
rtagwnvpigtlrpflnwtgppepieaavarffsascvpgadkgqfpnlcrlcagtgenk
cafssqepyfsysgafkclrdgagdvafirestvfedlsdeaerdeyellcpdntrkpvd
kfkdchlarvpshavvarsvngkedaiwnllrqaqekfgkdkspkfqlfgspsgqkdllf
kdsaigfsrvppridsglylgsgyftaiqnlrks
>d1b0l_2 3.84.1.2.1 (335-691) Lactoferrin {Human (Homo sapiens)}
eeevaarrarvvwcavgeqelrkcnqwsglsegsvtcssasttedcialvlkgeadamsl
dggyvytagkcglvpvlaenyksqqssdpdpncvdrpvegylavavvrrsdtsltwnsvk
gkkschtavdrtagwnipmgllfnqtgsckfdeyfsqscapgsdprsnlcalcigdeqge
nkcvpnsneryygytgafrclaenagdvafvkdvtvlqntdgnnneawakdlkladfall
cldgkrkpvtearschlamapnhavvsrmdkverlkqvllhqqakfgrngsdcpdkfclf
qsetknllfndnteclarlhgkttyekylgpqyvagitnlkkcstsplleaceflrk
>d1b0m_1 3.7.2.1.1 (529-754) Aconitase, C-terminal domain {Pig (Sus scrofa)}
vdvsptsqrlqllepfdkwdgkdledlqilikvkgkcttdhisaagpwlkfrghldnisn
nlligainienrkansvrnavtqefgpvpdtaryykqhgirwvvigdenygegssrehra
leprhlggraiitksfarihetnlkkqgllpltfadpadynkihpvdkltiqglkdfapg
kplkciikhpngtqetillnhtfnetqiewfragsalnrmkelqqk
>d1b0m_2 3.72.1.1.1 (2-528) Aconitase, first 3 domains {Pig (Sus scrofa)}
rakvamshfepheyirydlleknidivrkrlnrpltlsekivyghlddpanqeiergkty
lrlrpdrvamqdataqmamlqfissglpkvavpstihcdhlieaqlggekdlrrakdinq
evynflatagakygvgfwrpgsgiihqiilenyaypgvlligtdshtpnggglggicigv
ggadavdvmagipwelkcpkvigvkltgslsgwtspkdvilkvagiltvkggtgaiveyh
gpgvdsisctgmaticnmgaeigattsvfpynhrmkkylsktgradianladefkdhlvp
dpgchydqvieinlselkphingpftpdlahpvaevgsvaekegwpldirvgligsctns
syedmgrsaavakqalahglkcksqftitpgseqiratierdgyaqvlrdvggivlanac
gpcigqwdrkdikkgekntivtsynrnftgrndanpethafvtspeivtalaiagtlkfn
petdfltgkdgkkfkleapdadelpraefdpgqdtyqhppkdssgqr
>d1b0na1 1.35.1.1.1 (74-108) SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
ldseweklvrdamtsgvskkqfrefldyqkwrksq
>d1b0na2 1.36.1.3.1 (1-68) SinR repressor, DNA-binding domain {Bacillus subtilis}
migqrikqyrkekgyslselaekagvaksylssiernlqtnpsiqflekvsavldvsvht
lldekhet
>d1b0nb1 1.35.1.1.1 SinR repressor (dimerisation domain)-SinI anti-repressor complex {Bacillus subtilis}
feldqewvelmveakeanispeeirkyllln
>d1b0o__ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
ivtqtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkw
engecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslacqc
lvrtpevddealekfdkalkalpmhirlsfnptqleeqchi
>d1b0pa1 3.29.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pa2 3.29.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1b0pa3 3.39.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1b0pa4 3.54.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d1b0pa5 4.47.1.5.3 (669-785) Pyruvate-ferredoxin oxidoreductase, PFOR, domain V {Desulfovibrio africanus}
tsqfekrgvainvpqwvpenciqcnqcafvcphsailpvlakeeelvgapanftaleakg
kelkgykfriqintldcmgcgncadicppkekalvmqpldtqrdaqvpnleyaarip
>d1b0pb1 3.29.1.4.1 (2-258) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
gkkmmttdgntatahvayamsevaaiypitpsstmgeeaddwaaqgrknifgqtltirem
qseagaagavhgalaagaltttftasqglllmipnmykisgellpgvfhvtaraiaahal
sifgdhqdiyaarqtgfamlasssvqeahdmalvahlaaiesnvpfmhffdgfrtsheiq
kievldyadmaslvnqkalaefraksmnpehphvrgtaqnpdiyfqgreaanpyylkvpg
ivaeymqkvasltgrsy
>d1b0pb2 3.29.1.4.1 (786-1232) Pyruvate-ferredoxin oxidoreductase, PFOR, domains I and VI {Desulfovibrio africanus}
vksevlprdslkgsqfqeplmefsgacsgcgetpyvrvitqlfgermfianatgcssiwg
asapsmpyktnrlgqgpawgnslfedaaeygfgmnmsmfarrthladlaakalesdasgd
vkealqgwlagkndpikskeygdklkkllagqkdgllgqiaamsdlytkksvwifggdgw
aydigyggldhvlasgedvnvfvmdtevysntggqsskatptgavakfaaagkrtgkkdl
armvmtygyvyvatvsmgyskqqflkvlkeaesfpgpslviayatcinqglrkgmgksqd
vmntavksgywplfrydprlaaqgknpfqldskapdgsveeflmaqnrfavldrsfpeda
krlraqvaheldvrfkelehmaatnifesfapaggkadgsvdfgegaefctrddtpmmar
pdsgeacdqnragtseqqgdlskrtkk
>d1b0pb3 3.39.1.3.1 (259-415) Pyruvate-ferredoxin oxidoreductase, PFOR, domain II {Desulfovibrio africanus}
klfdyvgapdaervivsmgsscetieevinhlaakgekiglikvrlyrpfvseaffaalp
asakvitvldrtkepgapgdplyldvcsafvergeampkilagryglgskefspamvksv
ydnmsgakknhftvgieddvtgtslpvdnafadttpk
>d1b0pb4 3.54.1.1.1 (416-668) Pyruvate-ferredoxin oxidoreductase, PFOR, domain III {Desulfovibrio africanus}
gtiqcqfwglgadgtvgankqaikiigdntdlfaqgyfsydskksggitishlrfgekpi
qstylvnradyvachnpayvgiydilegikdggtfvlnspwssledmdkhlpsgikrtia
nkklkfynidavkiatdvglggrinmimqtaffklagvlpfekavdllkksihkaygkkg
ekivkmntdavdqavtslqefkypdswkdapaetkaepmtneffknvvkpiltqqgdklp
vsafeadgrfplg
>d1b0pb5 4.47.1.5.3 (669-785) Pyruvate-ferredoxin oxidoreductase, PFOR, domain V {Desulfovibrio africanus}
tsqfekrgvainvpqwvpenciqcnqcafvcphsailpvlakeeelvgapanftaleakg
kelkgykfriqintldcmgcgncadicppkekalvmqpldtqrdaqvpnleyaarip
>d1b0ra1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrqdtelvetrpagdgtfqkwaav
vvpsgqeqrytchvqheglpkpltlrwe
>d1b0ra2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1b0rb1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
miqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskd
wsfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1b0t__ 4.47.1.2.1 Ferredoxin {Azotobacter vinelandii}
afvvtdncikckycdcvevcpvdcfyegpnflvihpdecidcalcepecpaqaifsedev
pedmqefiqlnaelaevwpnitekkdplpdaedwdgvkgklqhler
>d1b0wa_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0wb_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0wc_ 2.1.1.1.147 Immunoglobulin (variable domains of L and H chains) {Bence-Jones VL (kappa) dimer BRE (human)}
diqmtqspsslsasvgdrvtitcqasqdisdyliwyqqklgkapnlliydastletgvps
rfsgsgsgteytftisslqpediatyycqqyddlpytfgqgtkveikr
>d1b0xa_ 1.61.1.2.1 EphA4 receptor tyrosine kinases {Mouse (Mus musculus)}
fsavvsvgdwlqaikmdrykdnftaagyttleavvhmsqddlarigitaithqnkilssv
qamrtqmqqmhg
>d1b0y__ 7.30.1.1.2 HIPIP (high potential iron protein) {Cromatium vinosum}
sapanavaaddataialkynqdatkservaaarpglppeeqqcancqfmqadaagatdew
kgcqlfpgklinvngwcaswtlkag
>d1b10__ 4.6.1.1.2 Prion protein domain {Golden hamster (Mesocricetus auratus)}
lggymlgsamsrpmmhfgndwedryyrenmnrypnqvyyrpvdqynnqnnfvhdcvniti
kqhtvttttkgenftetdikimervveqmcttqyqkesqayydg
>d1b11__ 2.44.1.1.2 Feline immunodeficiency virus (FIV) protease {Feline (Felis catus), immunodeficiency virus}
vgttttlekrpeilifvngypikflldtgaditilnrrdfqvknsiengrqnmigvgggk
rgtnyinvhleirdenyktqcifgnvcvlednsliqpllgrdnmikfnirlvm
>d1b13a_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcayiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1b1a__ 3.16.5.1.3 Glutamate mutase, small subunit {Clostridium cochlearium}
mekktivlgvigsdchavgnkildhaftnagfnvvnigvlspqevfikaaietkadaill
sslygqgeidckglrqkcdeaglegillyvggnivvgkqhwpdvekrfkdmgydrvyapg
tppevgiadlkkdlnie
>d1b1ea_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqhydakpqgrddrycesimrrrgltspcqdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1b1ga_ 1.42.1.1.1 Calbindin D9K {Bovine (Bos taurus)}
kspeelkgifekyaakegdpnqlskeelklllqtefpsllkggstldelfeeldkngdge
vsfeefqvlvkkisq
>d1b1ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b1ia_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
dnsrythfltqhydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenkn
gnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsifr
rp
>d1b1ja_ 4.5.1.1.7 Angiogenin {Human (Homo sapiens)}
qdnsrythfltqaydakpqgrddrycesimrrrgltspckdintfihgnkrsikaicenk
ngnphrenlriskssfqvttcklhggspwppcqyratagfrnvvvacenglpvhldqsif
rrp
>d1b1u__ 1.54.1.2.2 Trypsin/alpha-amylase inhibitor RBI {Ragi (Elucine coracana gaertneri), seeds}
gtscipgmaiphnpldscrwyvstrtcgvgprlatqemkarccrqleaipaycrceavri
lmdgvvtpsgqhegrllqdlpgcprqvqrafapklvtevecnlatihggpfclsllg
>d1b1xa1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b1xa2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>d1b1y__ 3.1.7.2.2 beta-Amylase {Barley (Hordeum vulgare)}
mkgnyvqvyvmlpldavsvnnrfekgdelraqlrklveagvdgvmvdvwwglvegkgpka
ydwsaykqlfelvqkaglklqaimsfhqcggnvgdavnipipqwvrdvgtrdpdifytdg
hgtrnieyltlgvdnqplfhgrsavqmyadymtsfrenmkdfldagvivdievglgpage
lrypsypqshgwsfpgigeficydkylqadfkaaaaavghpewefpndagqyndtpertq
ffrdngtylsekgrfflawysnnlikhgdrildeankvflgykvqlaikiagvhwwykvp
shaaeltagyynlhdrdgyrtiarmlkrhrasinftcaemrdseqppdamsapeelvqqv
lsagwreglnvscenalprydptayntilrnarphginqsgppehklfgftylrlsnqlv
egqnyvnfktfvdrmhanlprdpyvdpmaplprsgpeisiemilqaaqpklqpfpfqeht
dlpvgptggmggqaegptcg
>d1b20a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b20b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b20c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b21a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b21b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b21c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgstwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b23p1 2.38.3.1.2 (213-312) Elongation factor Tu (EF-Tu), domain 2 {Thermus aquaticus}
pvrdvdkpflmpvedvftitgrgtvatgriergkvkvgdeveivglapetrktvvtgvem
hrktlqegiagdnvglllrgvsreevergqvlakpgsitp
>d1b23p2 2.39.1.1.2 (313-405) Elongation factor Tu (EF-Tu), C-terminal domain {Thermus aquaticus}
htkfeasvyilkkeeggrhtgfftgyrpqfyfrttdvtgvvrlpqgvemvmpgdnvtftv
elikpvaleeglrfaireggrtvgagvvtkile
>d1b23p3 3.30.1.6.15 (1-212) Elongation factor Tu (EF-Tu), N-terminal (G) domain {Thermus aquaticus}
akgefirtkphvnvgtighvdhgkttltaaltyvaaaenpnvevkdygdidkapeerarg
itintahveyetakrhyshvdcpghadyiknmitgaaqmdgailvvsaadgpmpqtrehi
llarqvgvpyivvfmnkvdmvddpelldlvemevrdllnqyefpgdevpvirgsallale
emhknpktkrgenewvdkiwelldaideyipt
>d1b24a1 4.74.2.1.2 (7-99) I-dmoI {Desulfurococcus mobilis}
vsgisayllgliigdgglyklkykgnrseyrvvitqksenlikqhiaplxqflidelnvk
skiqivkgdtryelrvsskklyyyfanxlerir
>d1b24a2 4.74.2.1.2 (100-179) I-dmoI {Desulfurococcus mobilis}
lfnxreqiafikglyvaegdktlkrlriwnknkalleivsrwlnnlgvrntihlddhrhg
vyvlnislrdrikfvhtils
>d1b25a1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25a2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25b1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25b2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25c1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25c2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b25d1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b25d2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b27a_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b27b_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b27c_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>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
>d1b2ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b2ja_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2ma_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1b2mb_ 4.1.1.1.3 RNase T1 {Aspergillus oryzae}
acdytcgsncysssdvstaqaagyqlhedgetvgsnsyphkynnyegfdfsvsspyyewp
ilssgdvysggspgadrvvfnennqlagvithtgasgnnfvect
>d1b2na_ 2.61.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1b2nb_ 1.125.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1b2nc_ 2.61.1.1.1 Methanol dehydrogenase, heavy chain {Methylophilus methylotrophus, w3a1}
dadldkqvntagawpiatggyysqhnsplaqinksnvknvkaawsfstgvlnghegaplv
igdmmyvhsafpnntyalnlndpgkivwqhkpkqdastkavmccdvvdrglaygagqivk
kqanghllaldaktgkinwevevcdpkvgstltqapfvakdtvlmgcsgaelgvrgavna
fdlktgelkwrafatgsddsvrlakdfnsanphygqfglgtktwegdawkigggtnwgwy
aydpklnlfyygsgnpapwnetmrpgdnkwtmtiwgrdldtgmakwgyqktphdewdfag
vnqmvltdqpvngkmtpllshidrngilytlnrengnlivaekvdpavnvfkkvdlktgt
pvrdpefatrmdhkgtnicpsamgfhnqgvdsydpesrtlyaglnhicmdwepfmlpyra
gqffvgatlamypgpngptkkemgqirafdlttgkakwtkwekfaawggtlytkgglvwy
atldgylkaldnkdgkelwnfkmpsggigspmtysfkgkqyigsmygvggwpgvglvfdl
tdpsaglgavgafrelqnhtqmggglmvfsl
>d1b2nd_ 1.125.1.1.1 Methanol dehydrogenase, light chain {Methylophilus w3a1}
ydgqnckepgncwenkpgypekiagskydpkhdpvelnkqeesikamdarnakrian
>d1b2oa_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2ob_ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcvyiynpedgdpdngvnpgtdfkdipddwvcplcavgkdqfeevee
>d1b2pa_ 2.69.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1b2pb_ 2.69.1.1.4 Lectin (agglutinin) {Bluebell (Scilla campanulata)}
nniifskqpddnhpqilhatesleilfgthvyrfimqtdcnlvlydnnnpiwatntgglg
ngcravlqpdgvlvvitnenvtvwqspvagkaghyvlvlqpdrnvviygdalwatqtvr
>d1b2sa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2sb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2sc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>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
>d1b2ua_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2ub_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2uc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitaseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>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
>d1b2va_ 4.29.1.1.1 Heme-binding protein A (HasA) {Serratia marcescens}
afsvnydssfggysihdylgqwastfgdvnhtngnvtdansggfyggslsgsqyaissta
nqvtafvaggnltytlfnepahtlygqldslsfgdglsggdtspysiqvpdvsfgglnls
slqaqghdgvvhqvvyglmsgdtgaletalngilddyglsvnstfdqvaaata
>d1b2wh1 2.1.1.1.120 (2-117) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
vqlvqsgggvvqpgrslklsclasgyiftsswinwvkqrpgrglewigridpsdgevhyn
qdfkdrftisrdkskntlylqmnslrpedtavyycargflpwfadwgqgtlvtvss
>d1b2wh2 2.1.1.2.118 (118-220) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1b2wl1 2.1.1.1.120 (1-107) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
diqmtqspstlsasvgdrvtitckasenvdtyvswyqqkpgkapklliygasnrytgvps
rfsgsgsgtdftltisslqpddfatyycgqsynypftfgqgtkvevk
>d1b2wl2 2.1.1.2.118 (108-214) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1b2xa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2xb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2xc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1b2za_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b2zb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b2zc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinytsgfrnsdrilyssnwliykttdhyqtftkir
>d1b30a_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b31a_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b32a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b33a_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33b_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33c_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33d_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33e_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33f_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33g_ 4.25.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>d1b33h_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33i_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33j_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33k_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33l_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
sivtksivnadaearylspgeldriksfvssgekrlriaqiltdnrerivkqagdqlfqk
rpdvvspggnaygqemtatclrdldyylrlitygivagdvtpieeigivgvremykslgt
pidavaagvsamknvassilsaedaaeagayfdyvagala
>d1b33m_ 1.1.1.2.4 Allophycocyanin {Cyanobacterium (Mastigocladus laminosus)}
mqdaitavinssdvqgkyldtaaleklksyfstgelrvraattiaanaaaivkeavaksl
lysditrpggnmyttrryaacirdldyylryatyamlagdpsildervlnglketynslg
vpisatvqaiqamkevtaslvgpdagkemgvyfdyicsgls
>d1b33n_ 4.25.1.1.1 Allophycocyanin linker chain (domain) {Mastigocladus laminosus}
grlfkitacvpsqtrirtqrelqntyftklvpyenwfreqqriqkmggkivkvelatgkq
gintgla
>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
>d1b38a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>d1b39a_ 4.117.1.1.1 Cyclin-dependent PK (different isozymes) {Human (Homo sapiens)}
menfqkvekigegtygvvykarnkltgevvalkkirldtetegvpstaireisllkelnh
pnivklldvihtenklylvfeflhqdlkkfmdasaltgiplpliksylfqllqglafchs
hrvlhrdlkpqnllintegaikladfglarafgvpvrtythevvtlwyrapeillgckyy
stavdiwslgcifaemvtrralfpgdseidqlfrifrtlgtpdevvwpgvtsmpdykpsf
pkwarqdfskvvppldedgrsllsqmlhydpnkrisakaalahpffqdvtkpvphlrl
>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
>d1b3ca_ 7.3.7.1.2 Scorpion toxin {Centruroides sculpturatus ewing, beta}
kdgylvektgckktcyklgendfcnreckwkhiggsygycygfgcyceglpdstqtwplp
nktc
>d1b3ea_ 3.84.1.2.8 Transferrin {Human (Homo sapiens)}
ktvrwcavseheatkcqsfrdhmksvipsdgpsvacvkkasyldciraiaaneadavtld
aglvydaylapnnlkpvvaefygskedpqtfyyavavvkkdsgfqmnqlrgkkschtglg
rsagwnipigllycdlpeprkplekavanffsgscapcadgtdfpqlcqlcpgcgcstln
qyfgysgafkclkdgagdvafvkhstifenlankadrdnyellcldntrkpvdeykdchl
aqvpshtvvarsmggkedliwellnqaqehfgkdkskefqlfssphgkdllfkdsahgfl
kvpprmdakmylgyeyvtairnlregtcpe
>d1b3fa_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ga_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3ia_ 2.5.1.1.15 Plastocyanin {Photosynthetic prokaryote (Prochlorothrix hollandica)}
asvqikmgtdkyaplyepkalsisagdtvefvmnkvgphnvifdkvpagesapalsntkl
aiapgsfysvtlgtpgtysfyctphrgagmvgtitve
>d1b3ja1 2.1.1.2.19 (181-274) MHC I homolog Mic-a {Human (Homo sapiens)}
tvppmvnvtrseasegnitvtcrasgfypwnitlswrqdgvslshdtqqwgdvlpdgngt
yqtwvatricqgeeqrftcymehsgnhsthpvps
>d1b3ja2 4.17.1.1.26 (1-180) MHC I homolog Mic-a {Human (Homo sapiens)}
ephslrynltvlswdgsvqsgfltevhldgqpflrcdrqkcrakpqgqwaedvlgnktwd
retrdltgngkdlrmtlahikdqkeglhslqeirvceihednstrssqhfyydgelflsq
nletkewtmpqssraqtlamnvrnflkedamktkthyhamhadclqelrrylksgvvlrr
>d1b3la_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3lc_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b3na1 3.85.1.1.2 (2-251) Beta-ketoacyl carrier protein synthase {Escherichia coli}
krrvvvtglgmlspvgntvestwkallagqsgislidhfdtsayatkfaglvkdfncedi
isrkeqrkmdafiqygivagvqamqdsgleiteenatrigaaigsgigglglieenhtsl
mnggprkispffvpstivnmvaghltimyglrgpsisiatactsgvhnighaariiaygd
advmvaggaekastplgvggfgaaralstrndnpqaasrpwdkerdgfvlgdgagmlvle
eyehakkrga
>d1b3na2 3.85.1.1.2 (252-412) Beta-ketoacyl carrier protein synthase {Escherichia coli}
kiyaelvgfgmssdayhmtsppengagaalamanalrdagieasqigyvnahgtstpagd
kaeaqavktifgeaasrvlvsstksmtghllgaagavesiysilalrdqavpptinldnp
degcdldfvphearqvsgmeytlcnsfgfggtngslifkki
>d1b3oa1 3.1.6.2.2 (10-109,232-499) Inosine monophosphate dehydrogenase (IMPDH) {Human (Homo sapiens)}
tsyvpddgltaqqlfncgdgltyndflilpgyidftadqvdltsaltkkitlktplvssp
mdtvteagmaiamaltggigfihhnctpefqanevrkvkkXdyplaskdakkqllcgaai
gtheddkyrldllaqagvdvvvldssqgnsifqinmikyikdkypnlqviggnvvtaaqa
knlidagvdalrvgmgsgsicitqevlacgrpqatavykvseyarrfgvpviadggiqnv
ghiakalalgastvmmgsllaatteapgeyffsdgirlkkyrgmgsldamdkhlssqnry
fseadkikvaqgvsgavqdkgsihkfvpyliagiqhscqdigaksltqvrammysgelkf
ekrtssaqv
>d1b3ob1 3.1.6.2.2 (10-111,232-499) Inosine monophosphate dehydrogenase (IMPDH) {Human (Homo sapiens)}
tsyvpddgltaqqlfncgdgltyndflilpgyidftadqvdltsaltkkitlktplvssp
mdtvteagmaiamaltggigfihhnctpefqanevrkvkkyeXdyplaskdakkqllcga
aigtheddkyrldllaqagvdvvvldssqgnsifqinmikyikdkypnlqviggnvvtaa
qaknlidagvdalrvgmgsgsicitqevlacgrpqatavykvseyarrfgvpviadggiq
nvghiakalalgastvmmgsllaatteapgeyffsdgirlkkyrgmgsldamdkhlssqn
ryfseadkikvaqgvsgavqdkgsihkfvpyliagiqhscqdigaksltqvrammysgel
kfekrtssaqv
>d1b3ob2 4.30.1.1.1 (112-159) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
qgfitdpvvlspkdrvrdvfeakarhgfcgipitdtgrmgsrlvgiis
>d1b3ob3 4.30.1.1.1 (178-231) Type II inosine monophosphate dehydrogenase {Human (Homo sapiens)}
imtkredlvvapagitlkeaneilqrskkgklpivneddelvaiiartdlkknr
>d1b3ra1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3ra2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rb1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rb2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rc1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rc2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3rd1 3.2.1.4.9 (190-352) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
nlygcreslidgikratdvmiagkvavvagygdvgkgcaqalrgfgarviiteidpinal
qaamegyevttmdeackegnifvtttgcvdiilgrhfeqmkddaivcnighfdveidvkw
lnenavekvnikpqvdryllknghriillaegrlvnlgcamgh
>d1b3rd2 3.16.9.3.2 (4-189,353-431) S-adenosylhomocystein hydrolase {Rat (Rattus norvegicus)}
lpykvadiglaawgrkaldiaenempglmrmremysaskplkgariagclhmtvetavli
etlvalgaevrwsscnifstqdhaaaaiakagipvfawkgetdeeylwcieqtlhfkdgp
lnmilddggdltnlihtkhpqllsgirgiseetttgvhnlykmmangilkvpainvndsv
tkskfdXpsfvmsnsftnqvmaqielwthpdkypvgvhflpkkldeavaeahlgklnvkl
tkltekqaqylgmpingpfkpdhyry
>d1b3sa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>d1b3sb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>d1b3sc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyssdwliykttdayqtftkir
>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
>d1b3ta_ 4.47.8.1.4 Epstein barr virus nuclear antigen-1 (ebna1) {Epstein-Barr virus}
kggwfgkhrgqggsnpkfeniaeglrallarshverttdegtwvagvfvyggsktslynl
rrgtalaipqcrltplsrlpfgmapgpgpqpgplresivcyfmvflqthifaevlkdaik
dlvmtkpaptcnirvtvcsfddgvdlp
>d1b3tb_ 4.47.8.1.4 Epstein barr virus nuclear antigen-1 (ebna1) {Epstein-Barr virus}
kggwfgkhrgqggsnpkfeniaeglrallarshverttdegtwvagvfvyggsktslynl
rrgtalaipqcrltplsrlpfgmapgpgpqpgplresivcyfmvflqthifaevlkdaik
dlvmtkpaptcnirvtvcsfddgvdlp
>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
>d1b3ub_ 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
