interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR023317
23,317
Peptidase S1A, plasmin
Pept_S1A_plasmin
Family
1,136
false
false
Plasmin is a serine peptidase belonging to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A. Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes, including embryonic development, tissue remodeling, tumor invasion, and inflammation [ ]; ...
[ "GO:0004252" ]
[ "serine-type endopeptidase activity" ]
[ "molecular_function" ]
1
[ "PIRSF" ]
[ "PIRSF001150" ]
[ "Plasmin" ]
[ 1136 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.21.7", "GenProp2010", "R-HSA-114608", "R-HSA-1474228", "R-HSA-1592389", "R-HSA-186797", "R-HSA-381426", "R-HSA-75205", "R-MMU-114608", "R-MMU-1592389", "R-MMU-186797", "R-MMU-75205", "R-RNO-114608", "R-RNO-1592389", "R-RNO-186797", "R-RNO-381426", "R-RNO-75205" ]
[ "EC:3.4.21.7", "GP:GenProp2010", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-1592389", "REACTOME:R-HSA-186797", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-75205", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-1592389", "REACTOME:R-MMU-186797", "REACTOME:R-MMU-75205", "REACTOM...
17
[ "4a5t", "4dur", "4duu", "8uq6" ]
4
[ "PUB00100482" ]
[ "14699093" ]
[ "Protease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cells." ]
[ 2004 ]
1
[ "IPR001314" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1136 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 4, 2, 5 ]
4
true
Family
Peptidase S1A, plasmin
Peptidase S1A, plasmin
Pept_S1A_plasmin
6
IPR023318
23,318
Ubiquitin activating enzyme, alpha domain superfamily
Ub_act_enz_dom_a_sf
Homologous_superfamily
9,997
false
false
Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.10.520" ]
[ "" ]
[ 9997 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-3065676", "R-CEL-3065678", "R-CEL-8951664", "R-CEL-983168", "R-DDI-3065676", "R-DDI-3065678", "R-DDI-8951664", "R-DDI-983168", "R-DME-8951664", "R-DME-983168", "R-DRE-3065676", "R-DRE-3065678", "R-DRE-8951664", "R-DRE-983168", "R-HSA-3065676", "R-HSA-3065678", "R-HSA-5607761",...
[ "REACTOME:R-CEL-3065676", "REACTOME:R-CEL-3065678", "REACTOME:R-CEL-8951664", "REACTOME:R-CEL-983168", "REACTOME:R-DDI-3065676", "REACTOME:R-DDI-3065678", "REACTOME:R-DDI-8951664", "REACTOME:R-DDI-983168", "REACTOME:R-DME-8951664", "REACTOME:R-DME-983168", "REACTOME:R-DRE-3065676", "REACTOME:R...
40
[ "1r4m", "1r4n", "1tt5", "1y8q", "1y8r", "1yov", "2nvu", "2px9", "3dbh", "3dbl", "3dbr", "3gzn", "3kyc", "3kyd", "6cwy", "6cwz", "6xog", "6xoh", "6xoi", "9dqb", "9drj" ]
21
[ "PUB00044523", "PUB00044524" ]
[ "1986373", "11004499" ]
[ "Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1.", "Molecular cloning of cDNA encoding a ubiquitin-activating enzyme (E1) from goldfish (Carassius auratus) and expression analysis of the cloned gene." ]
[ 1991, 2000 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 9997 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 11, 2, 8, 4, 13, 5, 4, 5, 12, 2, 2, 27 ]
12
true
Homologous_superfamily
Ubiquitin activating enzyme, alpha domain superfamily
Ubiquitin activating enzyme, alpha domain superfamily
Ub_act_enz_dom_a_sf
2
IPR023319
23,319
Tex-like protein, HTH domain superfamily
Tex-like_HTH_dom_sf
Homologous_superfamily
26,703
false
false
Tex (toxin expression) is a highly conserved bacterial protein involved in expression of critical toxin genes [ ]. The overall structure is notably flat and elongated. The most striking structural feature is a long, central helix comprising from amino acid residue 274 to 322. The rest of the protein wraps around the ce...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.10.650" ]
[ "" ]
[ 26703 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-112382", "R-CEL-674695", "R-CEL-75955", "R-DME-112382", "R-DME-674695", "R-DME-75955", "R-HSA-112382", "R-HSA-674695", "R-HSA-75955", "R-MMU-112382", "R-MMU-674695", "R-MMU-75955" ]
[ "REACTOME:R-CEL-112382", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-75955", "REACTOME:R-DME-112382", "REACTOME:R-DME-674695", "REACTOME:R-DME-75955", "REACTOME:R-HSA-112382", "REACTOME:R-HSA-674695", "REACTOME:R-HSA-75955", "REACTOME:R-MMU-112382", "REACTOME:R-MMU-674695", "REACTOME:R-MMU-75955"...
12
[ "2oce", "3bzc", "3bzk", "3psf", "3psi", "6gmh", "6ted", "7o3d", "7o6b", "7oop", "7opc", "7opd", "7unc", "7und", "7xn7", "7xse", "7xsx", "7xsz", "7xt7", "7xtd", "7xti", "8a3y", "8oeu", "8oev", "8of0", "8xrm", "9egx", "9egy", "9egz", "9eh0", "9eh1", "9eh2"...
39
[ "PUB00044514", "PUB00050835" ]
[ "8755871", "18321528" ]
[ "A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins.", "Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa." ]
[ 1996, 2008 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 64, 19414, 7096, 129 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 11, 2, 9, 4, 1, 3, 3, 1, 1, 10, 1, 1, 14 ]
13
true
Homologous_superfamily
Tex-like protein, HTH domain superfamily
Tex-like protein, HTH domain superfamily
Tex-like_HTH_dom_sf
6
IPR023321
23,321
PINIT domain
PINIT
Domain
8,525
false
false
This entry represents the PINIT domain found in the Siz/PIAS RING family of SUMO E3 ligases [ ]. These proteins present a tripartite architecture with an N-terminal PINIT domain, a central zinc-containing RING-like SP-RING domain, and a C-terminal domain desginated SP-CTD. Structural and biochemical studies have shown ...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF14324", "PS51466" ]
[ "PINIT", "PINIT" ]
[ 8297, 8435 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "2.3.2.-", "PWY-6289", "PWY-6462", "PWY-6463", "PWY-6682", "PWY-6841", "PWY-7815", "PWY-7816", "PWY-7817", "PWY-7818", "PWY-7887", "R-CEL-3108214", "R-CEL-3232118", "R-CEL-3232142", "R-CEL-3899300", "R-CEL-4085377", "R-CEL-4090294", "R-CEL-4551638", "R-CEL-5696395", "R-CEL-8773...
[ "EC:2.3.2.-", "METACYC:PWY-6289", "METACYC:PWY-6462", "METACYC:PWY-6463", "METACYC:PWY-6682", "METACYC:PWY-6841", "METACYC:PWY-7815", "METACYC:PWY-7816", "METACYC:PWY-7817", "METACYC:PWY-7818", "METACYC:PWY-7887", "REACTOME:R-CEL-3108214", "REACTOME:R-CEL-3232118", "REACTOME:R-CEL-3232142"...
78
[ "3i2d", "4fo9", "4mvt", "5jne", "6u75" ]
5
[ "PUB00054205", "PUB00054206" ]
[ "19748360", "14596924" ]
[ "Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.", "The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L." ]
[ 2009, 2003 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 8525 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 1, 23, 16, 19, 15, 2, 32, 2, 1 ]
9
true
Domain
PINIT domain
PINIT domain
PINIT
6
IPR023322
23,322
Outer surface lipoprotein domain superfamily
OM_lipoprot_dom_sf
Homologous_superfamily
873
false
false
The ospA and ospB genes encode the major outer membrane proteins of the Lyme disease spirochaete Borrelia burgdorferi [ ]. The deduced gene products OspA and OspB, contain 273 and 296 residues respectively [ ]. The two Osp proteins show a high degree of sequence similarity, indicating a recent evolutionary event. Molec...
[]
[]
[]
0
[ "SSF" ]
[ "SSF51087" ]
[ "" ]
[ 873 ]
1
[]
[]
[]
0
[ "1fj1", "1osp", "1p4p", "1rjl", "2af5", "2fkg", "2fkj", "2g8c", "2hkd", "2i5v", "2i5z", "2ol6", "2ol7", "2ol8", "2oy1", "2oy5", "2oy7", "2oy8", "2oyb", "2pi3", "3aum", "3cka", "3ckf", "3ckg", "3ec5", "3eex", "5b2a", "5ys7", "5z1o", "6ais", "6ics", "6idc"...
65
[ "PUB00003793", "PUB00003832" ]
[ "2761388", "1560779" ]
[ "Molecular analysis of linear plasmid-encoded major surface proteins, OspA and OspB, of the Lyme disease spirochaete Borrelia burgdorferi.", "Molecular analysis and expression of a Borrelia burgdorferi gene encoding a 22 kDa protein (pC) in Escherichia coli." ]
[ 1989, 1992 ]
2
[]
[]
0
0
null
[ "Bacteria" ]
[ 873 ]
1
[]
[]
0
true
Homologous_superfamily
Outer surface lipoprotein domain superfamily
Outer surface lipoprotein domain superfamily
OM_lipoprot_dom_sf
4
IPR023323
23,323
Tex-like domain superfamily
Tex-like_dom_sf
Homologous_superfamily
27,161
false
false
This superfamily represents a domain comprising amino acids 115-327 and 456-502, flanking the YqgF domain ( ). Tex (toxin expression) is a highly conserved bacterial protein involved in expression of critical toxin genes [ ]. The overall structure is notably flat and elongated. The most striking structural feature is a...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.3500.10" ]
[ "" ]
[ 27161 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-112382", "R-CEL-674695", "R-CEL-75955", "R-DME-112382", "R-DME-674695", "R-DME-75955", "R-HSA-112382", "R-HSA-674695", "R-HSA-75955", "R-MMU-112382", "R-MMU-674695", "R-MMU-75955" ]
[ "REACTOME:R-CEL-112382", "REACTOME:R-CEL-674695", "REACTOME:R-CEL-75955", "REACTOME:R-DME-112382", "REACTOME:R-DME-674695", "REACTOME:R-DME-75955", "REACTOME:R-HSA-112382", "REACTOME:R-HSA-674695", "REACTOME:R-HSA-75955", "REACTOME:R-MMU-112382", "REACTOME:R-MMU-674695", "REACTOME:R-MMU-75955"...
12
[ "2oce", "3bzc", "3bzk", "3psf", "3psi", "6gmh", "6ted", "7o3d", "7o6b", "7oop", "7opc", "7opd", "7unc", "7und", "7xn7", "7xse", "7xsx", "7xsz", "7xt7", "7xtd", "7xti", "8a3y", "8oeu", "8oev", "8of0", "8xrm", "9egx", "9egy", "9egz", "9eh0", "9eh1", "9eh2"...
39
[ "PUB00044514", "PUB00050835" ]
[ "8755871", "18321528" ]
[ "A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins.", "Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa." ]
[ 1996, 2008 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 64, 19587, 7355, 155 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 11, 2, 9, 4, 1, 5, 3, 1, 1, 10, 1, 1, 11 ]
13
true
Homologous_superfamily
Tex-like domain superfamily
Tex-like domain superfamily
Tex-like_dom_sf
2
IPR023324
23,324
BH2638-like superfamily
BH2638-like_sf
Homologous_superfamily
2,432
false
false
This superfamily represents an orthogonal bundle domain found in proteins belonging to the uncharacterised protein family UPF0223, including protein BH2638.
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.10.220.80", "SSF158504" ]
[ "", "" ]
[ 2423, 2432 ]
2
[]
[]
[]
0
[ "2oy9" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Fervidicoccus fontis", "Opisthokonta", "metagenomes", "uncultured Caudovirales phage" ]
[ 2423, 2, 2, 4, 1 ]
5
[]
[]
0
true
Homologous_superfamily
BH2638-like superfamily
BH2638-like superfamily
BH2638-like_sf
8
IPR023330
23,330
Rhabdovirus nucleocapsid, N-terminal
Rhabdovirus_ncapsid_N
Homologous_superfamily
10,515
false
false
All negative-strand RNA viruses contain a ribonucleoprotein (RNP) complex that consists of the viral genome RNA completely enwrapped by the nucleoprotein (N). The crystal structure of the N protein in complex with a single-strand RNA has been determined for two members of the rhabdovirus family, VSV [ ] and RABV [ ]. T...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.3570.10" ]
[ "" ]
[ 10515 ]
1
[]
[]
[]
0
[ "2gic", "2gtt", "2qvj", "2wyy", "3hhw", "3hhz", "3pmk", "3pto", "3ptx", "3pu0", "3pu1", "3pu4", "5uk4", "5ukb", "6bjy", "7umk", "7uml", "7uws", "7xpn", "7yg7", "8b8v", "8ffr", "8fwl", "8u0a", "8u0b" ]
25
[ "PUB00041063", "PUB00041177", "PUB00049163" ]
[ "16778022", "16778023", "18003727" ]
[ "Structure of the vesicular stomatitis virus nucleoprotein-RNA complex.", "Crystal structure of the rabies virus nucleoprotein-RNA complex.", "Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation." ]
[ 2006, 2006, 2008 ]
3
[]
[]
0
0
null
[ "Protostomia", "Riboviria" ]
[ 166, 10349 ]
2
[]
[]
0
true
Homologous_superfamily
Rhabdovirus nucleocapsid, N-terminal
Rhabdovirus nucleocapsid, N-terminal
Rhabdovirus_ncapsid_N
5
IPR023331
23,331
Rhabdovirus nucleocapsid, C-terminal
Rhabdovirus_ncapsid_C
Homologous_superfamily
9,292
false
false
All negative-strand RNA viruses contain a ribonucleoprotein (RNP) complex that consists of the viral genome RNA completely enwrapped by the nucleoprotein (N). The crystal structure of the N protein in complex with a single-strand RNA has been determined for two members of the rhabdovirus family, VSV [ ] and RABV [ ]. T...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.3610.10" ]
[ "" ]
[ 9292 ]
1
[]
[]
[]
0
[ "2gic", "2gtt", "2qvj", "2wyy", "3hhw", "3hhz", "3pmk", "3pto", "3ptx", "3pu0", "3pu1", "3pu4", "5uk4", "5ukb", "6bjy", "7umk", "7uml", "7uws", "7xpn", "7yg7", "8b8v", "8ffr", "8fwl", "8u0a", "8u0b" ]
25
[ "PUB00041063", "PUB00041177", "PUB00049163" ]
[ "16778022", "16778023", "18003727" ]
[ "Structure of the vesicular stomatitis virus nucleoprotein-RNA complex.", "Crystal structure of the rabies virus nucleoprotein-RNA complex.", "Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation." ]
[ 2006, 2006, 2008 ]
3
[]
[]
0
0
null
[ "Protostomia", "Riboviria" ]
[ 181, 9111 ]
2
[]
[]
0
true
Homologous_superfamily
Rhabdovirus nucleocapsid, C-terminal
Rhabdovirus nucleocapsid, C-terminal
Rhabdovirus_ncapsid_C
9
IPR023332
23,332
Proteasome alpha-type subunit
Proteasome_alpha-type
Family
39,918
false
false
ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, clpXP) complex in other eubacteria. Gen...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51475" ]
[ "PROTEASOME_ALPHA_2" ]
[ 39918 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1169091", "R-BTA-1234176", "R-BTA-1236974", "R-BTA-1236978", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-187577", "R-BTA-195253", "R-BTA-202424", "R-BTA-2467813", "R-BTA-2871837", "R-BTA-349425", "R-BTA-350562", "R-BTA-382556", "R-BTA-450408", "R-B...
[ "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA-187577", "REACTOME:R-BTA-195253", "REACTOME:R-BTA-202424", "REACTOME:R-BTA...
365
[ "1fnt", "1g0u", "1g65", "1iru", "1j2p", "1j2q", "1jd2", "1pma", "1q5q", "1q5r", "1ryp", "1ya7", "1yar", "1yau", "1z7q", "2f16", "2fak", "2fhg", "2fhh", "2gpl", "2h6j", "2ku1", "2ku2", "2z5c", "2zcy", "3bdm", "3c91", "3c92", "3d29", "3dy3", "3dy4", "3e47"...
