TIM beta/alpha-barrel [51350] (33)
contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites
Amylase, catalytic domain [51446] (54) members of the family may contain various insert subdomains in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain
beta-glycanases [51487] (54) consist of a number of sequence families
Putative alpha-L-fucosidase, catalytic domain [102079] (1) glycosyl hydrolase family 29; contains additional beta-barrel with a topological similarity to the C-terminal domain of alpha amylases
1,4-beta-N-acetylmuraminidase [63912] (3) Glycosyl hydrolase family 25; probably have evolved from a type II chitinase ancestor permutation of the common fold; strand 8 is antiparallel to the rest of the barrel
Metallo-dependent hydrolases [51556] (18)
the beta-sheet barrel is similarly distorted and capped by a C-terminal helix has transition metal ions bound inside the barrel uperfamily
Aldolase [51569] (8)
Common fold covers whole protein structure uperfamily
Class I aldolase [51570] (37) the catalytic lysine forms schiff-base intermediate with substrate possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels
Enolase C-terminal domain-like [51604] (2)
binds metal ion (magnesium or manganese) in conserved site inside barrel N-terminal alpha+beta domain is common to this superfamily uperfamily
Mll9387-like [159416] (1) Pfam 09370; TIM-barrel signal transduction protein; forms a swapped dimer similar to the Phosphoenolpyruvate mutase/Isocitrate lyase-like and HpcH/HpaI aldolase families
FAD-linked oxidoreductase [51730] (2)
distinct cofactor-binding mode from both FMN- and NAD(P)-linked TIM-barrel oxidoreductases; families are related by a circular permutation uperfamily
NAD(P)-binding Rossmann-fold domains [51734] (1)
core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456 The nucleotide-binding modes of this and the next two folds/superfamilies are similar
Tyrosine-dependent oxidoreductases [51751] (108) also known as short-chain dehydrogenases and SDR family parallel beta-sheet is extended by 7th strand, order 3214567; left-handed crossover connection between strands 6 and 7
Aminoacid dehydrogenase-like, C-terminal domain [51883] (24) extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site
Ornithine cyclodeaminase-like [110436] (2) Pfam 02423; contains additional alpha+beta dimerisation subdomain mostly formed by the N-terminal meander beta-sheet
FAD/NAD(P)-binding domain [51904] (1)
core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
Nucleotide-binding domain [51970] (1)
3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like
Nucleotide-binding domain [51971] (3)
this superfamily shares the common nucleotide-binding site with and provides a link between the Rossmann-fold NAD(P)-binding and FAD/NAD(P)-binding domains uperfamily
D-aminoacid oxidase, N-terminal domain [51979] (2) This family is probably related to the FAD-linked reductases and shares with them the C-terminal domain fold
7-stranded beta/alpha barrel [51988] (3)
variant of beta/alpha barrel; parallel beta-sheet barrel, closed, n=7, S=8; strand order 1234567; some members may have fewer strands
PHP domain [89551] (2) putative phosphoesterase domain; contains trinuclear metal-binding site; some similarity to the metallohydrolases of TIM-barrel fold
PA1517-like [141965] (1) seven-stranded barrel with a detectable sequence similarity to the six-stranded barrel NodB-like family; member of the same Pfam family (Pfam 01522)
The "swivelling" beta/beta/alpha domain [52008] (10)
3 layers: b/b/a; the central sheet is parallel, and the other one is antiparallel; there are some variations in topology this domain is thought to be mobile in most multi-domain proteins known to contain it
AF0055-like [141979] (1) PF01989; DUF126; probable link between the LeuD-like and Phosphohistidine domain superfamilies (sequence similarity crosshits)
Ribosomal protein L32e [52043] (1) contains irregular N-terminal extension to the common fold
MurF and HprK N-domain-like [63417] (2)
core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1234; structural similarity of the MurF and HprK extends beyond the core.