>d1b3va_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3wa_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3xa_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3ya_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b3za_ 3.1.7.3.15 Xylanase A, catalytic core {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1b40a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b42__ 3.56.1.4.1 Polymerase regulatory subunit VP39 {Vaccinia virus}
mdvvsldkpfmyfeeidneldyepesanevakklpyqgqlklllgelfflsklqrhgild
gatvvyigsapgthirylrdhfynlgviikwmlidgrhhdpilnglrdvtlvtrfvdeey
lrsikkqlhpskiilisdvrskrggnepstadllsnyalqnvmisilnpvasslkwrcpf
pdqwikdfyiphgnkmlqpfapsysaemrllsiytgenmrltrvtksdavnyekkmyyln
kivrnkvvvnfdypnqeydyfhmyfmlrtvycnktfpttkakvlflqqsifrflnip
>d1b44d_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44e_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklagf
>d1b44f_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44g_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b44h_ 2.35.2.1.1 Heat-labile toxin {Escherichia coli, type IB}
apqsitelcseyhntqiytindkilsytesmagkremviitfksgatfqvevpgsqhids
qkkaiermkdtlrityltetkidklcvwnnktpnsiaaismeklag
>d1b46a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b47a1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47a2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47a3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47b1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47b2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47b3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b47c1 1.42.1.7.4 (178-263) Cbl {Human (Homo sapiens)}
tfritkadaaefwrkafgektivpwksfrqalhevhpissgleamalkstidltcndyis
vfefdiftrlfqpwssllrnwnslav
>d1b47c2 1.51.1.1.1 (47-177) N-terminal domain of cbl (N-cbl) {Human (Homo sapiens)}
ppgtvdkkmvekcwklmdkvvrlcqnpklalknsppyildllpdtyqhlrtilsryegkm
etlgeneyfrvfmenlmkktkqtislfkegkermyeensqprrnltklslifshmlaelk
gifpsglfqgd
>d1b47c3 4.72.1.1.19 (264-350) Cbl {Human (Homo sapiens)}
thpgymafltydevkarlqkfihkpgsyifrlsctrlgqwaigyvtadgnilqtiphnkp
lfqalidgfregfylfpdgrnqnpdlt
>d1b48a1 1.48.1.1.10 (80-222) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvrivlkf
>d1b48a2 3.38.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1b48b1 1.48.1.1.10 (80-222) Glutathione S-transferase {Mouse (Mus musculus)}
nlygkdlkervridmyadgtqdlmmmiavapfktpkekeesydlilsraktryfpvfeki
lkdhgeaflvgnqlswadiqlleailmveelsapvlsdfpllqafktrisniptikkflq
pgsqrkpppdgpyvevvrivlkf
>d1b48b2 3.38.1.5.10 (2-79) Glutathione S-transferase {Mouse (Mus musculus)}
aakpklyyfngrgrmesirwllaaagvefeeefletreqyekmqkdghllfgqvplveid
gmmltqtrailsylaaky
>d1b49a_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b49c_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b4aa1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4aa2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ab1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ab2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ac1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ac2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ad1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ad2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ae1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4ae2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4af1 1.4.3.3.2 (4-78) Arginine repressor (ArgR), N-terminal DNA-binding domain {Bacillus stearothermophilus}
gqrhikireiimsndietqdelvdrlreagfnvtqatvsrdikemqlvkvpmangrykys
lpsdqrfnplqklkr
>d1b4af2 4.56.2.1.2 (79-149) C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ba_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bb_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4bc_ 4.56.2.1.2 C-terminal domain of arginine repressor {Bacillus stearothermophilus}
alvdvfikldgtgnllvlrtlpgnahaigvlldnldwdeivgticgddtcliicrtpkda
kkvsnqllsml
>d1b4ca_ 1.42.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1b4cb_ 1.42.1.2.2 Calcyclin (S100) {Rat (Rattus norvegicus), s100b}
mselekamvalidvfhqysgregdkhklkkselkelinnelshfleeikeqevvdkvmet
ldedgdgecdfqefmafvsmvttacheffehe
>d1b4d__ 3.77.1.2.1 Glycogen phosphorylase {Rabbit (Oryctolagus cuniculus)}
isvrglagvenvtelkknfnrhlhftlvkdrnvatprdyyfalahtvrdhlvgrwirtqq
hyyekdpkriyylslefymgrtlqntmvnlalenacdeatyqlgldmeeleeieedaglg
ngglgrlaacfldsmatlglaaygygiryefgifnqkicggwqmeeaddwlrygnpweka
rpeftlpvhfygrvehtsqgakwvdtqvvlampydtpvpgyrnnvvntmrlwsakapndf
nlkdfnvggyiqavldrnlaenisrvlypndnffegkelrlkqeyfvvaatlqdiirrfk
sskfgcrdpvrtnfdafpdkvaiqlndthpslaipelmrvlvdlerldwdkawevtvktc
aytnhtvipealerwpvhlletllprhlqiiyeinqrflnrvaaafpgdvdrlrrmslve
egavkrinmahlciagshavngvarihseilkktifkdfyelephkfqnktngitprrwl
vlcnpglaeiiaerigeeyisdldqlrkllsyvddeafirdvakvkqenklkfaaylere
ykvhinpnslfdvqvkriheykrqllnclhvitlynrikkepnkfvvprtvmiggkaapg
yhmakmiiklitaigdvvnhdpvvgdrlrviflenyrvslaekvipaadlseqistagte
asgtgnmxfmlngaltigtmdganvemaeeageenffifgmrvedvdrldqrgynaqeyy
dripelrqiieqlssgffspkqpdlfkdivnmlmhhdrfkvfadyeeyvkcqervsalyk
nprewtrmvirniatsgkfssdrtiaqyareiwgvepsrqrlp
>d1b4fa_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fb_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
trpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkki
lnsiqvmraqmnqiqsv
>d1b4fc_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4fd_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqs
>d1b4fe_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqiqs
>d1b4ff_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsve
>d1b4fg_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
pdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkiln
siqvmraqmnqi
>d1b4fh_ 1.61.1.2.2 EphB2 receptor {Human (Homo sapiens)}
rpdytsfntvdewleaikmgqykesfanagftsfdvvsqmmmedilrvgvtlaghqkkil
nsiqvmraqmnqiqsv
>d1b4ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b4jh1 2.1.1.1.120 (2-117) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
vqlqqpgadlvmpgapvklsclasgyiftsswinwvkqrpgrglewigridpsdgevhyn
qdfkdkatltvdkssstayiqlnsltsedsavyycargflpwfadwgqgtlvtvsa
>d1b4jh2 2.1.1.2.118 (118-220) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkvepksc
>d1b4jl1 2.1.1.1.120 (1-107) Immunoglobulin (variable domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
nivmtqspksmyvsigervtlsckasenvdtyvswyqqkpeqspklliygasnrytgvpd
rftgsgsatdftltissvqaedladyhcgqsynypftfgsgtkleik
>d1b4jl2 2.1.1.2.118 (108-214) Immunoglobulin (constant domains of L and H chains) {Humanized and chimeric anti-gamma-interferon Fab}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1b4ka_ 3.1.9.3.2 5-aminolevulinate dehydratase (porphobilinogen synthase) {Pseudomonas aeruginosa}
ypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsidqll
ieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgiitdva
ldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigaireal
esaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhevaad
laegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesviles
ltafkragadgiltyfakqaaeqlrr
>d1b4kb_ 3.1.9.3.2 5-aminolevulinate dehydratase (porphobilinogen synthase) {Pseudomonas aeruginosa}
anraypytrlrrnrrddfsrrlvrenvltvddlilpvfvldgvnqresipsmpgverlsi
dqllieaeewvalgipalalfpvtpvekksldaaeaynpegiaqratralrerfpelgii
tdvaldpftthgqdgildddgyvlndvsidvlvrqalshaeagaqvvapsdmmdgrigai
realesaghtnvrimaysakyasayygpfrdavgsasnlgkgnkatyqmdpansdealhe
vaadlaegadmvmvkpgmpyldivrrvkdefraptfvyqvsgeyamhmgaiqngwlaesv
ilesltafkragadgiltyfakqaaeqlrr
>d1b4m__ 2.53.1.2.11 Cellular retinol-binding protein II (CRBP) {Rat (Rattus rattus)}
mtkdqngtwemesnenfegymkaldidfatrkiavrltqtkiivqdgdnfktktnstfrn
ydldftvgvefdehtkgldgrnvktlvtwegntlvcvqkgekenrgwkqwvegdklylel
tcgdqvcrqvfkkk
>d1b4na1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4na2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nb1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nb2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nc1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nc2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4nd1 1.104.1.1.2 (211-619) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
dkeelkklsqeayneilnspgypfwkrqgtmaavewcntnyalptrnfsdgyfefarsid
gytmegmkvqqrgcpycnmpcgnvvldaegqeseldyenvallgsnlgigklnevsvlnr
iademgmdtislgvsiahvmeavergilkegptfgdfkgakqlaldiayrkgelgnlaae
gvkamaeklgthdfamhvkglevsgyncyiypamalaygtsaigahhkeawviaweigta
piegekaekveykisydpikaqkvvelqrlrgglfemltacrlpwvevglsldyypkllk
aitgvtytwddlykaadrvysliraywvrefngkwdrkmdyppkrwfteglksgphkgeh
ldekkydellseyyrirgwdergipkketlkeldldfvipelekvtnle
>d1b4nd2 4.123.1.1.2 (1-210) Formaldehyde ferredoxin oxidoreductase {Pyrococcus furiosus}
mygwwgrilrvnlttgevkvqeypeevakkfiggrglaawilwneargveplspenklif
aagpfnglptpsggklvvaakspltggygdgnlgtmasvhlrragydalvvegkakkpvy
iyieddnvsilsaeglwgkttfeterelkeihgknvgvltigpagenlvkyavvisqegr
aagrpgmgavmgskklkavvirgtkeipva
>d1b4r__ 2.1.3.1.1 Polycystein-1, PKD-1 {Human (Homo sapiens)}
atlvgphgplasgqlaafhiaaplpvtatrwdfgdgsaevdaagpaashryvlpgryhvt
avlalgagsallgtdvqvea
>d1b4sa_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4sb_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4sc_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniiggsd
svesanreialwfkpeelltevkpnpnlye
>d1b4ua_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1b4ub_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1b4uc_ 1.85.1.1.1 LigA subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
idvhaylaefddipgtrvftaqrarkgynlnqfamslmkaenrerfkadesayldewnlt
paakaavlardynamideggnvyflsklfstdgksfqfaagsmtgmtqeeyaqmmidggr
spagvrsikggy
>d1b4ud_ 3.47.5.1.1 LigB subunit of an aromatic-ring-opening dioxygenase LigAB {Pseudomonas paucimobilis}
arvttgitsshipalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpdvvilvyndh
asafdmniiptfaigcaetfkpadegwgprpvpdvkghpdlawhiaqslildefdmtimn
qmdvdhgctvplsmifgepeewpckvipfpvnvvtypppsgkrcfalgdsiraavesfpe
dlnvhvwgtggmshqlqgpraglinkefdlnfidklisdpeelskmphiqylresgsegv
elvmwlimrgalpekvrdlytfyhipasntalgamilqpeetagtpleprkvmsghsl
>d1b4v_1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1b4v_2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaeiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyhplg
>d1b4za_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>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
>d1b51a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b52a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>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
>d1b54__ 3.1.5.2.1 "Hypothetical" protein ybl036c {Baker's yeast (Saccharomyces cerevisiae)}
gitydedrktqliaqyesvrevvnaeaknvhvnenaskilllvvsklkpasdiqilydhg
vrefgenyvqeliekakllpddikwhfigglqtnkckdlakvpnlysvetidslkkakkl
nesrakfqpdcnpilcnvqintshedqksglnneaeifevidfflseeckyiklnglmti
gswnvshedskenrdfatlvewkkkidakfgtslklsmgmsadfreairqgtaevrigtd
ifg
>d1b55a_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1b55b_ 2.49.1.1.5 Bruton's tyrosine kinase {Human (Homo sapiens)}
aavilesiflkrsqqkkktsplnfkkrlflltvhklsyyeydfergrrgskkgsidveki
tcvetvvpeknppperqiprrgeessemeqisiierfpypfqvvydegplyvfspteelr
krwihqlknvirynsdlvqkyhpcfwidgqylccsqtaknamgcqilen
>d1b56__ 2.53.1.2.5 Epidermal fatty acid binding protein {Human (Homo sapiens)}
tvqqlegrwrlvdskgfdeymkelgvgialrkmgamakpdciitcdgknltiktestlkt
tqfsctlgekfeettadgrktqtvcnftdgalvqhqewdgkestitrklkdgklvvecvm
nnvtctriyekve
>d1b58a_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5a__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5b__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1b5da_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
yvgkya
>d1b5dc_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
yvgkya
>d1b5ea_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>d1b5ec_ 4.91.1.1.7 dCMP hydroxymethylase {Bacteriophage T4}
misdsmtveeirlhlglalkekdfvvdktgvktieiigasfvadepfifgalndeyiqre
lewykskslfvkdipgetpkiwqqvasskgeinsnygwaiwsednyaqydmclaelgqnp
dsrrgimiytrpsmqfdynkdgmsdfmctntvqylirdkkinavvnmrsndvvfgfrndy
awqkyvldklvsdlnagdstrqykagsiiwnvgslhvysrhfylvdhwwktgethiskkd
y
>e1b5f.1a 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
gsavvaltndrdtsyfgeigigtppqkftvifdtgssvlwvpsskcinskacrahsmyes
sdsstykengtfgaiiygtgsitgffsqdsvtigdlvvkeqdfieatdeadnvflhrlfd
gilglsfqtisvpvwynmlnqglvkerrfsfwlnrnvdeeeggelvfggldpnhfrgdht
yvpvtyqyywqfgigdvligdkstgfcapgcqafadsgtsllsgptaivtqinhaigan
>e1b5f.1b 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>e1b5f.2c 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
savvaltndrdtsyfgeigigtppqkftvifdtgssvlwvpsskcinskacrahsmyess
dsstykengtfgaiiygtgsitgffsqdsvtigdlvvkeqdfieatdeadnvflhrlfdg
ilglsfqtisvpvwynmlnqglvkerrfsfwlnrnvdeeeggelvfggldpnhfrgdhty
vpvtyqyywqfgigdvligdkstgfcapgcqafadsgtsllsgptaivtqinhaigan
>e1b5f.2d 2.44.1.2.7 Plant acid proteinase, phytepsin {Cynara cardunculus}
eelqvdcntlssmpnvsftiggkkfgltpeqyilkvgkgeatqcisgftamdatllgplw
ilgdvfmrpyhtvfdygnllvgfaeaa
>e1b5g.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>e1b5g.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
eadcglrplfekksledkterellesyid
>d1b5ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5ia_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5ja_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b5l__ 1.27.1.3.7 Interferon-tau {Sheep (Ovis aries)}
cylsrklmldarenlklldrmnrlsphsclqdrkdfglpqemvegdqlqkdqafpvlyem
lqqsfnlfytehssaawdttlleqlctglqqqldhldtcrgqvmgeedselgnmdpivtv
kkyfqgiydylqekgysdcaweivrvemmraltvsttlqkrltk
>d1b5m__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
avtyyrleevakrntaeetwmvihgrvyditrflsehpggeevlleqagadatesfedvg
hspdaremlkqyyigdvhpndlkp
>d1b5sa_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5sb_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5sc_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfkai
aaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllvp
vikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhpe
vailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpelll
m
>d1b5sd_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5se_ 3.35.1.1.4 Dihydrolipoamide acetyltransferase {Bacillus stearothermophilus}
aaakpattegefpetrekmsgirraiakamvhskhtaphvtlmdeadvtklvahrkkfka
iaaekgikltflpyvvkalvsalreypvlntsiddeteeiiqkhyynigiaadtdrgllv
pvikhadrkpifalaqeinelaekardgkltpgemkgasctitnigsaggqwftpvinhp
evailgigriaekpivrdgeivaapmlalslsfdhrmidgataqkalnhikrllsdpell
lm
>d1b5ta_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
gainvsfeffpprtaemeatlwnsidrlsslapkfvsvtygansgerdathsiikgiadr
tgleaaphltcidatpdelrtiardywnngirhivalrgdlppgsgapamyasdlvtllk
evadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvs
agidveiipgilpvsnfkqakkfaamtnvripawmaqmfdgldddaetrklvganiamdm
vkilsaegvadfhfytlnraemsyaichtlgvrpa
>d1b5tb_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
qinvsfeffpprtaemeqtlwnsidrlsslapkfvsvtyganagaraathsiiagiadrt
gleaaphltcidatpdelrtiardywnngirhivalrgdlppgagapamyasdlvtllke
vadfdisvaaypevhpeaksaqadllnlkrkvdaganraitqfffdvesylrfrdrcvsa
gidvaiipgilpvsnfaqaaafadmtnvripawmaqmfdgldddaetrklvganiamdmv
ailsregvkdfhfytlnraemsyaichtlgvapg
>d1b5tc_ 3.1.21.1.1 Methylenetetrahydrofolate reductase {Escherichia coli}
qinvsfeffpprtaameqtlwnsidrlsslapafvsvtygaaageadathsiiagiadrt
gleaaphltcvdaapaelrtiaaaywaagiahivalrgdlppyasdlvtllkevadfdis
vaaypevhpeaasaqadllnlkrkvdaganraitqfffdvasylafrdrcvsagidveii
pgilpvsnfkqakafaamtnvripawmaqmfdgldddaetralvganiamdmvailsaeg
vadfhfytlnraemsyaichtlgvrpa
>d1b5u__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgialanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5v__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
arywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5w__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
arywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5x__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlacsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5y__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakweagyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b5za_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscaallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b5zb_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscaallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b62a1 4.12.1.3.1 (217-332) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlqq
>d1b62a2 4.96.1.2.2 (1-216) DNA mismatch repair protein MutL {Escherichia coli}
mpiqvlppqlanqiaagevverpasvvkelvensldagatrididierggaklirirdng
cgikkdelalalarhatskiaslddleaiislgfrgealasissvsrltltsrtaeqqea
wqayaegrdmnvtvkpaahpvgttlevldlfyntparrkflrtektefnhideiirrial
arfdvtinlshngkivrqyravpeggqkerrlgaic
>d1b63a1 4.12.1.3.1 (217-331) DNA mismatch repair protein MutL {Escherichia coli}
gtafleqalaiewqhgdltlrgwvadpnhttpalaeiqycyvngrmmrdrlinhairqac
edklgadqqpafvlyleidphqvdvnvhpakhevrfhqsrlvhdfiyqgvlsvlq
>d1b63a2 4.96.1.2.2 (1-216) DNA mismatch repair protein MutL {Escherichia coli}
mpiqvlppqlanqiaagevverpasvvkelvensldagatrididierggaklirirdng
cgikkdelalalarhatskiaslddleaiislgfrgealasissvsrltltsrtaeqqea
wqayaegrdmnvtvkpaahpvgttlevldlfyntparrkflrtektefnhideiirrial
arfdvtinlshngkivrqyravpeggqkerrlgaic
>d1b64__ 4.47.12.1.1 Guanine nucleotide exchange factor domain from elongation factor-1 beta {Human (Homo sapiens)}
mlvakssilldvkpwddetdmakleecvrsiqadglvwgssklvpvgygikklqiqcvve
ddkvgtdmleeqitafedyvqsmdvaafnki
>d1b65a_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65b_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65c_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65d_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65e_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b65f_ 4.125.1.1.1 L-aminopeptidase D-Ala-esterase/amidase {Ochrobactrum anthropi}
kprardlglpftgvtgpynaitdvdgvgvgfqtiieneprpgrkrparsgvtailphmqs
etpvpvyagvhrfngngemtgthwiedggyflgpvvitnthgigmahhatvrwmvdryas
tyqtddflwimpvvaetydgalndingfpvteadvrkaldnvasgpvqegncgggtgmit
ygfkggtgtasrvvefggrsftigalvqanhgqrdwltiagvpvgqhmrdgtpqsqlqer
gsiivvlatdlplmphqlkrlarrasigigrngtpggnnsgdifiafstanqrpmqhrsa
pfldvemvndepldtvylaavdsveeavvnamiaaedmggtpfdrllvqaidherlravl
rqygrla
>d1b66a_ 4.75.1.2.1 6-pyruvoyl tetrahydropterin synthase {Rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1b66b_ 4.75.1.2.1 6-pyruvoyl tetrahydropterin synthase {Rat (Rattus rattus)}
lrrrarlsrlvsfsashrlhspslsaeenlkvfgkcnnpnghghnykvvvtihgeidpvt
gmvmnltdlkeymeeaimkpldhknldldvpyfadvvsttenvavyiwenlqrllpvgal
ykvkvyetdnnivvykge
>d1b69a_ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdaislre
kiaelqkdi
>d1b6ca_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cb_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6cc_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cd_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6ce_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6cf_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6cg_ 4.23.1.1.1 FK-506 binding protein (FKBP12), an immunophilin {Human (Homo sapiens)}
gvqvetispgdgrtfpkrgqtcvvhytgmledgkkfdssrdrnkpfkfmlgkqevirgwe
egvaqmsvgqrakltispdyaygatghpgiipphatlvfdvellkle
>d1b6ch_ 4.117.1.1.19 Type I TGF-beta recetor R4 {Human (Homo sapiens)}
ttlkdliydmttsgsgsglpllvqrtiartivlqesigkgrfgevwrgkwrgeevavkif
ssreerswfreaeiyqtvmlrhenilgfiaadnkdngtwtqlwlvsdyhehgslfdylnr
ytvtvegmiklalstasglahlhmeivgtqgkpaiahrdlksknilvkkngtcciadlgl
avrhdsatdtidiapnhrvgtkrymapevlddsinmkhfesfkradiyamglvfweiarr
csiggihedyqlpyydlvpsdpsveemrkvvceqklrpnipnrwqscealrvmakimrec
wyangaarltalrikktlsqlsqqeg
>d1b6da1 2.1.1.1.153 (1-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
diqmtqspsslsasvgdrvtitcqasqdisrylrwyqqkpgkapkllihaassletgvps
rfsgsgsgtdfsftisslqpedlatyycqqydnlpltfgggtkveik
>d1b6da2 2.1.1.2.138 (108-212) Immunoglobulin (constant domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
rtvaapsvfifppsdeqlksgtasvvcllddfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1b6db1 2.1.1.1.153 (1-107) Immunoglobulin (variable domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
diqmtqspsslsasvgdrvtitcqasqdisrylrwyqqkpgkapkllihaassletgvps
rfsgsgsgtdfsftisslqpedlatyycqqydnlpltfgggtkveik
>d1b6db2 2.1.1.2.138 (108-212) Immunoglobulin (constant domains of L and H chains) {Bence-Jones kappa L chain DEL (human)}
rtvaapsvfifppsdeqlksgtasvvcllddfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrg
>d1b6e__ 4.139.1.1.2 CD94 {Human (Homo sapiens)}
cscqekwvgyrcncyfisseqktwnesrhlcasqkssllqlqntdeldfmsssqqfywig
lsyseehtawlwengsalsqylfpsfetfntknciaynpngnaldescedknryickqql
i
>d1b6g__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaxlmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqaxidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1b6ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b6q__ 1.31.1.1.1 ROP protein {Escherichia coli}
mtkqektalnmarfirsqtltlleklneldpdeqadiceslhdhadelyrsclarf