621
[ "PUB00000148", "PUB00000524", "PUB00001329", "PUB00004123", "PUB00005460", "PUB00011906", "PUB00014349", "PUB00014350", "PUB00030848", "PUB00080992" ]
[ "2643381", "7682410", "7697118", "1317508", "8882582", "12446803", "12646382", "12823960", "9087403", "2535672" ]
[ "The multicatalytic proteinase of mammalian cells.", "Proteasomes: multicatalytic proteinase complexes.", "Proteasomes. Multicatalytic proteinase complexes.", "Proteolysis, proteasomes and antigen presentation.", "Proteasomes: destruction as a programme.", "Eubacterial HslV and HslU subunits homologs in p...
[ 1989, 1993, 1993, 1992, 1996, 2002, 2003, 2003, 1997, 1989 ]
10
[ "IPR001353" ]
[ "IPR019982", "IPR022296", "IPR033812", "IPR034642", "IPR035144" ]
1
5
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1268, 3189, 35338, 123 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 40, 7, 11, 16, 40, 33, 8, 29, 39, 7, 7, 86 ]
12
true
Family
Proteasome alpha-type subunit
Proteasome alpha-type subunit
Proteasome_alpha-type
1
IPR023333
23,333
Proteasome B-type subunit
Proteasome_suB-type
Family
57,462
false
false
ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, clpXP) complex in other eubacteria. Gen...
[]
[]
[]
0
[ "PROFILE", "PANTHER" ]
[ "PS51476", "PTHR32194" ]
[ "PROTEASOME_BETA_2", "" ]
[ 51873, 54902 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "3.4.25", "R-BTA-1169091", "R-BTA-1234176", "R-BTA-1236974", "R-BTA-1236978", "R-BTA-174084", "R-BTA-174154", "R-BTA-174178", "R-BTA-174184", "R-BTA-187577", "R-BTA-195253", "R-BTA-202424", "R-BTA-2467813", "R-BTA-2871837", "R-BTA-349425", "R-BTA-350562", "R-BTA-382556", "R-BTA-450...
[ "EC:3.4.25", "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1234176", "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236978", "REACTOME:R-BTA-174084", "REACTOME:R-BTA-174154", "REACTOME:R-BTA-174178", "REACTOME:R-BTA-174184", "REACTOME:R-BTA-187577", "REACTOME:R-BTA-195253", "REACTOME:R-BTA-202424", ...
458
[ "1e94", "1fnt", "1g0u", "1g3i", "1g3k", "1g4a", "1g4b", "1g65", "1hqy", "1ht1", "1ht2", "1iru", "1j2q", "1jd2", "1jjw", "1kyi", "1m4y", "1ned", "1ofh", "1ofi", "1pma", "1q5q", "1q5r", "1ryp", "1ya7", "1yar", "1yau", "1yyf", "1z7q", "2f16", "2fak", "2fhg"...
628
[ "PUB00000148", "PUB00000524", "PUB00001329", "PUB00004123", "PUB00005460", "PUB00011906", "PUB00014349", "PUB00014350", "PUB00030848", "PUB00080992" ]
[ "2643381", "7682410", "7697118", "1317508", "8882582", "12446803", "12646382", "12823960", "9087403", "2535672" ]
[ "The multicatalytic proteinase of mammalian cells.", "Proteasomes: multicatalytic proteinase complexes.", "Proteasomes. Multicatalytic proteinase complexes.", "Proteolysis, proteasomes and antigen presentation.", "Proteasomes: destruction as a programme.", "Eubacterial HslV and HslU subunits homologs in p...
[ 1989, 1993, 1993, 1992, 1996, 2002, 2003, 2003, 1997, 1989 ]
10
[ "IPR001353" ]
[ "IPR000243", "IPR016295", "IPR033811", "IPR035206" ]
1
4
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1396, 16375, 39320, 371 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 37, 8, 32, 26, 1, 53, 30, 7, 24, 52, 7, 7, 87 ]
13
true
Family
Proteasome B-type subunit
Proteasome B-type subunit
Proteasome_suB-type
2
IPR023334
23,334
REKLES domain
REKLES_domain
Domain
3,585
false
false
This entry represents the REKLES domain, found at the C-terminal of Bright/Dril1/ARID3a proteins. These proteins are B cell-specific, matrix association (or attachment) region-binding transcriptional regulator of immunoglobulin heavy chain genes and of E2F1-dependent cell cycle progression. The REKLES domain is essenti...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51486" ]
[ "REKLES" ]
[ 3585 ]
1
[ "REACTOME" ]
[ "R-HSA-6804116" ]
[ "REACTOME:R-HSA-6804116" ]
1
[]
0
[ "PUB00054208", "PUB00054209" ]
[ "17400556", "16507996" ]
[ "REKLES is an ARID3-restricted multifunctional domain.", "A regulated nucleocytoplasmic shuttle contributes to Bright's function as a transcriptional activator of immunoglobulin genes." ]
[ 2007, 2006 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 5, 3580 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 31, 4, 7, 8, 7 ]
6
true
Domain
REKLES domain
REKLES domain
REKLES_domain
6
IPR023335
23,335
ATP12 orthogonal Bundle domain superfamily
ATP12_ortho_dom_sf
Homologous_superfamily
7,287
false
false
This superfamily represents an orthogonal bundle domain found in mitochondrial ATPase F1 complex assembly protein ATP12 [ ] and homologue protein ATPAF2 (assembly factor 2) [ ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.3580.10" ]
[ "" ]
[ 7287 ]
1
[]
[]
[]
0
[ "2p4x", "2r31", "2r6i", "2zd2" ]
4
[ "PUB00014715", "PUB00054212" ]
[ "1826907", "11410595" ]
[ "Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase.", "Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria." ]
[ 1991, 2001 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 2871, 4393, 23 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 2, 1, 2, 3, 2, 1, 3, 8, 1, 1, 4 ]
12
true
Homologous_superfamily
ATP12 orthogonal Bundle domain superfamily
ATP12 orthogonal Bundle domain superfamily
ATP12_ortho_dom_sf
2
IPR023336
23,336
RAG nonamer-binding domain
RAG_nonamer-bd_dom
Domain
9,824
false
false
The variable portions of immunoglobulin and T cell receptor genes are assembled in developing lymphocytes from variable (V), joining (J), and in some cases diversity (D) gene segments, which are widely separated in the genome. These segments are brought together in a highly regulated manner by a somatic site-specific r...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF12940", "PS51487" ]
[ "RAG1", "NBD" ]
[ 9035, 9761 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME" ]
[ "2.3.2.27", "PWY-7511", "R-HSA-1266695", "R-HSA-5687128" ]
[ "EC:2.3.2.27", "METACYC:PWY-7511", "REACTOME:R-HSA-1266695", "REACTOME:R-HSA-5687128" ]
4
[ "3gna", "3gnb", "3jbw", "3jbx", "3jby", "4wwx", "5zdz", "5ze0", "5ze1", "5ze2", "6b40", "6cg0", "6cij", "6cik", "6cil", "6cim", "6dbi", "6dbj", "6dbl", "6dbo", "6dbq", "6dbr", "6dbt", "6dbu", "6dbv", "6dbw", "6dbx", "6oem", "6oen", "6oeo", "6oep", "6oeq"...
44
[ "PUB00052188", "PUB00054210", "PUB00054211", "PUB00056079", "PUB00056080", "PUB00098031", "PUB00150929" ]
[ "19396172", "8861909", "8861910", "19621044", "7642230", "24464998", "25707801" ]
[ "Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis.", "RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination.", "The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination.", "RAG: a rec...
[ 2009, 1996, 1996, 2009, 1995, 2014, 2015 ]
7
[]
[]
0
0
null
[ "Archaeoglobus fulgidus", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 1, 14, 9807, 2 ]
4
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 3, 3, 3 ]
4
true
Domain
RAG nonamer-binding domain
RAG nonamer-binding domain
RAG_nonamer-bd_dom
4
IPR023337
23,337
c-Kit-binding domain
KBD
Domain
2,773
false
false
This entry represents the c-Kit binding domain found in metazoan Spread (Sprouty-related, EVH1 domain-containing) proteins. This domain has been shown to be necessary for Spread-1 phosphorylation and is not similar to other previously reported tyrosine kinase interacting domains, such as SH2 or c-Met binding domains [ ...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51488" ]
[ "KBD" ]
[ 2773 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DRE-5658623", "R-HSA-5658442", "R-HSA-5658623", "R-HSA-6802953", "R-MMU-5658442", "R-MMU-5658623", "R-RNO-5658442", "R-RNO-5658623", "R-XTR-5658623" ]
[ "REACTOME:R-DRE-5658623", "REACTOME:R-HSA-5658442", "REACTOME:R-HSA-5658623", "REACTOME:R-HSA-6802953", "REACTOME:R-MMU-5658442", "REACTOME:R-MMU-5658623", "REACTOME:R-RNO-5658442", "REACTOME:R-RNO-5658623", "REACTOME:R-XTR-5658623" ]
9
[]
0
[ "PUB00035332", "PUB00054213" ]
[ "11493923", "12646235" ]
[ "Spred is a Sprouty-related suppressor of Ras signalling.", "Molecular cloning of mammalian Spred-3 which suppresses tyrosine kinase-mediated Erk activation." ]
[ 2001, 2003 ]
2
[]
[]
0
0
null
[ "Bacillati", "Eukaryota" ]
[ 4, 2769 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 8, 6, 15 ]
4
true
Domain
c-Kit-binding domain
c-Kit-binding domain
KBD
3
IPR023338
23,338
Arterivirus NSP4 peptidase domain
Arterivirus_NSP4_peptidase
Domain
1,540
false
false
Ths entry represents the NSP4 proteinase of arteriviruses. Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries: Equine arteritis virus (EAV). Porcine reproductive and respiratory syndrome virus (PRRSV). Mice actate dehydr...
[ "GO:0008233" ]
[ "peptidase activity" ]
[ "molecular_function" ]
1
[ "PROFILE" ]
[ "PS51493" ]
[ "AV_NSP4_PRO" ]
[ 1540 ]
1
[ "EC", "EC", "EC", "EC", "EC", "EC", "EC", "METACYC" ]
[ "2.7.7.48", "3.4.19.12", "3.4.21.-", "3.4.22.-", "3.6.4.12", "3.6.4.13", "4.6.1.-", "PWY-7884" ]
[ "EC:2.7.7.48", "EC:3.4.19.12", "EC:3.4.21.-", "EC:3.4.22.-", "EC:3.6.4.12", "EC:3.6.4.13", "EC:4.6.1.-", "METACYC:PWY-7884" ]
8
[ "1mbm", "3fan", "3fao", "5y4l" ]
4
[ "PUB00027289", "PUB00052898" ]
[ "12163505", "19646449" ]
[ "Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole.", "Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PR...
[ 2002, 2009 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Nidovirales" ]
[ 4, 2, 1534 ]
3
[]
[]
0
true
Domain
Arterivirus NSP4 peptidase domain
Arterivirus NSP4 peptidase domain
Arterivirus_NSP4_peptidase
5
IPR023339
23,339
CVC domain
CVC
Domain
2,584
false
false
This entry represents the CVC (Chx10/Vsx-1 and ceh-10) domain, which is found in visual system homeobox proteins. Homeobox-containing genes encode transcription factors and are characterised by the homeodomain (HD), a motif that directs specific DNA binding to regulate the expression of target genes. Homeobox genes are...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51496" ]
[ "CVC" ]
[ 2584 ]
1
[]
[]
[]
0
[]
0
[ "PUB00054217", "PUB00054218", "PUB00054219" ]
[ "7789259", "11485319", "15767664" ]
[ "The C. elegans neuronally expressed homeobox gene ceh-10 is closely related to genes expressed in the vertebrate eye.", "Isolation and characterization of Vsx1, a novel mouse CVC paired-like homeobox gene expressed during embryogenesis and in the retina.", "Nuclear export is evolutionarily conserved in CVC pai...
[ 1995, 2001, 2005 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Thermosphaera chiliense", "marine metagenome" ]
[ 3, 2579, 1, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 5, 5, 6, 5 ]
6
true
Domain
CVC domain
CVC domain
CVC
5
IPR023340
23,340
UMA domain
UMA
Domain
5,175
false
false
This entry represents the UMA domain, which contains a conserved proline followed by a hydrophobic residue in the N terminus and a nearly absolutely conserved glutamate at the C terminus. It is predicted to adopt an α+β fold [ ]. A key aspect of eukaryotic intracellular trafficking is the sorting of cell-surface protei...
[]
[]
[]
0
[ "PROFILE" ]
[ "PS51497" ]
[ "UMA" ]
[ 5175 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-917729", "R-DRE-917729", "R-HSA-162588", "R-HSA-174490", "R-HSA-917729", "R-HSA-9610379", "R-HSA-9615710", "R-MMU-917729", "R-RNO-917729" ]
[ "REACTOME:R-BTA-917729", "REACTOME:R-DRE-917729", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-174490", "REACTOME:R-HSA-917729", "REACTOME:R-HSA-9610379", "REACTOME:R-HSA-9615710", "REACTOME:R-MMU-917729", "REACTOME:R-RNO-917729" ]
9
[]
0
[ "PUB00054220" ]
[ "20448139" ]
[ "UMA and MABP domains throw light on receptor endocytosis and selection of endosomal cargoes." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5175 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 18, 4, 12, 11, 18 ]
6
true
Domain
UMA domain
UMA domain
UMA
9
IPR023342
23,342
APO domain
APO_dom
Domain
2,828
false
false
This entry represents the APO domain which is found in plant APO (Accumulation of photosystem) proteins. The domain contains conserved cysteine and histidine residues [ ]. It functions as an RNA-binding domain [ ].
[ "GO:0003723" ]
[ "RNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF05634", "PS51499" ]
[ "APO_RNA-bind", "APO" ]
[ 2820, 2682 ]
2
[]
[]
[]
0
[]
0
[ "PUB00054221", "PUB00057416" ]
[ "15494558", "21421812" ]
[ "ACCUMULATION OF PHOTOSYSTEM ONE1, a member of a novel gene family, is required for accumulation of [4Fe-4S] cluster-containing chloroplast complexes and antenna proteins.", "APO1 promotes the splicing of chloroplast group II introns and harbors a plant-specific zinc-dependent RNA binding domain." ]
[ 2004, 2011 ]
2
[]
[]
0
0
null
[ "Eukaryota", "Paenibacillus prosopidis" ]
[ 2827, 1 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 18, 13, 14 ]
3
true
Domain
APO domain
APO domain
APO_dom
3
IPR023343
23,343
Penicillin amidase type, domain 1
Penicillin_amidase_dom1
Homologous_superfamily
17,670
false
false
Penicillin amidase or penicillin acylase catalyses the hydrolysis of benzylpenicillin to phenylacetic acid and 6-aminopenicillanic acid (6-APA) a key intermediate in the the synthesis of penicillins [ ]. This superfamily represents the N-terminal structural domain of the penicillin amidase peptidases. It forms an α-hel...
[ "GO:0016811" ]
[ "hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:1.10.439.10" ]
[ "" ]
[ 17670 ]
1
[ "EC" ]
[ "3.5.1.97" ]
[ "EC:3.5.1.97" ]
1
[ "1ai4", "1ai5", "1ai6", "1ai7", "1ajn", "1ajp", "1ajq", "1cp9", "1e3a", "1fm2", "1fxh", "1fxv", "1ghd", "1gk0", "1gk1", "1gk9", "1gkf", "1gm7", "1gm8", "1gm9", "1h2g", "1jvz", "1jw0", "1jx9", "1k5q", "1k5s", "1k7d", "1kec", "1keh", "1or0", "1pnk", "1pnl"...
84
[ "PUB00000144", "PUB00025281" ]
[ "9292993", "11601852" ]
[ "Molecular cloning and analysis of the gene encoding the thermostable penicillin G acylase from Alcaligenes faecalis.", "Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism." ]
[ 1997, 2001 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 297, 16926, 167, 280 ]
4
[]
[]
0
true
Homologous_superfamily
Penicillin amidase type, domain 1
Penicillin amidase type, domain 1
Penicillin_amidase_dom1
8
IPR023346
23,346
Lysozyme-like domain superfamily
Lysozyme-like_dom_sf
Homologous_superfamily
296,824
false
false
This entry represents a lysozyme-like domain superfamily found in glycosyl hydrolases and transglycosylases. Biosynthetic peptidoglycan transglycosylases are peptidoglycan polymerases that catalyse glycan chain elongation from lipid-linked precursors [ ].
[]
[]
[]
0
[ "SSF" ]
[ "SSF53955" ]
[ "" ]
[ 296824 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6798695", "R-BTA-6803157", "R-CFA-6798695", "R-CFA-6803157", "R-DME-5653890", "R-GGA-5653890", "R-GGA-6798695", "R-GGA-6803157", "R-HSA-5653890", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-9638771", "R-HSA-977225", "R-MMU-5653890", "R-MMU-6798695", "R-MMU-6803157", "R-RNO-679869...