Malic enzyme N-domain [53240] (4) Pfam 00390; decorated with additional structures; includes N-terminal additional subdomains and extra N-terminal strand
Toprim domain [110454] (1)
3 layers, a/b/a; parallel beta-sheet of 4 strands, order 2134
Putative acetylxylan esterase-like [142058] (2) Pfam 03629 (DUF303); contains a characteristic zinc(less) finger-like insertion after strand 1; lacks the conserved in other families Asn residue
N-(deoxy)ribosyltransferase-like [52309] (3)
there are similar active site architectures as well as the catalytic mechanisms of functionally characterised members uperfamily
Class I glutamine amidotransferase-like [52317] (9)
conserved positions of the oxyanion hole and catalytic nucleophile; different constituent families contain different additional structures uperfamily
A4 beta-galactosidase middle domain [82351] (1) probable non-catalytic branch of the class I GAT family; overall fold is very similar but the active site is not conserved
DJ-1/PfpI [52325] (9) contains a catalytic triad or dyad different from the class I GAT triad
Adenine nucleotide alpha hydrolases-like [52402] (6)
share similar mode of ligand (Adenosine group) binding can be subdivided into two group with closer relationships within each group than between the groups; the first three families form one group whereas the last two families form the other group uperfamily
5' to 3' exonuclease catalytic domain [53045] (8) contains an alpha-helical arch and additional strand 6 antiparallel to the rest; strand order 321456; similarity to the resolvase-like fold
Ribose/Galactose isomerase RpiB/AlsB [89622] (1)
3 layers: a/b/a, core: parallel beta-sheet of 5 strands, order 21354; topological similarity to a part of the arginase/deacetylase fold
PMT domain-like [159505] (1) This is the second from the PMT C-terminus; it retains the superfamily fold and the active site mainchain conformation but lacks the conserved in the other two families His and Glu residues
EreA-like [159508] (2) Pfam 05139; Erythromycin esterase-like; the superfamily core is decorated with insertion of a four-helical bundle and a C-terminal alpha+beta extension
alpha/beta knot [75216] (1)
core: 3 layers: a/b/a, parallel beta-sheet of 5 strands, order 21435; contains a deep trefoil knot
alpha/beta knot [75217] (8)
known or predicted SAM-dependent methytransferases including the SPOUT 'sequence' superfamily all known members have dimeric structures uperfamily
tRNA(m1G37)-methyltransferase TrmD [89629] (3) fold and dimerisation mode are similar to those of the YbeA-like family; contains additional C-terminal all-alpha subdomain
Dipeptide transport protein [63991] (1)
3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; also contains a C-terminal alpha+beta subdomain
Predicted hydrolases Cof [82388] (13) contains an alpha+beta subdomain inserted into a new site after strand 3
NagD-like [102317] (6) duplication: consists of two segment-swapped domains of this fold; this results in the insertion of a circularly permuted domain after strand 3, analogously to the Cof family
5' nucleotidase-like [142191] (1) Pfam 05761; the insertion domain cosists of 3-helical bundle and a pseudo beta-barrel; contains extra C-terminal long alpha hairpin subdomain (scop_cf 46556)
AF1437-like [159537] (1) the insertion subdomain is a rudiment 4-helical bundle; extra alpha-hairpin insertion after strand 3
NagB-like [52513] (3) share a common phosphate-binding site with the RpiA family
D-ribose-5-phosphate isomerase (RpiA), catalytic domain [75176] (4) share a common phosphate-binding site with the NagB-like family; part of sheet is folded upon itself and forms a barrel-like structure like the CoA transferase subunits
CoA transferase beta subunit-like [74657] (3) catalytic subunit: similar active site structure to the NagB and RpiA families; mixed beta-sheet of 7 strands, order 4321567; strand 3 is antiparallel to the rest