>d1b6va_ 4.5.1.1.6 Hybrid between ribonuclease A and seminal ribonuclease {Bos taurus}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqankhiivacggkpyvpvhf
dasv
>d1b6vb_ 4.5.1.1.6 Hybrid between ribonuclease A and seminal ribonuclease {Bos taurus}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvkavcsq
kkvtckngqtncyqskstmritdcretgsskypncaykttqankhiivacggkpyvpvhf
dasv
>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
>d1b76a1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1b76a2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnakarywtppryfnmmfqdlrgprggrglla
ylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmeieyf
vrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfphgsl
elegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviepsag
vdrgvlallaeaftreelpngeerivlklkp
>d1b76b1 3.42.1.1.3 (395-505) Glycyl-tRNA synthetase (GlyRS), C-terminal domain {Thermus thermophilus}
qlapikvaviplvknrpeiteyakrlkarllalglgrvlyedtgnigkayrrhdevgtpf
avtvdydtigqskdgttrlkdtvtvrdrdtmeqirlhvdelegflrerlrw
>d1b76b2 4.82.1.1.5 (1-394) Glycyl-tRNA synthetase (GlyRS) {Thermus thermophilus}
aassldelvalckrrgfifqsseiygglqgvydygplgvelknnlkqawwrrnvyerddm
egldasvlthrlvlhysgheatfadpmvdnakarywtppryfnmmfqdlrgprggrglla
ylrpetaqgifvnfknvldatsrklgfgiaqigkafrneitprnfifrvrefeqmeieyf
vrpgedeywhrywveerlkwwqemglsrenlvpyqqppessahyakatvdilyrfphgsl
elegiaqrtdfdlgshtkdqealgitarvlrnehstqrlayrdpetgkwfvpyviepsag
vdrgvlallaeaftreelpngeerivlklkp
>d1b77a1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77a2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b77b1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77b2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b77c1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b77c2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b79a_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1b79b_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivrer
>d1b79c_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivre
>d1b79d_ 1.78.1.1.1 N-terminal domain of DnaB helicase {Escherichia coli}
pphsieaeqsvlgglmldnerwddvaervvaddfytrphrhiftemarlqesgspidlit
laeslerqgqldsvggfaylaelskntpsaanisayadivrer
>d1b7aa_ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsgg
>d1b7ab_ 2.15.1.1.2 Phosphatidylethanolamine binding protein {Bovine (Bos taurus)}
pvdlskwsgplslqevderpqhplqvkyggaevdelgkvltptqvknrptsitwdgldpg
klytlvltdpdapsrkdpkyrewhhflvvnmkgnnissgtvlsdyvgsgppkgtglhryv
wlvyeqegplkcdepilsnrsgdhrgkfkvasfrkkyelgapvagtcyqaewddyvpkly
eqlsgg
>d1b7da_ 7.3.7.1.9 Scorpion toxin {Scorpion (Tityus serrulatus)}
kegylmdhegcklscfirpsgycgrecgikkgssgycawpacycyglpnwvkvwdratnk
c
>d1b7ea_ 3.46.3.4.1 Transposase inhibitor (Tn5 transposase) {Escherichia coli}
saeairkagamqtvklaqefpellaiedttslsyrhqvaeelgklgsiqdksrgwwvhsv
llleattfrtvgllhqewwmrpddpadadekesgkwlaaaatsrlrmgsmmsnviavcdr
eadihaylqdklahnerfvvrskhprkdvesglylydhlknqpelggyqisipqkgvvdk
rgkrknrparkaslslrsgritlkqgnitlnavlaeeinppkgetplkwllltsepvesl
aqalrvidiythrwrieefhkawktgagaerqrmeepdnlermvsilsfvavrllqlres
ftlpqalraqgllkeaehvesqsaetvltpdecqllgyldkgkrkrkekagslqwaymai
arlggfmdskrtgiaswgalwegwealqskldgflaakdlmaq
>d1b7fa1 4.47.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fa2 4.47.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1b7fb1 4.47.7.1.5 (123-204) Sex-lethal protein {Drosophila melanogaster}
sntnlivnylpqdmtdrelyalfraigpintcrimrdyktgysygyafvdftsemdsqra
ikvlngitvrnkrlkvsyarpg
>d1b7fb2 4.47.7.1.5 (205-289) Sex-lethal protein {Drosophila melanogaster}
gesikdtnlyvtnlprtitddqldtifgkygsivqknilrdkltgrprgvafvrynkree
aqeaisalnnvipeggsqplsvrla
>d1b7go1 3.2.1.3.5 (1-138,301-340) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
mvnvavngygtigkrvadaiikqpdmklvgvaktspnyeafiahrrgiriyvpqqsikkf
eesgipvagtvedliktsdivvdttpngvgaqykpiylqlqrnaifqggekaevadisfs
alcnynealgkkyirvvsXesivvpenidairasmklmsaedsmritneslgilkgyli
>d1b7go2 4.61.1.1.5 (139-300) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
cnttallrtictvnkvskvekvrativrraadqkevkkgpinslvpdpatvpshhakdvn
svirnldiatmaviapttlmhmhfinitlkdkvekkdilsvlentprivlisskydaeat
aelvevardlkrdrndipevmifsdsiyvkddevmlmyavhq
>d1b7gq1 3.2.1.3.5 (1-138,301-340) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
mvnvavngygtigkrvadaiikqpdmklvgvaktspnyeafiahrrgiriyvpqqsikkf
eesgipvagtvedliktsdivvdttpngvgaqykpiylqlqrnaifqggekaevadisfs
alcnynealgkkyirvvsXesivvpenidairasmklmsaedsmritneslgilkgyli
>d1b7gq2 4.61.1.1.5 (139-300) Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) {(Sulfolobus solfataricus)}
cnttallrtictvnkvskvekvrativrraadqkevkkgpinslvpdpatvpshhakdvn
svirnldiatmaviapttlmhmhfinitlkdkvekkdilsvlentprivlisskydaeat
aelvevardlkrdrndipevmifsdsiyvkddevmlmyavhq
>d1b7ha_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b7ia_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vrgyaa
>d1b7ja_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlammrsevvtpvgipaediprlvsmqvnravplgttlmpdm
vkgyaa
>d1b7ka_ 2.75.1.1.1 Antifreeze protein type III {Ocean pout (Macrozoarces americanus), different isoforms}
anqasvvanqlipintaltlvmmrsevvtpvgipaediprlvsmqvnhavplgttlmpdm
vkgyaa
>d1b7l__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmcllkwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7m__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7n__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwlsgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7o__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesqyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7p__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnacglscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7q__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislalwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7r__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifgin
srywcndgktpgavnachlscsallqdniadavacakrvvrdpqgirawnawrnrcqnrd
vrqyvqgcgv
>d1b7s__ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgasnachlscsallqdniadavacakrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1b7ta1 2.30.3.1.2 (29-76) Myosin S1 fragment, N-terminal domain {Bay scallop (Aequipecten irradians)}
dgkkncwvpdekegfasaeiqsskgdeitvkivadsstrtvkkddiqs
>d1b7ta2 3.30.1.7.2 (5-28) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
fsdpdfqylavdrkklmkeqtaaf
>d1b7ta3 3.30.1.7.2 (77-835) Myosin S1, motor domain {Bay scallop (Aequipecten irradians)}
mnppkfekledmanmtylneasvlynlrsrytsgliytysglfciavnpyrrlpiytdsv
iakyrgkrkteipphlfsvadnayqnmvtdrenqsclitgesgagktentkkvimylakv
acavkkkdeeasdkkegsledqiiqanpvleaygnakttrnnnssrfgkfirihfgptgk
iagadietylleksrvtyqqsaernyhifyqicsnaipelndvmlvtpdsglysfinqgc
ltvdniddveefklcdeafdilgftkeekqsmfkctasilhmgemkfkqrpreeqaesdg
taeaekvaflcginagdllkallkpkvkvgtemvtkgqnmnqvvnsvgalakslydrmfn
wlvrrvnktldtkakrnyyigvldiagfeifdfnsfeqlcinytnerlqqffnhhmfile
qeeykkegiawefidfgmdlqmcidliekpmgilsileeecmfpkaddksfqdklyqnhm
gknrmftkpgkptrpnqgpahfelhhyagnvpysitgwleknkdpinenvvallgaskep
lvaelfkapeepagggkkkkgkssafqtisavhreslnklmknlysthphfvrciipnel
kqpglvdaelvlhqlqcngvlegiricrkgfpsrliysefkqrysilapnaipqgfvdgk
tvsekilaglqmdpaeyrlgttkvffkagvlgnleemrderlskiismfqahirgylirk
aykklqdqriglsviqrnirkwlvlrnwqwwklyskvkp
>d1b7ty_ 1.42.1.5.15 Myosin Essential Chain {Bay scallop (Aequipecten irradians)}
pqkqiqemkeafsmidvdrdgfvskedikaiseqlgrapddkeltamlkeapgplnftmf
lsifsdklsgtdseetirnafamfdeqetkklnieyikdllenmgdnfnkdemrmtfkea
pveggkfdyvkftamikg
>d1b7tz_ 1.42.1.5.17 Myosin Regulatory Chain {Bay scallop (Aequipecten irradians)}
klsqdeiddlkdvfelfdfwdgrdgavdafklgdvcrclginprnedvfavggthkmgek
slpfeeflpayeglmdceqgtfadymeafktfdregqgfisgaelrhvltalgerlsded
vdeiikltdlqedlegnvkyedfvkkvmagpyp
>d1b7ua1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b7ua2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>e1b7x.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1b7x.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvclpd
retaasllqagykgrvtgwgnlkegqpsvlqvvnlpiverpvckdstriritdnmfcagy
kpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkigfythvfrlkkwi
qkvidq
>d1b7za1 3.84.1.2.4 (1-333) Lactoferrin {Horse (Equus caballus)}
aprksvrwctispaeaakcakfqrnmkkvrgpsvscirktssfeciqaiaankadavtld
gglvyeaglhpyklrpvaaevyqtrgkpqtryyavavvkkgsgfqlnqlqgvkschtglg
rsagwnipigtlrpylnwtgppeplqkavanffsascvpcadgkqypnlcrlcagteadk
cacssqepyfgysgafkclengagdvafvkdstvfenlpdeaerdkyellcpdntrkpvd
afkechlarvpshavvarsvdgredliwkllhraqeefgrnkssafqlfgstpgeqdllf
kdsalgfvripsqidsglylganyltatqnlre
>d1b7za2 3.84.1.2.4 (334-689) Lactoferrin {Horse (Equus caballus)}
taaevaarrervvwcavgpeeerkckqwsdvsnrkvacasastteecialvlkgeadaln
ldggfiyvagkcglvpvlaenqksqnsnapdcvhrppegylavavvrksdadltwnslsg
kkschtgvgrtaawnipmgllfnqtgsckfdkffsqscapgadpqsslcalcvgnnenen
kcmpnseeryygytgafrclaekagdvafvkdvtvlqntdgknsepwakdlkqedfellc
ldgtrkpvaeaeschlarapnhavvsqsdraqhlkkvlflqqdqfggngpdcpgkfclfk
setknllfndnteclaelqgkttyeqylgseyvtsitnlrrcsssplleacaflra
>d1b80a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
viekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispa
meaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagrv
alsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvxmlsa
hsvaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiri
qsdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpi
pgnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b80b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagrvalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvxmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b82a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
viekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispa
meaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagav
alsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvwmlsa
hsvaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiri
qsdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpi
pgnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b82b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagavalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvwmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b85a_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
iekratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispam
eaqgkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagava
lsncpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvfmlsah
svaavndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriq
sdhtiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpip
gnlpfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b85b_ 1.90.1.1.1 Lignin peroxidase {White rot basidiomycete (Phanerochaete chrysosporium)}
ratcsngktvgdasccawfdvlddiqqnlfhggqcgaeahesirlvfhdsiaispameaq
gkfggggadgsimifddietafhpnigldeivklqkpfvqkhgvtpgdfiafagavalsn
cpgapqmnfftgrapatqpapdglvpepfhtvdqiinrvndagefdelelvfmlsahsva
avndvdptvqglpfdstpgifdsqffvetqlrgtafpgsggnqgevesplpgeiriqsdh
tiardsrtacewqsfvnnqsklvddfqfiflaltqlgqdpnamtdcsdvipqskpipgnl
pfsffpagktikdveqacaetpfptlttlpgpetsvqrippppga
>d1b86a_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1b86b_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1b86c_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1b86d_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1b87a_ 4.84.1.1.1 Aminoglycoside 6'-N-acetyltransferase {Enterococcus faecium}
miisefdrnnpvlkdqlsdllrltwpeeygdssaeeveemmnperiavaavdqdelvgfi
gaipqygitgwelhplvvessrrknqigtrlvnylekevasrggitiylgtddldhgttl
sqtdlyehtfdkvasiqnlrehpyefyeklgykivgvlpnangwdkpdiwmaktiiprpd
s
>d1b88a_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1b88b_ 2.1.1.1.155 T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
mqqvrqspqsltvwegetailncsyensafdyfpwyqqfpgegpallisilsvsnkkedg
rftiffnkrekklslhiadsqpgdsatyfcaasasfgdnskliwglgtslvvnp
>d1b89a_ 1.110.1.3.1 Clathrin heavy chain proximal leg segment {Bovine (Bos taurus)}
rlaeleefingpnnahiqqvgdrcydekmydaakllynnvsnfgrlastlvhlgeyqaav
dgarkanstrtwkevcfacvdgkefrlaqxcglhivvhadeleelinyyqdrgyfeelit
xleaalglerahxgxftelailyskfkpqkxrehlelfwsrvnipkvlraaeqahlwael
vflydkyeeydnaiitxxnhptdawkegqfkdiitkvanvelyyraiqfylefkplllnd
llxvlsprldhtravnyfskvkqlplvkpylrsvqnhnnksvneslnnlfiteedyqalr
tsidaydnfdnislaqrlekheliefrriaaylfkg
>d1b8aa1 2.35.4.1.2 (1-103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1b8aa2 4.82.1.1.8 (104-438) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
plpldptgkvkaeldtrlnnrfmdlrrpevmaifkirssvfkavrdffhengfieihtpk
iiatateggtelfpmkyfeedaflaespqlykeimmasgldrvyeiapifraeehnttrh
lneawsidsemafiedeeevmsflerlvahainyvrehnakeldilnfeleepklpfprv
sydkaleilgdlgkeipwgedidtegerllgkymmenenaplyflyqypseakpfyimky
dnkpeicrafdleyrgveissggqrehrhdilveqikekglnpesfefylkafrygmpph
ggfglgaerlikqmldlpnirevilfprdrrrltp
>d1b8ab1 2.35.4.1.2 (1001-1103) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
myrthysseiteelngqkvkvagwvwevkdlggikflwirdrdgivqitapkkkvdpelf
klipklrsedvvavegvvnftpkaklgfeilpekivvlnraet
>d1b8ab2 4.82.1.1.8 (1104-1438) Aspartyl-tRNA synthetase (AspRS) {Pyrococcus kodakaraensis}
plpldptgkvkaeldtrlnnrfmdlrrpevmaifkirssvfkavrdffhengfieihtpk
iiatateggtelfpmkyfeedaflaespqlykeimmasgldrvyeiapifraeehnttrh
lneawsidsemafiedeeevmsflerlvahainyvrehnakeldilnfeleepklpfprv
sydkaleilgdlgkeipwgedidtegerllgkymmenenaplyflyqypseakpfyimky
dnkpeicrafdleyrgveissggqrehrhdilveqikekglnpesfefylkafrygmpph
ggfglgaerlikqmldlpnirevilfprdrrrltp
>d1b8ba_ 3.6.1.2.1 Class III anaerobic ribonucleotide triphosphate reductase NRDD subunit {Bacteriophage T4}
srvfptqrdlmagivskhiaknmvpsfimkahesgiihvhdidyspalpftncclvdlkg
mlengfklgnaqietpksigvataimaqitaqvashqyggttfanvdkvlspyvkrtyak
hiedaekwqiadalnyaqsktekdvydafqayeyevntlfssngqtpfvtltfgtgtdwt
ermiqkailknrikglgrdgitpifpklvmfveegvnlykddpnydikqlalecaskrmy
pdiisaknnkaitgssvpvspmgcrsflsvwkdstgneildgrnnlgvvtlnlprialds
yigtqfneqkfvelfnermdlcfealmcrisslkgvkatvapilyqegafgvrlkpdddi
ielfkngrssvslgyigihelnilvgrdigreiltkmnahlkqwtertgfafslystpae
nlcyrfckldtekygsvkdvtdkgwytnsfhvsveenitpfekisreapyhfiatgghis
yvelpdmknnlkgleavwdyaaqhldyfgvnmpvdkcftcgsthemtptengfvcsicge
tdpkkmntirrtcgylgnpnerg
>d1b8ca_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8cb_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8da_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mksvitttisaadaagrfpsssdlesiqgniqraaarleaaqklsgnheavvkeagdacf
akysylknageagdspekinkcyrdidhymrlinyslvvggtgpvdewgiagsrevyral
nlpgsayiaaftftrdrlcvprdmssqagveftsaldyvinslc
>d1b8db_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mldafsrvvvtsdakaayvggsdlqslksfindgnkrldavnyivsnascivsdavsgmi
cenpgliapggxcytnrrmaaclrdgeiilryvsyallagdssvlddrclnglketyial
gvptasssravsimkatatafitntasgrkvevaagdcqalqaeaasyfdkvgssid
>d1b8dk_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mksvitttisaadaagrfpsssdlesiqgniqraaarleaaqklsgnheavvkeagdacf
akysylknageagdspekinkcyrdidhymrlinyslvvggtgpvdewgiagsrevyral
nlpgsayiaaftftrdrlcvprdmssqagveftsaldyvinslc
>d1b8dl_ 1.1.1.2.6 Phycoerythrin {Red alga (Griffithsia monilis)}
mldafsrvvvtsdakaayvggsdlqslksfindgnkrldavnyivsnascivsdavsgmi
cenpgliapggxcytnrrmaaclrdgeiilryvsyallagdssvlddrclnglketyial
gvptasssravsimkatatafitntasgrkvevaagdcqalqaeaasyfdkvgssid
>d1b8fa_ 1.117.1.2.1 Histidine ammonia-lyase (HAL) {Pseudomonas putida}
teltlkpgtltlaqlraihaapvrlqldasaapaidasvacveqiiaedrtaygintgfg
llastriashdlenlqrslvlshaagigapldddlvrlimvlkinslsrgfsgirrkvid
alialvnaevyphiplkgsvgasgdlaplahmslvllgegkarykgqwlsatealavagl
epltlaakeglallngtqastayalrglfyaedlyaaaiacgglsveavlgsrspfdari
heargqrgqidtaacfrdllgdssevslshknadkvqdpyslrcqpqvmgacltqlrqaa
evlgieanavsdnplvfaaegdvisggnfhaepvamaadnlalaiaeigslserrislmm
dkhmsqlppflvenggvnsgfmiaqvtaaalasenkalshphsvdslptsanqedhvsma
paagkrlwemaentrgvlaiewlgacqgldlrkglktsaklekarqalrsevahydrdrf
fapdiekavellakgsltgllpagvlpsl
>d1b8ha1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8ha2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b8hb1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8hb2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>d1b8hc1 4.105.1.2.1 (1-110) gp45 sliding clamp {Bacteriophage rb69}
mklskdtiailknfasinsgillsqgkfimtravngttyaeanisdeidfdvalydlnsf
lsilslvsddaeismhtdgnikiadtrstvywpaadkstivfpnkpiqfp
>d1b8hc2 4.105.1.2.1 (111-228) gp45 sliding clamp {Bacteriophage rb69}
vasviteikaedlqqllrvsrglqidtiaitnkdgkivingynkvedsgltrpkysltlt
dydgsnnfnfvinmanmkiqpgnykvmlwgagdkvaakfessqvsyviameadsthdf
>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
>d1b8ja_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1b8jb_ 3.64.1.1.1 Alkaline phosphatase {Escherichia coli}
tpempvlenraaqgditapggarrltgdqtaalrdslsdkpakniilligdgmgdseita
arnyaegaggffkgidalpltgqythyalnkktgkpdyvtdxaasatawstgvktyngal
gvdihekdhptilemakaaglatgnvstaelqdatpaalvahvtsrkcygpsatsekcpg
nalekggkgsiteqllnaradvtlgggaktfaetatagewqgktlreqaqargyqlvsda
aslnsvteanqqkpllglfadgnmpvrwlgpkatyhgnidkpavtctpnpqrndsvptla
qmtdkaiellsknekgfflqvegasidkqdhaanpcgqigetvdldeavqralefakkeg
ntlvivtadhahasqivapdtkapgltqalntkdgavmvmsygnseedsqehtgsqlria
aygphaanvvgltdqtdlfytmkaalglk
>d1b8ka_ 7.17.1.3.1 Brain-derived neurotrophic factor/neurotrophin 3 heterodimer, BDNF/NT3 {Human (Homo sapiens)}
ysvcdseslwvtdkssaidirghqvtvlgeiktgnspvkqyfyetrckearpvkngcrgi
ddkhwnsqcktsqtyvraltsennklvgwrwiridtscvcal
>d1b8la_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvddwtalvka
>d1b8ma_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
gelsvcdsisewvtaadkktavdmsggtvtvlekvpvskgqlkqyfyetkcnpmgytkeg
crgidkrhwnsqcrttqsyvraltmdskkrigwrfiridtscvctltik
>d1b8mb_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
gelavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadnaeeggp
gaggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsrtgra
>d1b8na_ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
qngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestv
pghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaaggln
pnfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqm
geqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfsli
tnkvimdyesqgkanheevleagkqaaqkleqfvsllm
>d1b8oa_ 3.47.1.1.2 Purine nucleoside phosphorylase, PNP {Bovine (Bos taurus)}
ngytyedyqdtakwllshteqrpqvavicgsglgglvnkltqaqtfdyseipnfpestvp
ghagrlvfgilngracvmmqgrfhmyegypfwkvtfpvrvfrllgvetlvvtnaagglnp
nfevgdimlirdhinlpgfsgenplrgpneerfgvrfpamsdaydrdmrqkahstwkqmg
eqrelqegtyvmlggpnfetvaecrllrnlgadavgmstvpevivarhcglrvfgfslit
nkvimdyesqgkanheevleagkqaaqkleqfvsllmasi
>d1b8pa1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8pa2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8qa_ 2.32.1.1.6 Neuronal nitric oxide synthase, NNOS {Rat (Rattus norvegicus)}
gshmiepnvisvrlfkrkvgglgflvkervskppviisdlirggaaeqsgliqagdiila
vndrplvdlsydsalevlrgiasethvvlilrgpegftthlettftgdgtpktirvtqpl
gpptkav
>d1b8ra_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiidqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvdewtalvka
>d1b8sa1 3.3.1.2.2 (9-318,451-506) Cholesterol oxidase {Streptomyces}
gyvpavvigtgygaavsalrlgeagvqtlmlemgqlwnqpgpdgnifcgmlnpdkrsswf
knrteaplgsflwldvvnrnidpyagvldrvnydqmsvyvgrgvgggslvnggmavepkr
syfeeilprvdssemydryfpransmlrvnhidtkwfedtewykfarvsreqagkaglgt
vfvpnvydfgymqreaagevpksalateviygnnhgkqsldktylaaalgtgkvtiqtlh
qvktirqtkdggyaltveqkdtdgkllatkeiscrylflgagslgstellvrardtgtlp
nlnsevgagwXgcvlgkatddygrvagyknlyvtdgslipgsvgvnpfvtitalaernve
riikqdv
>d1b8sa2 4.14.1.1.2 (319-450) Cholesterol oxidase {Streptomyces}
gpngnimtaranhmwnptgahqssipalgidawdnsdssvfaqiapmpagletwvslyla
itknpqrgtfvydaatdraklnwtrdqnapavnaakalfdrinkangtiyrydlfgtqlk
afaddfcyhplg
>d1b8ta1 7.33.1.3.1 (1-35) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
mpnwgggkkcgvcqkavyfaeevqcegssfhkscf
>d1b8ta2 7.33.1.3.1 (36-100) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
lcmvckknldsttvavhgdeiyckscygkkygpkgkgkgmgagtlstdkgeslgikyeeg
qshrp
>d1b8ta3 7.33.1.3.1 (101-143) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
tnpnasrmaqkvggsdgcprcgqavyaaekvigagkswhkscf
>d1b8ta4 7.33.1.3.1 (144-192) Cysteine-rich (intestinal) protein, CRP, CRIP {Chicken (Gallus gallus)}
rcakcgkslesttladkdgeiyckgcyaknfgpkgfgfgqgagalihsq
>d1b8ua1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8ua2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8va1 3.2.1.5.6 (3-158) Malate dehydrogenase {Aquaspirillum arcticum}
ktpmrvavtgaagqicysllfriangdmlgkdqpvilqlleipnekaqkalqgvmmeidd
cafpllagmtahadpmtafkdadvallvgarprgpgmerkdlleanaqiftvqgkaidav
asrnikvlvvgnpantnayiamksapslpaknftam
>d1b8va2 4.132.1.1.6 (159-329) Malate dehydrogenase {Aquaspirillum arcticum}
lrldhnralsqiaaktgkpvssieklfvwgnhsptmyadyryaqidgasvkdminddawn
rdtflptvgkrgaaiidargvssaasaanaaidhihdwvlgtagkwttmgipsdgsygip
egvifgfpvttengeykivqglsidafsqerinvtlnelleeqngvqhllg
>d1b8wa_ 7.9.1.1.3 Defensin-like peptide 1 {Duckbilled platypus (Ornithorhynchus anatinus)}
fvqhrprdcesingvcrhkdtvncreifladcyndgqkccrk
>d1b8xa1 1.48.1.1.19 (81-260) Glutathione S-transferase {Escherichia coli}
lggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchkt
ylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyiaw
plqgwqatfgggdhppksdlvprgsrrasvgsrmhypgaftysptpvtsgigigmsamgs
>d1b8xa2 3.38.1.5.19 (1-80) Glutathione S-transferase {Escherichia coli}
spilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyidg
dvkltqsmaiiryiadkhnm
>d1b8ya_ 4.71.1.9.4 Stromelysin-1 (MMP-3) {Human (Homo sapiens), fibroblast}
frtfpgipkwrkthltyrivnytpdlpkdavdsavekalkvweevtpltfsrlyegeadi
misfavrehgdfypfdgpgnvlahayapgpgingdahfdddeqwtkdttgtnlflvaahe
ighslglfhsantealmyplyhsltdltrfrlsqddingiqslygpp
>d1b90a1 2.3.1.1.6 (418-516) beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1b90a2 3.1.7.2.3 (1-417) Bacterial beta-amylase, catalytic domain {Bacillus cereus}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaitvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakiylsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvtftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv
>d1b92a_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacwwagikqefgipynpqsqaviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiqt
>d1b93a_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryla
>d1b93b_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyqryladrl
>d1b93c_ 3.17.1.2.1 Methylglyoxal synthase, MgsA {Escherichia coli}
melttrtlparkhialvahdhckqmlmswverhqplleqhvlyatgttgnlisratgmnv
namlsgpmggdqqvgalisegkidvliffwdplnavphdpdvkallrlatvwnipvatnv
atadfiiqsphfndavdilipdyq
>d1b94a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b94b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b95a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b95b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b96a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqenhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b96b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqenhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b97a_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqlnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b97b_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqlnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1b98a_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
elavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadnaeeggpg
aggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsrtgraaa
qyffetrckadnaeaggpgaggggcrgvdrrhwvseckakqsyvraltavgwrwiridta
cvctllsat
>d1b98m_ 7.17.1.3.2 Neurotrophin 4 heterodimer {Human (Homo sapiens)}
agelavcdavsgwvtdrrtavdlrgrevevlgevpaaggsplrqyffetrckadgggpga
ggggcrgvdrrhwvseckakqsyvraltadaqgrvgwrwiridtacvctllsa
>d1b99a_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99b_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99c_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99d_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99e_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b99f_ 4.47.6.1.3 Nucleoside diphosphate kinases {Dictyostelium discodeum}
vnkertflavkpdgvarglvgeiiaryekkgfvlvglkqlvptkdlaeshyaehkerpff
gglvsfitsgpvvamvfegkgvvasarlmigvtnplasapgsirgdfgvdvgrniihgsd
svesanreialwfkpeelltevkpnpnlye
>d1b9aa_ 1.42.1.4.2 Parvalbumin {Carp (Cyprinus carpio)}
afagvlndadiaaaleackaadsfnhkaffakvgltsksaddvkkafaiiaqdksgfiee
delklflqnfkadaraltdgetktflkagdsdgdgkigvdewtalvka
>d1b9da_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaacwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnkkrkggiggysagerivdiiatdiqt
>d1b9fa_ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
cspgiwqldcthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvht
dngsnftsttvkaacwwagikqefaipynpqsqaviesmnkelkkiigqvrdqaehlkta
vqmavfihnkkrkggiggysagerivdiiatdiqt
>d1b9ga_ 7.1.1.1.5 Insulin-like growth factor {Human (Homo sapiens)}
gpetlcgaelvdalqfvcgdrgfyfnkpgivdeccfrscdlrrlemycaplkpaksa
>d1b9ha_ 3.57.1.4.8 3-amino-5-hydroxybenzoic acid synthase (AHBA synthase) {Amycolatopsis mediterranei}
kapefpawpqyddaernglvraleqgqwwrmggdevnsferefaahhgaahalavtngth
alelalqvmgvgpgtevivpaftfisssqaaqrlgavtvpvdvdaatynldpeavaaavt
prtkvimpvhmaglmadmdalakisadtgvpllqdaahahgarwqgkrvgeldsiatfsf
qngklmtageggavvfpdgetekyetaflrhscgrprddrryfhkiagsnmrlnefsasv
lraqlarldeqiavrderwtllsrllgaidgvvpqggdvradrnshymamfripglteer
rnalvdrlveaglpafaafraiyrtdafwelgapdesvdaiarrcpntdaissdcvwlhh
rvllagepelhataeiiadavara
>d1b9ia_ 3.57.1.4.8 3-amino-5-hydroxybenzoic acid synthase (AHBA synthase) {Amycolatopsis mediterranei}
kapefpawpqyddaernglvraleqgqwwrmggdevnsferefaahhgaahalavtngth
alelalqvmgvgpgtevivpaftfisssqaaqrlgavtvpvdvdaatynldpeavaaavt
prtkvimpvhmaglmadmdalakisadtgvpllqdaahahgarwqgkrvgeldsiatfsf
qngklmtageggavvfpdgetekyetaflrhscgrprddrryfhkiagsnmrlnefsasv
lraqlarldeqiavrderwtllsrllgaidgvvpqggdvradrnshymamfripglteer
rnalvdrlveaglpafaafraiyrtdafwelgapdesvdaiarrcpntdaissdcvwlhh
rvllagepelhataeiiadavgra
>d1b9ja_ 3.84.1.1.1 Oligo-peptide binding protein (OPPA) {Salmonella typhimurium}
advpagvqladkqtlvrnngsevqsldphkiegvpesnvsrdlfegllisdveghpspgv
aekwenkdfkvwtfhlrenakwsdgtpvtahdfvyswqrladpntaspyasylqyghian
iddiiagkkpatdlgvkalddhtfevtlsepvpyfykllvhpsvspvpksavekfgdkwt
qpanivtngayklknwvvnerivlernpqywdnaktvinqvtylpissevtdvnryrsge
idmtynnmpielfqklkkeipnevrvdpylctyyyeinnqkapfndvrvrtalklaldrd
iivnkvknqgdlpaysytppytdgaklvepewfkwsqqkrneeakkllaeagftadkplt
fdllyntsdlhkklaiavasiwkknlgvnvnlenqewktfldtrhqgtfdvaragwcady
neptsflntmlsdssnntahykspafdkliadtlkvaddtqrselyakaeqqldkdsaiv
pvyyyvnarlvkpwvggytgkdpldniyvknlyiikh
>d1b9ka1 2.1.9.1.1 (702-824) Alpa-adaptin AP2, N-terminal subdomain {Mouse (Mus musculus)}
ednfarfvcknngvlfenqllqiglksefrqnlgrmfifygnktstqflnftptlicadd
lqtnlnlqtkpvdptvdggaqvqqviniecisdfteapvlniqfryggtfqnvsvklpit
lnk
>d1b9ka2 4.83.1.1.1 (825-938) Alpa-adaptin AP2, C-terminal subdomain {Mouse (Mus musculus)}
ffqptemasqdffqrwkqlsnpqqevqnifkakhpmdteitkakiigfgsalleevdpnp
anfvgagiihtkttqigcllrlepnlqaqmyrltlrtskdtvsqrlcellseqf
>d1b9oa_ 4.2.1.2.14 alpha-Lactalbumin {Human (Homo sapiens)}
kqftkcelsqllkdidgyggialpelictmfhtsgydtqaivendesteyglfqisnklw
ckssqvpqsrnicdiscdkflddditddimcakkildikgidywlahkalctekleqwlc
ekl
>d1b9ra_ 4.13.6.1.12 Terpredoxin {Pseudomonas}
prvvfideqsgeyavdaqdgqslmevatqngvpgivaecggscvcatcrieiedawveiv
geanpdendllqstgepmtagtrlscqvfidpsmdglivrvplpa
>d1b9sa_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1b9ta_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>d1b9va_ 2.59.1.1.3 Influenza neuraminidase {Influenza virus B, different strains}
epewtyprlscqgstfqkallisphrfgeikgnsapliirepfvacgpkecrhfalthya
aqpggyyngtrkdrnklrhlvsvklgkiptvensifhmaawsgsachdgrewtyigvdgp
dndalvkikygeaytdtyhsyahnilrtqesacnciggdcylmitdgsasgiskcrflki
regriikeilptgrvehteectcgfasnktiecacrdnsytakrpfvklnvetdtaeirl
mctktyldtprpddgsiagpcesngdkwlggikggfvhqrmaskigrwysrtmsktnrmg
melyvrydgdpwtdsdaltlsgvmvsieepgwysfgfeikdkkcdvpcigiemvhdggkd
twhsaataiyclmgsgqllwdtvtgvdmal
>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
>d1b9xa_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
mseldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiya
mhwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldni
csiynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttf
tghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngna
fatgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdal
kadragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1b9xb_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1b9xc_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskermsrkme
iqeyelihqdkedegclrkyrrqcmqdmhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypmvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1b9ya_ 2.60.3.1.1 beta1-subunit of the signal-transducing G protein heterotrimer {Bovine (Bos taurus)}
mseldqlrqeaeqlknqirdarkacadatlsqitnnidpvgriqmrtrrtlrghlakiya
mhwgtdsrlllsasqdgkliiwdsyttnkvhaiplrsswvmtcayapsgnyvacggldni
csiynlktregnvrvsrelaghtgylsccrflddnqivtssgdttcalwdietgqqtttf
tghtgdvmslslapdtrlfvsgacdasaklwdvregmcrqtftghesdinaicffpngna
fatgsddatcrlfdlradqelmtyshdniicgitsvsfsksgrlllagyddfncnvwdal
kadragvlaghdnrvsclgvtddgmavatgswdsflkiwn
>d1b9yb_ 1.125.2.1.1 Transducin (heterotrimeric G protein), gamma chain {Bovine (Bos taurus)}
mpviniedltekdklkmevdqlkkevtlermlvskcceefrdyveersgedplvkgiped
knpfkelk
>d1b9yc_ 3.38.1.6.1 Phosducin {Rat (Rattus norvegicus)}
egqathtgpkgvindwrkfklesedgdsippskkeilrqmsspqsrddkdskermsrkms
iqeyelihqdkedegclrkyrrqcmqdmhqklsfgprygfvyeletgeqfletiekeqkv
ttivvniyedgvrgcdalnssleclaaeypmvkfckirasntgagdrfssdvlptllvyk
ggelisnfisvaeqfaedffaadvesflneygllper
>d1b9za1 2.3.1.1.6 (418-516) beta-amylase {Bacillus cereus}
tpvmqtivvknvpttigdtvyitgnraelgswdtkqypiqlyydshsndwrgnvvlpaer
niefkafikskdgtvkswqtiqqswnpvplkttshtssw
>d1b9za2 3.1.7.2.3 (1-417) Bacterial beta-amylase, catalytic domain {Bacillus cereus}
avngkgmnpdykaylmaplkkipevtnwetfendlrwakqngfyaitvdfwwgdmekngd
qqfdfsyaqrfaqsvknagmkmipiisthqcggnvgddcnvpipswvwnqksddslyfks
etgtvnketlnplasdvirkeygelytafaaamkpykdviakiylsggpagelrypsytt
sdgtgypsrgkfqaytefakskfrlwvlnkygslnevnkawgtkliselailppsdgeqf
lmngylsmygkdylewyqgilenhtkligelahnafdttfqvpigakiagvhwqynnpti
phgaekpagyndyshlldafksakldvtftclemtdkgsypeysmpktlvqniatlanek
givlngenalsigneeeykrvaemafnynfagftllryqdvmynnslmgkfkdllgv
>d1ba0_1 3.46.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgttyscvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba0_2 3.46.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfkvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba1_1 3.46.1.1.1 (4-188) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
gpavgidlgttyskvgvfqhgkveiiandqgnrttpsyvaftdterligdaaknqvamnp
tntvfdakrligrrfddavvqsdmkhwpfmvvndagrpkvqveykgetksfypeevssmv
ltkmkeiaeaylgktvtnavvtvpayfndsqrqatkdagtiaglnvlriineptaaaiay
gldkk
>d1ba1_2 3.46.1.1.1 (189-381) Heat shock protein 70kDa, ATPase fragment {Bovine (Bos taurus)}
vgaernvlifdlgggtfdvsiltiedgifevkstagdthlggedfdnrmvnhfiaefkrk
hkkdisenkravrrlrtacerakrtlssstqasieidslyegidfytsitrarfeelnad
lfrgtldpvekalrdakldksqihdivlvggstripkiqkllqdffngkelnksinpdea
vaygaavqaails
>d1ba2a_ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba2b_ 3.83.1.1.1 D-ribose-binding protein {Escherichia coli, strain k-12}
kdtialvvstlnnpffvslkdgaqkeadklgynlvvldsqnnpakelanvqdltvrgtki
llinptrsdavgnavkmanqanipvitldrqatkgevvshiasdnvlggkiagdyiakka
gegakvielqgiagtsaarergegfqqavaahkfnvlasqpadfdrikglnvmqnlltah
pdvqavfaqndemalgalralqtagksdvmvvgfdgtpdgekavndgklaatiaqlpdqi
gakgvetadkvlkgekvqakypvdlklvvkq
>d1ba3__ 5.19.1.1.1 Luciferase {Firefly (Phontinus pyralis)}
daknikkgpapfypledgtageqlhkamkryalvpgtiaftdahievnityaeyfemsvr
laeamkryglntnhrivvcsenslqffmpvlgalfigvavapandiynerellnsmnisq
ptvvfvskkglqkilnvqkklpiiqkiiimdsktdyqgfqsmytfvtshlppgfneydfv
pesfdrdktialimnssgstglpkgvalphrtacvrfshardpifgnqiipdtailsvvp
fhhgfgmfttlgylicgfrvvlmyrfeeelflrslqdykiqsallvptlfsffakstlid
kydlsnlheiasggaplskevgeavakrfhlpgirqgygltettsailitpegddkpgav
gkvvpffeakvvdldtgktlgvnqrgelcvrgpmimsgyvnnpeatnalidkdgwlhsgd
iaywdedehffivdrlkslikykgyqvapaelesillqhpnifdagvaglpdddagelpa
avvvlehgktmtekeivdyvasqvttakklrggvvfvdevpkgltgkldarkireilika
kk
>d1ba5__ 1.4.1.4.1 DNA-binding domain of human telomeric protein, htrf1 {Human (Homo sapiens)}
rkrqawlweedknlrsgvrkygegnwskillhykfnnrtsvmlkdrwrtmkkl
>d1ba7a_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>d1ba7b_ 2.37.4.1.4 Soybean trypsin inhibitor {Soybean (Glycine max)}
dfvldnegnplenggtyyilsditafggiraaptgnercpltvvqsrneldkgigtiiss
pyrirfiaeghplslkfdsfavimlcvgiptewsvvedlpegpavkigenkdamdgwfrl
ervsddefnnyklvfcpqqaeddkcgdigisidhddgtrrlvvsknkplvvqfqkl
>e1ba8.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1ba8.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfge
>d1ba9__ 2.1.8.1.2 Cu,Zn superoxide dismutase, SOD {Human (Homo sapiens)}
atkavavlkgdgpvqgiinfeqkesngpvkvwgsikglteglhgfhvheeedntagctsa
gphfnplsrkhggpkdeerhvgdlgnvtadkdgvadvsiedsvislsgdhsiigrtlvvh
ekaddlgkggneqstktgnagsrlacgvigiaq
>d1baba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1babb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1babc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
xmelspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkgh
gkkvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeft
pavhasldkflasvstvltskyr
>d1babd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bafh1 2.1.1.1.14 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
dvqlqesgpglvkpsqsqsltctvtgysitsdyawnwirqfpgnklewmgymsysgstry
npslrsrisitrdtsknqfflqlksvttedtatyfcargwplaywgqgtqvsvse
>d1bafh2 2.1.1.2.24 (116-217) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
akttppsvyplapgsaaqtnsmvtlgclvkgyfpepvtvtwnsgslssgvhtfpavlqsd
lytlsssvtvpssprpsetvtcnvahpasstkvdkkivprdc
>d1bafl1 2.1.1.1.14 (1-108) Immunoglobulin (variable domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
qivltqspaimsaspgekvtmtcsasssvyymywyqqkpgssprlliydtsnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwssyppitfgvgtklelkr
>d1bafl2 2.1.1.2.24 (109-214) Immunoglobulin (constant domains of L and H chains) {Fab ANO2 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrnec
>d1bag_1 2.62.1.1.3 (348-425) Bacterial alpha-Amylase (BLA) {Bacillus subtilis}
qpeelsnpngnnqifmnqrgshgvvlanagsssvsintatklpdgrydnkagagsfqvnd
gkltgtinarsvavlypd
>d1bag_2 3.1.7.1.3 (1-347) Bacterial alpha-amylase (BLA) {Bacillus subtilis}
ltapsiksgtilhawnwsfntlkhnmkdihdagytaiqtspinqvkegnqgdksmsnwyw
lyqptsyqignrylgteqefkemcaaaeeygikvivdavinhttfdyaaisnevksipnw
thgntqiknwsdrwdvtqnsllglydwntqntqvqsylkrfleralndgadgfrfdaakh
ielpddgsygsqfwpnitntsaefqygqilqdsasrdaayanymdvtasnyghsirsalk
nrnlgvsnishyasdvsadklvtwveshdtyanddeestwmsdddirlgwaviasrsgst
plffsrpegggngvrfpgksqigdrgsalfedqaitavnrfhnvmag
>d1bah__ 7.3.7.2.7 Charybdotoxin {Scorpion (Leiurus quinquestriatus hebraeus)}
ftnvscttskexwsvcqrlhntsrgkcmnkkxrcys
>d1baia_ 2.44.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldtgaddtviseedwptdwpvmeaa
npqihgigggipvrksrdmielgvinrdgslerplllfplvamtpvnilgrdclqglglr
ltnl
>d1baib_ 2.44.1.1.4 Rous sarcoma virus protease {Rous sarcoma virus, strain pr-C}
lamtmehkdrplvrviltntgshpvkqrsvyitalldtgaddtviseedwptdwpvmeaa
npqihgigggipvrksrdmielgvinrdgslerplllfplvamtpvnilgrdclqglglr
ltnl
>d1baj__ 1.29.3.1.3 HIV capsid protein, dimerisation domain {Human immunodeficiency virus, type 1, HIV-1}
tsildirqgpkepfrdyvdrfyktlraeqasqevknwmtetllvqnanpdcktilkalgp
gatleemmtac
>d1bak__ 2.49.1.1.9 G-protein coupled receptor kinase 2 (beta-adrenergic receptor kinase 1) {Human (Homo sapiens)}
gshmgkdcimhgymskmgnpfltqwqrryfylfpnrlewrgegeapqslltmeeiqsvee
tqikerkclllkirggkqfilqcdsdpelvqwkkelrdayreaqqlvqrvpkmknkprs
>d1bal__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
yasleeqnndalspairrllaehnldasaikgtgvggrltredvekhlaka
>d1bam__ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkdkvenk
>d1bana_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1banb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1banc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
qvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnreg
klpgksgrtwreadinytsgfrnsdrilyasdwliykttdhyqtftkir
>d1baoa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1baob_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
vintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregk
lpgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1baoc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
intfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnregkl
pgksgrtwreadinftsgfrnsdrilyssdwliykttdhyqtftkir
>d1bap__ 3.83.1.1.2 L-arabinose-binding protein {Escherichia coli}
nlklgflvkqpeepwfqtewkfadkagkdlgfevikiavpdgektlnaidslaasgakgf
victpdpklgsaivakargydmkviavddqfvnakgkpmdtvplvmmaatkigerqgqel
ykemqkrgwdvkesavmaitaneldtarrrttgsmdalkaagfpekqiyqvptksndipg
afdaansmlvqhpevkhwlivgmndstvlggvrategqgfkaadiigigingvdavsels
kaqatgfygsllgspdvhgykssemlynwvakdveppkftevtdvvlitrdnfkeelekk
glggk
>d1baq__ 1.77.1.1.1 Antitermination factor NusB {Escherichia coli}
mkpaarrrarecavqalyswqlsqndiadveyqflaeqdvkdvdvlyfrellagvatnta
yldglmkpylsrlleelgqvekavlrialyelskrsdvpykvaineaielaksfgaedsh
kfvngvldkaapvirpnkk
>d1bara_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
pkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikstetgqflamdtd
gllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklgprthfgqkai
lflplpv
>d1barb_ 2.37.1.1.2 Acidic FGF {Bovine (Bos taurus)}
fnlplgnykkpkllycsnggyflrilpdgtvdgtkdrsdqhiqlqlaaesigevyikste
tgqflamdtdgllygsqtpneeclflerleengyntyiskkhaekhwfvglkkngrsklg
prthfgqkailflplpvs
>d1bas__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpms
>d1bava_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavb_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavc_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bavd_ 3.47.4.1.1 Carboxypeptidase A {Bovine (Bos taurus)}
arstntfnyatyhtldeiydfmdllvaqhpelvsklqigrsyegrpiyvlkfstggsnrp
aiwidlgihsrewitqatgvwfakkftenygqnpsftaildsmdifleivtnpngfafth
senrlwrktrsvtssslcvgvdanrnwdagfgkagassspcsetyhgkyansevevksiv
dfvknhgnfkaflsihsysqlllypygyttqsipdktelnqvaksavaalkslygtsyky
gsiittiyqasggsidwsynqgikysftfelrdtgrygfllpasqiiptaqetwlgvlti
mehtvnn
>d1bawa_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bawb_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bawc_ 2.5.1.1.12 Plastocyanin {Cyanobacterium (Phormidium laminosum)}
etftvkmgadsgllqfepanvtvhpgdtvkwvnnklpphnilfddkqvpgaskeladkls
hsqlmfspgesyeitfssdfpagtytyycaphrgagmvgkitveg
>d1bax__ 1.62.1.3.1 Mason-pfizer monkey virus matrix protein {Simian mason-pfizer virus, MPMV}
mgqelsqheryveqlkqalktrgvkvkyadllkffdfvkdtcpwfpqegtidikrwrrvg
dcfqdyyntfgpekvpvtafsywnlikelidkke
>d1baya1 1.48.1.1.2 (79-209) Glutathione S-transferase {Mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1baya2 3.38.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1bayb1 1.48.1.1.2 (79-209) Glutathione S-transferase {Mouse (Mus musculus)}
ygknqreaaqmdmvndgvedlrgkyvtliytnyengkndyvkalpghlkpfetllsqnqg
gkafivgdqisfadynlldlllihqvlapgcldnfpllsayvarlsarpkikaflsspeh
vnrpingngkq
>d1bayb2 3.38.1.5.2 (1-78) Glutathione S-transferase {Mouse (Mus musculus), class pi}
ppytivyfpvrgrceamrmlladqgqswkeevvtidtwmqglkptclygqlpkfedgdlt
lyqsnailrhlgrslgl
>d1baza_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
skmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bazb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
kmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>d1bazc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bazd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfk
>e1bb0.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>e1bb0.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqfg
>d1bb3a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb3b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb4a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirahvawrnrcqnrd
vrqyvqgcgv
>d1bb4b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirahvawrnrcqnrd
vrqyvqgcgv
>d1bb5a_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb5b_ 4.2.1.2.8 Lysozyme {Human (Homo sapiens)}
kvfercelartlkrlgmdgyrgislanwmclakwesgyntratnynagdrstdygifqin
srywcndgktpgavnachlscsallqdniadavaclkrvvrdpqgirawvawrnrcqnrd
vrqyvqgcgv
>d1bb6__ 4.2.1.2.11 Lysozyme {Rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1bb7__ 4.2.1.2.11 Lysozyme {Rainbow trout (Oncorhynchus mykiss)}
kvydrcelaralkasgmdgyagnslpnwvclskwessyntqatnrntdgstdygifqins
rywcddgrtpgaknvcgircsqlltddltvaircakrvvldpngigawvawrlhcqnqdl
rsyvagcgv
>d1bb8__ 4.9.1.1.1 DNA-binding domain from tn916 integrase {Enterococcus faecalis}
ekrrdnrgrilktgesqrkdgrylykyidsfgepqfvyswklvatdrvpagkrdcislre
kiaelqkdihd
>d1bb9__ 2.30.2.1.23 Amphiphysin 2 {Rat (Rattus norvegicus)}
ttgrldlppgfmfkvqaqhdytatdtdelqlkagdvvlvipfqnpeeqdegwlmgvkesd
wnqhkelekcrgvfpenftervq
>d1bbba_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bbbb_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bbbc_ 1.1.1.1.16 Hemoglobin, alpha-chain {Human (Homo sapiens)}
vlspadktnvkaawgkvgahageygaealermflsfpttktyfphfdlshgsaqvkghgk
kvadaltnavahvddmpnalsalsdlhahklrvdpvnfkllshcllvtlaahlpaeftpa
vhasldkflasvstvltskyr
>d1bbbd_ 1.1.1.1.28 Hemoglobin, beta-chain {Human (Homo sapiens)}
vhltpeeksavtalwgkvnvdevggealgrllvvypwtqrffesfgdlstpdavmgnpkv
kahgkkvlgafsdglahldnlkgtfatlselhcdklhvdpenfrllgnvlvcvlahhfgk
eftppvqaayqkvvagvanalahkyh
>d1bbc__ 1.123.1.2.11 Phospholipase A2 {Human (Homo sapiens), synovial fluid}
nlvnfhrmiklttgkeaalsygfygchcgvggrgspkdatdrccvthdccykrlekrgcg
tkflsykfsnsgsritcakqdscrsqlcecdkaaatcfarnkttynkkyqyysnkhcrgs
tprc
>d1bbdh1 2.1.1.1.15 (1-119) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
evqlqqsgaelvrpgasvklscttsgfnikdiyihwvkqrpeqglewigrldpangytky
dpkfqgkatitvdtssntaylhlssltsedtavyycdgyysyydmdywgpgtsvtvssa
>d1bbdh2 2.1.1.2.25 (120-218) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
kttapsvyplapvcgdttgssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdl
ytlsssvtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bbdl1 2.1.1.1.15 (1-114) Immunoglobulin (variable domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
divmtqspssltvttgekvtmtckssqsllnsrtqknyltwyqqkpgqspklliywastr
esgvpdrftgsgsgtdftlsisgvqaedlavyycqnnynypltfgagtklelkr
>d1bbdl2 2.1.1.2.25 (115-219) Immunoglobulin (constant domains of L and H chains) {Fab 8F5 (mouse), kappa L chain}
adaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqds
kdstysmsstltltkdeyerhnsytceathktstspivksfnrne
>d1bbg__ 7.6.1.1.1 <i>Amb</i> V allergen {Giant ragweed (Ambrosia trifida), pollen}
ddglcyegtncgkvgkyccspigkycvcydskaicnknct
>d1bbha_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbhb_ 1.25.3.2.2 Cytochrome c' {Chromatium vinosum}
aglspeeqietrqagyefmgwnmgkikanlegeynaaqveaaanviaaiansgmgalygp
gtdknvgdvktrvkpeffqnmedvgkiarefvgaantlaevaatgeaeavktafgdvgaa
ckschekyrak
>d1bbi__ 7.3.13.1.1 Bowman-Birk inhibitor {Soybean (Glycine max)}
ddesskpccdqcactksnppqcrcsdmrlnschsackscicalsypaqcfcvditdfcye
pckpseddken
>d1bbjh1 2.1.1.1.16 (1-115) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
xvqlqqsdaelvkpgasvkisckasgytftdhaihwakqkpeqglewigyispgnddiky
nekfkgkatltadkssstaymqlnsltsedsavyfckrsyyghwgqgttltvssa
>d1bbjh2 2.1.1.2.26 (116-212) Immunoglobulin (constant domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
stkgpsvfplapcsrstsestaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqssg
lyslssvvtvpssslgtktytcnvdhkpsntkvdkrv
>d1bbjl1 2.1.1.1.16 (1-109) Immunoglobulin (variable domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
diqmtqspaslsvsvgetvtitcraseniysnlawyqqkqgkspqllvyaatnladgvps
rfsgsgsgtqyslkinslqsedfgsyycqhfwgtpytfgggtrleikra
>d1bbjl2 2.1.1.2.26 (110-211) Immunoglobulin (constant domains of L and H chains) {Fab B72.3 (mouse/human chimera), kappa L chain}
daaptvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqdsk
dstyslsstltlskadyekhkvyacevthqglsspvtksfnr
>d1bbl__ 1.9.1.1.2 E3-binding domain of dihydrolipoamide succinyltransferase {Escherichia coli}
lspairrllaehnldasaikgtgvggrltredvekhl
>d1bbn__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1bbo_1 7.31.1.1.9 (1-28) Enhancer binding protein {Human (Homo sapiens)}
kyiceecgirxkkpsmlkkhirthtdvr
>d1bbo_2 7.31.1.1.9 (29-57) Enhancer binding protein {Human (Homo sapiens)}
pyhctycnfsfktkgnltkhmkskahskk
>d1bbpa_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpb_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpc_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>d1bbpd_ 2.53.1.1.13 Bilin-binding protein {Cabbage butterfly (Pieris brassicae)}
nvyhdgacpevkpvdnfdwsnyhgkwwevakypnsvekygkcgwaeytpegksvkvsnyh
vihgkeyfiegtaypvgdskigkiyhkltyggvtkenvfnvlstdnknyiigyyckyded
kkghqdfvwvlsrskvltgeaktavenyligspvvdsqklvysdfseaackvn
>e1bbr.1e 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
svaevqpsvlqvvnlplverpvckastriritdnmfcagykpgegkrgdacegdsggpfv
mkspynnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidrlgs
>e1bbr.1h 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwtt
>e1bbr.1l 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2j 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.2k 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>e1bbr.3m 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
tfgageadcglrplfekkqvqdqtekelfesyiegr
>e1bbr.3n 2.41.1.2.12 Thrombin {Bovine (Bos taurus)}
ivegqdaevglspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftvddll
vrigkhsrtryerkvekismldkiyihprynwkenldrdiallklkrpielsdyihpvcl
pdkqtaakllhagfkgrvtgwgnrretwttsvaevqpsvlqvvnlplverpvckastrir
itdnmfcagykpgegkrgdacegdsggpfvmkspynnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidrlgs
>d1bbs__ 2.44.1.2.16 Chymosin (synonim: renin) {Human (Homo sapiens)}
ttssviltnymdtqyygeigigtppqtfkvvfdtgssnvwvpsskcsrlytacvyhklfd
asdsssykhngteltlrystgtvsgflsqdiitvggitvtqmfgevtempalpfmlaefd
gvvgmgfieqaigrvtpifdniisqgvlkedvfsfyynrdsensqslggqivlggsdpqh
yegnfhyinliktgvwqiqmkgvsvgsstllcedgclalvdtgasyisgstssieklmea
lgakkrlfdyvvkcnegptlpdisfhlggkeytltsadyvfqesysskklctlaihamdi
ppptgptwalgatfirkfytefdrrnnrigfalar
>d1bbt1_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
ttsagesadpvtttvenyggetqiqrrqhtdvsfimdrfvkvtpqnqinildlmqvpsht
lvggllrastyyfsdleiavkhegdltwvpngapekaldnttnptayhkapltrlalpyt
aphrvlatvyngecrysrnavpnlrgdlqvlaqkvartlptsfnygaikatrvtellyrm
kraetycprpllaihptearhkqkivap
>d1bbt2_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
lledrilttrnghttsttqssvgvtygyataedfvsgpntsgletrvvqaerffkthlfd
wvtsdsfgrchllelptdhkgvygsltdsyaymrngwdvevtavgnqfnggcllvamvpe
lcsiqkrelyqltlfphqfinprtnmtahitvpfvgvnrydqykvhkpwtlvvmvvaplt
vntegapqikvyaniaptnvhvagefpske
>d1bbt3_ 2.9.1.4.2 Foot-and-mouth desease virus {Foot-and-mouth disease virus (strain bfs, 1860)}
gifpvacsdgygglvttdpktadpvygkvfnpprnqlpgrftnlldvaeacptflrfegg
vpyvttktdsdrvlaqfdmslaakhmsntflaglaqyytqysgtinlhfmftgptdakar
ymvayappgmeppktpeaaahcihaewdtglnskftfsipylsaadytytasdvaettnv
qgwvclfqithgkadgdalvvlasagkdfelrlpvdarae
>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
>d1bby__ 1.4.3.13.1 DNA-binding domain from rap30 {Human (Homo sapiens)}
raradkqhvldmlfsafekhqyynlkdlvditkqpvvylkeilkeigvqnvkgihkntwe
lkpeyrhyq
>d1bbza_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbzc_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bbze_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
alfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvas
>d1bbzg_ 2.30.2.1.5 Abl tyrosine kinase, SH3 domain {Human (Homo sapiens)}
nlfvalydfvasgdntlsitkgeklrvlgynhngewceaqtkngqgwvpsnyitpvns
>d1bc0__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkseltgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkagtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bc1__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtkgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretkgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tkgdykkallllcggedd
>d1bc2a_ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bc2b_ 4.128.1.1.1 Zn metallo-beta-lactamase {Bacillus cereus}
tviknetgtisisqlnknvwvhtelgsfngeavpsnglvlntskglvlvdsswddkltke
liemvekkfqkrvtdviithahadriggiktlkergikahstaltaelakkngyeeplgd
lqtvtnlkfgnmkvetfypgkghtednivvwlpqynilvggclvkstsakdlgnvadayv
newstsienvlkryrninavvpghgevgdkglllhtldllk
>d1bc3__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtkgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretkgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bc4__ 4.5.1.1.4 Cytotoxic ribonuclease {Bullfrog (Rana catesbeiana)}
nwatfqqkhiintpiincntimdnniyivggqckrvntfiissattvkaictgvinmnvl
sttrfqlntctrtsitprpcpyssrtetnyicvkcenqypvhfagigrcp
>d1bc5a1 1.60.1.1.1 (16-91) Chemotaxis receptor methyltransferase CheR, N-terminal domain {Salmonella typhimurium}
mtqrlalsdahfrricqliyqragivladhkrdmvynrlvrrlralglddfgrylsmlea
nqnsaewqafinaltt
>d1bc5a2 3.56.1.3.1 (92-284) Chemotaxis receptor methyltransferase CheR, C-terminal domain {Salmonella typhimurium}
nltaffreahhfpilaeharrrhgeyrvwsaaastgeepysiaitladalgmapgrwkvf
asdidtevlekarsgiyrlselktlspqqlqryfmrgtgpheglvrvrqelanyvefssv
nllekqynvpgpfdaifcrnvmiyfdkttqedilrrfvpllkpdgllfaghsenfsnlvr
efslrgqtvyals
>d1bc6__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bc7c_ 1.4.3.16.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1bc8c_ 1.4.3.16.6 Serum responce factor accessory protein 1a, SAP-1 {Human (Homo sapiens)}
mdsaitlwqfllqllqkpqnkhmicwtsndgqfkllqaeevarlwgirknkpnmnydkls
ralryyyvkniikkvngqkfvykfvsypeilnm
>d1bc9__ 1.110.3.1.2 Cytohesin-1/b2-1 {Human (Homo sapiens)}
mknmqrnkqvamgrkkfnmdpkkgiqfliendllkntcediaqflykgeglnktaigdyl
gerdefniqvlhafvelheftdlnlvqalrqflwsfrlpgeaqkidrmmeafaqrycqcn
ngvfqstdtcyvlsfaiimlntslhnpnvkdkptverfiamnrgindggdlpeellrnly
esiknepfkipelehhhhhh
>d1bcca_ 4.106.1.1.2 Core 1 subunit {Chicken (Gallus gallus)}
yaqalqsvpetqvsqldngvrvaseqssqptctvgvwidagsryeseknngagyflehla
fkgtknrpqnalekevesmgahlnayssrehtayyikalskdvpkavelladivqncsle
dsqiekerdvivrelqendtsmrevvfnylhatafqgtglaqsvegpsenirklsradlt
eylsthytaprmvlaaaggvehqqllelaqkhfggvpftydddavptlskcrftgsqirh
redglplahvaiavegpgwahpdlvalqvanaiighydrtyggglhsssplasiavtnkl
cqsfqtfsicysetglfgfyfvcdrmsiddmmfvlqgqwmrlctsisesevlrgknflrn
alvshldgttpvcedigrelltygrripleeweerlaevdarmvrevcskyiydqcpava
gpgpieqlpdynrirsgmfwlr
>d1bccb_ 4.106.1.1.4 Core 2 subunit {Chicken (Gallus gallus)}
pphpqdleitklpnglviaslenyspgstigvfikagsryenssnlgtshllrlassltt
kgassfkitrgieavggklsvestrenmaytveclrddveilmefllnvttapefrpwev
adlqpqlkidkavafqnpqthvienlhaaayrnaladslycpdyrigkvtsvelhdfvqn
hftsarmalvglgvshpvlknvaeqllnirgglglsgakakyrggeireqngdslvhaai
vaesaaiggaeanafsvlqhvlganphvkrglnatsslyqavakgvhqpfdvsafnasys
dsglfgfytisqaayagqvikaaynqvktiaqgnvsnenvqaaknklkakylmsvesseg
fleevgsqalaagsynppstvlqqidavadadvikaakkfvsrqksmaasgnlghtpfvd
el
>d1bccc1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
apnirkshpllkminnslidlpapsnisawwnfgsllavclmtqiltglllamhytadts
lafssvahtcrnvqygwlirnlhangasffficiflhigrglyygsylyketwntgvill
ltlmatafvgyvlpwgqmsfwgatvitnlfsaipyightlvewawggfsvdnptltrffa
lhfllpfaiagitiihltflhesgsnnplgissdsdkipfhpyysfkdilgltlmltpfl
tlalfspnllgdpenftpanplvtpphikpewyflfayailrsipnklggvlalaasvli
lflipflhkskqrtmtfrplsqtlfwllvanlliltwigsqpvehpfiiigqmaslsyft
illilfptigtlenkmlny
>d1bccd1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
sdlelhppsypwshrgplssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvsvreglyfnpyfpgqaigmappiyndvlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmgllvplvyymkrhkwsvlksrklayrpp
k
>d1bcce1 2.29.1.1.2 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Chicken (Gallus gallus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1bcce2 6.2.1.1.10 (1-69) Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
shtdikvpnfsdyrrppddystkssresdpsrkgfsylvtavttlgvayaaknvvtqfvs
smsasadvl
>d1bccf1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
srwlegirkwyynaagfnkyglmrddtiyenddvkeairrlpenlyddrmfrikraldln
mrqqilpkeqwtkyeedvpylepylkevirerkereewdk
>d1bccg1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
rqfghltrvrhlityslspfeqrpfphyfskgvpnvwrrlracilrvappflafyllytw
gtqefekskrknpaayvn
>d1bcch1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
lvdplttvreqceqlekcvkarerlelcdervssrsqteedcteelfdflhardhcvahk
lfnslk
>d1bccj1 6.2.1.1.10 Cytochrome bc1 transmembrane subunits {Chicken (Gallus gallus)}
tltarlysllfrrtstfaltivvgallferafdqgadaiyehinegklwkhikhkyenk
>d1bcd__ 2.65.1.1.2 Carbonic anhydrase {Human (Homo sapiens), erythrocytes, isozyme II}
hhwgygkhngpehwhkdfpiakgerqspvdidthtakydpslkplsvsydqatslrilnn
ghafnvefddsqdkavlkggpldgtyrliqfhfhwgsldgqgsehtvdkkkyaaelhlvh
wntkygdfgkavqqpdglavlgiflkvgsakpglqkvvdvldsiktkgksadftnfdprg
llpesldywtypgslttppllecvtwivlkepisvsseqvlkfrklnfngegepeelmvd
nwrpaqplknrqikasfk
>d1bcfa_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bcfb_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bcg__ 7.3.7.1.7 Scorpion toxin {Scorpion (Buthotus judaicus), BJXTR-IT}
mkkngypldrngkttecsgvnaiaphycnsectkvyyaesgyccwgacycfgleddkpig
pmkditkkycdvqi
>d1bch11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bch21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bch31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktsaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bci__ 2.6.1.1.2 Domain from cytosolic phospholipase A2 {Human (Homo sapiens)}
yshkftvvvlratkvtkgafgdmldtpdpyvelfisttpdsrkrtrhfnndinpvwnetf
efildpnqenvleitlmdanyvmdetlgtatftvssmkvgekkevpfifnqvtemvlems
lev
>d1bcj11 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcj21 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcj31 4.139.1.1.7 (105-226) Mannose-binding protein A, lectin domain {Rat (Rattus rattus)}
kksgkkffvtnhermpfskvkalcselrgtvaiprnaeenkaiqevaktvaflgitdevt
egqfmyvtggrltysnwkkdqpddwyghglgggedcvhivdnglwndiscqashtavcef
pa
>d1bcka_ 2.55.1.1.1 Cyclophilin (eukaryotic) {Human (Homo sapiens), variant A}
mvnptvffdiavdgeplgrvsfelfadkvpktaenfralstgekgfgykgscfhriipgf
mcqggdftrhngtggksiygekfedenfilkhtgpgilsmanagpntngsqffictakte
wldgkhvvfgkvkegmniveamerfgsrngktskkitiadcgqle
>d1bcma1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcma2 3.46.3.3.1 (257-480) mu transposase, core domain {Bacteriophage mu}
vehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirl
sfmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhw
tsvvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelf
lktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcmb1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bcmb2 3.46.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcn__ 1.27.1.2.3 Interleukin-4 (IL-4) {Human (Homo sapiens)}
eaeahkcditlqeiiktlnslteqktlcteltvtdifaaskdtteketfcraatvlrqfy
shhekdtrclgataqqfhrhkqlirflkrldrnlwglaglnscpvkeadqstlenflerl
ktimrekyskcss
>d1bco_1 2.42.1.1.1 (481-560) mu transposase, C-terminal domain {Bacteriophage mu}
teeqkrmlllpaeavnvsrkgeftlkvggslkgaknvyynmalmnagvkkvvvrfdpqql
hstvycytldgrficeaecl
>d1bco_2 3.46.3.3.1 (258-480) mu transposase, core domain {Bacteriophage mu}
ehldamqwingdgylhnvfvrwfngdvirpktwfwqdvktrkilgwrcdvsenidsirls
fmdvvtrygipedfhitidntrgaankwltggapnryrfkvkeddpkglfllmgakmhwt
svvagkgwgqakpverafgvggleeyvdkhpalagaytgpnpqakpdnygdravdaelfl
ktlaegvamfnartgretemcggklsfddvfereyartivrkp
>d1bcpa_ 4.136.1.1.5 Pertussis toxin, S1 subunit {Bordetella pertussis}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcpb1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcpb2 4.139.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpc1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
tiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmydal
rrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpc2 4.139.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1bcpd_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpe_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpf_ 2.35.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>d1bcpg_ 4.136.1.1.5 Pertussis toxin, S1 subunit {Bordetella pertussis}
dppatvyrydsrppedvfqngftawgnndnvlehltgrscqvgssnsafvstsssrryte
vylehrmqeaveaeragrgtghfigyiyevradnnfygaassyfeyvdtygdnagrilag
alatyqseylahrrippenirrvtrvyhngitgetttteysnaryvsqqtranpnpytsr
rsvasivgtlvrmapvvgacmarqaesseamaawserageamvlvyyesiaysf
>d1bcph1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
ttrntgqpatdhyysnvtatrllsstnsrlcavfvrsgqpvigactspydgkywsmysrl
rkmlyliyvagisvrvhvskeeqyydyedatfetyaltgisicnpgsslc
>d1bcph2 4.139.1.2.1 (3-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
pgivippqeqitqhgspygrcanktraltvaelrgsgdlqeylrhvtrgwsifalydgty
lggeyggvikdgtpggafdlkttfcim
>d1bcpi1 2.35.2.1.6 (90-199) Pertussis toxin S2/S3 subunits, C-terminal domain {Bordetella pertussis}
tiyktgqpaadhyyskvtatrllastnsrlcavfvrdgqsvigacaspyegryrdmydal
rrllymiymsglavrvhvskeeqyydyedatfqtyaltgislcnpaasic
>d1bcpi2 4.139.1.2.1 (4-89) Pertussis toxin, S2/S3 subunits, N-terminal domain {Bordetella pertussis}
givippkalftqqggaygrcpngtraltvaelrgnaelqtylrqitpgwsiyglydgtyl
gqayggiikdappgagfiyretfcit
>d1bcpj_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpk_ 2.35.2.1.7 Pertussis toxin S4 subunit {Bordetella pertussis}
dvpyvlvktnmvvtsvamkpyevtptrmlvcgiaaklgaaasspdahvpfcfgkdlkrpg
sspmevmlravfmqqrplrmflgpkqltfegkpalelirmvecsgkqdcp
>d1bcpl_ 2.35.2.1.8 Pertussis toxin S5 subunit {Bordetella pertussis}
lpthlyknftvqelalklkgknqefcltafmsgrslvraclsdaghehdtwfdtmlgfai
sayalksrialtvedspypgtpgdllelqicplngyce
>e1bcr.1a 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcn
>e1bcr.1b 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpg
>e1bcs.1a 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
haadriarlpgqpavdfdmysgyitvdegagrslfyllqeapedaqpaplvlwlnggpgc
ssvaygaseelgafrvkprgaglvlneyrwnkvanvlfldspagvgfsytntssdiytsg
dnrtahdsyaflakwferfphykyrdfyiagesyaghyvpelsqlvhrsknpvinlkgfm
vgngliddyhdyvgtfefwwnhgivsddtyrrlkeaclhdsfihpspacdaatdvataeq
gnidmyslytpvcni
>e1bcs.1b 3.59.1.4.1 Serine carboxypeptidase II {Wheat (Triticum vulgaris)}
sydpcterystayynrrdvqmalhanvtgamnytwatcsdtinthwhdaprsmlpiyrel
iaaglriwvfsgdtdavvpltatrysigalglptttswypwyddqevggwsqvykgltlv
svrgaghevplhrprqalvlfqyflqgkpmpgq
>e1bcu.1h 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlketwtanvgkgqpsvlqvvnlpiverpvckdstrir
itdnmfcagykpdegkrgdacegdsggpfvmkspfnnrwyqmgivswgegcdrdgkygfy
thvfrlkkwiqkvidqf
>e1bcu.1l 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
adcglrplfekksledkterellesy
>d1bcw__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselagkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bcx__ 2.26.1.10.1 Xylanase II {Bacillus circulans}
astdywqnwtdgggivnavngsggnysvnwsntgnfvvgkgwttgspfrtinynagvwap
ngngyltlygwtrsplieyyvvdswgtyrptgtykgtvksdggtydiytttrynapsidg
drttftqywsvrqskrptgsnatitftnhvnawkshgmnlgsnwayqvmatcgyqssgss
nvtvw
>d1bcy__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselkgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bcz__ 1.66.1.1.6 Annexin V {Rat (Rattus norvegicus)}
alrgtvtdfsgfdgradaevlrkamkglgtdedsilnlltarsnaqrqqiaeefktlfgr
dlvndmkselsgkfeklivalmkpsrlydayelkhalkgagtdekvlteiiasrtpeelr
aikqayeeeygsnleddvvgdtsgyyqrmlvvllqanrdpdtaiddaqveldaqalfqag
elkwgtdeekfitilgtrsvshlrrvfdkymtisgfqieetidretsgnlenlllavvks
irsipaylaetlyyamkgagtddhtlirvivsrseidlfnirkefrknfatslysmikgd
tsgdykkallllcggedd
>d1bd0a1 2.43.2.1.1 (2-11,245-382) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnaig
>d1bd0a2 3.1.5.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d1bd0b1 2.43.2.1.1 (2-11,245-381) Alanine racemase {Bacillus stearothermophilus}
ndfhrdtwaeXfslhsrlvhvkklqpgekvsygatytaqteewigtipigyadgwlrrlq
hfhvlvdgqkapivgricmdqcmirlpgplpvgtkvtligrqgdevisiddvarhletin
yevpctisyrvpriffrhkrimevrnai
>d1bd0b2 3.1.5.1.1 (12-244) Alanine racemase {Bacillus stearothermophilus}
vdldaiydnvenlrrllpddthimavvkanayghgdvqvartaleagasrlavafldeal
alrekgieapilvlgasrpadaalaaqqrialtvfrsdwleeasalysgpfpihfhlkmd
tgmgrlgvkdeeetkrivalierhphfvleglythfatadevntdyfsyqytrflhmlew
lpsrpplvhcansaaslrfpdrtfnmvrfgiamyglapspgikpllpyplkea
>d1bd2a1 2.1.1.2.4 (182-275) Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
tdapkthmthhavsdheatlrcwalsfypaeitltwqrdgedqtqdtelvetrpagdgtf
qkwaavvvpsgqeqrytchvqheglpkpltlrwe
>d1bd2a2 4.17.1.1.11 (1-181) MHC class I, alpha-1 and alpha-2 domains {Human HLA-a0201}
gshsmryfftsvsrpgrgeprfiavgyvddtqfvrfdsdaasqrmeprapwieqegpeyw
dgetrkvkahsqthrvdlgtlrgyynqseagshtvqrmygcdvgsdwrflrgyhqyaydg
kdyialkedlrswtaadmaaqttkhkweaahvaeqlraylegtcvewlrrylengketlq
r
>d1bd2b1 2.1.1.2.4 Class I MHC, beta2-microglobulin and alpha-3 domain {Human (Homo sapiens), HLA-a0201}
iqrtpkiqvysrhpaengksnflncyvsgfhpsdievdllkngeriekvehsdlsfskdw
sfyllyyteftptekdeyacrvnhvtlsqpkivkwdrdm
>d1bd2d1 2.1.1.1.155 (1-117) T-cell antigen receptor {Human (Homo sapiens), alpha-chain}
qqvkqnspslsvqegrisilncdytnsmfdyflwykkypaegptflisissikdknadgr
ftvflnksakhlslhivpsqpgdsavyfcaamegaqklvfgqgtrltinpn
>d1bd2d2 2.1.1.2.144 (118-203) T-cell antigen receptor {Human (Homo sapiens)}
iqnpdpavyqlrdskssdksvclftdfdsqtnvsqskdsdvyitdktvldmrsmdfksns
avawsnksdfacanafnnsiipedtf
>d1bd2e1 2.1.1.1.157 (3-118) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
gvtqtpkfqvlktgqsmtlqcaqdmnheymswyrqdpgmglrlihysvgagitdqgevpn
gynvsrsttedfplrllsaapsqtsvyfcassypgggfyeqyfgpgtrltvte
>d1bd2e2 2.1.1.2.146 (119-247) T-cell antigen receptor {Human (Homo sapiens), beta-chain}
dlknvfppevavfepseaeishtqkatlvclatgfypdhvelswwvngkevhsgvstdpq
plkeqpalndsryalssrlrvsatfwqdprnhfrcqvqfyglsendewtqdrakpvtqiv
saeawgrad
>d1bd3a_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3b_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3c_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd3d_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4a_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4b_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4c_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd4d_ 3.51.1.1.13 Uracil PRTase {Toxoplasma gondii}
qeesilqdiitrfpnvvlmkqtaqlrammtiirdketpkeefvfyadrlirllieealne
lpfqkkevttpldvsyhgvsfyskicgvsivragesmesglravcrgvrigkiliqrdet
taepkliyeklpadirerwvmlldpmcatagsvckaievllrlgvkeeriifvnilaapq
giervfkeypkvrmvtaavdiclnsryyivpgigdfgdryfgtm
>d1bd6__ 4.47.1.2.2 Ferredoxin {Bacillus schlegelii}
ayvitepcigtkdascvevcpvdcihegedqyyidpdvcidcgaceavcpvsaiyhedfv
peewksyiqknrdffkk
>d1bd7a_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1bd7b_ 2.10.1.1.6 beta-Crystallin {Rat (Rattus norvegicus), isoform E}
ehkiilyenpnftgkkmeivdddvpsfhahgyqekvssvrvqsgtwvgyqypgyrglqyl
lekgdykdnsdfgaphpqvqsvrrirdmqgnpkiiifeqenfqghshelsgpcpnlketg
mekagsvlvqagpwvgyeqanckgeqfvfekgeyprwdswtssrrtdslsslrpik
>d1bd8__ 1.110.2.1.3 Cell cycle inhibitor p19ink4D {Human (Homo sapiens)}
ragdrlsgaaargdvqevrrllhrelvhpdalnrfgktalqvmmfgstaialellkqgas
pnvqdtsgtspvhdaartgfldtlkvlvehgadvnvpdgtgalpihlavqeghtavvsfl
aaesdlhrrdargltplelalqrgaqdlvdilqghm
>d1bd9a_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
lskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgkly
tlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvwlv
yeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklyeql
>d1bd9b_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
pvdlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsg
klytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryv
wlvyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpkly
eqlsg
>d1bdaa_ 2.41.1.2.29 Single chain tissue plasminogen activator {Human (Homo sapiens)}
tcglrqysqpqfrikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaah
cfqerfpphhltvilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdss
rcaqessvvrtvclppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrct
sqhllnrtvtdnmlcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgc
gqkdvpgvytkvtnyldwirdnmrp
>d1bdab_ 2.41.1.2.29 Single chain tissue plasminogen activator {Human (Homo sapiens)}
tcglrqysqpqfrikgglfadiashpwqaaifakhrrspgerflcggilisscwilsaah
cfqerfpphhltvilgrtyrvvpgeeeqkfevekyivhkefdddtydndiallqlksdss
rcaqessvvrtvclppadlqlpdwtecelsgygkhealspfyserlkeahvrlypssrct
sqhllnrtvtdnmlcagdtrsggpqanlhdacqgdsggplvclndgrmtlvgiiswglgc
gqkdvpgvytkvtnyldwirdnmrp
>d1bdb__ 3.2.1.2.11 Cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase {Pseudomonas lb400}
mklkgeavlitggasglgralvdrfvaegakvavldksaerlaeletdhgdnvlgivgdv
rsledqkqaasrcvarfgkidtlipnagiwdystalvdlpeesldaafdevfhinvkgyi
havkaclpalvasrgnviftisnagfypngggplytaakhaivglvrelafelapyvrvn
gvgsgginsdlrgpsslgmgskaistvpladmlksvlpigrmpeveeytgayvffatrgd
aapatgallnydgglgvrgffsgaggndlleqlnih
>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
>d1bdfa1 4.56.3.1.1 (2-52,179-232) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
qgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriayn
veaarveqrtdldklviemetngtidpeeairraatilaeqleafv
>d1bdfa2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfb1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfb2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfc1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfc2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdfd1 4.56.3.1.1 (1-52,179-235) Dimerization subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
mqgsvteflkprlvdieqvssthakvtleplergfghtlgnalraillssmpXpveriay
nveaarveqrtdldklviemetngtidpeeairraatilaeqleafvdlr
>d1bdfd2 4.150.1.1.1 (53-178) Insert subdomain of RNA polymerase alpha subunit N-terminal domain {Escherichia coli}
gcavteveidgvlheystkegvqedileillnlkglavrvqgkdeviltlnksgigpvta
adithdgdveivkpqhvichltdenasismrikvqrgrgyvpastrihseederpigrll
vdacys
>d1bdg_1 3.46.1.2.1 (13-222) Hexokinase {Blood fluke (Schistosoma mansoni)}
fsdqqlfekvveilkpfdlsvvdyeeicdrmgesmrlglqkstnekssikmfpsyvtktp
ngtetgnflaldlggtnyrvlsvtlegkgkspriqertycipaekmsgsgtelfkyiaet
ladflenngmkdkkfdlgftfsfpcvqkglthatlvrwtkgfsadgveghnvaellqtel
dkrelnvkcvavvndtvgtlascaledp
>d1bdg_2 3.46.1.2.1 (223-460) Hexokinase {Blood fluke (Schistosoma mansoni)}
kcavglivgtgtnvayiedsskvelmdgvkepevvintewgafgekgeldcwrtqfdksm
didslhpgkqlyekmvsgmylgelvrhiivylveqkilfrgdlperlkvrnslltryltd
verdpahllynthymltddlhvpvvepidnrivryacemvvkraaylagagiacilrrin
rsevtvgvdgslykfhpkfcermtdmvdklkpkntrfclrlsedgsgkgaaaiaasc
>d1bdha1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslavnh
>d1bdha2 3.83.1.1.7 (59-340) Purine repressor (PurR), C-terminal domain {Escherichia coli}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdia1 1.36.1.4.1 (3-58) Purine repressor (PurR), N-terminal domain {Escherichia coli}
tikdvakranvstttvshvinktrfvaeetrnavwaaikelhyspsavarslkvnh
>d1bdia2 3.83.1.1.7 (59-340) Purine repressor (PurR), C-terminal domain {Escherichia coli}
tksigllatsseaayfaeiieavekncfqkgytlilgnawnnlekqraylsmmaqkrvdg
llvmcseypepllamleeyrhipmvvmdwgeakadftdavidnafeggymagryliergh
reigvipgplerntgagrlagfmkameeamikvpeswivqgdfepesgyramqqilsqph
rptavfcggdimamgalcaademglrvpqdvsligydnvrnaryftpalttihqpkdslg
etafnmlldrivnkreepqsievhprlierrsvadgpfrdyr
>d1bdja_ 3.16.2.1.1 CheY protein {Escherichia coli}
adkelkflvvddfstmrrivrnllkelgfnnveeaedgvdalnklqaggygfvisdwnmp
nmdglellktiradgamsalpvlmvtaeakkeniiaaaqagasgyvvkpftaatleekln
kifeklgm
>d1bdjb_ 1.25.9.1.1 Aerobic respiration control sensor protein, ArcB {Escherichia coli}
ksealldipmleqylelvgpklitdglavfekmmpgyvsvlesnltaqdkkgiveeghki
kgaagsvglrhlqqlgqqiqspdlpawednvgewieemkeewrhdvevlkawvakat
>d1bdla_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdlb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdma1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bdma2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdmb1 3.2.1.5.4 (0-154) Malate dehydrogenase {Thermus flavus}
mkapvrvavtgaagqigysllfriaagemlgkdqpvilqlleipqamkalegvvmeledc
afpllagleatddpdvafkdadyallvgaaprkagmerrdllqvngkifteqgralaeva
kkdvkvlvvgnpantnaliayknapglnprnftam
>d1bdmb2 4.132.1.1.4 (155-332) Malate dehydrogenase {Thermus flavus}
trldhnrakaqlakktgtgvdrirrmtvwgnhssimfpdlfhaevdgrpalelvdmewye
kvfiptvaqrgaaiiqargassaasaanaaiehirdwalgtpegdwvsmavpsqgeygip
egivysfpvtakdgayrvvegleinefarkrmeitaqelldemeqvkalgli
>d1bdo__ 2.74.1.1.1 Biotinyl domain of acetyl-CoA carboxylase {Escherichia coli}
eisghivrspmvgtfyrtpspdakafievgqkvnvgdtlciveamkmmnqieadksgtvk
ailvesgqpvefdeplvvie
>d1bdqa_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmvggiggfikvrqyd
qilieicghkaigtvlvgptpiniigrnlltqigctlnf
>d1bdqb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsivagielpgrwkpkmvggiggfikvrqyd
qilieicghkaigtvlvgptpiniigrnlltqigctlnf
>d1bdra_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsvvagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bdrb_ 2.44.1.1.1 Human immunodeficiency virus type 1 protease {HIV-1}
pqitlwqrplvtikiggqlkealldtgaddsvvagielpgrwkpkmiggiggfikvrqyd
qilieicghkaigtvlvgptpvniigrnlltqigctlnf
>d1bds__ 7.9.1.1.4 BDs-I defensin {Sea anemone (Anemonia sulcata)}
aapcfcsgkpgrgdlwilrgtcpggygytsncykwpniccyph
>d1bdta_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdtb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdtc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdtd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqfnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdu__ 4.91.1.1.1 Thymidylate synthase {Escherichia coli}
mkqylelmqkvldegtqkndrtgtgtlsifghqmrfnlqdgfplvttkrchlrsiihell
wflqgdtniaylhennvtiwdewadengdlgpvygkqwrawptpdgrhidqittvlnqlk
ndpdsrriivsawnvgeldkmalapchaffqfyvadgklscqlyqrscdvflglpfnias
yallvhmmaqqcdlevgdfvwtggdthlysnhmdqthlqlsreprplpkliikrkpesif
dyrfedfeiegydphpgikapvai
>d1bdva_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegrig
>d1bdvb_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegriga
>d1bdvc_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkeg
>d1bdvd_ 1.46.1.1.1 Arc repressor {Bacteriophage p22 (Salmonella)}
mkgmskmpqvnlrwprevldlvrkvaeengrsvnseiyqrvmesfkkegr
>d1bdxa1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxa2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxa3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxb1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxb2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxb3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxc1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxc2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxc3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>d1bdxd1 1.5.1.1.1 (156-203) DNA helicase RuvA subunit, C-terminal domain {Escherichia coli}
tddaeqeavaalvalgykpqeasrmvskiarpdassetlirealraal
>d1bdxd2 1.61.6.1.1 (65-142) DNA helicase RuvA subunit, middle domain {Escherichia coli}
nkqertlfkeliktngvgpklalailsgmsaqqfvnavereevgalvklpgigkktaerl
ivemkdrfkglhgdlftp
>d1bdxd3 2.35.4.2.1 (1-64) DNA helicase RuvA subunit, N-terminal domain {Escherichia coli}
migrlrgiiiekqpplvlievggvgyevhmpmtcfyelpeagqeaivfthfvvredaqll
ygfn
>e1bdy.1a 2.6.1.1.3 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>e1bdy.1b 2.6.1.1.3 Domain from protein kinase C delta {Rat (Rattus norvegicus)}
mapflrisfnsyelgslqaeddasqpfcavkmkealttdrgktlvqkkptmypewkstfd
ahiyegrviqivlmraaedpmsevtvgvsvlaerckknngkaefwldlqpqakvlmcvqy
fle
>d1be0__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftawkydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1be1__ 3.16.5.1.2 Glutamate mutase, small subunit {Clostridium tetanomorphum}
mekktivlgvigsdchavgnkildhsftnagfnvvnigvlssqedfinaaietkadlicv
sslygqgeidckglrekcdeaglkgiklfvggnivvgkqnwpdveqrfkamgfdrvyppg
tspettiadmkevlgve
>d1be2__ 1.54.1.1.3 Plant non-specific lipid-transfer protein (ns-LTP) {Barley (Hordeum vulgare)}
lncgqvdskmkpcltyvqggpgpsgeccngvrdlhnqaqssgdrqtvcnclkgiargihn
lnlnnaasipskcnvnvpytispdidcsriy
>d1be3a_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1be3b_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1be3c1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1be3d1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1be3e1 2.29.1.1.1 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1be3e2 6.2.1.1.9 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1be3f1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1be3g1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1be3h1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1be3j1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1be3k1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1be4a_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be4b_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be4c_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrglmgeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfrpeelvnykscaqnwiye
>d1be6__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1be7__ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplsgvgkdqfeevee
>d1be8__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1be9a_ 2.32.1.1.3 Synaptic protein PSD-95, 3rd PDZ domain {Rat (Rattus norvegicus)}
flgeedipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqil
svngvdlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1bea__ 1.54.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>d1beba_ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bebb_ 2.53.1.1.8 beta-Lactoglobulin {Bovine (Bos taurus)}
qtmkgldiqkvagtwyslamaasdislldaqsaplrvyveelkptpegdleillqkweng
ecaqkkiiaektkipavfkidalnenkvlvldtdykkyllfcmensaepeqslvcqclvr
tpevddealekfdkalkalpmhirlsfnptqleeqc
>d1bec_1 2.1.1.1.156 (3-117) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
avtqsprnkvavtggkvtlscqqtnnhnnmywyrqdtghglrlihysygagstekgdipd
gykasrpsqeqfslilelatpsqtsvyfcasgggrgsyaeqffgpgtrltvle
>d1bec_2 2.1.1.2.145 (118-246) T-cell antigen receptor {Mouse (Mus musculus), beta-chain}
dlrqvtppkvslfepskaeiankqkatlvclargffpdhvelswwvngkevhsgvstdpq
aykesnysyclssrlrvsatfwhnprnhfrcqvqfhglseedkwpegspkpvtqnisaea
wgrad
>d1bed_1 1.47.1.1.2 (63-126) Disulphide-bond formation facilitator (DSBA), insertion domain {Vibrio cholerae}
gnmgqamskayatmialevedkmvpvmfnrihtlrkppkdeqelrqifldegidaakfda
ayng
>d1bed_2 3.38.1.4.2 (1-62,127-181) Disulphide-bond formation facilitator (DSBA) {Vibrio cholerae}
aqfkegehyqvlktpassspvvseffsfycphcntfepiiaqlkqqlpegakfqknhvsf
mgXfavdsmvrrfdkqfqdsgltgvpavvvnnrylvqgqsvksldeyfdlvnylltlk
>d1bee__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftaykydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1befa_ 2.41.1.3.4 NS3 protease {Dengue virus serotype 2}
wdvpspppvgkaeledgayrikqkgilgysqigagvykegtfhtmwhvtrgavlmhkgkr
iepswadvkkdlvscgggwklegewkegeevqvlalepgknpravqtkpglfktnagtig
avsldfspgtsgspiidkkgkvvgiygngvvtrsgayvsaiaqteksiednpeiedd
>d1beg__ 1.124.1.1.1 beta-cryptogein {Phytophthora cryptogea}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1beha_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
vdlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgk
lytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvw
lvyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklye
qlsg
>d1behb_ 2.15.1.1.1 Phosphatidylethanolamine binding protein {Human (Homo sapiens)}
dlskwsgplslqevdeqpqhplhvtyagaavdelgkvltptqvknrptsiswdgldsgkl
ytlvltdpdapsrkdpkyrewhhflvvnmkgndissgtvlsdyvgsgppkgtglhryvwl
vyeqdrplkcdepilsnrsgdhrgkfkvasfrkkyelrapvagtcyqaewddyvpklyeq
lsg
>d1bei__ 7.19.1.1.2 Sea anemone toxin k {Sun anemone (Stichodactyla helianthus), SHK}
rscidtipksrctafqckhsmxyrlsfcrktcgtc
>d1bej__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpggaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bek__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnaigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bela_ 4.5.1.1.1 Ribonuclease A (also ribonuclease B, S) {Bovine (Bos taurus)}
ketaaakferqhmdsstsaasssnycnqmmksrnltkdrckpvntfvhesladvqavcsq
knvackngqtncyqsystmsitdcretgsskypncaykttqankhiivacegnpyvpvhf
dasv
>d1bem__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpqgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>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
>d1beo__ 1.124.1.1.1 beta-cryptogein {Phytophthora cryptogea}
tactatqqtaayktlvsilsdasfnqcstdsgysmltakalpttaqyklmcastacntmi
kkivtlnppncdltvptsglvlnvysyangfsnkcssl
>d1bep__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpwgaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1beq__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpygaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bera1 1.4.3.4.1 (138-207) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivvyg
>d1bera2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1berb1 1.4.3.4.1 (138-205) Catabolite gene activator protein (CAP), C-terminal domain {Escherichia coli}
dvtgriaqtllnlakqpdamthpdgmqikitrqeigqivgcsretvgrilkmledqnlis
ahgktivv
>d1berb2 2.73.4.1.1 (9-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli}
ptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsylnqgd
figelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlqvts
ekvgnlafl
>d1bes__ 1.90.1.1.3 Cytochrome c peroxidase, CCP {Baker's yeast (Saccharomyces cerevisiae)}
lvhvasvekgrsyedfqkvynaialklreddeydnyigygpvlvrlawhisgtwdkhdnt
ggsyggtyrfkkefndpsnaglqngfkflepihkefpwissgdlfslggvtavqemqgpk
ipwrcgrvdtpedttpdngrlpdadkdagyvrtffqrlnmndrevvalmgahalgkthlk
nsgyegpygaannvftnefylnllnedwklekndanneqwdsksgymmlptdysliqdpk
ylsivkeyandqdkffkdfskafeklledgitfpkdapspfifktleeqgl
>d1bet__ 7.17.1.3.3 beta-Nerve growth factor {Mouse (Mus musculus)}
gefsvcdsvsvwvgdkttatdikgkevtvlaevninnsvfrqyffetkcrasnpvesgcr
gidskhwnsycttthtfvkalttdekqaawrfiridtacvcvlsrka
>d1beua_ 3.1.2.2.5 Trp synthase alpha-subunit {Salmonella typhimurium}
meryenlfaqlndrregafvpfvtlgdpgieqslkiidtlidagadalelgvpfsdplan
gptiqnanlrafaagvtpaqcfemlalirekhptipigllmyanlvfnngidafyarceq
vgvdsvlvadvpveesapfrqaalrhniapificppnadddllrqvasygrgytyllsrs
gvtgaenrgalplhhlieklkeyhaapalqgfgisspeqvsaavragaagaisgsaivki
ieknlaspkqmlaelrsfvsamkaasra
>d1beub_ 3.67.1.1.1 Tryptophan synthase, beta-subunit {Salmonella typhimurium}
tllnpyfgefggmyvpqilmpalnqleeafvraqkdpefqaqfadllknyagrptaltkc
qnitagtrttlylkredllhggahktnqvlgqallakrmgkseiiaetgagqhgvasala
sallglkcriymgakdverqspnvfrmrlmgaevipvhsgsatlkdacnealrdwsgsye
tahymlgtaagphpyptivrefqrmigeetkaqildkegrlpdaviacvgggsnaigmfa
dfindtsvgligvepgghgietgehgaplkhgrvgiyfgmkapmmqtadgqieesysisa
gldfpsvgpqhaylnsigradyvsitddealeafktlcrhegiipalesshalahalkmm
reqpekeqllvvnlsgrgdkdiftvhdil
>d1bev1_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
qaagalvagtststhsvatdstpalqaaetgatstardesmietrtivpthgihetsves
ffgrsslvgmpllatgtsithwridfrefvqlrakmswftymrfdveftiiatsstgqnv
tteqhttyqvmyvppgapvpsnqdsfqwqsgcnpsvfadtdgppaqfsvpfmssanayst
vydgyarfmdtdpdrygilpsnflgfmyfrtledaahqvrfriyakikhtscwipraprq
apykkrynlvfsgdsdricsnrasltsy
>d1bev2_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
eacgysdrvaqltlgnstittqeaanicvaygcwpaklsdtdatsvdkptepgvsadrfy
tlrskpwqadskgwywklpdalnntgmfgqnaqfhylyrggwavhvqcnatkfhqgtllv
laipehqiatqeqpafdrtmpgseggtfqepfwledgtslgnsliyphqwinlrtnnsat
lilpyvnaipmdsairhsnwtlaiipvaplkyaaettplvpitvtiapmeteynglrrai
asnq
>d1bev3_ 2.9.1.4.12 Bovine enterovirus coat protein {Bovine enterovirus, VG-5-27}
glptkpgpgsyqfmttdedcspcilpdfqptpeifipgkvnnlleiaqvesileannreg
vegveryvipvsvqdaldaqiyalrlelggsgplsssllgtlakhytqwsgsveitcmft
gtfmttgkvllaytppggdmprnreeamlgthviwdfglqssitlvipwisashfrgvsn
ddvlnyqyyaaghvtiwyqtnmvippgfpntagiimmiaaqpnfsfriqkdredmtqtai
lq
>d1bexa_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1bexb_ 2.5.1.1.23 Azurin {Pseudomonas aeruginosa}
aecsvdiqgndqmqfntnaitvdksckqftvnlshpgnlpknvmghnwvlstaadmqgvv
tdgmasgldkdylkpddsrviahtkligsgekdsvtfdvsklkegeqymffctfpghsal
mkgtltlk
>d1beyh1 2.1.1.1.123 (1-121) Immunoglobulin (variable domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
qvqlqesgpglvrpsqtlsltctvsgftftdfymnwvrqppgrglewigfirdkakgytt
eynpsvkgrvtmlvdtsknqfslrlssvtaadtavyycareghtaapfdywgqgslvtvs
s
>d1beyh2 2.1.1.2.121 (122-219) Immunoglobulin (constant domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
astkgpsvfplapsskstsggtaalgclvkdyfpepvtvswnsgaltsgvhtfpavlqss
glyslssvvtvpssslgtqtyicnvnhkpsntkvdkkv
>d1beyl1 2.1.1.1.123 (1-107) Immunoglobulin (variable domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
diqmtqspsslsasvgdrvtitckasqnidkylnwyqqkpgkapklliyntnnlqtgvps
rfsgsgsgtdftftisslqpediatyyclqhisrprtfgqgtkveik
>d1beyl2 2.1.1.2.121 (108-214) Immunoglobulin (constant domains of L and H chains) {Antibody to CAMPATH-1H humanized fab, kappa L chain}
rtvaapsvfifppsdeqlksgtasvvcllnnfypreakvqwkvdnalqsgnsqesvteqd
skdstyslsstltlskadyekhkvyacevthqglsspvtksfnrgec
>d1bez__ 3.59.1.6.1 Haloalkane dehalogenase {Xanthobacter autotrophicus}
mvnairtpdqrfsnldqypfspnylddlpgypglrahyldegnsdaedvflclhgeptws
ylyrkmipvfaesgarviapdffgfgksdkpvdeedytfefhrnfllalierldlrnitl
vvqdwggflgltlpmadpsrfkrliimnaclmtdpvtqpafsafvtqpadgftaykydlv
tpsdlrldqfmkrwaptlteaeasayaapfpdtsyqagvrkfpkmvaqrdqacidistea
isfwqndwngqtfmaigmkdkllgpdvmypmkalingcpepleiadaghfvqefgeqvar
ealkhfaete
>d1bf0__ 7.8.1.1.11 Calcicludine (cac) {Green mamba (Dendroaspis angusticeps)}
wqppwyckepvrigsckkqfssfyfkwtakkclpflfsgcggnanrfqtigecrkkclgk
>d1bf2_1 2.1.1.5.9 (1-162) Isoamylase, N-terminal domain {Pseudomonas amyloderamosa}
ainsmslgasydaqqanitfrvyssqatrivlylysagygvqesatytlspagsgvwavt
vpvssikaagitgavyygyrawgpnwpyasnwgkgsqagfvsdvdangdrfnpnkllldp
yaqevsqdplnpsnqngnvfasgasyrttdsgiyapkgvvlv
>d1bf2_2 2.62.1.1.14 (638-750) Isoamylase {Pseudomonas amyloderamosa}
ysgsqltwyqpsgavadsnywnntsnyaiayaingpslgdsnsiyvayngwsssvtftlp
appsgtqwyrvtdtcdwndgastfvapgsetliggagttygqcgqsllllisk
>d1bf2_3 3.1.7.1.14 (163-637) Isoamylase, central domain {Pseudomonas amyloderamosa}
pstqstgtkptraqkddviyevhvrgfteqdtsipaqyrgtyygaglkasylaslgvtav
eflpvqetqndandvvpnsdanqnywgymtenyfspdrryaynkaaggptaefqamvqaf
hnagikvymdvvynhtaeggtwtssdpttatiyswrgldnatyyeltsgnqyfydntgig
anfntyntvaqnlivdslaywantmgvdgfrfdlasvlgnsclngaytasapncpnggyn
fdaadsnvainrilreftvrpaaggsgldlfaepwaiggnsyqlggfpqgwsewnglfrd
slrqaqnelgsmtiyvtqdandfsgssnlfqssgrspwnsinfidvhdgmtlkdvyscng
annsqawpygpsdggtstnyswdqgmsagtgaavdqrraartgmafemlsagtplmqggd
eylrtlqcnnnaynldssanwltyswttdqsnfytfaqrliafrkahpalrpssw
>d1bf3_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgkiragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bf3_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bf4a_ 4.8.2.1.1 DNA-binding protein {Sulfolobus solfataricus, Sso7d}
atvkfkykgeekevdiskikkvwrvgkmisftydegggktgrgavsekdapkellqmlek
qkk
>d1bf5a1 1.50.1.1.1 (136-316) STAT-1, coiled coil domain {Human (Homo sapiens)}
ldkqkeldskvrnvkdkvmcieheiksledlqdeydfkcktlqnrehlllkkmylmldnk
rkevvhkiiellnvteltqnalindelvewkrrqqsaciggppnacldqlqnwftivaes
lqqvrqqlkkleeleqkytyehdpitknkqvlwdrtfslfqqliqss
>d1bf5a2 2.2.5.1.9 (317-568) STAT-1, DNA-binding domain {Human (Homo sapiens)}
fvverqpcmpthpqrplvlktgvqftvklrllvklqelnynlkvkvlfdkdvnerntvkg
frkfnilgthtkvmnmeestngslaaefrhlqlkeqknagtrtnegplivteelhslsfe
tqlcqpglvidlettslpvvvisnvsqlpsgwasilwynmlvaeprnlsffltppcarwa
qlsevlswqfssvtkrglnvdqlnmlgekllgpnaspdglipwtrfckenindknfpfwl
wiesilelikkh
>d1bf5a3 4.72.1.1.17 (569-710) STAT-1 {Human (Homo sapiens)}
llplwndgcimgfiskererallkdqqpgtfllrfsessregaitftwversqnggepdf
havepytkkelsavtfpdiirnykvmaaenipenplkylypnidkdhafgkyysrgxikt
elisvs
>d1bf6a_ 3.1.8.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1bf6b_ 3.1.8.3.2 Phosphotriesterase homology protein {Escherichia coli}
sfdptgytlahehlhidlsgfknnvdcrldqyaficqemndlmtrgvrnviemtnrymgr
naqfmldvmretginvvactgyyqdaffpehvatrsvqelaqemvdeieqgidgtelkag
iiaeigtsegkitpleekvfiaaalahnqtgrpisthtsfstmgleqlallqahgvdlsr
vtvghcdlkdnldnilkmidlgayvqfdtigknsyypdekriamlhalrdrgllnrvmls
mditrrshlkanggygydyllttfipqlrqsgfsqadvdvmlrenpsqffq
>d1bf8_1 2.1.10.1.2 (1-121) Periplasmic chaperone FimC {Escherichia coli}
gvalgatrviypagqkqeqlavtnndenstyliqswvenadgvkdgrfivtpplfamkgk
kentlrildatnnqlpqdreslfwmnvkaipsmdkskltentlqlaiisriklyyrpakl
a
>d1bf8_2 2.6.2.1.2 (122-205) FimC {Escherichia coli}
lppdqaaeklrfrrsansltlinptpyyltvtelnagtrvlenalvppmgestvklpsda