[ "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6803157", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-6803157", "REACTOME:R-DME-5653890", "REACTOME:R-GGA-5653890", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-6803157", "REACTOME:R-HSA-5653890", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6803157", "REACTOM...
21
[ "102l", "103l", "104l", "107l", "108l", "109l", "110l", "111l", "112l", "113l", "114l", "115l", "118l", "119l", "120l", "122l", "123l", "125l", "126l", "127l", "128l", "129l", "130l", "131l", "132l", "133l", "134l", "135l", "137l", "138l", "139l", "140l"...
2,752
[ "PUB00042230" ]
[ "17347437" ]
[ "Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis." ]
[ 2007 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 36, 263006, 23925, 6883, 9, 2965 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 68, 11, 20, 31, 14, 28, 27, 37, 36, 90 ]
10
true
Homologous_superfamily
Lysozyme-like domain superfamily
Lysozyme-like domain superfamily
Lysozyme-like_dom_sf
6
IPR023347
23,347
Lysozyme domain superfamily
Lysozyme_dom_sf
Homologous_superfamily
18,101
false
false
This entry represents a domain superfamily found in phage lysozyme and related proteins [ ], including Bacteriophage lambda lysozyme and Escherichia coli endolysin [ ]. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages bet...
[ "GO:0003796" ]
[ "lysozyme activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:1.10.530.40" ]
[ "" ]
[ 18101 ]
1
[ "EC" ]
[ "3.2.1.17" ]
[ "EC:3.2.1.17" ]
1
[ "102l", "103l", "104l", "107l", "108l", "109l", "110l", "111l", "112l", "113l", "114l", "115l", "118l", "119l", "120l", "122l", "123l", "125l", "126l", "127l", "128l", "129l", "130l", "131l", "137l", "138l", "139l", "140l", "141l", "142l", "143l", "144l"...
897
[ "PUB00003216", "PUB00004082", "PUB00084188" ]
[ "3586019", "2234094", "22389108" ]
[ "Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.", "A mutant T4 lysozyme displays five different crystal conformations.", "Protein determinants of phage T4 lysis inhibition." ]
[ 1987, 1990, 2012 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3, 14033, 1418, 2505, 142 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Homologous_superfamily
Lysozyme domain superfamily
Lysozyme domain superfamily
Lysozyme_dom_sf
4
IPR023349
23,349
Ammonia monooxygenase/particulate methane monooxygenase, subunit C domain superfamily
NH3_CH4_mOase_C_sf
Homologous_superfamily
475
false
false
This superfamily represents the structural domain of the C subunit of ammonia monooxygenase/particulate methane monooxygenase. Ammonia monooxygenase and the particulate methane monooxygenase are both integral membrane proteins, occurring in ammonia oxidisers and methanotrophs respectively, which are thought to be evolu...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.20.1050.50" ]
[ "" ]
[ 475 ]
1
[]
[]
[]
0
[ "1yew", "3chx", "3rfr", "3rgb", "4phz", "4pi0", "4pi2", "6cxh", "7ev9", "7s4h", "7s4i", "7s4j", "7s4k", "7s4l", "7s4m", "7t4o", "7t4p", "7yzy", "8oyi", "8sqw", "8sr1", "8sr2", "8sr4", "8sr5", "9cl1", "9cl2", "9cl3", "9cl4", "9cl5", "9cl6" ]
30
[ "PUB00016963", "PUB00016964", "PUB00016965" ]
[ "7590173", "12209257", "15674245" ]
[ "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related.", "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea.", "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane." ]
[ 1995, 2002, 2005 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 85, 356, 34 ]
3
[]
[]
0
true
Homologous_superfamily
Ammonia monooxygenase/particulate methane monooxygenase, subunit C domain superfamily
Ammonia monooxygenase/particulate methane monooxygenase, subunit C domain superfamily
NH3_CH4_mOase_C_sf
5
IPR023351
23,351
YppE-like superfamily
YppE-like_sf
Homologous_superfamily
1,247
false
false
This superfamily represents a domain which consists of a four α-helical up-and-down bundle. It is found in a family of uncharacterised proteins [ ].
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.120.440", "SSF140415" ]
[ "", "" ]
[ 1213, 1245 ]
2
[]
[]
[]
0
[ "2a2m", "2a2o", "2ets", "2hfi", "2huj", "2im8", "6r80", "7jrq" ]
8
[ "PUB00047405" ]
[ "18324683" ]
[ "Crystal structures of MW1337R and lin2004: representatives of a novel protein family that adopt a four-helical bundle fold." ]
[ 2008 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "marine sediment metagenome" ]
[ 1236, 7, 3, 1 ]
4
[]
[]
0
true
Homologous_superfamily
YppE-like superfamily
YppE-like superfamily
YppE-like_sf
1
IPR023352
23,352
Membrane associated eicosanoid/glutathione metabolism-like domain superfamily
MAPEG-like_dom_sf
Homologous_superfamily
29,209
false
false
This domain is found in a widespread superfamily known as MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) [ ]. Included in this superfamily are: 5-lipoxygenase activating protein (gene FLAP), which seems to be required for the activation of 5-lipoxygenase. Leukotriene C4 synthase ( ), whic...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.120.550", "SSF161084" ]
[ "", "" ]
[ 28828, 29074 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.5.1", "R-BTA-156590", "R-BTA-2142688", "R-BTA-2142691", "R-BTA-2142700", "R-BTA-2162123", "R-BTA-5423646", "R-BTA-9026762", "R-BTA-9026766", "R-CFA-2162123", "R-DDI-156590", "R-DDI-2142688", "R-DDI-2142691", "R-DDI-2142700", "R-DDI-5423646", "R-DDI-9026762", "R-DDI-9026766", "R-...
[ "EC:2.5.1", "REACTOME:R-BTA-156590", "REACTOME:R-BTA-2142688", "REACTOME:R-BTA-2142691", "REACTOME:R-BTA-2142700", "REACTOME:R-BTA-2162123", "REACTOME:R-BTA-5423646", "REACTOME:R-BTA-9026762", "REACTOME:R-BTA-9026766", "REACTOME:R-CFA-2162123", "REACTOME:R-DDI-156590", "REACTOME:R-DDI-2142688"...
47
[ "2h8a", "2pno", "2q7m", "2q7r", "2uuh", "2uui", "3b29", "3dww", "3hkk", "3leo", "3pcv", "4al0", "4al1", "4bpm", "4j7t", "4j7y", "4jc7", "4jcz", "4jrz", "4nta", "4ntb", "4ntf", "4wab", "4yk5", "4yl0", "4yl1", "4yl3", "5bqg", "5bqh", "5bqi", "5hv9", "5i9k"...
50
[ "PUB00005060", "PUB00048888" ]
[ "10091672", "17600184" ]
[ "Common structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism.", "Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein." ]
[ 1999, 2007 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes", "uncultured Caudovirales phage", "uncultured Poseidoniia archaeon" ]
[ 13409, 15639, 159, 1, 1 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 8, 24, 17, 1, 20, 19, 3, 3, 27, 7 ]
10
true
Homologous_superfamily
Membrane associated eicosanoid/glutathione metabolism-like domain superfamily
Membrane associated eicosanoid/glutathione metabolism-like domain superfamily
MAPEG-like_dom_sf
4
IPR023353
23,353
LemA-like domain superfamily
LemA-like_dom_sf
Homologous_superfamily
21,251
false
false
The exact molecular function of the LemA protein is uncertain. Structurally LemA consists of a four-helical bundle where helices 2 and 3 are shorter than helices 1 and 4. It is predicted to be a transmembrane protein with an extracellular N terminus [ ].
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.1440.20", "SSF140478" ]
[ "", "" ]
[ 20939, 20825 ]
2
[]
[]
[]
0
[ "2etd" ]
1
[ "PUB00009805" ]
[ "8758895" ]
[ "Identification of an H2-M3-restricted Listeria epitope: implications for antigen presentation by M3." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 205, 20487, 41, 28, 490 ]
5
[]
[]
0
true
Homologous_superfamily
LemA-like domain superfamily
LemA-like domain superfamily
LemA-like_dom_sf
9
IPR023355
23,355
Myotoxin/Anemone neurotoxin domain superfamily
Myo_ane_neurotoxin_sf
Homologous_superfamily
387
false
false
This superfamily represents the β-sheet domain found in snake myotoxin and anemone neurotoxins [ , ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.20.20.10" ]
[ "" ]
[ 387 ]
1
[]
[]
[]
0
[ "1ahl", "1apf", "1atx", "1b8w", "1bds", "1d6b", "1h5o", "1sh1", "1shi", "1wqk", "1wxn", "1z99", "1zlh", "1zli", "1zue", "1zuf", "2bds", "2h9x", "2jto", "2k2x", "2k2z", "2mn3", "2mub", "2rng", "2sh1", "3d4u", "3lms", "3osl", "4gv5", "6qbk", "6qbl", "7bwi"...
33
[ "PUB00016458", "PUB00097364" ]
[ "2566326", "24100315" ]
[ "Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.", "Structure of the polypeptide crotamine from the Brazilian ra...
[ 1989, 2013 ]
2
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 387 ]
1
[]
[]
0
true
Homologous_superfamily
Myotoxin/Anemone neurotoxin domain superfamily
Myotoxin/Anemone neurotoxin domain superfamily
Myo_ane_neurotoxin_sf
3
IPR023356
23,356
Leucyl-tRNA synthetase, domain 3
Leu-tRNA-synth_dom3
Domain
57
false
false
Leucine-tRNA ligase ( ) is an alpha monomer that belongs to class Ia. The crystal structure of leucine-tRNA ligase from the hyperthermophile Thermus thermophilus has an overall architecture that is similar to that of isoleucine-tRNA ligase, except that the putative editing domain is inserted at a different position in ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF14795" ]
[ "Leucyl-specific" ]
[ 57 ]
1
[]
[]
[]
0
[ "1h3n", "1obc", "1obh", "2bte", "2byt", "2v0c", "2v0g" ]
7
[ "PUB00006534" ]
[ "10811626" ]
[ "The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Thermaceae" ]
[ 57 ]
1
[]
[]
0
true
Domain
Leucyl-tRNA synthetase, domain 3
Leucyl-tRNA synthetase, domain 3
Leu-tRNA-synth_dom3
3
IPR023358
23,358
Peptidase M18, domain 2
Peptidase_M18_dom2
Homologous_superfamily
15,207
false
false
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase...
[ "GO:0004177" ]
[ "aminopeptidase activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:2.30.250.10" ]
[ "" ]
[ 15207 ]
1
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "3.4.11.-", "PWY-6423", "PWY-7694", "PWY-7954" ]
[ "EC:3.4.11.-", "METACYC:PWY-6423", "METACYC:PWY-7694", "METACYC:PWY-7954" ]
4
[ "1y7e", "2glf", "2glj", "2ijz", "3var", "3vat", "3wt4", "4dyo", "4eme", "4njq", "4njr", "4oid", "4oiw", "4r8f", "5jgf", "5jh9", "5jm6", "5jm9", "6pev", "7u5h" ]
20
[ "PUB00002544", "PUB00003579" ]
[ "2651436", "7674922" ]
[ "Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae.", "Evolutionary families of metallopeptidases." ]
[ 1989, 1995 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 22, 8499, 6567, 119 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "S...
[ 8, 2, 2, 14, 8, 2, 4, 10, 2, 1, 9 ]
11
true
Homologous_superfamily
Peptidase M18, domain 2
Peptidase M18, domain 2
Peptidase_M18_dom2
8
IPR023359
23,359
Dihydroorotate dehydrogenase A, chain A, domain 2
Dihydro_DH_chainA_dom2
Homologous_superfamily
1,976
false
false
Dihydroorotate dehydrogenase ( ) (DHOdehase) catalyses the fourth step in the de novo biosynthesis of pyrimidine, the conversion of dihydroorotate into orotate. DHOdehase is a ubiquitous FAD flavoprotein. In bacteria (gene pyrD), DHOdease is located on the inner side of the cytosolic membrane. In some yeasts, such as i...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.30.26.10" ]
[ "" ]
[ 1976 ]
1
[ "EC", "METACYC" ]
[ "1.3.98.1", "PWY-7790" ]
[ "EC:1.3.98.1", "METACYC:PWY-7790" ]
2
[ "1dor", "1jqv", "1jqx", "1jrb", "1jrc", "1jub", "1jue", "1ovd", "2bsl", "2bx7", "2dor", "3oix", "4wzh", "9cb8", "9n67", "9n68", "9n6o", "9n6q" ]
18
[ "PUB00004801" ]
[ "1409592" ]
[ "Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts." ]
[ 1992 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 50, 892, 997, 7, 30 ]
5
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 1, 1 ]
2
true
Homologous_superfamily
Dihydroorotate dehydrogenase A, chain A, domain 2
Dihydroorotate dehydrogenase A, chain A, domain 2
Dihydro_DH_chainA_dom2
7
IPR023362
23,362
PH-BEACH domain
PH-BEACH_dom
Domain
22,050
false
false
This entry represents a domain with a fold similar to that of the PH (pleckstrin homology) domain, despite displaying little sequence homology with canonical PH domains. Furthermore, this domain is incapable of binding phospholipids [ ]. This domain is found preceding the BEACH domain in beige-like and BEACH-domain con...
[]
[]
[]
0
[ "PFAM", "PROFILE", "CDD" ]
[ "PF14844", "PS51783", "cd01201" ]
[ "PH_BEACH", "PH_BEACH", "PH_BEACH" ]
[ 18723, 21938, 16764 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-6798695", "R-DRE-6798695", "R-HSA-112314", "R-HSA-163615", "R-HSA-2122947", "R-HSA-5626978", "R-HSA-6798695", "R-HSA-9609736", "R-MMU-5626978", "R-MMU-6798695" ]
[ "REACTOME:R-DDI-6798695", "REACTOME:R-DRE-6798695", "REACTOME:R-HSA-112314", "REACTOME:R-HSA-163615", "REACTOME:R-HSA-2122947", "REACTOME:R-HSA-5626978", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9609736", "REACTOME:R-MMU-5626978", "REACTOME:R-MMU-6798695" ]
10
[ "1mi1", "1t77" ]
2
[ "PUB00031364" ]
[ "15554694" ]
[ "Crystal structure of the PH-BEACH domains of human LRBA/BGL." ]
[ 2004 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 4, 22046 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 29, 6, 111, 11, 51, 31, 1, 14, 42, 1, 1, 37 ]
12
true
Domain
PH-BEACH domain
PH-BEACH domain
PH-BEACH_dom
9
IPR023364
23,364
Trans-sialidase, domain 3
Trans_sialidase_dom3
Homologous_superfamily
982
false
false
This entry represents a β-barrel domain found in bacterial trans-sialidase NanA, NanB and in the leech sialidase [ , , ]. Both act as intramolecular trans-sialidases. Trans-sialidases are responsible for the transfer of previously cleaved sialic acid to other glyconjugates.
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.40.220.10" ]
[ "" ]
[ 982 ]
1
[ "EC" ]
[ "3.2.1.18" ]
[ "EC:3.2.1.18" ]
1
[ "1sli", "1sll", "2bf6", "2jkb", "2sli", "2vk5", "2vk6", "2vk7", "2vvz", "2vw0", "2vw1", "2vw2", "2w20", "2ya4", "2ya5", "2ya6", "2ya7", "2ya8", "3h71", "3h72", "3h73", "3sli", "4foq", "4fov", "4fow", "4foy", "4fp2", "4fp3", "4fpc", "4fpe", "4fpf", "4fpg"...
95
[ "PUB00014147", "PUB00049929", "PUB00052248" ]
[ "9878409", "18835278", "19284989" ]
[ "The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism.", "Crystal structure of the NanB sialidase from Streptococcus pneumoniae.", "Crystal structures of respiratory pathogen neuraminidases." ]
[ 1999, 2008, 2009 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "bioreactor metagenome" ]
[ 978, 3, 1 ]
3
[]
[]
0
true
Homologous_superfamily
Trans-sialidase, domain 3
Trans-sialidase, domain 3
Trans_sialidase_dom3
2
IPR023365
23,365
Sortase domain superfamily
Sortase_dom-sf
Homologous_superfamily
35,738
false
false
This superfamily represents the β barrel structural domain found in sortases, which are cysteine transpeptidases involved in protein sorting activities.