Thiamin diphosphate-binding fold (THDP-binding) [52518] (8)
there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules uperfamily
TK-like Pyr module [88735] (5) different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain
Branched-chain alpha-keto acid dehydrogenase Pyr module [88741] (6) parent family to TK and PFOR heterodimeric protein related to TK; alpha-subunit is the PP module and the N-terminal domain of beta-subunit is the Pyr module
PFOR Pyr module [88746] (1) domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
Pyruvate oxidase and decarboxylase PP module [88749] (12) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology
TK-like PP module [88760] (5) different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain
Branched-chain alpha-keto acid dehydrogenase PP module [88766] (5) parent family to TK and PFOR heterodimeric protein related to TK; alpha-subunit is the PP module and the N-terminal domain of beta-subunit is the Pyr module
PFOR PP module [88771] (1) domains VI, I and II are arranged in the same way as the TK PP, Pyr and C domains
RecA protein-like (ATPase-domain) [52670] (29) core: mixed beta-sheet of 8 strands, order 32451678; strand 7 is antiparallel to the rest
Bacterial cell division inhibitor SulA [89678] (1) homologous to RecA but lacks its P-loop motif; the fold is C-terminally truncated; 5-stranded parallel beta-sheet, order: 15423
ABC transporter ATPase domain-like [52686] (29) there are two additional subdomains inserted into the central core that has a RecA-like topology
Extended AAA-ATPase domain [81269] (34) fold is similar to that of RecA, but lacks the last two strands, followed by a family-specific Arg-finger domain
RNA helicase [52724] (3) duplication: consists of two similar domains, one binds NTP and the other binds RNA; also contains an all-alpha subdomain in the C-terminal extension
DNA helicase UvsW [102396] (1) contains extra N-terminal alpha+beta subdomain
YjeE-like [75213] (1) mixed beta-sheet; order 234156(0), strands 2 and 6 are antiparallel to the rest
Type II thymidine kinase [117558] (3) N-terminal part of Pfam 00265; parallel beta-sheet of 6 strands, order 324516; topological similarity to the RecA-like proteins, especially CobA (scop_pr 52684)
Atu3015-like [142332] (2) unknown function; similar to the nucleotide/nucleoside kinases
PTS IIb component [52727] (1)
3 layers: a/b/a, parallel beta-sheet of 6 strands, order 324156
YpsA-like [159579] (1) Pfam 06908; DUF1273; lacking the last strand 7; different set of conserved residues in the putative active site than in the MoCo carrier protein-like family
CoA-dependent acyltransferases [52776] (1)
core: 2 layers, a/b; mixed beta-sheet of 6 strands, order 324561; strands 3 & 6 are antiparallel to the rest
Rhodanese/Cell cycle control phosphatase [52821] (4)
Pfam 00581 the active site structure is similar to those of the families I and II protein phosphatases; the topology can be related by a different circular permutation to the family I topology uperfamily
Atu2684-like [142398] (1) Pfam 06764; DUF1223; contains extra C-terminal domain of Immunoglobulin-like fold (scop_cf 48725), intimately associated with the N-terminal thioredixin-like domain and contributing to the active site
HyaE-like [142401] (2) Pfam 07449; have evolved a different function; contains no conserved cysteine residues
NQO2-like [142405] (1) complex I 24 kDa subunit; contains 2Fe-2S cluster in the active site; includes extra N-terminal four-helical bundle
MTH1675-like [110616] (2) PfamB 019040; probable flavoenzyme, binds FMN; the phosphoribityl group binds in the equivalent site to the binding site of the PK allosteric regulator FBP
Brix domain [142420] (2) Pfam 04427; tandem repeat of two ABD-like structural repeats, which are associated together with the formation of single beta-sheet, folded into half-barrel
XCC0632-like [159594] (2)
short crossover loop between strands 2 and 3; the antiparallel part of the beta-sheet (strands 3, 4 and 5) and the C-terminal helix are quite long