gsnityrtindygaltpkmtgvme
>d1bf9__ 7.3.11.1.8 Factor VII, N-terminal domain {Human (Homo sapiens)}
sdgdqcasspcqnggsckdqlqsyicfclpafegrncethk
>d1bfa__ 1.54.1.2.3 Hageman factor/amylase inhibitor {Maize (Zea mays)}
scvpgwaiphnplpscrwyvtsrtcgigprlpwpelkrrccreladipaycrctalsilm
dgaippgpdaqlegrledlpgcprevqrgfaatlvteaecnlatisgvaecpwilg
>d1bfb__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfc__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
pkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamked
grllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkailf
lpms
>d1bfd_1 3.25.1.3.5 (182-341) Benzoylformate decarboxylase {Pseudomonas putida}
svrlndqdldilvkalnsasnpaivlgpdvdaananadcvmlaerlkapvwvapsaprcp
fptrhpcfrglmpagiaaisqlleghdvvlvigapvfryhqydpgqylkpgtrlisvtcd
pleaarapmgdaivadigamasalanlveessrqlptaap
>d1bfd_2 3.29.1.1.5 (2-181) Benzoylformate decarboxylase {Pseudomonas putida}
asvhgttyellrrqgidtvfgnpgsnelpflkdfpedfryilalqeacvvgiadgyaqas
rkpafinlhsaagtgnamgalsnawnshsplivtagqqtramigvealltnvdaanlprp
lvkwsyepasaaevphamsraihmasmapqgpvylsvpyddwdkdadpqshhlfdrhvss
>d1bfd_3 3.29.1.1.5 (342-524) Benzoylformate decarboxylase {Pseudomonas putida}
epakvdqdagrlhpetvfdtlndmapenaiylneststtaqmwqrlnmrnpgsyyfcaag
glgfalpaaigvqlaeperqviavigdgsanysisalwtaaqyniptifvimnngtygal
rwfagvleaenvpgldvpgidfralakgygvqalkadnleqlkgslqealsakgpvliev
stv
>d1bfea_ 2.32.1.1.3 Synaptic protein PSD-95, 3rd PDZ domain {Rat (Rattus norvegicus)}
dipreprrivihrgstglgfniiggedgegifisfilaggpadlsgelrkgdqilsvngv
dlrnasheqaaialknagqtvtiiaqykpeeysrfeansrvnssgrivtn
>d1bff__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
kdpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvcanrylamk
edgrllaskcvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkai
lflpmsaks
>d1bfg__ 2.37.1.1.1 Basic FGF {Human (Homo sapiens)}
dpkrlycknggfflrihpdgrvdgvreksdphiklqlqaeergvvsikgvsanrylamke
dgrllasksvtdecffferlesnnyntyrsrkytswyvalkrtgqyklgsktgpgqkail
flpmsa
>d1bfi__ 4.72.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {Human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfj__ 4.72.1.1.11 Phosphatidylinositol 3-kinase, p85-alpha subunit {Human (Homo sapiens)}
edlphhdektwnvgssnrnkaenllrgkrdgtflvresskqgcyacsvvvdgevkhcvin
ktatgygfaepynlysslkelvlhyqhtslvqhndslnvtlaypvyaqqrr
>d1bfk__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1bfma_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfmb_ 1.23.1.2.2 Histone B {Methanothermus fervidus}
melpiapigriikdagaervsddaritlakileemgrdiaseaiklarhagrktikaedi
elavrrfkk
>d1bfn__ 3.1.7.2.1 beta-Amylase {Soybean (Glycine max)}
nmllnyvpvyvmlplgvvnvdnvfedpdglkeqllqlraagvdgvmvdvwwgiielkgpk
qydwrayrsllqlvqecgltlqaimsfhqcggnvgdivnipipqwvldigesnhdifytn
rsgtrnkeyltvgvdnepifhgrtaieiysdymksfrenmsdflesgliidievglgpag
elrypsypqsqgwefpgigefqcydkylkadfkaavaraghpewelpddagkyndvpest
gffksngtyvtekgkffltwysnkllnhgdqildeankaflgckvklaikvsgihwwykv
enhaaeltagyynlndrdgyrpiarmlsrhhailnftclemrdseqpsdaksgpqelvqq
vlsggwredirvagenalprydataynqiilnarpqgvnnngppklsmfgvtylrlsddl
lqksnfnifkkfvlkmhadqdycanpqkynhaitplkpsapkipievlleatkptlpfpw
lpetdmkvdg
>d1bfoa1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoa2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfob1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfob2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfoc1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoc2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfod1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfod2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfoe1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfoe2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfof1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfof2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfog1 2.1.1.1.121 (1-107) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
dikmtqspsflsasvgdrvtlnckasqnidkylnwyqqklgespklliyntnnlqtgips
rfsgsgsgtdftltisslqpedvatyfclqhisrprtfgtgtklelk
>d1bfog2 2.1.1.2.119 (108-214) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
ranaaptvsifppsteqlatggasvvclmnkfyprdisvkwkidgterngvlnsvtdqds
adstysmsstlsltkadyqshnlytcqvvhktssspvvaknfnrnec
>d1bfoh1 2.1.1.1.121 (1-121) Immunoglobulin (variable domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
evkllesggglvqpggsmrlscagsgftftdfymnwirqpagkapewlgfirdkakgytt
eynpsvkgrftisrdntqnmlylqmntlraedtatyycareghtaapfdywgqgvmvtvs
s
>d1bfoh2 2.1.1.2.119 (122-216) Immunoglobulin (constant domains of L and H chains) {CAMPATH-1G igg2b monoclonal fab (rat), kappa L chain}
aqttapsvyplapgcgdttsstvtlgclvkgyfpepvtvtwnsgalssdvhtfpavlqsg
lytltssvtsstwpsqtvtcnvahpasstkvdkkv
>d1bfp__ 4.20.1.1.1 Green fluorescent protein, GFP {Jellyfish (Aequorea victoria)}
mskgeelftgvvpilveldgdvnghkfsvsgegegdatygkltlkficttgklpvpwptl
vttfxvqcfsrypdhmkrhdffksampegyvqertiffkddgnyktraevkfegdtlvnr
ielkgidfkedgnilghkleynfnshnvyimadkqkngikvnfkirhniedgsvqladhy
qqntpigdgpvllpdnhylstqsalskdpnekrdhmvllefvtaagi
>d1bfra_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrb_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrc_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrd_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfre_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrf_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrg_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrh_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfri_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrj_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrk_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrl_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrm_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrn_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfro_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrp_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrq_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrr_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrs_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrt_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfru_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrv_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrw_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>d1bfrx_ 1.26.1.1.2 Bacterioferritin (cytochrome b1) {Escherichia coli}
mkgdtkvinylnkllgnelvainqyflharmfknwglkrlndveyhesidemkhadryie
rilfleglpnlqdlgklnigedveemlrsdlaleldgaknlreaigyadsvhdyvsrdmm
ieilrdeeghidwleteldliqkmglqnylqaqireeg
>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
>d1bftb_ 2.1.1.5.22 p50 subunit of NF-kappa B transcription factor, C-terminal domain {Mouse (Mus musculus)}
taelkicrvnrnsgsclggdeifllcdkvqkedievyftgpgweargsfsqadvhrqvai
vfrtppyadpslqapvrvsmqlrrpsdrelsepmefqylpd
>d1bfu__ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgfkganvkvavldtgiqashpdlnvvggasfvageayntdg
nghgthvagtvaaldnttgvlgvapsvslyavkvlnssgsgsysgivsgiewattngmdv
inmslggasgstamkqavdnayargvvvvaaagnsgnsgstntigypakydsviavgavd
snsnrasfssvgaelevmapgagvystyptntyatlngtsmasphvagaaalilskhpnl
sasqvrnrlsstatylgssfyygkglinveaaaq
>d1bfvh_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
qvqlqesggglvnlggsmtlscvasgftfntyymswvrqtpektlelvaainsdgepiyy
pdtlkgrvtisrdnakktlylqmsslnfedtalyycarlnyavygmdywgqgttvtvss
>d1bfvl_ 2.1.1.1.88 Immunoglobulin (variable domains of L and H chains) {Fv 4155 (mouse), kappa L chain}
dieltqsppslpvslgdqvsiscrssqslvsnnrrnylhwylqkpgqspklviykvsnrf
sgvpdrfsgsgsgtdftlkisrvaaedlglyfcsqsshvpltfgsgtkleikr
>d1bfx__ 4.94.1.1.2 Cytochrome b5 {Rat (Rattus norvegicus)}
dkdvkyytleeiqkhkdskstwvilhhkvydltkfleehpggeevlreqaggdatenfed
vghstdarelsktyiigelhpddrskiakpsetl
>d1bfy__ 7.35.4.1.4 Rubredoxin {Clostridium pasteurianum}
mkkytctvcgyiynpedgdpdngvnpgtdfkdipddwvcplcgvgkdqfeevee
>d1bg0_1 1.80.1.1.3 (2-95) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
vdqatldkleagfkklqeasdcksllkkhltkdvfdsiknkktgmgatlldviqsgvenl
dsgvgiyapdaesyrtfgplfdpiiddyhggfkl
>d1bg0_2 4.102.1.2.3 (96-357) Arginine kinase {Horseshoe crab (Limulus polyphemus)}
tdkhppkqwgdintlvgldpagqfiistrvrcgrslqgypfnpcltaeqykemeekvsst
lssmedelkgtyypltgmskatqqqliddhflfkegdrflqtanacrywptgrgifhnda
ktflvwvneedhlriismqkggdlktvykrlvtavdniesklpfshddrfgfltfcptnl
gttmrasvhiqlpklakdrkvlediaskfnlqvrgtrgehteseggvydisnkrrlglte
yqavremqdgilemikmekaaa
>d1bg1a1 1.50.1.1.2 (136-321) STAT3b {Mouse (Mus musculus)}
vvtekqqmleqhlqdvrkrvqdleqkmkvvenlqddfdfnyktlksqgdmqdlngnnqsv
trqkmqqleqmltaldqmrrsivselagllsameyvqktltdeeladwkrrqqiaciggp
pnicldrlenwitslaesqlqtrqqikkleelqqkvsykgdpivqhrpmleerivelfrn
lmksaf
>d1bg1a2 2.2.5.1.10 (322-575) STAT3b {Mouse (Mus musculus)}
vverqpcmpmhpdrplviktgvqfttkvrllvkfpelnyqlkikvcidkdsgdvaalrgs
rkfnilgtntkvmnmeesnngslsaefkhltlreqrcgnggrancdaslivteelhlitf
etevyhqglkidlethslpvvvisnicqmpnawasilwynmltnnpknvnfftkppigtw
dqvaevlswqfssttkrglsieqlttlaekllgpgvnysgcqitwakfckenmagkgfsf
wvwldniidlvkky
>d1bg1a3 4.72.1.1.18 (576-716) STAT3b {Mouse (Mus musculus)}
ilalwnegyimgfiskererailstkppgtfllrfsesskeggvtftwvekdisgstqiq
svepytkqqlnnmsfaeiimgykimdatnilvsplvylypdipkeeafgkycrpesqehp
eadpgsaapxlktkficvtpf
>d1bg2__ 3.30.1.7.4 Kinesin {Human (Homo sapiens)}
dlaecnikvmcrfrplnesevnrgdkyiakfqgedtvviaskpyafdrvfqsstsqeqvy
ndcakkivkdvlegyngtifaygqtssgkthtmegklhdpegmgiiprivqdifnyiysm
denlefhikvsyfeiyldkirdlldvsktnlsvhedknrvpyvkgcterfvcspdevmdt
idegksnrhvavtnmnehssrshsiflinvkqentqteqklsgklylvdlagsekvsktg
aegavldeakninkslsalgnvisalaegstyvpyrdskmtrilqdslggncrttivicc
spssynesetkstllfgqrakti
>d1bg3a1 3.46.1.2.3 (1-222) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
miaaqllayyftelkddqvkkidkylyamrlsdeilidiltrfkkemknglsrdynptas
vkmlptfvrsipdgsekgdfialdlggssfrilrvqvnheknqnvsmeseiydtpenivh
gsgtqlfdhvadclgdfmekkkikdkklpvgftfsfpcrqskideavlitwtkrfkasgv
egadvvkllnkaikkrgdydanivavvndtvgtmmtcgyddq
>d1bg3a2 3.46.1.2.3 (223-465) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreld
rgslnpgkqlfekmvsgmymgelvrlilvkmakegllfegritpelltrgkfntsdvsai
ekdkegiqnakeiltrlgvepsdvdcvsvqhictivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykmhpqysrrfhktlrrlvpdsdvrfllsesgtgkgaamvtavayr
lae
>d1bg3a3 3.46.1.2.3 (466-670) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qhirqieetlahfrlskqtlmevkkrlrtememglrketnskatvkmlpsfvrsipdgte
hgdflaldlggtnfrvllvkirsgkkrtvemhnkiysipleimqgtgdelfdhivscisd
fldymgikgprmplgftfsfpchqtnldcgiliswtkgfkatdceghdvasllrdavkrr
eefdldvvavvndtvgtmmtcayeep
>d1bg3a4 3.46.1.2.3 (671-911) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
tceiglivgtgtnacymeemknvemvegnqgqmcinmewgafgdngclddirtdfdkvvd
eyslnsgkqrfekmisgmylgeivrnilidftkkgflfrgqiseplktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvskraaqlcgagmaavvekirenrg
ldhlnvtvgvdgtlyklhphfsrimhqtvkelspkctvsfllsedgsgkgaalitavgvr
lrgdpsia
>d1bg3b1 3.46.1.2.3 (1-222) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
miaaqllayyftelkddqvkkidkylyamrlsdeilidiltrfkkemknglsrdynptas
vkmlptfvrsipdgsekgdfialdlggssfrilrvqvnheknqnvsmeseiydtpenivh
gsgtqlfdhvadclgdfmekkkikdkklpvgftfsfpcrqskideavlitwtkrfkasgv
egadvvkllnkaikkrgdydanivavvndtvgtmmtcgyddq
>d1bg3b2 3.46.1.2.3 (223-465) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qcevgliigtgtnacymeelrhidlvegdegrmcintewgafgddgsledirtefdreld
rgslnpgkqlfekmvsgmymgelvrlilvkmakegllfegritpelltrgkfntsdvsai
ekdkegiqnakeiltrlgvepsdvdcvsvqhictivsfrsanlvaatlgailnrlrdnkg
tprlrttvgvdgslykmhpqysrrfhktlrrlvpdsdvrfllsesgtgkgaamvtavayr
lae
>d1bg3b3 3.46.1.2.3 (466-670) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
qhirqieetlahfrlskqtlmevkkrlrtememglrketnskatvkmlpsfvrsipdgte
hgdflaldlggtnfrvllvkirsgkkrtvemhnkiysipleimqgtgdelfdhivscisd
fldymgikgprmplgftfsfpchqtnldcgiliswtkgfkatdceghdvasllrdavkrr
eefdldvvavvndtvgtmmtcayeep
>d1bg3b4 3.46.1.2.3 (671-911) Mammalian type I hexokinase {Rat (Rattus norvegicus)}
tceiglivgtgtnacymeemknvemvegnqgqmcinmewgafgdngclddirtdfdkvvd
eyslnsgkqrfekmisgmylgeivrnilidftkkgflfrgqiseplktrgifetkflsqi
esdrlallqvrailqqlglnstcddsilvktvcgvvskraaqlcgagmaavvekirenrg
ldhlnvtvgvdgtlyklhphfsrimhqtvkelspkctvsfllsedgsgkgaalitavgvr
l
>d1bg4__ 3.1.7.3.2 Xylanase {Penicillium simplicissimum}
asvsidakfkahgkkylgtigdqytltkntknpaiikadfgqltpensmkwdatepnrgq
ftfsgsdylvnfaqsngklirghtlvwhsqlpgwvssitdkntlisvlknhittvmtryk
gkiyawdvlneifnedgslrnsvfynvigedyvriafetarsvdpnaklyindynldsag
yskvngmvshvkkwlaagipidgigsqthlgagagsavagalnalasagtkeiaiteldi
agasstdyvnvvnaclnqakcvgitvwgvadpdswrsssspllfdgnynpkaaynaiana
l
>d1bg5_1 1.48.1.1.14 (81-254) Glutathione S-transferase {Schistosoma japonicum}
mlggcpkeraeismlegavldirygvsriayskdfetlkvdflsklpemlkmfedrlchk
tylngdhvthpdfmlydaldvvlymdpmcldafpklvcfkkrieaipqidkylksskyia
wplqgwqatfgggdhppksdlvprgssyyqeaksskimesfknmvpqqalvnss
>d1bg5_2 3.38.1.5.14 (1-80) Glutathione S-transferase {Schistosoma japonicum}
mspilgywkikglvqptrllleyleekyeehlyerdegdkwrnkkfelglefpnlpyyid
gdvkltqsmaiiryiadkhn
>d1bg6_1 1.96.1.4.1 (188-359) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
nvlhtsltnvnavmhplptllnaarcesgtpfqyylegitpsvgslaekvdaeriaiaka
fdlnvpsvcewykesygqspatiyeavqgnpayrgiagpinlntryffedvstglvplse
lgravnvptplidavldlisslidtdfrkegrtleklglsgltaagirsave
>d1bg6_2 3.2.1.6.6 (4-187) N-(1-D-carboxylethyl)-L-norvaline dehydrogenase {Arthrobacter strain 1c}
sktyavlglgngghafaaylalkgqsvlawdidaqrikeiqdrgaiiaegpglagtahpd
lltsdiglavkdadvilivvpaihhasiaaniasyisegqliilnpgatggalefrkilr
engapevtigetssmlftcrserpgqvtvnaikgamdfaclpaakagwaleqigsvlpqy
vave
>d1bg7__ 1.26.1.1.6 (Apo)ferritin {Bullfrog (Rana catesbeiana)}
dsqvrqnfhrdceaainrmvnmelyasytylsmafyfdrddialhnvakffkeqsheere
haeklmkdqnkrggrivlqdvqkperdewgntleamqaalqlektvnqalldlhkvgsdk
vdphlcdfleteypeeqvksikqlgdyitnlkrlglpqngmgeylfdkhtmge
>d1bg8a_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8b_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg8c_ 1.59.1.1.1 HdeA {Escherichia coli}
kkpvnswtcedflavdesfqptavgfaealnnkdkpedavldvqgiatvtpaivqactqd
kqanfkdkvkgewdki
>d1bg9_1 2.62.1.1.16 (347-403) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
hnesklqiieadadlylaeidgkvivklgprydvgnlipggfkvaahgndyavweki
>d1bg9_2 3.1.7.1.16 (1-346) Plant alpha-amylase {Barley (Hordeum vulgare), seeds, AMY2 isozyme}
qvlfqgfnweswkhnggwynflmgkvddiaaagithvwlppasqsvaeqgympgrlydld
askygnkaqlksligalhgkgvkaiadivinhrtaehkdgrgiycifeggtpdarldwgp
hmicrddrpyadgtgnpdtgadfgaapdidhlnlrvqkelvewlnwlkadigfdgwrfdf
akgysadvakiyidrsepsfavaeiwtslayggdgkpnlnqdqhrqelvnwvdkvggkgp
attfdfttkgilnvavegelwrlrgtdgkapgmigwwpakavtfvdnhdtgstqhmwpfp
sdrvmqgyayilthpgtpcifydhffdwglkeeidrlvsvrtrhgi
>d1bgaa_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgab_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgac_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgad_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgba_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bgbb_ 3.43.1.2.1 Restriction endonuclease EcoRV {Escherichia coli}
slrsdlinalydenqkydvcgiisaegkiyplgsdtkvlstifelfsrpiinkiaekhgy
iveepkqqnhypdftlykpsepnkkiaidikttytnkenekikftlggytsfirnntkni
vypfdqyiahwiigyvytrvatrksslktyninelneipkpykgvkvflqdkwviagdla
gsgnttnigsihahykdfvegkgifdsedefldywrnyertsqlrndkynniseyrnwiy
rgrk
>d1bgc__ 1.27.1.1.2 Granulocyte-colony stimulating factor (G-CSF) {Bovine (Bos taurus)}
slpqsfllkcleqvrkiqadgaelqerlcaahklchpeelmllrhslgipqaplsscssq
slqlrgclnqlhgglflyqgllqalagispelaptldtlqldvtdfatniwlqmedlgaa
pavqptqgamptftsafqrraggvlvasqlhrflelayrglryla
>d1bgd__ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
lpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssqa
lqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgmap
avpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgea_ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfak
>d1bgeb_ 1.27.1.1.3 Granulocyte-colony stimulating factor (G-CSF) {Canine (Canis familiaris)}
plpqsfllkcleqmrkvqadgtalqetlcathqlchpeelvllghalgipqpplsscssq
alqlmgclrqlhsglflyqgllqalagispelaptldtlqldttdfainiwqqmedlgma
pavpptqgtmpaftsafqrraggvlvasnlqsflelayralrhfa
>d1bgf__ 1.87.1.1.1 Transcription factor STAT-4 N-domain {Mouse (Mus musculus)}
ggsqwnqvqqleikfleqvdqfyddnfpmeirhllaqwietqdwevasnnetmatillqn
lliqldeqlgrvskeknlllihnlkrirkvlqgkfhgnpmhvavvisnclreerrilaaa
nmpi
>d1bgga_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggb_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggc_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bggd_ 3.1.7.4.4 Beta-glucosidase A {Bacillus polymyxa}
tifqfpqdfmwgtataayqiegayqedgrglsiwdtfahtpgkvfngdngnvacdsyhry
eedirlmkelgirtyrfsvswprifpngdgevnqegldyyhrvvdllndngiepfctlyh
wdlpqalqdaggwgnrrtiqafvqfaetmfrefhgkiqhwltfnepwciaflsnmlgvha
pgltnlqtaidvghhllvahglsvrrfrelgtsgqigiapnvswavpystseedkaacar
tislhsdwflqpiyqgsypqflvdwfaeqgatvpiqdgdmdiigepidmiginyysmsvn
rfnpeagflqseeinmglpvtdigwpvesrglyevlhylqkygnidiyitengacindev
vngkvqddrrisymqqhlvqvhrtihdglhvkgymawslldnfewaegynmrfgmihvdf
rtqvrtpkesyywyrnvvsnnwletrr
>d1bgi__ 4.2.1.2.1 Lysozyme {Chicken (Gallus gallus)}
kvfgrcelaaamkrhgldnyrgyslgnwvcaakfesnfntqatnrntdgstdygilqins
rwwcndgrtpgsrnlcnipcsallssditasvncakkivsdgngmnawvawrnrckgtdv
qawirgcrl
>d1bgj_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfrgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bgj_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiaplrsfvvep
>d1bgk__ 7.19.1.1.1 Sea anemone toxin k {Sea anemone (Bunodosoma granulifera), BGK}
vcrdwfketacrhakslgncrtsqkyrancaktcelc
>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
>d1bgla3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgla4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgla5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglb1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglb2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglb3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglb4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglb5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglc1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglc2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglc3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglc4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglc5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgld1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgld2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgld3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgld4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgld5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgle1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgle2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgle3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgle4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgle5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglf1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglf2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglf3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglf4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglf5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglg1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglg2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglg3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglg4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglg5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bglh1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bglh2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bglh3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bglh4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bglh5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmi1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmi2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmi3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmi4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmi5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmj1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmj2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmj3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmj4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmj5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmk1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmk2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmk3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmk4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmk5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgml1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgml2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgml3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgml4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgml5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmm1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmm2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmm3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmm4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmm5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmn1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmn2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmn3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmn4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmn5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmo1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmo2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmo3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmo4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmo5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgmp1 2.1.4.1.1 (220-333) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