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:2.40.260.10", "SSF63817" ]
[ "", "" ]
[ 35708, 35275 ]
2
[ "EC" ]
[ "3.4.22.-" ]
[ "EC:3.4.22.-" ]
1
[ "1ija", "1ng5", "1qwz", "1qx6", "1qxa", "1rz2", "1t2o", "1t2p", "1t2w", "2cz4", "2kid", "2kw8", "2ln7", "2mlm", "2oqw", "2oqz", "2rui", "2w1j", "2w1k", "2wts", "2xwg", "3fn5", "3fn6", "3fn7", "3g66", "3g69", "3o0p", "3psq", "3rbi", "3rbj", "3rbk", "3rcc"...
86
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanomada group", "Viruses", "unclassified sequences" ]
[ 35294, 15, 81, 3, 345 ]
5
[ "Arabidopsis thaliana" ]
[ 1 ]
1
true
Homologous_superfamily
Sortase domain superfamily
Sortase domain superfamily
Sortase_dom-sf
4
IPR023366
23,366
ATP synthase subunit alpha, N-terminal domain-like superfamily
ATP_synth_asu-like_sf
Homologous_superfamily
85,815
false
false
In F-ATPases, there are three copies each of the alpha and beta subunits that form the catalytic core of the F1 complex, while the remaining F1 subunits (gamma, delta, epsilon) form part of the stalks. There is a substrate-binding site on each of the alpha and beta subunits, those on the beta subunits being catalytic, ...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.40.30.20" ]
[ "" ]
[ 85815 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "...
[ "7.1.2.2", "PWY-7980", "R-BTA-1222556", "R-BTA-77387", "R-BTA-917977", "R-BTA-9639288", "R-BTA-983712", "R-CEL-1222556", "R-CEL-163210", "R-CEL-77387", "R-CEL-8949613", "R-CEL-917977", "R-CEL-9639288", "R-CEL-983712", "R-CEL-9837999", "R-DDI-1222556", "R-DDI-77387", "R-DDI-917977",...
[ "EC:7.1.2.2", "METACYC:PWY-7980", "REACTOME:R-BTA-1222556", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-917977", "REACTOME:R-BTA-9639288", "REACTOME:R-BTA-983712", "REACTOME:R-CEL-1222556", "REACTOME:R-CEL-163210", "REACTOME:R-CEL-77387", "REACTOME:R-CEL-8949613", "REACTOME:R-CEL-917977", "REACT...
65
[ "1bmf", "1cow", "1e1q", "1e1r", "1e79", "1efr", "1fx0", "1h8e", "1h8h", "1hze", "1i18", "1i8d", "1kmh", "1kzl", "1mab", "1nbm", "1ohh", "1pkv", "1qo1", "1sky", "1v0e", "1v0f", "1vdz", "1w0j", "1w0k", "2ck3", "2f43", "2hld", "2jdi", "2jiz", "2jj1", "2jj2"...
505
[ "PUB00020611", "PUB00020612", "PUB00025941" ]
[ "12745923", "12885621", "11377200" ]
[ "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review).", "The unbinding of ATP from F1-ATPase.", "Crystal structure of riboflavin synthase." ]
[ 2003, 2003, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1423, 52134, 30532, 553, 1173 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 21, 2, 3, 9, 2, 11, 7, 3, 23, 10, 3, 3, 28 ]
13
true
Homologous_superfamily
ATP synthase subunit alpha, N-terminal domain-like superfamily
ATP synthase subunit alpha, N-terminal domain-like superfamily
ATP_synth_asu-like_sf
8
IPR023367
23,367
Peptidase M42, domain 2
Peptidase_M42_dom2
Homologous_superfamily
18,553
false
false
This entry represents the β barrel structural domain (sometimes annotated as domain 2) found in bacterial M42 peptidases.
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.40.30.40" ]
[ "" ]
[ 18553 ]
1
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "3.4.11.-", "PWY-6423", "PWY-7694", "PWY-7954" ]
[ "EC:3.4.11.-", "METACYC:PWY-6423", "METACYC:PWY-7694", "METACYC:PWY-7954" ]
4
[ "1vhe", "1vho", "1xfo", "1y0r", "1y0y", "1ylo", "2cf4", "2fvg", "2gre", "2pe3", "2wyr", "2wzn", "3isx", "3kl9", "4p6y", "4wwv", "4x8i", "5ds0", "5l6z", "5ne6", "5ne7", "5ne8", "5ne9", "6f3k", "6nw5", "6r8n" ]
26
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured marine phage" ]
[ 1104, 17240, 21, 187, 1 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 3 ]
2
true
Homologous_superfamily
Peptidase M42, domain 2
Peptidase M42, domain 2
Peptidase_M42_dom2
2
IPR023368
23,368
Uncharacterised protein family UPF0066, conserved site
UPF0066_cons_site
Conserved_site
6,811
false
false
This conserved site is found in proteins belonging to the uncharacterised protein family UPF0066. It is found in the central part of the tsaA-like domain ( ).
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01318" ]
[ "TSAA_1" ]
[ 6811 ]
1
[]
[]
[]
0
[ "1xqb", "2nv4", "7btu", "7btz", "7bu1" ]
5
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 399, 5857, 490, 65 ]
4
[ "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 2, 5 ]
4
true
Conserved_site
Uncharacterised protein family UPF0066, conserved site
Uncharacterised protein family UPF0066, conserved site
UPF0066_cons_site
3
IPR023370
23,370
TrmO-like, N-terminal domain
TrmO-like_N
Domain
12,878
false
false
TrmO (also known as TsaA or YaeB) is a RNA methyltransferase responsible for N6-methylation of N6-threonylcarbamoyladenosine in tRNAs. It has a unique single-sheeted β-barrel structure and represent a new category of AdoMet-dependent methyltransferases [ ]. The following uncharacterised proteins have been shown to be e...
[]
[]
[]
0
[ "PFAM", "PROFILE", "NCBIFAM", "CDD" ]
[ "PF01980", "PS51668", "TIGR00104", "cd09281" ]
[ "TrmO_N", "TSAA_2", "tRNA_TsaA", "UPF0066" ]
[ 12749, 12861, 10179, 11794 ]
4
[]
[]
[]
0
[ "1xqb", "2nv4", "3okx", "7btu", "7btz", "7bu1" ]
6
[ "PUB00086552" ]
[ "25063302" ]
[ "Discovery of the β-barrel-type RNA methyltransferase responsible for N6-methylation of N6-threonylcarbamoyladenosine in tRNAs." ]
[ 2014 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 780, 9465, 2435, 198 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 7, 2, 3, 1, 7, 2, 3, 5, 13 ]
9
true
Domain
TrmO-like, N-terminal domain
TrmO-like, N-terminal domain
TrmO-like_N
6
IPR023372
23,372
Restriction endonuclease, type II, EcoRII, N-terminal
Rest_endonuc_II_EcoRII_N
Domain
703
false
false
There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi...
[]
[]
[]
0
[ "PFAM" ]
[ "PF09217" ]
[ "EcoRII-N" ]
[ 703 ]
1
[]
[]
[]
0
[ "1na6", "3hqf" ]
2
[ "PUB00029018", "PUB00035691", "PUB00035692", "PUB00035693", "PUB00035694", "PUB00035705", "PUB00035707" ]
[ "14659759", "15770420", "14576294", "11827971", "11557805", "15121719", "12665693" ]
[ "Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold.", "Type II restriction endonucleases: structure and mechanism.", "Diversity of type II restriction endonucleases that require two DNA recognition sites.", "Evolutionary relation...
[ 2004, 2005, 2003, 2002, 2001, 2004, 2003 ]
7
[]
[]
0
0
null
[ "Bacteria", "Cyprideis torosa", "Methanohalophilus portucalensis", "metagenomes" ]
[ 695, 1, 2, 5 ]
4
[]
[]
0
true
Domain
Restriction endonuclease, type II, EcoRII, N-terminal
Restriction endonuclease, type II, EcoRII, N-terminal
Rest_endonuc_II_EcoRII_N
1
IPR023373
23,373
YmcC-like superfamily
YmcC_sf
Homologous_superfamily
3,035
false
false
This superfamily represents the β-barrel structural domain found in YmcC-related proteins, which belong to the DUF2886 family.
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:2.40.360.10", "SSF159270" ]
[ "", "" ]
[ 3027, 3032 ]
2
[]
[]
[]
0
[ "2in5" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "ecological metagenomes" ]
[ 3017, 2, 16 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Homologous_superfamily
YmcC-like superfamily
YmcC-like superfamily
YmcC_sf
3
IPR023374
23,374
AttH-like domain superfamily
AttH-like_dom_sf
Homologous_superfamily
6,142
false
false
This superfamily represents a β barrel domain found in bacterial AttH proteins, as well as in survival factors, such as survival factor 1 (Svf1) .
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.40.370.10" ]
[ "" ]
[ 6142 ]
1
[]
[]
[]
0
[ "2ich", "7a0q", "7a0t" ]
3
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 36, 4842, 1216, 48 ]
4
[ "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1 ]
1
true
Homologous_superfamily
AttH-like domain superfamily
AttH-like domain superfamily
AttH-like_dom_sf
6
IPR023375
23,375
Acetoacetate decarboxylase domain superfamily
ADC_dom_sf
Homologous_superfamily
14,623
false
false
Acetoacetate decarboxylase (ADC) is involved in solventogenesis in certain bacteria, which occurs at the end of the exponential growth phase when there is a metabolic switch from classical sugar fermentation with the production of acetate and butyrate to the re-internalisation and oxidation of these acids to acetate an...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:2.40.400.10", "SSF160104" ]
[ "", "" ]
[ 12967, 14513 ]
2
[ "EC", "METACYC", "METACYC" ]
[ "4.1.1.4", "PWY-6588", "PWY-6876" ]
[ "EC:4.1.1.4", "METACYC:PWY-6588", "METACYC:PWY-6876" ]
3
[ "3bgt", "3bh2", "3bh3", "3c8w", "3cmb", "4jm3", "4jmc", "4jmd", "4jme", "4zbo", "4zbt", "5upb", "6eej" ]
13
[ "PUB00014916", "PUB00014917" ]
[ "11824611", "10972834" ]
[ "Changes in protein synthesis and identification of proteins specifically induced during solventogenesis in Clostridium acetobutylicum.", "Spo0A directly controls the switch from acid to solvent production in solvent-forming clostridia." ]
[ 2002, 2000 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "uncultured virus" ]
[ 700, 10500, 3204, 218, 1 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 5, 3, 9 ]
3
true
Homologous_superfamily
Acetoacetate decarboxylase domain superfamily
Acetoacetate decarboxylase domain superfamily
ADC_dom_sf
7
IPR023376
23,376
YqcC-like domain
YqcC-like_dom
Domain
3,747
false
false
This entry represents the structural domain found in the N-terminal of some tRNA pseudouridine synthase C proteins, as well as other uncharacterised proteins.
[]
[]
[]
0
[ "PFAM" ]
[ "PF04287" ]
[ "DUF446" ]
[ 3747 ]
1
[]
[]
[]
0
[ "2hgk" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 3730, 4, 13 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
YqcC-like domain
YqcC-like domain
YqcC-like_dom
5
IPR023378
23,378
YheA/YmcA-like domain superfamily
YheA/YmcA-like_dom_sf
Homologous_superfamily
8,573
false
false
This domain superfamily is found in a number of proteins including YlbF and YmcA, which are involved in the formation of biofilms [ ].
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.1500.10", "SSF158622" ]
[ "", "" ]
[ 8500, 8568 ]
2
[]
[]
[]
0
[ "2iaz", "2oee", "2oeq", "2pih", "6prh", "6prk" ]
6
[ "PUB00043614" ]
[ "15175311" ]
[ "Genes involved in formation of structured multicellular communities by Bacillus subtilis." ]
[ 2004 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Moazamivirus", "metagenomes" ]
[ 8153, 32, 343, 2, 43 ]
5
[]
[]
0
true
Homologous_superfamily
YheA/YmcA-like domain superfamily
YheA/YmcA-like domain superfamily
YheA/YmcA-like_dom_sf
6
IPR023379
23,379
BART domain
BART_dom
Domain
4,694
false
false
This domain is found in ADP-ribosylation factor-like 2 (ARF2) binding protein, also known as BART. BART binds specifically to ARF2.GTP with a high affinity. However, it does not bind to ARF2.GDP. It is thought that this specific interaction is due to BART being the first identified ARF2-specific effector. The function ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF11527" ]
[ "ARL2_Bind_BART" ]
[ 4694 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-83936", "R-DRE-83936", "R-HSA-83936", "R-MMU-83936", "R-RNO-83936", "R-XTR-83936" ]
[ "REACTOME:R-BTA-83936", "REACTOME:R-DRE-83936", "REACTOME:R-HSA-83936", "REACTOME:R-MMU-83936", "REACTOME:R-RNO-83936", "REACTOME:R-XTR-83936" ]
6
[ "2k0s", "2k9a", "3doe", "3dof", "4zi2", "4zi3" ]
6
[ "PUB00051437", "PUB00053516", "PUB00053517", "PUB00088519" ]
[ "19368893", "10488091", "11809823", "26455799" ]
[ "Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector.", "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization.", "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter.", "T...
[ 2009, 1999, 2002, 2015 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadati" ]
[ 4692, 2 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 2, 8, 5, 13 ]
6
true
Domain
BART domain
BART domain
BART_dom
3
IPR023380
23,380
DsbB-like superfamily
DsbB-like_sf
Homologous_superfamily
15,784
false
false
Disulphide bonds contribute to folding, maturation, stability, and regulation of proteins, in particular those localized out of the cytosol. Oxidation of selected pairs of cysteines to disulphide in vivo requires cellular factors present in the bacterial periplasmic space or in the endoplasmic reticulum of eukaryotic c...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.1550.10", "SSF158442" ]
[ "", "" ]
[ 15652, 15779 ]
2
[]
[]
[]
0
[ "2hi7", "2k73", "2k74", "2leg", "2ltq", "2zup", "2zuq", "3e9j", "6wvf" ]
9
[ "PUB00008228", "PUB00008229", "PUB00014003", "PUB00041412", "PUB00054232" ]
[ "8430071", "7957076", "12524212", "17110337", "12415301" ]
[ "A pathway for disulfide bond formation in vivo.", "Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation.", "Protein disulfide bond formation in prokaryotes.", "Crystal structure of the DsbB-DsbA complex reveals a mechanism of ...
[ 1993, 1994, 2003, 2006, 2002 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacillus phage SPbeta", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 187, 1, 15395, 18, 183 ]
5
[ "Escherichia coli (strain K12)", "Zea mays" ]
[ 1, 1 ]
2
true
Homologous_superfamily
DsbB-like superfamily
DsbB-like superfamily
DsbB-like_sf
9
IPR023381
23,381
YP001051499.1-like domain superfamily
YP001051499.1-like_dom_sf
Homologous_superfamily
2,859
false
false
This domain superfamily is found in a family of uncharacterised proteins including protein YP_001051499.1 from Shewanella baltica.
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.20.1590.10" ]
[ "" ]
[ 2859 ]
1
[]
[]
[]
0
[ "2q9r", "3f7c" ]
2
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 2847, 7, 5 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Homologous_superfamily
YP001051499.1-like domain superfamily
YP001051499.1-like domain superfamily
YP001051499.1-like_dom_sf
3
IPR023382
23,382
tRNA-specific 2-thiouridylase MnmA-like, central domain superfamily
MnmA-like_central_sf
Homologous_superfamily
29,971
false
false
This entry represents the central PRC-barrel domain of tRNA-specific 2-thiouridylase MnmA and similar proteins from bacteria and eukaryotes. MnmA catalyses the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s2U34 [ , ].
[ "GO:0016783" ]
[ "sulfurtransferase activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:2.30.30.280" ]
[ "" ]
[ 29971 ]
1
[ "EC", "METACYC", "METACYC", "REACTOME" ]
[ "2.8.1.13", "PWY-7887", "PWY-7892", "R-HSA-6787450" ]
[ "EC:2.8.1.13", "METACYC:PWY-7887", "METACYC:PWY-7892", "REACTOME:R-HSA-6787450" ]
4
[ "2der", "2det", "2deu", "2hma" ]
4
[ "PUB00017420", "PUB00040232" ]
[ "3298234", "16871210" ]
[ "Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities.", "Snapshots of tRNA sulphuration via an adenylated intermediate." ]
[ 1987, 2006 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 26243, 3158, 570 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (s...