Restriction endonuclease-like [52979] (4)
core: 3 layers, a/b/a; mixed beta-sheet of 5 strands, order 12345; strands 2 &, in some families, 5 are antiparallel to the rest
Hypothetical protein VC1899 [117625] (1) contains 2 extra N-terminal domains; d1: [alpha/beta; 3 layers: a/b/a; mixed beta-sheet of 7 strands, order 3214567; strand 6 is antiparallel to the rest; topological similarity to the Formyltransferase fold (scop_cf 53327)]; d2: [distorted "winged helix" fold (scop_sf 46785)]
PA4535-like [142449] (1) contains the PD motif at the beginning of strand 2 and putative catalytic glutamate in strand 3, whereas the putative catalytic lysine is migrated to an alpha-helix
YaeQ-like [159605] (2) Pfam 07152; contains extra N- and C-terminal beta-structures forming additional five-stranded beta-sheet; retains the PD motif in the putative active site
YeaZ-like [110633] (2) Pfam 00814; ubiquitous cytoplasmic protein; annotated as Glycoprotease (Peptidase_M22 family) on the basis of one member's known extracellular activity
Phosphorylase/hydrolase-like [53162] (8)
core: 3 layers, a/b/a ; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops
HybD-like [53163] (2)
the HybD fold coincides with the consensus core structure uperfamily
Germination protease [64095] (1) elaborated with the N-terminal alpha+beta subdomain and the insertion all-alpha dimerisation subdomain
Purine and uridine phosphorylases [53167] (1)
complex architecture; contains mixed beta-sheet of 8 strands, order 23415867, strands 3, 6 & 7 are antiparallel to the rest; and barrel, closed; n=5, S=8 uperfamily
Molybdenum cofactor biosynthesis proteins [53217] (1)
3 layers: a/b/a; mixed beta-sheet of 5 strands; order: 21354, strand 5 is antiparallel to the rest; permutation of the Phosphorylase/hydrolase-like fold
CobE/GbiG C-terminal domain-like [159663] (1)
3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32154; strand 5 is antiparallel to the rest
CobE/GbiG C-terminal domain-like [159664] (1)
probably involved in deacylation steps in both anaerobic and aerobic pathways of cobalamin biosynthesis
CobE/GbiG C-terminal domain-like [159665] (3) C-terminal part of Pfam 01890 (CbiG); corresponds to standalone protein CobE in the aerobic pathway; also includes resent structure 3BY5
CbiG N-terminal domain-like [159671] (1)
3 layers: a/b/a; mixed beta-sheet of 6 strands, order 213456, strand 5 is antiparallel to the rest
CbiG N-terminal domain-like [159672] (1)
probable biological unit is a homodimer; putative active site is formed by residues from both subunits
CbiG N-terminal domain-like [159673] (1) N-terminal part of Pfam 01890; also includes variable linker domain to CobE-like C-terminal domain; the linker domain may be in a rudimentary form or missing
Bacterial fluorinating enzyme, N-terminal domain [102521] (1)
3 layers: a/b/a; mixed beta-sheet of 6 strands; order: 213546, strand 5 is antiparallel to the rest; topological similarity to the MogA-like family fold
FabD-like [52152] (2) the superfamily common core covers almost all of the family fold
Lysophospholipase [53645] (1) common core is decorated with many additional structures; mixed beta-sheet of 9 strands, order 654321798; strands 4, 6 and 8 are antiparallel to the rest
Patatin [89729] (1) plant proteins; structurally and functionally related to animal cytosolic phospholipase A2
L-sulfolactate dehydrogenase-like [89732] (1)
core: 3 layers, a/b/a; mixed sheet of 7 strands, order 1237456; strands 1, 6 and 7 are antiparallel to the rest
CAC2371-like [117688] (3) similar overall fold to the Glycine N-methyltransferase (scop_fa 53348) and mRNA cap (Guanine N-7) methyltransferase (scop_fa 102560) families
N-6 DNA Methylase-like [142606] (3) Pfam 02384; contains C-terminal extension to the canonical fold and extra N-terminal all-alpha domain similar to the insert domain of the DAM family (scop_fa 88788)