tqisdfhvatrfnddfsravleaevqmcgelrdylrvtvslwqgetqvasgtapfggeii
derggyadrvtlrlnvenpklwsaeipnlyravvelhtadgtlieaeacdvgfr
>d1bgmp2 2.1.4.1.1 (626-730) beta-Galactosidase, domains 2 and 4 {Escherichia coli}
ffqfrlsgqtievtseylfrhsdnellhwmvaldgkplasgevpldvapqgkqlielpel
pqpesagqlwltvrvvqpnatawseaghisawqqwrlaenlsvtl
>d1bgmp3 2.16.1.4.1 (3-219) beta-Galactosidase {Escherichia coli}
itdslavvlqrrdwenpgvtqlnrlaahppfaswrnseeartdrpsqqlrslngewrfaw
fpapeavpeswlecdlpeadtvvvpsnwqmhgydapiytnvtypitvnppfvptenptgc
ysltfnvdeswlqegqtriifdgvnsafhlwcngrwvgygqdsrlpsefdlsaflragen
rlavmvlrwsdgsyledqdmwrmsgifrdvsllhkpt
>d1bgmp4 2.27.1.1.1 (731-1023) beta-Galactosidase, domain 5 {Escherichia coli}
paashaiphlttsemdfcielgnkrwqfnrqsgflsqmwigdkkqlltplrdqftrapld
ndigvseatridpnawverwkaaghyqaeaallqctadtladavlittahawqhqgktlf
isrktyridgsgqmaitvdvevasdtphpariglncqlaqvaervnwlglgpqenypdrl
taacfdrwdlplsdmytpyvfpsenglrcgtrelnygphqwrgdfqfnisrysqqqlmet
shrhllhaeegtwlnidgfhmgiggddswspsvsaefqlsagryhyqlvwcqk
>d1bgmp5 3.1.7.3.12 (334-625) beta-Galactosidase, domain 3 {Escherichia coli}
evriengllllngkpllirgvnrhehhplhgqvmdeqtmvqdillmkqnnfnavrcshyp
nhplwytlcdryglyvvdeaniethgmvpmnrltddprwlpamservtrmvqrdrnhpsv
iiwslgnesghganhdalyrwiksvdpsrpvqyegggadttatdiicpmyarvdedqpfp
avpkwsikkwlslpgetrplilceyahamgnslggfakywqafrqyprlqggfvwdwvdq
slikydengnpwsayggdfgdtpndrqfcmnglvfadrtphpalteakhqqq
>d1bgn_1 3.3.1.2.4 (1-173,276-391) p-Hydroxybenzoate hydroxylase (PHBH) {Pseudomonas aeruginosa}
mktqvaiigagpsglllgqllhkagidnvilerqtpdyvlgriragvleqgmvdllreag
vdrrmardglvhegveiafagqrrridlkrlsggktvtvygqtevtrdlmeareasgatt
vyqaaevrlhdlqgerpyvtferdgerlrldcdyiagcdgfhgisrqsipaerXmqhgrl
flagdaahivpptgakglnlaasdvstlyrlllkayregrgellerysaiclrriwkaer
fswwmtsvlhrfpdtdafsqriqqteleyylgseaglatiaenyvglpye
>d1bgn_2 4.14.1.2.2 (174-275) p-Hydroxybenzoate hydroxylase, PHBH {Pseudomonas aeruginosa}
lkvfervypfgwlglladtppvsheliyanhprgfalcsqrsatrsryyvqvpltekved
wsderfwtelkarlpaevaeklvtgpsleksiapltsfvvep
>d1bgo__ 4.3.1.1.13 (Pro)cathepsin K {Human (Homo sapiens)}
apdsvdyrkkgyvtpvknqgqcgscwafssvgalegqlkkktgkllnlspqnlvdcvsen
dgcgggymtnafqyvqknrgidsedaypyvgqeescmynptgkaakcrgyreipegneka
lkravarvgpvsvaidasltsfqfyskgvyydescnsdnlnhavlavgygiqkgnkhwii
knswgenwgnkgyilmarnknnacgianlasfpkm
>d1bgp__ 1.90.1.1.8 Peroxidase 1 {Barley (Hordeum vulgare), grain}
aeppvapglsfdfywqtcpraesivrefvqeavrkdiglaagllrlhfhdcfvqgcdasv
lldgsatgpgeqqappnltlrpsafkavndirdrlerecrgavvscsdilalaardsvvv
sggpdyrvplgrrdsrsfastqdvlsdlpgpssnvqsllallgrlgldatdlvtisgght
iglahcssfedrlfprpdptisptflsrlkrtcpakgtdrrtvldvrtpnvfdnkyyidl
vnreglfvsdqdlftnaitrpiverfaqsqqdffeqfgvsigkmgqmrvrtsdqgevrrn
csvrnpgpg
>d1bgq__ 4.96.1.1.1 HSP90 {Baker's yeast (Saccharomyces cerevisiae)}
masetfefqaeitqlmsliintvysnkeiflrelisnasdaldkirykslsdpkqletep
dlfiritpkpeqkvleirdsgigmtkaelinnlgtiaksgtkafmealsagadvsmigqf
gvgfyslflvadrvqvisksnddeqyiwesnaggsftvtldevnerigrgtilrlflkdd
qleyleekrikevikrhsefvaypiqlvvtkeve
>d1bgsa_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bgsb_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>d1bgsc_ 4.1.1.1.5 Barnase/Binase {Bacillus amyloliquefaciens}
aqvintfdgvadylqtyhklpdnyitkseaqalgwvaskgnladvapgksiggdifsnre
gklpgksgrtwreadinytsgfrnsdrilyssdwliykttdhyqtftkir
>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
>d1bgt__ 3.77.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgu__ 3.77.1.1.1 beta-Glucosyltransferase (DNA-modifying) {Bacteriophage T4}
mkiaiinmgnnvinfktvpssetiylfkvisemglnvdiislkngvytksfdevdvndyd
rlivvnssinffggkpnlailsaqkfmakykskiyylftdirlpfsqswpnvknrpwayl
yteeellikspikvisqginldiakaahkkvdnviefeyfpieqykihmndfqlskptkk
tldviyggsfrsgqreskmveflfdtglnieffgnarekqfknpkypwtkapvftgkipm
nmvseknsqaiaaliigdknyndnfitlrvwetmasdavmlideefdtkhriindarfyv
nnraelidrvnelkhsdvlrkemlsiqhdilnktrakkaewqdafkkaidl
>d1bgva1 3.2.1.7.1 (195-449) Glutamate dehydrogenase {Clostridium symbiosum}
karsfggslvrpeatgygsvyyveavmkhendtlvgktvalagfgnvawgaakklaelga
kavtlsgpdgyiydpegitteekinymlemrasgrnkvqdyadkfgvqffpgekpwgqkv
diimpcatqndvdleqakkivannvkyyievanmpttnealrflmqqpnmvvapskavna
ggvlvsgfemsqnserlswtaeevdsklhqvmtdihdgsaaaaeryglgynlvaganivg
fqkiadammaqgiaw
>d1bgva2 3.48.1.1.1 (1-194) Glutamate dehydrogenase {Clostridium symbiosum}
skyvdrviaevekkyadepefvqtveevlsslgpvvdahpeyeevallermvipervief
rvpweddngkvhvntgyrvqfngaigpykgglrfapsvnlsimkflgfeqafkdslttlp
mggakggsdfdpngksdrevmrfcqafmtelyrhigpdidvpagdlgvgareigymygqy
rkivggfyngvltg
>d1bgw__ 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
ketelenllklsakdiwntdlkafevgyqeflqrdaear
>d1bgxh1 2.1.1.1.105 (5-115) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
qesgpglvkpyqslslsctvtgysitsdyawnwirqfpgnklewmgyitysgttdynpsl
ksrisitrdtsknqfflqlnsvttedtatyycaryyygywyfdvwgqgttltvss
>d1bgxh2 2.1.1.2.106 (116-209) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
akttapsvyplapvssvtlgclvkgyfpepvtltwnsgslssgvhtfpavlqsdlytlss
svtvtsstwpsqsitcnvahpasstkvdkkiepr
>d1bgxl1 2.1.1.1.105 (1-107) Immunoglobulin (variable domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
diqmtqspaimsaspgekvtmtcsasssvsymywyqqkpgssprlliydstnlasgvpvr
fsgsgsgtsysltisrmeaedaatyycqqwstypltfgagtklelk
>d1bgxl2 2.1.1.2.106 (108-211) Immunoglobulin (constant domains of L and H chains) {Fab TP7 (mouse), kappa L chain}
radaaptvsifppsseqltsggasvvcflnnfypkdinvkwkidgserqngvlnswtdqd
skdstysmsstltltkdeyerhnsytceathktstspivksfnr
>d1bgxt1 1.61.3.1.2 (174-289) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
lrpdqwadyraltgdesdnlpgvkgigektarklleewgsleallknldrlkpairekil
ahmddlklswdlakvrtdlplevdfakrrepdrerlraflerlefgsllhefglle
>d1bgxt2 3.44.1.2.2 (1-173) 5' to 3' exonuclease domain of DNA polymerase <i>Taq</i> {Thermus aquaticus}
mrgmlplfepkgrvllvdghhlayrtfhalkglttsrgepvqavygfaksllkalkedgd
avivvfdakapsfrheayggykagraptpedfprqlalikelvdllglarlevpgyeadd
vlaslakkaekegyevriltadkdlyqllsdrihvlhpegylitpawlwekyg
>d1bgxt3 3.46.3.5.2 (290-450) Exonuclease domain of DNA polymerase {Thermus aquaticus}
spkaleeapwpppegafvgfvlsrkepmwadllalaaarggrvhrapepykalrdlkear
gllakdlsvlalreglglppgddpmllaylldpsnttpegvarryggewteeageraals
erlfanlwgrlegeerllwlyreverplsavlahmeatgvr
>d1bgxt4 5.8.1.1.2 (451-832) DNA polymerase I (Klenow fragment) {Thermus aquaticus}
ldvaylralslevaeeiarleaevfrlaghpfnlnsrdqlervlfdelglpaigktektg
krstsaavlealreahpivekilqyreltklkstyidplpdlihprtgrlhtrfnqtata
tgrlsssdpnlqnipvrtplgqrirrafiaeegwllvaldysqielrvlahlsgdenlir
vfqegrdihtetaswmfgvpreavdplmrraaktinfgvlygmsahrlsqelaipyeeaq
afieryfqsfpkvrawiektleegrrrgyvetlfgrrryvpdlearvksvreaaermafn
mpvqgtaadlmklamvklfprleemgarmllqvhdelvleapkeraeavarlakevmegv
yplavplevevgigedwlsake
>d1bgya_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1bgyb_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1bgyc1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1bgyd1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1bgye1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvlamskie
>d1bgyf1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1bgyg1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyh1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyj1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyk1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bgym_ 4.106.1.1.1 Core 1 subunit {Bovine (Bos taurus)}
tatyaqalqsvpetqvsqldnglrvaseqssqptctvgvwidagsryeseknngagyfve
hlafkgtknrpgnalekevesmgahlnaystrehtayyikalskdlpkavelladivqnc
sledsqiekerdvilqelqendtsmrdvvfnylhatafqgtplaqsvegpsenvrklsra
dlteylsrhykaprmvlaaagglehrqlldlaqkhfsglsgtydedavptlspcrftgsq
ichredglplahvaiavegpgwahpdnvalqvanaiighydctygggahlssplasiaat
nklcqsfqtfnicyadtgllgahfvcdhmsiddmmfvlqgqwmrlctsatesevlrgknl
lrnalvshldgttpvcedigrslltygrriplaewesriaevdarvvrevcskyfydqcp
avagfgpieqlpdynrirsgmfwlrf
>d1bgyn_ 4.106.1.1.3 Core 2 subunit {Bovine (Bos taurus)}
pqdleftrlpnglviaslenyapasriglfikagsryensnnlgtshllrlasslttkga
ssfkitrgieavggklsvtstrenmaytveclrddvdilmefllnvttapefrrwevaal
qpqlridkavalqnpqahvienlhaaayrnalanslycpdyrigkvtpvelhdyvqnhft
sarmaliglgvshpvlkqvaeqflnirgglglsgakakyhggeireqngdslvhaalvae
saaigsaeanafsvlqhvlgagphvkrgsnatsslyqavakgvhqpfdvsafnasysdsg
lfgfytisqaasagdvikaaynqvktiaqgnlsnpdvqaaknklkagylmsvessegfld
evgsqalaagsytppstvlqqidavadadvinaakkfvsgrksmaasgnlghtpfidel
>d1bgyo1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
mtnirkshplmkivnnafidlpapsnisswwnfgsllgiclilqiltglflamhytsdtt
tafssvthicrdvnygwiirymhangasmfficlymhvgrglyygsytfletwnigvill
ltvmatafmgyvlpwgqmsfwgatvitnllsaipyigtnlvewiwggfsvdkatltrffa
fhfilpfiimaiamvhllflhetgsnnptgissdvdkipfhpyytikdilgalllilalm
llvlfapdllgdpdnytpanplntpphikpewyflfayailrsipnklggvlalafsili
lalipllhtskqrsmmfrplsqclfwalvadlltltwiggqpvehpyitigqlasvlyfl
lilvlmptagtienkllkw
>d1bgyp1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
sdlelhppsypwshrgllssldhtsirrgfqvykqvcsschsmdyvayrhlvgvcytede
akalaeevevqdgpnedgemfmrpgklsdyfpkpypnpeaaraanngalppdlsyivrar
hggedyvfslltgycepptgvslreglyfnpyfpgqaigmappiynevlefddgtpatms
qvakdvctflrwaaepehdhrkrmglkmllmmglllplvyamkrhkwsvlksrklayrpp
k
>d1bgyq1 2.29.1.1.1 (70-196) ISP subunit of the mitochondrial cytochrome bc1-complex {Bovine (Bos taurus)}
amskieiklsdipegknmafkwrgkplfvrhrtkkeidqeaavevsqlrdpqhdlervkk
pewviligvcthlgcvpianagdfggyycpchgshydasgrirkgpaplnlevpsyefts
ddmvivg
>d1bgyq2 6.2.1.1.9 (1-69) Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
shtdikvpdfsdyrrpevldstksskessearkgfsylvtatttvgvayaaknvvsqfvs
smsasadvl
>d1bgyr1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
avsassrwlegirkwyynaagfnklglmrddtihenddvkeairrlpenlyddrvfrikr
aldlsmrqqilpkeqwtkyeedksylepylkevirerkereewakk
>d1bgys1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
grqfghltrvrhvityslspfeqrafphyfskgipnvlrrtracilrvappfvafylvyt
wgtqefekskrknpaayendr
>d1bgyt1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
dplttvreqceqlekcvkarerlelcdervssrsqteedcteelldflhardhcvahklf
nslk
>d1bgyv1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
vaptltarlysllfrrtstfaltivvgalfferafdqgadaiyehinegklwkhikhkye
nk
>d1bgyw1 6.2.1.1.9 Cytochrome bc1 transmembrane subunits {Bovine (Bos taurus)}
rnwvptaqlwgavgavglvsat
>d1bh2_1 1.67.1.1.2 (61-181) Transducin (alpha subunit), insertion domain {Rat (Rattus rattus)}
yseeeckqykavvysntiqsiiaiiramgrlkidfgdaaraddarqlfvlagaaeegfmt
aelagvikrlwkdsgvqacfnrsreyqlndsaayylndldriaqpnyiptqqdvlrtrvk
t
>d1bh2_2 3.30.1.6.13 (32-60,182-346) Transducin (alpha subunit) {Rat (Rattus rattus)}
revkllllgagesgkstivkqmkiiheagXtgivethftfkdlhfkmfdvggqrserkkw
ihcfegvtaiifcvalsdydlvlaedeemnrmhesmklfdsicnnkwftdtsiilflnkk
dlfeekikksplticypeyagsntyeeaaayiqcqfedlnkrkdtkeiythftcstdtkn
vqfvfdavtdviikn
>d1bh3__ 6.4.3.1.3 Porin {Rhodopseudomonas blastica, strain DSM2131}
mislngygrfglqyvedrgvgledtiissrlrinivgttetdqgvtfgaklrmqwddgda
fagtagnaaqfwtsyngvtvsvgnvdtafdsvaltydsemgyeassfgdaqssffkynsk
ydasgaldnyngiavtysisgvnlylsyvdpdqtvdsslvteefgiaadwsndmislaaa
yttdaggivdndiafvgaaykfndagtvglnwydnglstagdqvtlygnyafgattvray
vsdidragadtaygigadyqfaegvkvsgsvqsgfanetvadvgvrfdf
>d1bh4__ 7.3.5.1.1 Circulin A {Chassalia parviflora}
cgescvwipcisaalgcscknkvcyrngip
>d1bh5a_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
sggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcdfpimk
fslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfgh
igiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmatlm
>d1bh5b_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
epqppsggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcd
fpimkfslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdp
rgfghigiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmat
lm
>d1bh5c_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
sggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcdfpimk
fslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdprgfgh
igiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmatlm
>d1bh5d_ 4.27.1.1.1 Glyoxalase I {Human (Homo sapiens)}
epqppsggltdeaalsccsdadpstkdfllqetmlrvkdpkksldfytrvlgmtliqkcd
fpimkfslyflayedkndipkekdekiawalsrkatlelthnwgteddetqsyhngnsdp
rgfghigiavpdvysackrfeelgvkfvkkpddgkmkglafiqdpdgywiqilnpnkmat
lm
>d1bh6a_ 3.33.1.1.2 Subtilisin Carlsberg {Bacillus licheniformis}
aqtvpygiplikadkvqaqgykganvkvgiidtgiasshtdlkvvggasfvsgesyntdg
nghgthvagtvaaldnttgvlgvapnvslyaikvlnssgsgsysaivsgiewatqngldv
inmslggpsgstalkqavdkayasgivvvaaagnsgnsgsqntigypakydsviavgavd
snknrasfssvgselevmapgvsvystypsntytslngtsmasphvagaaalilskyptl
sasqvrnrlsstatnlgdsfyygkglinveaaaq
>d1bh8a_ 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
>d1bh9a_ 1.23.1.3.3 TAF(II)18 {Human (Homo sapiens)}
lfskelrcmmygfgddqnpytesvdiledlviefitemthkamsi
>d1bh9b_ 1.23.1.3.4 TAF(II)28 {Human (Homo sapiens)}
fseeqlnryemyrrsafpkaaikrliqsitgtsvsqnvviamsgiskvfvgevveealdv
cekwgempplqpkhmreavrrlkskgqip
>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
>d1bhda_ 1.43.1.1.3 Utrophin {Human (Homo sapiens)}
lqqtnsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkms
pierlehafskaqtylgieklldpedvavrlpdkksiimyltslfevl
>d1bhdb_ 1.43.1.1.3 Utrophin {Human (Homo sapiens)}
nsekillswvrqttrpysqvnvlnfttswtdglafnavlhrhkpdlfswdkvvkmspier
lehafskaqtylgieklldpedvavrlpdkksiimyltslfevlpqqv
>d1bhe__ 2.71.1.5.1 Polygalacturonase {Erwinia carotovora}
sdsrtvsepktpsscttlkadsstatstiqkalnncdqgkavrlsagstsvflsgplslp
sgvsllidkgvtlravnnaksfenapsscgvvdkngkgcdafitavsttnsgiygpgtid
gqggvklqdkkvswwelaadakvkklkqntprliqinksknftlynvslinspnfhvvfs
dgdgftawkttiktpstarntdgidpmssknitiaysniatgddnvaikaykgraetrni
silhndfgtghgmsigsetmgvynvtvddlkmngttnglriksdksaagvvngvrysnvv
mknvakpividtvyekkegsnvpdwsditfkdvtsetkgvvvlngenakkpievtmknvk
ltsdstwqiknvnvkk
>d1bhfa_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
lepepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhy
kirnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhga1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhga2 2.16.1.4.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhga3 3.1.7.3.13 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1bhgb1 2.1.4.1.2 (226-328) beta-Glucuronidase {Human (Homo sapiens)}
tyidditvttsveqdsglvnyqisvkgsnlfklevrlldaenkvvangtgtqgqlkvpgv
slwwpylmherpaylyslevqltaqtslgpvsdfytlpvgirt
>d1bhgb2 2.16.1.4.2 (22-225) beta-Glucuronidase {Human (Homo sapiens)}
glqggmlypqespsreckeldglwsfradfsdnrrrgfeeqwyrrplwesgptvdmpvps
sfndisqdwrlrhfvgwvwyerevilperwtqdlrtrvvlrigsahsyaivwvngvdtle
heggylpfeadisnlvqvgplpsrlritiainntltpttlppgtiqyltdtskypkgyfv
qntyfdffnyaglqrsvllyttpt
>d1bhgb3 3.1.7.3.13 (329-632) beta-Glucuronidase, domain 3 {Human (Homo sapiens)}
vavtksqflingkpfyfhgvnkhedadirgkgfdwpllvkdfnllrwlganafrtshypy
aeevmqmcdrygivvidecpgvglalpqffnnvslhhhmqvmeevvrrdknhpavvmwsv
anepashlesagyylkmviahtksldpsrpvtfvsnsnyaadkgapyvdviclnsyyswy
hdyghleliqlqlatqfenwykkyqkpiiqseygaetiagfhqdpplmfteeyqkslleq
yhlgldqkrrkyvvgeliwnfadfmteqsptrvlgnkkgiftrqrqpksaafllrerywk
iane
>d1bhha_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
epepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyk
irnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhhb_ 4.72.1.1.1 p56-lck tyrosine kinase {Human (Homo sapiens)}
pepwffknlsrkdaerqllapgnthgsfliresestagsfslsvrdfdqnqgevvkhyki
rnldnggfyispritfpglhelvrhytnasdglctrlsrpcqt
>d1bhi__ 7.31.1.1.11 Transactivation domain of cre-bp1/atf-2 {Human (Homo sapiens)}
msddkpflctapgcgqrftnedhlavhkhkhemtlkfg
>d1bhja_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1bhjb_ 3.56.1.2.1 Glycine <i>N</i>-methyltransferase {Rat (Rattus norvegicus)}
vdsvyrtrslgvaaegipdqyadgeaarvwqlyigdtrsrtaeykawllgllrqhgchrv
ldvacgtgvdsimlveegfsvtsvdasdkmlkyalkerwnrrkepafdkwvieeanwltl
dkdvpagdgfdaviclgnsfahlpdskgdqsehrlalkniasmvrpggllvidhrnydyi
lstgcappgkniyyksdltkdittsvltvnnkahmvtldytvqvpgagrdgapgfskfrl
syyphclasftelvqeafggrcqhsvlgdfkpyrpgqayvpcyfihvlkktg
>d1bhl__ 3.46.3.2.2 HIV-1 integrase, catalytic domain {Human immunodeficiency virus, type 1}
spgiwqldxthlegkvilvavhvasgyieaevipaetgqetayfllklagrwpvktvhtd
ngsnftsttvkaaxwwagikqefgipynpqsqgviesmnkelkkiigqvrdqaehlktav
qmavfihnhkrkggiggysagerivdiiatd
>d1bhma_ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgm
>d1bhmb_ 3.43.1.3.1 Restriction endonuclease BamHI {Bacillus amyloliquefaciens}
mevekefitdeakellskdkliqqaynevktsicspiwpatsktftinntekncngvvpi
kelcytlledtynwyrekpldilklekkkggpidvykefienselkrvgmefetgnissa
hrsmnklllglkhgeidlaiilmpikqlayyltdrvtnfeelepyfeltegqpfifigfn
aeaynsnvplipkgsdgmskrsikkwkd
>d1bhna_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnb_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnc_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnd_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhne_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bhnf_ 4.47.6.1.2 Nucleoside diphosphate kinases {Bovine (Bos taurus)}
ansertfiaikpdgvqrgligeiikrfeqkgfrlvamkfmrasedllkehyidlkdrpff
aglvkymhsgpvvamvweglnvvktgrvmlgetnpadskpgtirgdfciqvgrniihgsd
svesaekeialwfhpeelvnykscaqnwiye
>d1bho1_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bho2_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhp__ 7.13.1.1.2 beta-Purothionin {Wheat (Triticum aestivum)}
kscckstlgrncynlcrargaqklcanvcrckltsglscpkdfpk
>d1bhq1_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhq2_ 3.52.1.1.4 Integrin CR3 (CD11b/CD18, Mac-1), alpha subunit {Human (Homo sapiens)}
xsdiaflidgsgsiiphdfrrmkefvstvmeqlkksktlfslmqyseefrihftfkefqn
npnprslvkpitqllgrthtatgirkvvrelfnitngarknafkilvvitdgekfgdplg
yedvipeadregviryvigvgdafrseksrqelntiaskpprdhvfqvnnfealktiqnq
lrekifaieg
>d1bhs__ 3.2.1.2.8 Human estrogenic 17beta-hydroxysteroid dehydrogenase {Human (Homo sapiens)}
artvvlitgcssgiglhlavrlasdpsqsfkvyatlrdlktqgrlweaaralacppgsle
tlqldvrdsksvaaarervtegrvdvlvcnaglgllgplealgedavasvldvnvvgtvr
mlqaflpdmkrrgsgrvlvtgsvgglmglpfndvycaskfaleglceslavlllpfgvhl
sliecgpvhtafmekvlgspeevldrtdihtfhrfyqylahskqvfreaaqnpeevaevf
ltalrapkptlryftterflpllrmrlddpsgsnyvtamhrevf
>d1bhta1 7.10.1.1.1 (35-126) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rrntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkark
qclwfpfnsmssgvkkefghefdlyenkdyir
>d1bhta2 7.14.1.1.9 (127-210) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcseve
>d1bhtb1 7.10.1.1.1 (336-426) Hairpin loop containing domain of hepatocyte growth factor {Human (Homo sapiens)}
rntihefkksakttlikidpalkiktkkvntadqcanrctrnkglpftckafvfdkarkq
clwfpfnsmssgvkkefghefdlyenkdyir
>d1bhtb2 7.14.1.1.9 (427-509) NK1 fragment of hepatocyte growth factor {Human (Homo sapiens)}
nciigkgrsykgtvsitksgikcqpwssmiphehsflpssyrgkdlqenycrnprgeegg
pwcftsnpevryevcdipqcsev
>d1bhu__ 2.10.1.4.1 Streptomyces metalloproteinase inhibitor, SMPI {Streptomyces nigrescens}
apscpagslctysgtglsgartvipasdmekagtdgvklpasarsfangthftlrygpar
kvtcvrfpcyqyatvgkvapgaqlrslpspgatvtvgqdlgd
>d1bhwa_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwb_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwc_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>d1bhwd_ 3.1.13.2.6 D-xylose isomerase {Actinoplanes missouriensis}
vqatredkfsfglwtvgwqardafgdatrtaldpveavhklaeigaygitfhdddlvpfg
sdaqtrdgiiagfkkaldetglivpmvttnlfthpvfkdggftsndrsvrryairkvlrq
mdlgaelgaktlvlwggregaeydsakdvsaaldryrealnllaqysedrgyglrfaiep
kpneprgdillptaghaiafvqelerpelfginpetgneqmsnlnftqgiaqalwhkklf
hidlngqhgpkfdqdlvfghgdllnafslvdllengpdgapaydgprhfdykpsrtedyd
gvwesakanirmylllkerakafradpevqealaaskvaelktptlnpgegyaelladrs
afedydadavgakgfgfvklnqlaiehllgar
>e1bhx.1a 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
sgeadcglrplfekksledkterellesyi
>e1bhx.1b 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
ivegsdaeigmspwqvmlfrkspqellcgaslisdrwvltaahcllyppwdknftendll
vrigkhsrtryerniekismlekiyihprynwrenldrdialmklkkpvafsdyihpvcl
pdretaasllqagykgrvtgwgnlket
>e1bhx.1f 2.41.1.2.11 Thrombin {Human (Homo sapiens)}
gqpsvlqvvnlpiverpvckdstriritdnmfcagykpdegkrgdacegdsggpfvmksp
fnnrwyqmgivswgegcdrdgkygfythvfrlkkwiqkvidqfge
>d1bhy_1 3.3.1.5.10 (117-275,401-470) Dihydrolipoamide dehydrogenase {Neisseria meningitidis}
gsadaeydvvvlgggpggysaafaaadeglkvaiveryktlggvclnvgcipskallhna
avidevrhlaangikypepeldidmlraykdgvvsrltgglagmaksrkvdviqgdgqfl
dphh