[ 6, 1, 2, 2, 1, 4, 1, 4, 3, 1, 1, 6 ]
12
true
Homologous_superfamily
tRNA-specific 2-thiouridylase MnmA-like, central domain superfamily
tRNA-specific 2-thiouridylase MnmA-like, central domain superfamily
MnmA-like_central_sf
5
IPR023383
23,383
Ferredoxin, chloroplast transit peptide
Ferredoxin_transit_pept
Domain
17
false
false
This entry represent the N-terminal transit peptide of a number of algal petF genes. The peptide is removed during transit into the chloroplast lumen.
[]
[]
[]
0
[ "PFAM" ]
[ "PF11591" ]
[ "2Fe-2S_Ferredox" ]
[ 17 ]
1
[]
[]
[]
0
[ "1fct", "7wzn" ]
2
[ "PUB00028492", "PUB00054235" ]
[ "8174712", "17660315" ]
[ "NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution.", "Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii." ]
[ 1994, 2007 ]
2
[]
[]
0
0
null
[ "Chlamydomonadales" ]
[ 17 ]
1
[]
[]
0
true
Domain
Ferredoxin, chloroplast transit peptide
Ferredoxin, chloroplast transit peptide
Ferredoxin_transit_pept
7
IPR023384
23,384
Bacteriocin, class IIa, conserved site
Bacteriocin_IIa_CS
Conserved_site
195
false
false
Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, often termed bacteriocins. One important and well studied class of bacteriocins is the class IIa or pediocin-like bacteriocins produced by lactic acid bacteria. All class IIa bacteriocins are produced by food-associated strains, isolate...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS60030" ]
[ "BACTERIOCIN_IIA" ]
[ 195 ]
1
[]
[]
[]
0
[ "1cw5", "1cw6", "1og7", "1ohm", "1ohn", "1ry3", "2a2b", "2leu", "2n4k", "3leu", "5ukz", "7vly", "7xno", "7xtg" ]
14
[ "PUB00033828", "PUB00033829", "PUB00033830" ]
[ "16232543", "15611086", "16059970" ]
[ "Class IIa bacteriocins from lactic acid bacteria: antibacterial activity and food preservation.", "The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial sp...
[ 1999, 2005, 2005 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "uncultured prokaryote" ]
[ 187, 7, 1 ]
3
[]
[]
0
true
Conserved_site
Bacteriocin, class IIa, conserved site
Bacteriocin, class IIa, conserved site
Bacteriocin_IIa_CS
4
IPR023385
23,385
YopX-like, C-terminal
YopX-like_C
Homologous_superfamily
3,333
false
false
This superfamily represents the β barrel domain found in bacterial YopX and related proteins. It is found towards the C terminus.
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.30.30.290" ]
[ "" ]
[ 3333 ]
1
[]
[]
[]
0
[ "2ox7", "2p84", "2qyz" ]
3
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Methanobacteriota", "Opisthokonta", "Viruses", "metagenomes" ]
[ 2489, 5, 4, 580, 255 ]
5
[]
[]
0
true
Homologous_superfamily
YopX-like, C-terminal
YopX-like, C-terminal
YopX-like_C
5
IPR023387
23,387
DUF1653-like domain
DUF1653-like_dom
Domain
5,055
false
false
This entry represents the structural domain found in DUF1653, a protein family of unknown function.
[]
[]
[]
0
[ "PFAM" ]
[ "PF07866" ]
[ "DUF1653" ]
[ 5055 ]
1
[]
[]
[]
0
[ "3be3" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 4918, 2, 6, 71, 58 ]
5
[]
[]
0
true
Domain
DUF1653-like domain
DUF1653-like domain
DUF1653-like_dom
9
IPR023388
23,388
Bacteriocin class IIa domain superfamily
Bacteriocin_IIa_dom_sf
Homologous_superfamily
252
false
false
This superfamily represents a domain found in class II bacteriocins. It consists of a well-defined central helical structure and a disordered N terminus, as described for carnobacteriocin B2, a type IIa bacteriocin [ ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.20.5.130" ]
[ "" ]
[ 252 ]
1
[]
[]
[]
0
[ "1cw5", "1cw6", "1og7", "1ohm", "1ohn", "1ry3", "2a2b", "2leu", "2ljq", "2ljt", "2n4k", "3leu", "5ukz", "7vly", "7xno", "7xtg" ]
16
[ "PUB00021358" ]
[ "10569926" ]
[ "Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Bacteria", "uncultured prokaryote" ]
[ 250, 2 ]
2
[]
[]
0
true
Homologous_superfamily
Bacteriocin class IIa domain superfamily
Bacteriocin class IIa domain superfamily
Bacteriocin_IIa_dom_sf
9
IPR023390
23,390
Bacteriophage M13, G8P, capsid domain superfamily
Phage_M13_G8P_capsid_dom_sf
Homologous_superfamily
178
false
false
This superfamily represents the capsid domain of the Inoviridae. The type example is bacteriophage M13 Gp8 (capsid or major coat protein); which forms the baseplate structural protein. It consists largely of an α-helix with a slight curve [ , ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.20.5.80" ]
[ "" ]
[ 178 ]
1
[]
[]
[]
0
[ "1fdm", "1hgv", "1hgz", "1hh0", "1ifd", "1ifi", "1ifj", "1ifk", "1ifl", "1mzt", "1nh4", "2c0w", "2c0x", "2cpb", "2cps", "2hi5", "2mjz", "6a7f", "8b3o", "8b3p", "8b3q", "8ch5", "8ixj", "8ixk", "8ixl", "8jwt", "8jww", "8jwx" ]
28
[ "PUB00010511", "PUB00028619" ]
[ "8289247", "11371161" ]
[ "Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe.", "The protein capsid of filamentous bacteriophage PH75 from Thermus thermophilus." ]
[ 1994, 2001 ]
2
[]
[]
0
0
null
[ "Bacteria", "Tubulavirales", "ecological metagenomes" ]
[ 154, 21, 3 ]
3
[]
[]
0
true
Homologous_superfamily
Bacteriophage M13, G8P, capsid domain superfamily
Bacteriophage M13, G8P, capsid domain superfamily
Phage_M13_G8P_capsid_dom_sf
2
IPR023391
23,391
Protein translocase SecE domain superfamily
Prot_translocase_SecE_dom_sf
Homologous_superfamily
5,385
false
false
The Sec61 complex (eukaryotes) or SecY complex (prokaryotes) forms a conserved heterotrimeric integral membrane protein complex and forms a protein-conducting channel that allows polypeptides to be transferred across (or integrated into) the endoplasmic reticulum (eukaryotes) or across the cytoplasmic membrane (prokary...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.5.820", "SSF103456" ]
[ "", "" ]
[ 5368, 5235 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9609523", "R-CEL-9609523", "R-CFA-9609523", "R-DDI-9609523", "R-DME-9609523", "R-HSA-1236974", "R-HSA-1799339", "R-HSA-9609523", "R-MMU-9609523", "R-SCE-9609523", "R-SPO-9609523" ]
[ "REACTOME:R-BTA-9609523", "REACTOME:R-CEL-9609523", "REACTOME:R-CFA-9609523", "REACTOME:R-DDI-9609523", "REACTOME:R-DME-9609523", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-9609523", "REACTOME:R-MMU-9609523", "REACTOME:R-SCE-9609523", "REACTOME:R-SPO-9609523" ]
11
[ "1rh5", "1rhz", "2ww9", "2wwa", "2wwb", "2yxq", "2yxr", "3bo0", "3bo1", "3dkn", "3j7q", "3j7r", "3jc2", "3mp7", "4cg5", "4cg6", "4cg7", "4v4n", "4v7i", "5a6u", "6ftg", "6fti", "6ftj", "6n3q", "6nd1", "6r7q", "6w6l", "6z3t", "7aft", "7kah", "7kai", "7kaj"...
69
[ "PUB00022601", "PUB00028068" ]
[ "14661030", "11597451" ]
[ "X-ray structure of a protein-conducting channel.", "The Sec protein-translocation pathway." ]
[ 2004, 2001 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 867, 18, 4468, 32 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 8, 1, 1, 6, 1, 4, 1, 6, 11, 1, 1, 8 ]
12
true
Homologous_superfamily
Protein translocase SecE domain superfamily
Protein translocase SecE domain superfamily
Prot_translocase_SecE_dom_sf
5
IPR023392
23,392
Mitochondrial outer membrane translocase complex, Tom20 domain superfamily
Tom20_dom_sf
Homologous_superfamily
4,109
false
false
The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents. These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of ...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.20.960.10", "SSF47157" ]
[ "", "" ]
[ 4085, 4099 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-5205685", "R-BTA-5689880", "R-CEL-5205685", "R-CEL-5689880", "R-DRE-5205685", "R-DRE-5689880", "R-HSA-1268020", "R-HSA-5205685", "R-HSA-5689880", "R-MMU-5205685", "R-MMU-5689880", "R-RNO-5205685", "R-RNO-5689880", "R-SCE-5205685", "R-SPO-5205685", "R-SPO-5689880", "R-XTR-52056...
[ "REACTOME:R-BTA-5205685", "REACTOME:R-BTA-5689880", "REACTOME:R-CEL-5205685", "REACTOME:R-CEL-5689880", "REACTOME:R-DRE-5205685", "REACTOME:R-DRE-5689880", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-5205685", "REACTOME:R-HSA-5689880", "REACTOME:R-MMU-5205685", "REACTOME:R-MMU-5689880", "REACTOM...
18
[ "1om2", "2v1s", "2v1t", "3awr", "3ax2", "3ax3", "3ax5", "5az6", "5az7", "5az8", "5az9", "7vby", "7vc9", "8uy3", "8xva", "9eih", "9eii", "9eij", "9i7s", "9i7t", "9j79", "9j7a", "9j7b", "9jce" ]
24
[ "PUB00022363", "PUB00054236", "PUB00054237", "PUB00054238", "PUB00054239" ]
[ "10721992", "9442867", "8223428", "9774109", "10519552" ]
[ "Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.", "Mitochondrial preprotein translocase.", "Functional cooperation of mitochondrial protein import receptors in yeast.", "Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see c...
[ 2000, 1997, 1993, 1998, 1999 ]
5
[]
[]
0
0
null
[ "Eukaryota", "Pseudogemmatithrix spongiicola" ]
[ 4108, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 2, 3, 4, 2, 4, 1, 6, 1, 1 ]
9
true
Homologous_superfamily
Mitochondrial outer membrane translocase complex, Tom20 domain superfamily
Mitochondrial outer membrane translocase complex, Tom20 domain superfamily
Tom20_dom_sf
2
IPR023393
23,393
START-like domain superfamily
START-like_dom_sf
Homologous_superfamily
285,464
false
false
This superfamily represents an α/β sandwich structural domain found in a wide variety of protein families, including STAR-related lipid transfer proteins and homeobox-leucine zipper proteins. START (StAR-related lipid-transfer) is a lipid-binding domain in StAR, HD-ZIP and signalling proteins [ ]. StAR (Steroidogenic A...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:3.30.530.20" ]
[ "" ]
[ 285464 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1483191", "R-BTA-1483196", "R-BTA-159418", "R-BTA-1660661", "R-BTA-196108", "R-BTA-77289", "R-BTA-9837999", "R-DDI-1483196", "R-DME-1483226", "R-DME-611105", "R-DME-9864848", "R-DRE-1660661", "R-DRE-196108", "R-DRE-611105", "R-DRE-9837999", "R-DRE-9864848", "R-GGA-196108", "...
[ "REACTOME:R-BTA-1483191", "REACTOME:R-BTA-1483196", "REACTOME:R-BTA-159418", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-196108", "REACTOME:R-BTA-77289", "REACTOME:R-BTA-9837999", "REACTOME:R-DDI-1483196", "REACTOME:R-DME-1483226", "REACTOME:R-DME-611105", "REACTOME:R-DME-9864848", "REACTOME:R-D...
66
[ "1b6f", "1btv", "1bv1", "1e09", "1em2", "1fm4", "1fsk", "1h2o", "1icx", "1ifv", "1jss", "1kcm", "1llt", "1ln1", "1ln2", "1ln3", "1qmr", "1t17", "1t27", "1tw0", "1txc", "1uw5", "1vjh", "1x53", "1xdf", "1xfs", "1xn5", "1xn6", "1xuv", "1z94", "1zxf", "2a1l"...
399
[ "PUB00002877", "PUB00005851", "PUB00007207", "PUB00007208" ]
[ "7961770", "10322415", "11276083", "10802740" ]
[ "The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR).", "START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins.", "Adaptations of the helix-...
[ 1994, 1999, 2001, 2000 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 3101, 164875, 115711, 1, 18, 1758 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 401, 17, 101, 25, 1, 119, 93, 4, 160, 107, 2, 3, 377 ]
13
true
Homologous_superfamily
START-like domain superfamily
START-like domain superfamily
START-like_dom_sf
2
IPR023394
23,394
Sec7, C-terminal domain superfamily
Sec7_C_sf
Homologous_superfamily
44,076
false
false
The Sec7 domain was named after the first protein found to contain such a region [ ]. It has been shown to be linked with guanine nucleotide exchange function [ , ]. The 3D structure of the domain displays several α-helices [ ]. It was found to be associated with other domains involved in guanine nucleotide exchange (e...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.1000.11" ]
[ "" ]
[ 44076 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-199992", "R-CEL-6807878", "R-CEL-6811434", "R-HSA-199992", "R-HSA-390471", "R-HSA-5620916", "R-HSA-6807878", "R-HSA-6811434", "R-HSA-6811438", "R-HSA-9768919", "R-MMU-199992", "R-MMU-5620916", "R-MMU-6807878", "R-MMU-6811434", "R-MMU-6811438", "R-RNO-6811438", "R-SCE-199992", ...
[ "REACTOME:R-CEL-199992", "REACTOME:R-CEL-6807878", "REACTOME:R-CEL-6811434", "REACTOME:R-HSA-199992", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-5620916", "REACTOME:R-HSA-6807878", "REACTOME:R-HSA-6811434", "REACTOME:R-HSA-6811438", "REACTOME:R-HSA-9768919", "REACTOME:R-MMU-199992", "REACTOME:R-...
26
[ "1bc9", "1ku1", "1pbv", "1r8m", "1r8q", "1r8s", "1re0", "1s9d", "1xsz", "1xt0", "2r09", "2r0d", "3l8n", "3ltl", "3swv", "4a4p", "4c0a", "4c7p", "4d7q", "4d7r", "4jmi", "4jmo", "4jwl", "4jxh", "4l5m", "4oiy", "4z21", "5nlv", "5nly", "6bbp", "6bbq", "6fae"...
43
[ "PUB00005683", "PUB00005779", "PUB00005806", "PUB00005826", "PUB00005838" ]
[ "3042778", "9072969", "9442017", "9653114", "9868368" ]
[ "SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus.", "Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains.", "Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide ...
[ 1988, 1997, 1998, 1998, 1998 ]
5
[]
[]
0
0
null
[ "Eukaryota", "Pseudomonadota", "metagenomes" ]
[ 44036, 37, 3 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 38, 9, 146, 14, 80, 64, 5, 22, 79, 5, 6, 215 ]
12
true
Homologous_superfamily
Sec7, C-terminal domain superfamily
Sec7, C-terminal domain superfamily
Sec7_C_sf
4
IPR023395
23,395
Mitochondrial carrier protein domain superfamily
MCP_dom_sf
Homologous_superfamily
216,008
false
false
This superfamily represents a structural domain found in mitochondrial carrier proteins. A variety of substrate carrier proteins involved in energy transfer are found in the inner mitochondrial membrane or are integral to the membranes of other eukaryotic organelles such as the peroxisome [ , , , , ]. Such proteins inc...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.50.40.10", "SSF103506" ]
[ "", "" ]
[ 214918, 215942 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-1268020", "R-BTA-166187", "R-BTA-167826", "R-BTA-196819", "R-BTA-352230", "R-BTA-425393", "R-BTA-428643", "R-BTA-71064", "R-BTA-83936", "R-BTA-9837999", "R-BTA-9856872", "R-CEL-1614517", "R-CEL-200425", "R-CEL-428643", "R-CEL-8963693", "R-CEL-9856872", "R-DDI-1268020", "R-DD...
[ "REACTOME:R-BTA-1268020", "REACTOME:R-BTA-166187", "REACTOME:R-BTA-167826", "REACTOME:R-BTA-196819", "REACTOME:R-BTA-352230", "REACTOME:R-BTA-425393", "REACTOME:R-BTA-428643", "REACTOME:R-BTA-71064", "REACTOME:R-BTA-83936", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9856872", "REACTOME:R-CEL-16...
