Class d: Alpha and beta proteins (a+b) [53931] (224 folds) |
Fold d.58: Ferredoxin-like [54861] (44 superfamilies) alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
d.58.1: 4Fe-4S ferredoxins [54862] (5 families) |
d.58.2: Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain [54893] (1 family) |
d.58.3: Protease propeptides/inhibitors [54897] (3 families) |
d.58.4: Dimeric alpha+beta barrel [54909] (3 families) dimerises through the beta-sheet; forms beta-sheet barrel, closed (n=8, S=12); dimers may assemble in higher oligomers |
d.58.5: GlnB-like [54913] (2 families) form timeric structures with the orthogonally packed beta-sheets |
d.58.6: Nucleoside diphosphate kinases [54919] (1 family) |
d.58.7: RNA-binding domain, RBD [54928] (3 families) |
d.58.8: Viral DNA-binding domain [54957] (1 family) |
d.58.9: RuBisCO, large subunit, small (N-terminal) domain [54966] (1 family) C-terminal domain is beta/alpha barrel |
d.58.10: Acylphosphatase-like [54975] (1 family) |
d.58.11: EF-G/eEF-2 domains III and V [54980] (1 family) |
d.58.12: eEF-1beta-like [54984] (1 family) |
d.58.13: Anticodon-binding domain of PheRS [54991] (1 family) |
d.58.14: Ribosomal protein S6 [54995] (1 family) |
d.58.15: Ribosomal protein S10 [54999] (1 family) |
d.58.16: Poly(A) polymerase, C-terminal domain [55003] (1 family) |
d.58.17: Metal-binding domain [55008] (1 family) |
d.58.18: Regulatory domain in the aminoacid metabolism [55021] (3 families) |
d.58.19: Bacterial exopeptidase dimerisation domain [55031] (1 family) |
d.58.20: NAD-binding domain of HMG-CoA reductase [55035] (1 family) |
d.58.21: Molybdenum cofactor biosynthesis protein C, MoaC [55040] (1 family) |
d.58.22: TRADD, N-terminal domain [55044] (1 family) |
d.58.23: Probable ACP-binding domain of malonyl-CoA ACP transacylase [55048] (1 family) |
d.58.24: CheY-binding domain of CheA [55052] (1 family) |
d.58.25: Killer toxin KP6 alpha-subunit [55056] (1 family) |
d.58.26: GHMP Kinase [55060] (4 families) common fold is elaborated with additional secondary structures |
d.58.27: Translational regulator protein regA [55064] (1 family) common fold is elaborated with additional secondary structures |
d.58.28: Peptide methionine sulfoxide reductase [55068] (1 family) common fold is elaborated with additional secondary structures |
d.58.29: Adenylyl and guanylyl cyclase catalytic domain [55073] (1 family) common fold is elaborated with additional secondary structures |
d.58.30: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK [55083] (1 family) common fold is elaborated with additional secondary structures |
d.58.31: Methyl-coenzyme M reductase subunits [55088] (2 families) each of the three different subunits, alpha, beta and gamma, contains this fold decorated with additional secondary structures |
d.58.32: FAD-linked oxidases, C-terminal domain [55103] (3 families) duplication: contains two subdomains of this fold |
d.58.33: Formylmethanofuran:tetrahydromethanopterin formyltransferase [55112] (1 family) duplication: contains two subdomains of this fold |
d.58.34: Formiminotransferase domain of formiminotransferase-cyclodeaminase. [55116] (1 family) duplication: contains two subdomains of this fold |
d.58.35: Pseudouridine synthase [55120] (3 families) duplication: contains two subdomains of this fold |
d.58.36: Sulfite reductase, domains 1 and 3 [55124] (1 family) duplication: contains two subdomains of this fold |
d.58.38: Urease metallochaperone UreE, C-terminal domain [69737] (1 family) |
d.58.39: Glutamyl tRNA-reductase catalytic, N-terminal domain [69742] (1 family) common fold is elaborated with additional secondary structures |
d.58.40: D-ribose-5-phosphate isomerase (RpiA), lid domain [75445] (1 family) |
d.58.41: SEA domain [82671] (1 family) |
d.58.42: N-utilization substance G protein NusG, N-terminal domain [82679] (1 family) |
d.58.43: Mechanosensitive channel protein MscS (YggB), C-terminal domain [82689] (1 family) the last strand of the fold is flipped away and involved in oligomerisation |
d.58.44: Multidrug efflux transporter AcrB pore domain; PN1, PN2, PC1 and PC2 subdomains [82693] (1 family) duplication: the N- and C-terminal halves of the whole proteins are structurally similar; each half contains two domains of this fold |
d.58.45: PurS subunit of FGAM synthetase [82697] (1 family) segment-swapped dimer: the swapped segment is made of the first helix and second strand; a single long strand is formed by strands 2 and 3 of each subunit |
Timeline for Fold d.58: Ferredoxin-like: