E-set domains of sugar-utilizing enzymes [81282] (30) domains of unknown function associated with different type of catalytic domains in a different sequential location subgroup of the larger IPT/TIG domain family
Other IPT/TIG domains [89191] (1) apart from the domains of transcription factors and sugar-utilizing enzymes
C-terminal domain of mollusc hemocyanin [81277] (1)
analogous to the Ig-like domain of arthropod hemocyanin; similar sequential but different spatial position relative the shared domain uperfamily
HPA-like [141085] (1)
sandwich, 6 strands in 2 sheets; jelly-roll (truncated); also includes the pending PCSK9 V domain-like superfamily (the C-terminal domains of 2p4e and 2pmw)
Agglutinin HPA-like [141086] (1)
forms similar trimers to the PCSK9 V domain; strand directions of the subunit beta-sheets are parallel to the three-fold symmetry axis; uperfamily
Atu1913-like [141098] (1)
sandwich; 7 strands in two sheets, greek-key/jelly-roll; forms segment swapped dimers, swapping is probably facilitated by the helix insertion after strand 3
Nucleoplasmin-like/VP (viral coat and capsid proteins) [88632] (7)
sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies
Picornaviridae-like VP (VP1, VP2, VP3 and VP4) [88634] (18) the order of the chains N-VP0-VP3-VP1-C is as in the polyprotein; VP0 is cleaved later upon capsid assembly to VP4 and VP2 there is a different order in the shuffled genome of insect picorna-like proteins (Cricket paralysis virus)
Comoviridae-like VP [88636] (3) duplication: mature coat protein consists of three similar domains that can be in a single chain or in two separate chains
Birnaviridae-like VP [141109] (1) dsRNA virus but unlike the other dsRNA viruses has a genomic arrangement and genomic replication strategy similar to +sRNA viruses; includes Pfam 01766; Birnavirus VP2 protein
Group II dsDNA viruses VP [49749] (3)
duplication: consists of two domains of this fold packed together like the nucleoplasmin subunits trimeric; in the trimers, the domains are arranged around pseudo six-fold axis uperfamily
PHM/PNGase F [49742] (2)
members of this superfamily bind peptide substrates duplication: consists of two domains of this fold packed together like the adjacent nucleoplasmin subunits uperfamily
EssC N-terminal domain-like [141143] (1) PfamB 051221 covers two consecutive domains; the first one is of canonical topology, whereas the second domain has a cirular permutation, beginnig at strand 2 and ending at strand 1 of the canonical fold
alpha-mannosidase, C-terminal domain [88656] (2) family 38 glycoside hydrolase; overall domain organization is similar to that of the 4-alpha-glucanotransferase family the supersandwich domain is elaborated with additional beta-strands and beta-sandwich subdomains
MdoG-like [110148] (1) Pfam 04349; Pfam coverage extends to the C-terminal immunoglobulin-like domain
Viral chemokine binding protein m3 [82045] (1)
consists of two different beta-sandwich domains of partial topological similarity to immunoglobulin-like folds
Flagellar hook protein flgE [117142] (1)
consists of two different domains; d1: [complex fold made of bifurcated beta-sheets]; d2 (inserted into d1): [beta-sandwich; 8 strands in 2 sheets]
ISP domain [50021] (1)
consists of two all-beta subdomains: conserved small domain has a rubredoxin-like fold; larger domain consists of 6 beta-stands packed in either sandwich of two 3-stranded sheets or closed barrel (n=6; S=8)
Trm112p-like [158997] (1)
possibly have evolved from a metal ion (or cofactor)-binding protein of a rubredoxin-like fold; in the known members, from one to three of the four metal-binding positions are occupied by cysteine residues
YopX-like [159005] (1)
consists of two domains: the N-terminal dimerisation domain of variable structure and the C-terminal domain with similarity to the SH3-like fold
YopX-like [159006] (1)
conmrises proteins of plasmid and phage origins
Obg-fold [82050] (1)
this fold is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together
Ply C-terminal domain-like [141198] (1) duplication: tandem repeat of two SH3-like domains swapped with the N-terminal strands; non-overlapping parts of sequence are covered by PfamB 062324 and PfamB 020199
Chromo domain [54165] (10) lacks the SH3-like barrel first strand that can be complemented by bound peptide ligand; in shadow chromo domain the corresponding site is altered by insertion; similarity to the IL8-like fold
Chromo barrel domain [117157] (3) typical SH3-like barrel fold; similar sequence motif to the canonical chromo domain
YgdI/YgdR-like [159052] (6) Pfam 06004; DUF903, putative lipoprotein; both homohexameric and homoheptameric ring assemblies are observed in the crystals
Dom34/Pelota N-terminal domain-like [159066] (2) Warning: Pfam incorrectly assigns this domain to the same family as the structurally unrelated N-terminal domain of eRF1 (Pfam 03463)
RNase P subunit p29-like [101745] (3) two available NMR structures display similar topologies but different barrel shapes the barrel shape of the full-length X-ray structures of AF1917 differs from both earlier NMR structures
NfeD domain-like [141322] (1)
close structural similarity to some members of the Nucleic acid-binding OB-fold proteins, possibly related to this superfamily uperfamily
Gar1-like SnoRNP [141341] (1) stand alone proteins, which are similar structurally but not sequentially to the elongation factor domains, unlike PF0907
UbiD middle domain-like [141368] (1) N terminal part of Pfam 01977; overall structural similarity to one subunit of the NADH:FMN oxidoreductase-like family (scop_fa 50482); not known to bind a flavin cofactor; also includes the N-terminal alpha+beta subdomain (~110 residues)
MTH863-like [159164] (3) Pfam 04289; DUF447; a new dimerisation mode involving (included) all-alpha subdomain of the spectrin-like fold (scop_cf 46965)
Baseplate protein-like [69280] (5) duplication: consists of two similar barrel domains that differ by the first strand directions; the barrels are differently decorated by alpha+beta insertions
gpFII-like [74966] (2) similar to the N-terminal barrel of T4 gp27
Surface presentation of antigens (SPOA) [101800] (1)
segment-swapped dimer forming two identical conjoint barrels (n=6, S=10) topologically similar to the FMN-binding split barrel
Pepsin-like [50646] (26) duplication: consists of two similar barrel domains N-terminal: barrel, partly opened; n*=6, S*=10
LPG0085-like [159190] (1) Pfam 05618; DUF785; single-domain protein similar to one pepsin domain with the conserved catalytic Asp motif (not in a few archaeal members of this Pfam family)
ValRS/IleRS/LeuRS editing domain [50676] (1)
core: barrel, closed; n=6, S=8; topology is similar to that of the acid proteases barrel
Fatty acid binding protein-like [50847] (28) ten-stranded meander beta-sheet folded upon itself relates to the common fold by opening the barrel and insertion of beta-hairpin
Thrombin inhibitor [50872] (1) topology permutation: strands 2 and 3 swapped their positions in the barrel
FomD barrel-like [159233] (1)
barrel, closed; n=8, S=12; meander; similar topology to the AOC barrel-like fold (reversed to the lipocalin barrel topology)
PH0987 C-terminal domain-like [159249] (1) lacks the N-terminal strand of cyclophilin but the beta-barrel (7,10) remains closed; corresponds to the C-terminal part of Pfam 02682; Allophanate hydrolase subunit 1 (AHS1)
triple barrel [50915] (1)
dimer of two non-identical subunits; forms two similar barrels, n=8, S=10 each, that are fused together with the formation of third barrel, n=6, S=8
Endo-alpha-sialidase [117276] (1) possibly related by the other family by circular permutation; includes extra N-terminal domain [dN: alpha/beta ] and insert domain [dI: beta-barrel, similar to the Reductase/isomerase/elongation factor common domain (scop_cf 50412)]
GyrA/ParC C-terminal domain-like [101904] (1)
beta-pinwheel, a variant of beta-propeller fold; unlike an canonical beta-propeller, strands 1 and 4 of each four-strand repeat unit are in one blade whereas strands 2 and 3 are in the next blade uperfamily
Kelch motif [117282] (2) Pfam 01344; sequence motif corresponding to one beta-sheet blade; similar sequences are found in the Galactose oxidase 7-bladed beta-propeller domain (scop_pr 50967)
Methylamine dehydrogenase, H-chain [50970] (2) less regular propeller without notable sequence repeats; quinone cofactor is a tryptophan derivative in another subunit
Cell cycle arrest protein BUB3 [110289] (1) possibly related to the WD-repeat family; both sequence similarity between the blades and the WD40 repeat signature are very weak
RCC1/BLIP-II [50985] (2)
two families are clearly related but differ by the number of strands per blade uperfamily
Tricorn protease domain 2 [69322] (1)
distorted 7-bladed beta-propeller fold; possibly related to the N-terminal domain of tricorn protease (a 6-bladed beta-propeller) uperfamily
LppX-like [141566] (1) Pfam 07161; DUF1396; contains a large cavity between the 'flattened' beta-sheet and helix-containing loops
YmcC-like [159269] (1)
12-stranded meander beta-sheet, folded into a deformed beta-barrel; topological similarity to the LolA-like fold (scop_cf 89391)
Spiral beta-roll [159274] (1)
a large 15-stranded beta-sheet rolled about a single helix core; overlapping edges form a sandwich-like structure; topological similarity to the LolA-like fold (scop_cf 89391)
beta-Prism II [51109] (1)
consists of 3 4-stranded sheets; strands are perpendicular to the 3-fold axis duplication: consists of two domains of this fold
Pentapeptide repeat-like [141571] (1)
superhelix turns are made of four short strands each; duplication: the sequence pentapeptide repeats correspond to individual strands uperfamily
Trimeric LpxA-like enzymes [51161] (8)
superhelical turns are made of three short strands; duplication: the sequence hexapeptide repeats correspond to individual strands uperfamily
Double-stranded beta-helix [51181] (7)
one turn of helix is made by two pairs of antiparallel strands linked with short turns has appearance of a sandwich of distinct architecture and jelly-roll topology
YlbA-like [101979] (4) Pfam 05899; formerly pfam06038; duplication: consists of two germin-like domains
Pirin-like [101984] (2) Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
Quercetin 2,3-dioxygenase-like [75035] (2) Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
Type I phosphomannose isomerase [51191] (3) Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin
Homogentisate dioxygenase [51194] (1) Share a common two-domain fold with the 7S protein; there is a metal-binding site in the C-terminal domain similar to the metal-binding site of germin
PA5104-like [141609] (1) Pfam 05962; DUF886; duplication: consists of two germin-like domains; overall structural similarity to the YlbA-like family (scop_fa 101979) except a deletion in the interdomain linker region
Gentisate 1,2-dioxygenase-like [159299] (3) Share a common two-domain fold with the 7S protein; there is a metal-binding site in the N-terminal domain similar to the metal-binding site of germin; homotetramer
SET domain [82199] (3)
duplication: the core is composed of two structural repeats similar to (circularly permuted) repeats of AFPIII also contains a substrate-binding alpha+beta subdomain inserted in the core uperfamily
dUTPase-like [51283] (1)
forms tight trimer through an additional beta-sheet in each subunit subunit beta-sheets are orthogonally packed around the three-fold axis uperfamily
MOSC N-terminal domain-like [141672] (1)
complex fold; comprises a beta-hairpin and a meander 3-stranded sheet packed against beta-barrel: closed, n=5, S=8; contains three short helices
DNA-binding pseudobarrel domain [101935] (1)
core: barrel, open; n=7, S*=10; capped with helices at both ends; partial similarity to the AbrB/MazE/MraZ-like fold (scop_cf 89446)
PG0164-like [141695] (1) duplication: comprises two intertwinned beta(2)-alpha-beta structural repeats
AF2212-like [159360] (1) Pfam 01954; DUF104; intertwinned homodimer of beta(2)-loop-beta subunits; the capping helices are replaced with extended loops
PUA domain-like [88696] (1)
pseudobarrel; mixed folded sheet of 5 strands; order 13452; strand 1 and 3 are parallel to each other
FimD N-terminal domain-like [141728] (1)
pseudo barrel, capped by an alpha-helix; some topological similarity to the PRC-barrel domain (scop_sf 50346) and the N-terminal domain of Glutamine synthetase (scop_sf 54368)
HisI-like [141733] (1)
pseudo barrel, capped by an alpha-helix; contains a beta-triangle structure on one side; some topological similarity to the Ribosomal protein L25-like fold (scop_cf 50714) and the N-terminal domain of Glutamine synthetase (scop_sf 54368)
HisI-like [141735] (1) Pfam 01502; PRA-CH; metalloenzyme, probable biological unit is dimeric
MFPT repeat-like [141738] (1)
consists of two similar pseudo barrel subdomains with structural similarity to a circularly permuted SAND domain (scop_fa 63764)