135
[ "1okc", "2c3e", "2lck", "4c9g", "4c9h", "4c9j", "4c9q", "6gci", "7w5z", "8b6h", "8bqs", "8g8w", "8gym", "8gzu", "8hbv", "8hbw", "8j1n", "9fzq" ]
18
[ "PUB00001005", "PUB00001675", "PUB00003301", "PUB00005084", "PUB00005351", "PUB00005407", "PUB00029479", "PUB00101069" ]
[ "8325039", "8206158", "8487299", "8140286", "2158156", "8291088", "14603310", "21785437" ]
[ "The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.", "Mitochondrial carrier proteins.", "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.", "Expansion of the mitochondrial carrie...
[ 1993, 1994, 1993, 1993, 1990, 1993, 2003, 2011 ]
8
[]
[]
0
0
null
[ "Bacteria", "Candidatus Nitrosocosmicus arcticus", "Eukaryota", "Viruses", "metagenomes" ]
[ 146, 1, 215714, 74, 73 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 270, 49, 158, 119, 273, 169, 40, 204, 239, 35, 24, 414 ]
12
true
Homologous_superfamily
Mitochondrial carrier protein domain superfamily
Mitochondrial carrier protein domain superfamily
MCP_dom_sf
5
IPR023397
23,397
S-adenosyl-L-methionine-dependent methyltransferase, MraW, recognition domain superfamily
SAM-dep_MeTrfase_MraW_recog
Homologous_superfamily
29,892
false
false
This domain superfamily is found inserted into bacterial SAM-dependent methyltransferases and is thought to be involved in methyl acceptor selectivity. In contrast with recognition domains found in other methyltransferases, it is inserted into the centre of the protein sequence and has an α orthogonal structure rather ...
[ "GO:0008168" ]
[ "methyltransferase activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:1.10.150.170", "SSF81799" ]
[ "", "" ]
[ 29518, 29828 ]
2
[ "EC" ]
[ "2.1.1.199" ]
[ "EC:2.1.1.199" ]
1
[ "1m6y", "1n2x", "1wg8", "3tka", "6sg9", "6sga", "6sgb", "7pnv", "7pnx", "7pny", "7pnz", "8ipi", "8ipk", "8ipl", "8ipm", "8qrl", "9g5c", "9g5d", "9hny" ]
19
[ "PUB00027239" ]
[ "12824489" ]
[ "Crystal complexes of a predicted S-adenosylmethionine-dependent methyltransferase reveal a typical AdoMet binding domain and a substrate recognition domain." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences", "uncultured marine group II/III euryarchaeote KM3_94_C01" ]
[ 26360, 2900, 1, 630, 1 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 5, 13, 1, 1, 3, 2, 3, 3, 5 ]
9
true
Homologous_superfamily
S-adenosyl-L-methionine-dependent methyltransferase, MraW, recognition domain superfamily
S-adenosyl-L-methionine-dependent methyltransferase, MraW, recognition domain superfamily
SAM-dep_MeTrfase_MraW_recog
4
IPR023398
23,398
Translation Initiation factor eIF- 4e-like
TIF_eIF4e-like
Homologous_superfamily
20,699
false
false
This entry includes a group of eIF4E-like protein. These proteins consist of a curved eight-stranded antiparallel β-sheet, decorated with three helices on the convex face and three smaller helices inserted in connecting loops [ ]. Eukaryotic translation initiation factor 4E (eIF-4E) [ ] is a protein that binds to the c...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.30.760.10", "SSF55418" ]
[ "", "" ]
[ 20625, 20610 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-1169408", "R-CEL-156827", "R-CEL-72649", "R-CEL-72662", "R-CEL-72702", "R-DDI-1169408", "R-DDI-156827", "R-DDI-166208", "R-DDI-72662", "R-DDI-72702", "R-DME-110523", "R-DME-1169408", "R-DME-156827", "R-DME-159227", "R-DME-159230", "R-DME-159231", "R-DME-166208", "R-DME-72649...
[ "REACTOME:R-CEL-1169408", "REACTOME:R-CEL-156827", "REACTOME:R-CEL-72649", "REACTOME:R-CEL-72662", "REACTOME:R-CEL-72702", "REACTOME:R-DDI-1169408", "REACTOME:R-DDI-156827", "REACTOME:R-DDI-166208", "REACTOME:R-DDI-72662", "REACTOME:R-DDI-72702", "REACTOME:R-DME-110523", "REACTOME:R-DME-116940...
72
[ "1ap8", "1ej1", "1ej4", "1ejh", "1ipb", "1ipc", "1l8b", "1rf8", "1wkw", "1ztp", "2gpq", "2idr", "2idv", "2jgb", "2jgc", "2q4k", "2v8w", "2v8x", "2v8y", "2w97", "2wmc", "3am7", "3hxg", "3hxi", "3m93", "3m94", "3tf2", "3u7x", "4axg", "4aza", "4b6u", "4b6v"...
115
[ "PUB00000866", "PUB00001603", "PUB00036324" ]
[ "1733496", "1672854", "9302999" ]
[ "Cap recap: the involvement of eIF-4F in regulating gene expression.", "Combination of Trp and Glu residues for recognition of mRNA cap structure. Analysis of m7G base recognition site of human cap binding protein (IF-4E) by site-directed mutagenesis.", "Structure of translation factor eIF4E bound to m7GDP and ...
[ 1992, 1991, 1997 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 105, 95, 20168, 94, 237 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 17, 6, 26, 18, 27, 30, 5, 3, 28, 1, 2, 18 ]
12
true
Homologous_superfamily
Translation Initiation factor eIF- 4e-like
Translation Initiation factor eIF- 4e-like
TIF_eIF4e-like
9
IPR023399
23,399
Baseplate-like, two-layer sandwich fold
Baseplate-like_2-layer_sand
Homologous_superfamily
2,563
false
false
This entry represents an α/β two layer sandwich found in baseplate proteins and related sequences.
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:3.30.1920.10" ]
[ "" ]
[ 2563 ]
1
[]
[]
[]
0
[ "1wru", "3cdd", "3d37", "9ki1" ]
4
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Caldiarchaeum subterraneum", "Eukaryota", "Viruses", "metagenomes" ]
[ 2483, 1, 8, 58, 13 ]
5
[]
[]
0
true
Homologous_superfamily
Baseplate-like, two-layer sandwich fold
Baseplate-like, two-layer sandwich fold
Baseplate-like_2-layer_sand
5
IPR023400
23,400
DNA recombination and repair protein RecA, C-terminal, superfamily
RecA_C_sf
Homologous_superfamily
29,694
false
false
The recA gene product is a multifunctional enzyme that plays a role in homologous recombination, DNA repair and induction of the SOS response [ ]. In homologous recombination, the protein functions as a DNA-dependent ATPase, promoting synapsis, heteroduplex formation and strand exchange between homologous DNAs [ ]. Rec...
[]
[]
[]
0
[ "SSF" ]
[ "SSF54752" ]
[ "" ]
[ 29694 ]
1
[]
[]
[]
0
[ "1aa3", "1g18", "1g19", "1mo3", "1mo4", "1mo5", "1mo6", "1n03", "1rea", "1u94", "1u98", "1u99", "1ubc", "1ube", "1ubf", "1ubg", "1xms", "1xmv", "1xp8", "2g88", "2odn", "2odw", "2oe2", "2oep", "2oes", "2ofo", "2reb", "2rec", "2zr0", "2zr7", "2zr9", "2zra"...
85
[ "PUB00002285", "PUB00003439", "PUB00003747", "PUB00004797", "PUB00004946", "PUB00037852", "PUB00043276" ]
[ "7592482", "8587109", "1896024", "1518831", "9187054", "15364575", "12045091" ]
[ "Bacterial classifications derived from recA protein sequence comparisons.", "The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.", "Characterization of recA genes and recA mutants of Rhizobium meliloti and Rhizobiu...
[ 1995, 1995, 1991, 1992, 1997, 2004, 2002 ]
7
[]
[]
0
0
null
[ "Bacteria", "Candidatus Methanofastidiosum methylothiophilum", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 27100, 1, 1877, 129, 587 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 12, 1, 10, 22 ]
4
true
Homologous_superfamily
DNA recombination and repair protein RecA, C-terminal, superfamily
DNA recombination and repair protein RecA, C-terminal, superfamily
RecA_C_sf
5
IPR023401
23,401
Ornithine cyclodeaminase, N-terminal
ODC_N
Homologous_superfamily
26,318
false
false
This entry represents the N-terminal domain of the ornithine cyclodeanimase family. This is an α/β two layer sandwich domain. Members of this family includes ornithine cyclodeanimase [ ], alanine dehydrogenase from Archaeoglobus [ ] and human cytosolic 3,5,39-triiodo-L-thyronine-binding protein, also called mu-crystall...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:3.30.1780.10" ]
[ "" ]
[ 26318 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-71064", "R-DDI-71064", "R-HSA-71064", "R-MMU-71064", "R-RNO-71064", "R-SCE-71064", "R-SPO-71064" ]
[ "REACTOME:R-BTA-71064", "REACTOME:R-DDI-71064", "REACTOME:R-HSA-71064", "REACTOME:R-MMU-71064", "REACTOME:R-RNO-71064", "REACTOME:R-SCE-71064", "REACTOME:R-SPO-71064" ]
7
[ "1omo", "1u7h", "1vll", "1x7d", "2i99", "3hdj", "4bv8", "4bv9", "4bva", "4m54", "4mp3", "4mp6", "4mp8", "4mpd", "5gzi", "5gzj", "5gzl", "5gzm", "5yu0", "5yu1", "5yu3", "5yu4", "6rqa", "6t3e", "7rbp", "8h8p", "8j1c", "8j1g" ]
28
[ "PUB00029492", "PUB00031693", "PUB00047686" ]
[ "15313611", "15518536", "17242435" ]
[ "Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin.", "Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.", "Crystal structure of human micro-crystallin complexed...
[ 2004, 2004, 2007 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1328, 20608, 4059, 2, 321 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "...
[ 5, 3, 1, 5, 2, 1, 2, 4, 1, 1, 5 ]
11
true
Homologous_superfamily
Ornithine cyclodeaminase, N-terminal
Ornithine cyclodeaminase, N-terminal
ODC_N
3
IPR023403
23,403
Uncharacterised protein MG237, N-terminal
Uncharacterised_MG237_N
Homologous_superfamily
7
false
false
This superfamily represents the N-terminal domain of hypothetical protein mg237 and homologues. It consists of four α helices [ ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.20.1480.10" ]
[ "" ]
[ 7 ]
1
[]
[]
[]
0
[ "1td6" ]
1
[ "PUB00037695" ]
[ "15562512" ]
[ "Crystal structure of the conserved hypothetical protein MPN330 (GI: 1674200) from Mycoplasma pneumoniae." ]
[ 2005 ]
1
[]
[]
0
0
null
[ "Mycoplasmoides" ]
[ 7 ]
1
[]
[]
0
true
Homologous_superfamily
Uncharacterised protein MG237, N-terminal
Uncharacterised protein MG237, N-terminal
Uncharacterised_MG237_N
9
IPR023404
23,404
Radical SAM, alpha/beta horseshoe
rSAM_horseshoe
Homologous_superfamily
115,606
false
false
Radical SAM domains catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. Evidence exists that these proteins generate a radical species by reductive cleavage of S:-adenosylmethionine (SAM) through an unusual Fe-S...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:3.80.30.20" ]
[ "" ]
[ 115606 ]
1
[ "EC", "REACTOME" ]
[ "2.8.4", "R-HSA-6782315" ]
[ "EC:2.8.4", "REACTOME:R-HSA-6782315" ]
2
[ "2qgq", "4jc0", "5ul2", "5ul3", "5ul4", "6fd2", "6wte", "6wtf", "7kdx", "7kdy", "7mjv", "7mjw", "7mjx", "7mjy", "7mjz", "9ccb" ]
16
[ "PUB00010539", "PUB00015124", "PUB00054243" ]
[ "11222759", "15317939", "20007320" ]
[ "Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.", "Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybd...
[ 2001, 2004, 2010 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3252, 102318, 6859, 26, 3151 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 12, 2, 4, 2, 4, 7, 2, 6, 11, 11 ]
10
true
Homologous_superfamily
Radical SAM, alpha/beta horseshoe
Radical SAM, alpha/beta horseshoe
rSAM_horseshoe
8
IPR023405
23,405
DNA topoisomerase, type IA, core domain
Topo_IA_core_domain
Homologous_superfamily
62,065
false
false
DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi...
[]
[]
[]
0
[ "SSF" ]
[ "SSF56712" ]
[ "" ]
[ 62065 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "5.6.2.1", "R-CEL-5693607", "R-HSA-5685938", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693607", "R-HSA-5693616", "R-HSA-6804756", "R-HSA-69473", "R-HSA-912446", "R-HSA-9701192", "R-HSA-9704331", "R-HSA-9704646", "R-HSA-9709570", "R-HSA-9709603", "R...
[ "EC:5.6.2.1", "REACTOME:R-CEL-5693607", "REACTOME:R-HSA-5685938", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554", "REACTOME:R-HSA-5693568", "REACTOME:R-HSA-5693579", "REACTOME:R-HSA-5693607", "REACTOME:R-HSA-5693616", "REACTOME:R-HSA-6804756", "REACTOME:R-HSA-69473", "REACTOME:R-HSA-912446...
26
[ "1cy0", "1cy1", "1cy2", "1cy4", "1cy6", "1cy7", "1cy8", "1cy9", "1cyy", "1d6m", "1ecl", "1gku", "1gl9", "1i7d", "1mw8", "1mw9", "2gai", "2gaj", "2o19", "2o54", "2o59", "2o5c", "2o5e", "3pwt", "3px7", "4cgy", "4cht", "4ddt", "4ddu", "4ddv", "4ddw", "4ddx"...
65
[ "PUB00005230", "PUB00005437", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00020798", "PUB00081702", "PUB00081703", "PUB00081704", "PUB00081705" ]
[ "9488644", "7770916", "11395412", "12596227", "12042765", "11239459", "21087076", "20644584", "17722649", "17293019" ]
[ "Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.", "The mechanisms of DNA topoisomerases.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles of DNA topoisomerases: a molecular perspective.",...
[ 1998, 1995, 2001, 2003, 2002, 2001, 2010, 2010, 2007, 2007 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 1309, 48827, 10543, 61, 10, 1315 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 19, 4, 3, 6, 2, 24, 19, 1, 12, 3, 1, 1, 75 ]
13
true
Homologous_superfamily
DNA topoisomerase, type IA, core domain
DNA topoisomerase, type IA, core domain
Topo_IA_core_domain
1
IPR023406
23,406
DNA topoisomerase, type IA, active site
Topo_IA_AS
Active_site
48,054
false
false
This entry represents a number of conserved residues in the region around the active site tyrosine of type IA topoisomerases. DNA topoisomerase I ( ) is one of the two types of enzyme that catalyze the interconversion of topological DNA isomers [ , , ]. Type I topoisomerases act by catalyzing the transient breakage of ...
[ "GO:0003917" ]
[ "DNA topoisomerase type I (single strand cut, ATP-independent) activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00396" ]
[ "TOPO_IA_1" ]
[ 48054 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "5.6.2.1", "R-CEL-5693607", "R-HSA-5685938", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693607", "R-HSA-5693616", "R-HSA-6804756", "R-HSA-69473", "R-HSA-912446", "R-HSA-9701192", "R-HSA-9704331", "R-HSA-9704646", "R-HSA-9709570", "R-HSA-9709603", "R...
[ "EC:5.6.2.1", "REACTOME:R-CEL-5693607", "REACTOME:R-HSA-5685938", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554", "REACTOME:R-HSA-5693568", "REACTOME:R-HSA-5693579", "REACTOME:R-HSA-5693607", "REACTOME:R-HSA-5693616", "REACTOME:R-HSA-6804756", "REACTOME:R-HSA-69473", "REACTOME:R-HSA-912446...
26
[ "1cy0", "1cy1", "1cy2", "1cy4", "1cy6", "1cy7", "1cy8", "1cy9", "1cyy", "1d6m", "1ecl", "1mw8", "1mw9", "2gai", "2gaj", "2o19", "2o54", "2o59", "2o5c", "2o5e", "3pwt", "3px7", "4cgy", "4cht", "4rul", "5d5h", "5gvc", "5gve", "5uj1", "5ujy", "6cq2", "6cqi"...