Nsp15 N-terminal domain-like [142625] (2) rudiment methyltransferase fold that probably has lost the enzymatic activity; contains extra N-terminal alpha+beta subdomain
BC2162-like [142629] (1) contains extra helical regions inserted after strands 5 and 6 of the canonical fold
CmcI-like [142632] (1) Pfam 04989; may have evolved different enzymatic activity
FkbM-like [159691] (1) contains extra N-terminal alpha/beta and all-alpha subdomains
ML2640-like [159694] (1) Pfam 02409; O-methyltransferase N-terminus (DUF142); most similar structure to the Leucine carboxy methyltransferase Ppm1 family
TRM1-like [159697] (1) Pfam 02005; contains extra C-terminal alpha+beta subdomain
LmbE-like [102587] (1)
3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest; topological similarity to SAM-dependent methyltransferases
PLP-dependent transferase-like [53382] (3)
main domain: 3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest
RibA-like [142694] (1)
3 layers: a/b/a; mixed beta-sheet of 7 strands, order 1235467, strands 1 and 3 are antiparallel to the rest; partial topological similarity to some alpha/beta hydrolases (scop_cf 53473)
Activating enzymes of the ubiquitin-like proteins [69572] (2)
transfer adenylyl group to the C-terminal carboxyl group of the ubiquitin and MoaD/ThiS-related proteins the ATP nucleotide-binding site is similar to that of the NAD-binding Rossmann-folds uperfamily
TTHA1544-like [159753] (1) minimal hydrolase fold (one strand less than the cutinase-like family); there is neither catalytic triad, nor nucleopilic residue in the elbow motif
Ribokinase-like [53612] (3)
core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest potential superfamily: members of this fold have similar functions but different ATP-binding sites
CoaB-like [102645] (1)
combination of the Rossmann-like and Ribokinase-like topologies; mixed beta-sheet of 8 strands, order 32145678, strand 7 is antiparallel to the rest uperfamily
YjeF N-terminal domain-like [64152] (1)
3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 32145678; strand 8 is antiparallel to the rest
Carbamate kinase-like [53632] (1)
3 layers: a/b/a; mixed (mainly parallel) beta-sheet of 8 strands, order 34215786; strand 8 is antiparallel to the rest
Carbamate kinase-like [53633] (3)
the sheet topology is similar to those of undecaprenyl diphosphate synthase and the N-terminal domain of phosphoglycerate kinase uperfamily
DeoB catalytic domain-like [142735] (1) Pfam 08342 in the N-terminal part; Pfam 01676 in the C-terminal part; there is an alpha+beta domain between the two parts, inserted in the same location as the substrate-binding domain of 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase
TTHA0583/YokD-like [110709] (1)
3 layers: a/b/a; mixed beta-sheet of 8 strands, order 78612354; strands 3, 4 and 8 are antiparallel to the rest
Glycerol-3-phosphate (1)-acyltransferase [69592] (1)
3 layers: a/b/a; mixed beta-sheet of 9 strands, order 918736452; strands 1, 2 and 8 are antiparallel to the rest
SurE-like [64166] (1)
3 layers: a/b/a; mixed beta-sheet of 9 strands, order 342156798; strands 3, 8 and 9 are antiparallel to the rest; left-handed crossover connection between strands 6 and 7
SurE-like [64167] (1)
some topological similarity to the N-terminal domain of Glutaminase/Asparaginase family uperfamily
YerB-like [159773] (1)
3 layers: b/b/a; central mixed beta-sheet of 9 strands, order 541329678; strands 3 and 7 are antiparallel to the rest; an unusual "over the other end" connection between strands 3 and 4
Isocitrate/Isopropylmalate dehydrogenase-like [53658] (1)
consists of two intertwined (sub)domains related by pseudo dyad; duplication 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213A945867 (A=10); strands from 5 to 9 are antiparallel to the rest
PdxA-like [102656] (2) Pfam 04166; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PlsX-like and phosphotransacetylase families
PlsX-like [102660] (2) Pfam 02504; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PdxA-like and phosphotransacetylase families
Phosphotransacetylase [102663] (4) Pfam 01515; contains extra beta-alpha unit between strands 2 and 3; closer relationships to the PdxA-like and PlsX-like families
Monomeric isocitrate dehydrogenase [82526] (1) the active site is contained within one subunit between the canonical ICDH fold and a large insert domain that itself is a probable rudiment form of ICDH fold resulted from duplication, domain swapping and deletion
Amidase signature (AS) enzymes [75303] (1)
possible duplication: the topologies of N- and C-terminal halves are similar; 3 layers: a/b/a; single mixed beta-sheet of 10 strands, order 213549A867 (A=10); strands from 5 to 9 are antiparallel to the rest
ATC-like [53670] (2)
consists of two similar domains related by pseudo dyad; duplication core: 3 layers, a/b/a, parallel beta-sheet of 4 strands, order 2134
Formate dehydrogenase/DMSO reductase, domains 1-3 [53705] (1)
contains of two similar intertwined domains related by pseudo dyad; duplication core: 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451
NadA-like [142753] (1)
duplication; consists of three similar domains related by pseudo threefold symmetry; 3 layers, a/b/a; parallel beta sheet, order: 2134
Aconitase iron-sulfur domain [53731] (1)
consists of three similar domains with 3 layers (a/b/a) each; duplication core: parallel beta-sheet of 5 strands, order 32145
Aconitase iron-sulfur domain [53733] (4) duplication: consists of three structurally similar subdomains with subdomains 1 and 3 being related by pseudo twofold symmetry
Phosphoglucomutase, first 3 domains [53737] (1)
consists of three similar domains with 3 layers (a/b/a) each; duplication core: mixed beta-sheet of 4 strands, order 2134, strand 4 is antiparallel to the rest
FucI/AraA N-terminal and middle domains [53742] (1)
consists of two domains of similar topology, 3 layers (a/b/a) each Domain 1 (1-173) has parallel beta-sheet of 5 strands, order 21345 Domain 2 (174-355) has parallel beta-sheet of 4 strands, order 2134
YgbK-like [142763] (1)
consists of two domains with partial topological similarity to the P-loop kinases but without the P-loop motif; the domain association results in the formation of a single mixed beta-sheet of 15 strands
YgbK-like [142765] (1) Pfam 07005; DUF1537; the B-fam model-covered region is non-compact in structure and distributed between the two domains
Phosphoglycerate kinase [53747] (1)
consists of two non-similar domains, 3 layers (a/b/a) each Domain 1 has parallel beta-sheet of 6 strands, order 342156 Domain 2 has parallel beta-sheet of 6 strands, order 321456
UDP-Glycosyltransferase/glycogen phosphorylase [53755] (1)
consists of two non-similar domains with 3 layers (a/b/a) each domain 1: parallel beta-sheet of 7 strands, order 3214567 domain 2: parallel beta-sheet of 6 strands, order 321456
Trehalose-6-phosphate synthase, OtsA [82540] (1) family 20 glycosyltransferase; good structural similarity in the active site to the Oligosaccharide phosphorylases
FucT-like [159794] (1) Pfam 00852; Glycosyltransferase family 10 (fucosyltransferase)
Glutaminase/Asparaginase [53773] (1)
consists of two non-similar alpha/beta domains, 3 layers (a/b/a) each Domain 1 has mixed beta-sheet of 6 strands, order 213456, strand 6 is antiparallel to the rest; left-handed crossover connection between strands 4 and 5 Domain 2 has parallel beta-sheet of 4 strands, order 1234
Phosphofructokinase [53783] (1)
consists of two non-similar domains, 3 layers (a/b/a) each Domain 1 has mixed sheet of 7 strands, order 3214567; strands 3 & 7 are antiparallel to the rest Domain 2 has parallel sheet of 4 strands, order 2314
Tetrapyrrole methylase [53789] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 5 strands, order 32415 Domain 2 has mixed sheet of 5 strands, order 12534; strands 4 & 5 are antiparallel to the rest