49
[ "PUB00001050", "PUB00001088", "PUB00005230", "PUB00005437", "PUB00016842", "PUB00020793", "PUB00020794", "PUB00081702", "PUB00081703", "PUB00081704", "PUB00081705" ]
[ "2560656", "7773745", "9488644", "7770916", "11395412", "12596227", "12042765", "21087076", "20644584", "17722649", "17293019" ]
[ "DNA topoisomerases.", "DNA topoisomerases.", "Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.", "The mechanisms of DNA topoisomerases.", "DNA topoisomerases: structure, function, and mechanism.", "Phylogenomics of type II DNA topoisomerases.", "Cellular roles...
[ 1989, 1995, 1998, 1995, 2001, 2003, 2002, 2010, 2010, 2007, 2007 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 750, 39031, 7513, 54, 5, 701 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (s...
[ 18, 3, 3, 3, 2, 6, 12, 8, 3, 1, 1, 51 ]
12
true
Active_site
DNA topoisomerase, type IA, active site
DNA topoisomerase, type IA, active site
Topo_IA_AS
7
IPR023407
23,407
Small ribosomal subunit protein eS27, zinc-binding domain superfamily
Ribosomal_eS27_Zn-bd_dom_sf
Homologous_superfamily
9,148
false
false
This superfamily represents a domain found in the zinc-binding ribosomal protein eS27 (previously known as S27). It consists of a β-sandwich of two three-stranded sheets. This a novel fold due to the uniqueness of the strands arrangement [ ].
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.20.25.100" ]
[ "" ]
[ 9148 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-141444", "R-BTA-156827", "R-BTA-1799339", "R-BTA-2467813", "R-BTA-2500257", "R-BTA-5663220", "R-BTA-6791226", "R-BTA-68877", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-9648025", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-179...
[ "REACTOME:R-BTA-141444", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-2467813", "REACTOME:R-BTA-2500257", "REACTOME:R-BTA-5663220", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-68877", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72...
107
[ "1qxf", "3j6x", "3j6y", "3j77", "3j78", "3j7a", "3j7p", "3j7r", "3j80", "3j81", "3jag", "3jah", "3jai", "3jaj", "3jam", "3jan", "3jap", "3jbn", "3jbo", "3jbp", "4bts", "4d5l", "4d61", "4kzx", "4kzy", "4kzz", "4u3m", "4u3n", "4u3u", "4u4n", "4u4o", "4u4q"...
622
[ "PUB00030432" ]
[ "15096641" ]
[ "The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold." ]
[ 2004 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 865, 6, 8253, 24 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 12, 1, 4, 1, 6, 8, 1, 7, 22, 2, 1, 8 ]
12
true
Homologous_superfamily
Small ribosomal subunit protein eS27, zinc-binding domain superfamily
Small ribosomal subunit protein eS27, zinc-binding domain superfamily
Ribosomal_eS27_Zn-bd_dom_sf
7
IPR023408
23,408
Mechanosensitive ion channel MscS, beta-domain superfamily
MscS_beta-dom_sf
Homologous_superfamily
94,297
false
false
Mechanosensitive (MS) channels provide protection against hypo-osmotic shock, responding both to stretching of the cell membrane and to membrane depolarisation. They are present in the membranes of organisms from the three domains of life: bacteria, archaea, and eukarya [ ]. There are two families of MS channels: large...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.30.30.60" ]
[ "" ]
[ 94297 ]
1
[]
[]
[]
0
[ "1vie", "1vif", "2gqv", "2oau", "2p4t", "2rh2", "2rk1", "2rk2", "2vv5", "3sfm", "3t9n", "3udc", "4age", "4agf", "4hw9", "4hwa", "5aji", "5y4o", "6lyp", "6nxz", "6ny0", "6pwn", "6pwo", "6pwp", "6rld", "6urt", "6uzh", "6vxm", "6vxn", "6vxp", "6vyk", "6vyl"...
74
[ "PUB00013956", "PUB00013957", "PUB00089654", "PUB00097362", "PUB00101036" ]
[ "12446901", "12626684", "22910366", "25041276", "34376558" ]
[ "Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel.", "Two families of mechanosensitive channel proteins.", "Organellar mechanosensitive channels in fission yeast regulate the hypo-osmotic shock response.", "Mechanosensitive channels Msy1 and Msy2 are required for ma...
[ 2002, 2003, 2012, 2014, 2021 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3679, 80407, 9186, 9, 1016 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 44, 6, 2, 12, 2, 24 ]
6
true
Homologous_superfamily
Mechanosensitive ion channel MscS, beta-domain superfamily
Mechanosensitive ion channel MscS, beta-domain superfamily
MscS_beta-dom_sf
2
IPR023409
23,409
14-3-3 protein, conserved site
14-3-3_CS
Conserved_site
19,656
false
false
The 14-3-3 proteins are a family of closely related acidic homodimeric proteins of about 30kDa which were first identified as being very abundant in mammalian brain tissues and located preferentially in neurons [ , , ]. The 14-3-3 proteins seem to have multiple biological activities and play a key role in signal transd...
[]
[]
[]
0
[ "PROSITE", "PROSITE" ]
[ "PS00796", "PS00797" ]
[ "1433_1", "1433_2" ]
[ 18383, 16009 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-111447", "R-BTA-2028269", "R-BTA-205025", "R-BTA-2565942", "R-BTA-3371453", "R-BTA-3371511", "R-BTA-3769402", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-392517", "R-BTA-430116", "R-BTA-450604", "R-BTA-512988", "R-BTA-5620912", "R-BTA-5625740", "R-...
[ "REACTOME:R-BTA-111447", "REACTOME:R-BTA-2028269", "REACTOME:R-BTA-205025", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371453", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-3769402", "REACTOME:R-BTA-380259", "REACTOME:R-BTA-380270", "REACTOME:R-BTA-380284", "REACTOME:R-BTA-380320", "REACTOME:R-BT...
242
[ "1a37", "1a38", "1a4o", "1ib1", "1o9c", "1o9d", "1o9e", "1o9f", "1qja", "1qjb", "1ywt", "1yz5", "2b05", "2bq0", "2br9", "2btp", "2c1j", "2c1n", "2c23", "2c63", "2c74", "2npm", "2o02", "2o98", "2v7d", "2wh0", "3axy", "3cu8", "3e6y", "3iqj", "3iqu", "3iqv"...
677
[ "PUB00004213", "PUB00005192", "PUB00005447" ]
[ "7603573", "7939645", "7709434" ]
[ "Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.", "14-3-3: modulators of signaling proteins?", "14-3-3 proteins on the MAP." ]
[ 1995, 1994, 1995 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 2, 19654 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 60, 5, 16, 6, 46, 21, 1, 13, 32, 2, 2, 92 ]
12
true
Conserved_site
14-3-3 protein, conserved site
14-3-3 protein, conserved site
14-3-3_CS
5
IPR023410
23,410
14-3-3 domain
14-3-3_domain
Domain
24,437
false
false
This entry represents the structural domain found in 14-3-3 proteins. The 14-3-3 proteins are a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells [ , ]. These are structurally similar phospho-binding proteins that regulate multiple signaling ...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF00244", "SM00101" ]
[ "14-3-3", "14_3_3" ]
[ 24432, 22999 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-111447", "R-BTA-2028269", "R-BTA-205025", "R-BTA-2565942", "R-BTA-3371453", "R-BTA-3371511", "R-BTA-3769402", "R-BTA-380259", "R-BTA-380270", "R-BTA-380284", "R-BTA-380320", "R-BTA-392517", "R-BTA-430116", "R-BTA-450604", "R-BTA-512988", "R-BTA-5620912", "R-BTA-5625740", "R-...
[ "REACTOME:R-BTA-111447", "REACTOME:R-BTA-2028269", "REACTOME:R-BTA-205025", "REACTOME:R-BTA-2565942", "REACTOME:R-BTA-3371453", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-3769402", "REACTOME:R-BTA-380259", "REACTOME:R-BTA-380270", "REACTOME:R-BTA-380284", "REACTOME:R-BTA-380320", "REACTOME:R-BT...
242
[ "1a37", "1a38", "1a4o", "1ib1", "1o9c", "1o9d", "1o9e", "1o9f", "1qja", "1qjb", "1ywt", "1yz5", "2b05", "2bq0", "2br9", "2btp", "2c1j", "2c1n", "2c23", "2c63", "2c74", "2npm", "2o02", "2o8p", "2o98", "2v7d", "2wh0", "3axy", "3cu8", "3e6y", "3efz", "3iqj"...
700
[ "PUB00003264", "PUB00007085", "PUB00097184" ]
[ "1671102", "11911880", "29915393" ]
[ "Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases.", "How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis.", "The dynamic and stress-adaptive signaling hub of 14-3-3: emerging mechanisms of regulation and context-dependent ...
[ 1991, 2002, 2018 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 5, 24432 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 70, 6, 16, 7, 48, 23, 3, 19, 33, 2, 2, 123 ]
12
true
Domain
14-3-3 domain
14-3-3 domain
14-3-3_domain
8
IPR023411
23,411
Ribonuclease A, active site
RNaseA_AS
Active_site
2,855
false
false
Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [ ]. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cycli...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00127" ]
[ "RNASE_PANCREATIC" ]
[ 2855 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6803157", "R-DRE-418990", "R-DRE-6798695", "R-DRE-6803157", "R-GGA-418990", "R-GGA-6798695", "R-GGA-6803157", "R-HSA-418990", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-9613829", "R-HSA-9615710", "R-HSA-9708296", "R-HSA-9925561", "R-MMU-418990", "R-MMU-6798695", "R-MMU-6803157",...
[ "REACTOME:R-BTA-6803157", "REACTOME:R-DRE-418990", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-6803157", "REACTOME:R-GGA-418990", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-6803157", "REACTOME:R-HSA-418990", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-9613829", "REACTOME:R...
19
[ "11ba", "11bg", "1a2w", "1a4y", "1a5q", "1afk", "1afl", "1afu", "1agi", "1ang", "1aqp", "1awz", "1b1i", "1b1j", "1b6v", "1bc4", "1bel", "1bsr", "1bzq", "1c0b", "1c0c", "1c9v", "1c9x", "1cjq", "1cjr", "1d5d", "1d5e", "1d5h", "1dfj", "1dy5", "1dyt", "1dza"...
515
[ "PUB00000315", "PUB00001546", "PUB00003106", "PUB00004682", "PUB00004932", "PUB00005063" ]
[ "2611266", "3940901", "2473157", "2734298", "3074337", "2710786" ]
[ "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily.", "Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases.", "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclea...
[ 1989, 1986, 1989, 1989, 1988, 1989 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Myoviridae sp. ctwSu1" ]
[ 21, 2833, 1 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 1, 22, 46, 30 ]
5
true
Active_site
Ribonuclease A, active site
Ribonuclease A, active site
RNaseA_AS
7
IPR023412
23,412
Ribonuclease A-domain
RNaseA_domain
Domain
4,491
false
false
Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [ ]. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cycli...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF00074", "SM00092" ]
[ "RnaseA", "RNAse_Pc" ]
[ 4391, 4223 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6803157", "R-DRE-418990", "R-DRE-6798695", "R-DRE-6803157", "R-GGA-418990", "R-GGA-6798695", "R-GGA-6803157", "R-HSA-418990", "R-HSA-6798695", "R-HSA-6803157", "R-HSA-9613829", "R-HSA-9615710", "R-HSA-9708296", "R-HSA-9925561", "R-MMU-418990", "R-MMU-6798695", "R-MMU-6803157",...
[ "REACTOME:R-BTA-6803157", "REACTOME:R-DRE-418990", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-6803157", "REACTOME:R-GGA-418990", "REACTOME:R-GGA-6798695", "REACTOME:R-GGA-6803157", "REACTOME:R-HSA-418990", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-6803157", "REACTOME:R-HSA-9613829", "REACTOME:R...
19
[ "11ba", "11bg", "1a2w", "1a4y", "1a5p", "1a5q", "1afk", "1afl", "1afu", "1agi", "1ang", "1aqp", "1awz", "1b1e", "1b1i", "1b1j", "1b6v", "1bc4", "1bel", "1bsr", "1bzq", "1c0b", "1c0c", "1c8w", "1c9v", "1c9x", "1cjq", "1cjr", "1d5d", "1d5e", "1d5h", "1dfj"...
525
[ "PUB00000315", "PUB00001546", "PUB00003106", "PUB00004682" ]
[ "2611266", "3940901", "2473157", "2734298" ]
[ "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily.", "Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases.", "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclea...
[ 1989, 1986, 1989, 1989 ]
4
[]
[]
0
0
null
[ "Bilateria" ]
[ 4491 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 1, 43, 59, 50 ]
5
true
Domain
Ribonuclease A-domain
Ribonuclease A-domain
RNaseA_domain
1
IPR023415
23,415
Low-density lipoprotein (LDL) receptor class A, conserved site
LDLR_class-A_CS
Conserved_site
74,308
false
false
Low-density lipoprotein (LDL) receptors are the major cholesterol-carrying lipoproteins of plasma. Seven successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein [ ]. Similar domains have been found (see references in [ ]) in other extracellular and mem...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS01209" ]
[ "LDLRA_1" ]
[ 74308 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-166665", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8964026", "R-BTA-8964038", "R-BTA-9758890", "R-BTA-977606", "R-CFA-444821", "R-DME-9758890", "R-DRE-9842663", "R-GGA-8866376", "R-GGA-8866427", "R-HSA-1474228", "R-HSA-166665", "R-HSA-196791", "R-HSA-1971475", "R-HSA-201681", ...
[ "REACTOME:R-BTA-166665", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8964026", "REACTOME:R-BTA-8964038", "REACTOME:R-BTA-9758890", "REACTOME:R-BTA-977606", "REACTOME:R-CFA-444821", "REACTOME:R-DME-9758890", "REACTOME:R-DRE-9842663", "REACTOME:R-GGA-8866376", "REACTOME:R...
100
[ "1ajj", "1cr8", "1d2j", "1d2l", "1f5y", "1f8z", "1j8e", "1ldl", "1ldr", "1n7d", "1v9u", "1xfe", "2fcw", "2fyj", "2fyl", "2gtl", "2i1p", "2jm4", "2knx", "2kny", "2kri", "2lgp", "2m0p", "2m7p", "2m96", "2xrc", "3a7q", "3dpr", "3m0c", "3ojy", "3p5c", "3t5o"...
160
[ "PUB00000086", "PUB00000411", "PUB00000798", "PUB00004868", "PUB00005112" ]
[ "7979249", "7548065", "6091915", "7603991", "3283935" ]
[ "Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP).", "Disulfide bridges of a cysteine-rich repeat of the LDL receptor ligand-binding domain.", "The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its m...
[ 1994, 1995, 1984, 1995, 1988 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 7, 74297, 2, 2 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 30, 226, 120, 193, 131, 149 ]
6
true
Conserved_site
Low-density lipoprotein (LDL) receptor class A, conserved site
Low-density lipoprotein (LDL) receptor class A, conserved site
LDLR_class-A_CS
7
IPR023416
23,416
Transthyretin/hydroxyisourate hydrolase domain
Transthyretin/HIU_hydrolase_d
Domain
16,503
false
false
This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyse the conversion of 5-hydroxyisourat...
[]
[]
[]
0
[ "PFAM", "PANTHER", "SMART" ]
[ "PF00576", "PTHR10395", "SM00095" ]
[ "Transthyretin", "", "TR_THY" ]
[ 16492, 15177, 6212 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-2453902", "R-BTA-6798695", "R-BTA-975634", "R-CEL-3000171", "R-CEL-6798695", "R-CEL-975634", "R-HSA-2453902", "R-HSA-3000171", "R-HSA-6798695", "R-HSA-975634", "R-HSA-977225", "R-HSA-9918449", "R-MMU-2453902", "R-MMU-6798695", "R-MMU-975634", "R-RNO-2453902", "R-RNO-6798695", ...
[ "REACTOME:R-BTA-2453902", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-975634", "REACTOME:R-CEL-3000171", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-975634", "REACTOME:R-HSA-2453902", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-975634", "REACTOME:R-HSA-977225", "REACTOME:R-...
25
[ "1bm7", "1bmz", "1bz8", "1bzd", "1bze", "1dvq", "1dvs", "1dvt", "1dvu", "1dvx", "1dvy", "1dvz", "1e3f", "1e4h", "1e5a", "1eta", "1etb", "1f41", "1f86", "1fh2", "1fhn", "1g1o", "1gke", "1gko", "1ict", "1ie4", "1iii", "1iik", "1ijn", "1kgi", "1kgj", "1oo2"...