GckA/TtuD-like [82543] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 6 strands, order 321456, Rossmann-like topology Domain 2 has mixed sheet of 6 strands, order 126345; strands 5 and 6 are antiparallel to the rest; some similarity to CbiF Domain 2
DAK1/DegV-like [82548] (1)
2 different domains; d1: [core: 3 layers, a/b/a; parallel sheet of 5 strands, order: 2134]; D2: [2 layers, a/b; mixed sheet of 6 strands, order 321645; strands 2 and 6 are antiparallel to the rest]
DAK1/DegV-like [82549] (2)
domain folds and architecture show some similarity to the tubulin-like GTPases; the nucleotide-binding sites of the Dihydroxyacetone kinase and tubulin families are different uperfamily
DHH phosphoesterases [64181] (1)
consists of two non-similar domains Domain 1 has parallel sheet of 6 strands, order 321456 Domain 2 has mixed sheet of 5 strands, order 12345; strands 1 & 4 are antiparallel to the rest
DHH phosphoesterases [64182] (2)
constituent families have similar domain organization with variable interdomain linker and spatial arrangement of the domains uperfamily
Glycerate kinase I [110737] (1)
consists of two different alpha/beta domains; (1) of the Flavodoxin-like fold (scop_cf 52171); (2) similar to the Restriction endonuclease-like fold (scop_cf 52979), inserted into domain 1
PEP carboxykinase-like [53794] (1)
contains a P-loop NTP-binding motif; mixed beta-sheet folds into a barrel-like structure with helices packed on one side
Nitrogenase iron-molybdenum protein [53816] (6) contains three domains of this fold; "Helical backbone" holds domains 2 and 3 both chains are homologous; the inter-chain arrangement of domains 1 is similar to the intra-chain arrangement of domains 2 and 3
TM0189-like [142789] (3) Part of Pfam 01497 that include some other superfamily members
PrpR receptor domain-like [159801] (1) N-terminal domain corresponds to Pfam 06506; C-terminal domain, assigned to Pfam 00158, is distinct from other structures of this Pfam family
HemD-like [69617] (1)
duplication: consists of two similar 'swapped' domain with 3 layers (a/b/a) each; parallel beta-sheet of 5 strands, order 21345
CAC2185-like [142794] (1)
consists of two non-similar domains, 3 layers (a/b/a) each; d1 has parallel sheet of 4 strands, order 2134; d2 has parallel sheet of 5 strands, order 21345, and antiparallel meander sheet of 3 strands
Periplasmic binding protein-like I [53821] (1)
consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication parallel beta-sheet of 6 strands, order 213456
Periplasmic binding protein-like II [53849] (1)
consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest
Transferrin [53888] (11) further duplication: composed of two two-domain lobes
PG0945 N-terminal domain-like [159818] (1) truncated to one domain; extra C-terminal region provides dimerisation interface
Thiolase-like [53900] (1)
consists of two similar domains related by pseudo dyad; duplication 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32451; strand 5 is antiparallel to the rest
NIF3 (NGG1p interacting factor 3)-like [102704] (1)
consist of two intertwined domains; duplication: contains two structural repeats of alpha-beta-(beta-alpha)3 motif with mixed beta-sheet, order: 1432, strand 1 is antiparallel to the rest
ComB-like [142822] (1)
contains of two similar intertwined domains related by pseudo dyad; duplication; core: 3 layers: a/b/a; parallel beta-sheet of 4 strands, order 1423
CoA-transferase family III (CaiB/BaiF) [89795] (1)
consist of two different alpha/beta domains; N-terminal domain has a SurE-like topology with a left-handed beta-alpha-beta unit
Cytidine deaminase-like [53926] (2)
core: alpha-beta(2)-(alpha-beta)2; 3 layers (a/b/a); mixed beta-sheet of 4 strands, order 2134; strand 1 is antiparallel to the rest
FdhD/NarQ [159821] (1) Pfam 02634; contains extra N-terminal beta-hairpin arm, involved in dimerization, and an alpha+beta subdomain of beta-grasp fold (scop_cf 54235)