488
[ "PUB00001401", "PUB00001752", "PUB00002809", "PUB00034597", "PUB00041243", "PUB00042841", "PUB00071851", "PUB00101389" ]
[ "1833190", "4054629", "8428915", "16098976", "16952372", "16462750", "24422526", "33001386" ]
[ "Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin. Implications for the evolution of structure and function of transthyretin in vertebrates.", "Structure of the chromosomal gene for human serum prealbumin.", "The x-ray crystal structure refinements of normal human transthy...
[ 1991, 1985, 1993, 2005, 2006, 2006, 2014, 2020 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 10987, 5393, 42, 1, 80 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 6, 2, 4, 1, 1, 6, 7, 1, 5, 11, 1, 8 ]
12
true
Domain
Transthyretin/hydroxyisourate hydrolase domain
Transthyretin/hydroxyisourate hydrolase domain
Transthyretin/HIU_hydrolase_d
3
IPR023418
23,418
Transthyretin, thyroxine binding site
Thyroxine_BS
Binding_site
11,964
false
false
Transthyretin (prealbumin) is a thyroid hormone-binding protein that seems to transport thyroxine (T4) from the bloodstream to the brain. It is a protein of about 130 amino acids that assembles as a homotetramer and forms an internal channel that binds thyroxine. In humans, transthyretin is mainly synthesised in the br...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00768" ]
[ "TRANSTHYRETIN_1" ]
[ 11964 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-2453902", "R-BTA-6798695", "R-BTA-975634", "R-CEL-3000171", "R-CEL-6798695", "R-CEL-975634", "R-HSA-2453902", "R-HSA-3000171", "R-HSA-6798695", "R-HSA-975634", "R-HSA-977225", "R-HSA-9918449", "R-MMU-2453902", "R-MMU-6798695", "R-MMU-975634", "R-RNO-2453902", "R-RNO-6798695", ...
[ "REACTOME:R-BTA-2453902", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-975634", "REACTOME:R-CEL-3000171", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-975634", "REACTOME:R-HSA-2453902", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-975634", "REACTOME:R-HSA-977225", "REACTOME:R-...
25
[ "1bm7", "1bmz", "1bz8", "1bzd", "1bze", "1dvq", "1dvs", "1dvt", "1dvu", "1dvx", "1dvy", "1dvz", "1e3f", "1e4h", "1e5a", "1etb", "1f41", "1f86", "1fhn", "1g1o", "1gke", "1gko", "1ict", "1ie4", "1iii", "1iik", "1ijn", "1kgi", "1kgj", "1qab", "1qwh", "1rlb"...
395
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 8464, 3444, 56 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe...
[ 6, 2, 2, 1, 7, 3, 1, 5, 4, 1, 8 ]
11
true
Binding_site
Transthyretin, thyroxine binding site
Transthyretin, thyroxine binding site
Thyroxine_BS
2
IPR023419
23,419
Transthyretin, conserved site
Transthyretin_CS
Conserved_site
8,045
false
false
Transthyretin (prealbumin) is a thyroid hormone-binding protein that seems to transport thyroxine (T4) from the bloodstream to the brain. It is a protein of about 130 amino acids that assembles as a homotetramer and forms an internal channel that binds thyroxine. In humans, transthyretin is mainly synthesized in the br...
[]
[]
[]
0
[ "PROSITE" ]
[ "PS00769" ]
[ "TRANSTHYRETIN_2" ]
[ 8045 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-2453902", "R-BTA-6798695", "R-BTA-975634", "R-CEL-3000171", "R-CEL-6798695", "R-CEL-975634", "R-HSA-2453902", "R-HSA-3000171", "R-HSA-6798695", "R-HSA-975634", "R-HSA-977225", "R-HSA-9918449", "R-MMU-2453902", "R-MMU-6798695", "R-MMU-975634", "R-RNO-2453902", "R-RNO-6798695", ...
[ "REACTOME:R-BTA-2453902", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-975634", "REACTOME:R-CEL-3000171", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-975634", "REACTOME:R-HSA-2453902", "REACTOME:R-HSA-3000171", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-975634", "REACTOME:R-HSA-977225", "REACTOME:R-...
22
[ "1bm7", "1bmz", "1bz8", "1bzd", "1bze", "1dvq", "1dvs", "1dvt", "1dvu", "1dvx", "1dvy", "1dvz", "1e3f", "1e4h", "1e5a", "1eta", "1etb", "1f41", "1f86", "1fh2", "1fhn", "1g1o", "1gke", "1gko", "1ict", "1ie4", "1kgi", "1kgj", "1qab", "1qwh", "1rlb", "1tfp"...
456
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Halobacteriales", "unclassified sequences" ]
[ 5532, 2422, 42, 49 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 6, 2, 1, 5, 6, 1, 9, 1 ]
8
true
Conserved_site
Transthyretin, conserved site
Transthyretin, conserved site
Transthyretin_CS
5
IPR023420
23,420
Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily
Kinase_SYK/ZAP-70_inter-SH2_sf
Homologous_superfamily
2,093
false
false
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra...
[ "GO:0004715" ]
[ "non-membrane spanning protein tyrosine kinase activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:1.10.930.10" ]
[ "" ]
[ 2093 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.10.2", "R-GGA-114604", "R-GGA-2029481", "R-GGA-2029482", "R-GGA-2029485", "R-GGA-2424491", "R-GGA-354192", "R-GGA-912631", "R-GGA-9674555", "R-GGA-9705462", "R-GGA-983695", "R-HSA-114604", "R-HSA-202430", "R-HSA-202433", "R-HSA-2029481", "R-HSA-2029482", "R-HSA-2029485", "R-HS...
[ "EC:2.7.10.2", "REACTOME:R-GGA-114604", "REACTOME:R-GGA-2029481", "REACTOME:R-GGA-2029482", "REACTOME:R-GGA-2029485", "REACTOME:R-GGA-2424491", "REACTOME:R-GGA-354192", "REACTOME:R-GGA-912631", "REACTOME:R-GGA-9674555", "REACTOME:R-GGA-9705462", "REACTOME:R-GGA-983695", "REACTOME:R-HSA-114604"...
72
[ "1a81", "1m61", "2oq1", "2ozo", "4fl2", "4fl3", "4k2r", "4xz0", "4xz1", "7q5t", "7q5u", "7q5w", "7q63", "7sa7" ]
14
[ "PUB00005115", "PUB00015362", "PUB00015714", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00042254", "PUB00052410", "PUB00052411", "PUB00052412", "PUB00052529", "PUB00052530", "PUB00052531" ]
[ "3291115", "12368087", "1423621", "12471243", "15078142", "15320712", "7659156", "19275641", "16700535", "15845350", "19592646", "19670961", "8124727" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain.", "The protein kinase complement of the human genome.", "High-through...
[ 1988, 2002, 1992, 2002, 2004, 2004, 1995, 2009, 2006, 2005, 2009, 2009, 1994 ]
13
[]
[]
0
0
null
[ "Vertebrata" ]
[ 2093 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 7, 6, 9 ]
4
true
Homologous_superfamily
Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily
Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily
Kinase_SYK/ZAP-70_inter-SH2_sf
4
IPR023421
23,421
Axin interactor, dorsalization-associated protein, N-terminal
AIDA_N
Domain
1,178
false
false
This entry represents the N-terminal domain of the axin interactor, dorsalization-associated protein family AIDA [ ]. AIDA acts as a ventralizing factor during embryogenesis. It inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. This in turn antagonizes a Wnt/beta-catenin-indepe...
[]
[]
[]
0
[ "PFAM" ]
[ "PF08910" ]
[ "Aida_N" ]
[ 1178 ]
1
[]
[]
[]
0
[ "1ug7" ]
1
[ "PUB00053882" ]
[ "17681137" ]
[ "A beta-catenin-independent dorsalization pathway activated by Axin/JNK signaling and antagonized by aida." ]
[ 2007 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 1178 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 2, 5 ]
4
true
Domain
Axin interactor, dorsalization-associated protein, N-terminal
Axin interactor, dorsalization-associated protein, N-terminal
AIDA_N
9
IPR023424
23,424
Oxaloacetate decarboxylase, gamma chain
OadG
Family
2,962
false
false
Oxaloacetate decarboxylases (OAD) catalyse the formation of pyruvate and CO 2 from oxaloacetate which utilises the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. They are formed of three subunits; the alpha, beta and gamma subunits [ , ]. This entry represents the g...
[]
[]
[]
0
[ "HAMAP" ]
[ "MF_00404" ]
[ "OadG" ]
[ 2962 ]
1
[ "EC" ]
[ "7.2.4.2" ]
[ "EC:7.2.4.2" ]
1
[ "6iva", "6iww" ]
2
[ "PUB00019952", "PUB00099625" ]
[ "2549031", "32459174" ]
[ "The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma.", "Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump." ]
[ 1989, 2020 ]
2
[ "IPR005899" ]
[]
1
0
1
[ "Bacteria", "ecological metagenomes" ]
[ 2944, 18 ]
2
[]
[]
0
true
Family
Oxaloacetate decarboxylase, gamma chain
Oxaloacetate decarboxylase, gamma chain
OadG
2
IPR023425
23,425
Galactose-1-phosphate uridyl transferase, class II, conserved site
GalP_uridyl_Trfase_II_CS
Conserved_site
3,329
false
false
Galactose-1-phosphate uridyl transferase (GalT) catalyses the transfer of an uridyldiphosphate group on galactose (or glucose) 1-phosphate. During the reaction, the uridyl moiety links to a histidine residue. In the Escherichia coli enzyme, it has been shown [ ] that two histidine residues separated by a single proline...
[ "GO:0008108" ]
[ "UDP-glucose:hexose-1-phosphate uridylyltransferase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01163" ]
[ "GAL_P_UDP_TRANSF_II" ]
[ 3329 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "2.7.7.12", "PWY-6317", "PWY-6527" ]
[ "EC:2.7.7.12", "METACYC:PWY-6317", "METACYC:PWY-6527" ]
3
[]
0
[ "PUB00002146", "PUB00004352" ]
[ "2066342", "2845364" ]
[ "Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes.", "Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implication...
[ 1991, 1988 ]
2
[]
[]
0
0
null
[ "Bacteria", "Phytophthora kernoviae 00238/432", "unclassified sequences" ]
[ 3321, 1, 7 ]
3
[]
[]
0
true
Conserved_site
Galactose-1-phosphate uridyl transferase, class II, conserved site
Galactose-1-phosphate uridyl transferase, class II, conserved site
GalP_uridyl_Trfase_II_CS
8
IPR023426
23,426
Flap endonuclease 1
Flap_endonuc
Family
5,591
false
false
This entry represents an endonuclease that cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment [ ]. It has 5'-endo-/exonuclease and 5'-pseudo-Y-endonuclease activities and cleaves the junction between single and...
[ "GO:0016788" ]
[ "hydrolase activity, acting on ester bonds" ]
[ "molecular_function" ]
1
[ "HAMAP" ]
[ "MF_00614" ]
[ "Fen" ]
[ 5591 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-110362", "R-BTA-174437", "R-BTA-5651801", "R-BTA-5685939", "R-BTA-69166", "R-CEL-5651801", "R-CEL-5685939", "R-CEL-69166", "R-DDI-110362", "R-DDI-5651801", "R-DDI-69166", "R-DME-5651801", "R-DME-5685939", "R-DME-69166", "R-DRE-110362", "R-GGA-5685939", "R-HSA-110362", "R-HSA...
[ "REACTOME:R-BTA-110362", "REACTOME:R-BTA-174437", "REACTOME:R-BTA-5651801", "REACTOME:R-BTA-5685939", "REACTOME:R-BTA-69166", "REACTOME:R-CEL-5651801", "REACTOME:R-CEL-5685939", "REACTOME:R-CEL-69166", "REACTOME:R-DDI-110362", "REACTOME:R-DDI-5651801", "REACTOME:R-DDI-69166", "REACTOME:R-DME-5...
38
[ "1a76", "1a77", "1b43", "1mc8", "1rxv", "1rxw", "1ul1", "2izo", "3ory", "3q8k", "3q8l", "3q8m", "4wa8", "5fv7", "5k97", "5kse", "5um9", "5zod", "5zoe", "5zof", "5zog", "6tnz", "7qo1", "8yjh", "8yjl", "8yjq", "8yjr", "8yjs", "8yju", "8yjv", "8yjw", "8yjz"...
34
[ "PUB00054247" ]
[ "9852084" ]
[ "Characterization of FEN-1 from Xenopus laevis. cDNA cloning and role in DNA metabolism." ]
[ 1998 ]
1
[ "IPR006084" ]
[ "IPR019973" ]
1
1
0
[ "Archaea", "Bacteria", "Emiliania huxleyi virus 86 (isolate United Kingdom/English Channel/1999)", "Eukaryota", "ecological metagenomes" ]
[ 948, 3, 1, 4614, 25 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 6, 1, 1, 1, 3, 7, 1, 3, 1, 1, 1, 11 ]
12
true
Family
Flap endonuclease 1
Flap endonuclease 1
Flap_endonuc
7
IPR023427
23,427
Acetyl-CoA decarbonylase/synthase complex, gamma subunit, archaea
AcylCoA_decarb/synth_gsu_arc
Family
209
false
false
This entry represents the ACDS gamma subunit in archaea. This group represents the gamma subunit of acetyl-CoA decarbonylase/synthase (ACDS), a complex catalysing the reversible cleavage of acetyl-CoA. Depending on the direction of the reaction this complex allows either growth on acetate as sole carbon and energy sour...
[ "GO:0008168", "GO:0006084" ]
[ "methyltransferase activity", "acetyl-CoA metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP" ]
[ "MF_01136" ]
[ "CdhE" ]
[ 209 ]
1
[ "EC" ]
[ "2.1.1.245" ]
[ "EC:2.1.1.245" ]
1
[]
0
[ "PUB00043434", "PUB00043435", "PUB00043436" ]
[ "14709073", "14664578", "18442256" ]
[ "Chemically distinct Ni sites in the A-cluster in subunit beta of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila: Ni L-edge absorption and X-ray magnetic circular dichroism analyses.", "The A-cluster in subunit beta of the acetyl-CoA decarbonylase/synthase complex from Methanosarcin...
[ 2004, 2003, 2008 ]
3
[ "IPR016218" ]
[]
1
0
1
[ "Archaea", "candidate division TA06 bacterium", "ecological metagenomes" ]
[ 206, 1, 2 ]
3
[]
[]
0
true
Family
Acetyl-CoA decarbonylase/synthase complex, gamma subunit, archaea
Acetyl-CoA decarbonylase/synthase complex, gamma subunit, archaea
AcylCoA_decarb/synth_gsu_arc
6
IPR023428
23,428
Photosystem II PsbX, type 2 subfamily
PSII_PsbX_type_2_subfam
Family
21
false
false
The protein family of PsbX, also known as Photosystem II reaction center protein X, can be divided into two subfamilies; this one, which is found only in some Prochlorococcus, and a shorter one with a wider taxonomic distribution. This entry represents type 1 subfamily, whose members are currently uncharacterised. The ...
[]
[]
[]
0
[ "HAMAP" ]
[ "MF_01388" ]
[ "PSII_PsbX_2" ]
[ 21 ]
1
[]
[]
[]
0
[]
0
[ "PUB00014965", "PUB00015357", "PUB00015358", "PUB00015359", "PUB00015378", "PUB00097583", "PUB00152828" ]
[ "11230572", "12518057", "15100025", "14871485", "11202442", "30076221", "33846594" ]
[ "Targeted disruption of psbX and biochemical characterization of photosystem II complex in the thermophilic cyanobacterium Synechococcus elongatus.", "Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.", "The evolutionary development of the protein complem...
[ 2001, 2003, 2004, 2004, 2000, 2018, 2021 ]
7
[ "IPR009518" ]
[]
1
0
1
[ "Prochlorococcus marinus" ]
[ 21 ]
1
[]
[]
0
true
Family
Photosystem II PsbX, type 2 subfamily
Photosystem II PsbX, type 2 subfamily
PSII_PsbX_type_2_subfam
2
IPR023430
23,430
Peptidase HybD-like domain superfamily
Pept_HybD-like_dom_sf
Homologous_superfamily
16,899
false
false
This superfamily represents a structural domain described for HybD and related proteins such as the germination protease from Gram-positive bacteria. It consists of a twisted five-stranded β-sheet surrounded by four and three helices, respectively, on each side [ ].
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.40.50.1450", "SSF53163" ]
[ "", "" ]
[ 13738, 16859 ]
2
[ "EC" ]
[ "3.4.24.78" ]
[ "EC:3.4.24.78" ]
1
[ "1c8b", "1cfz", "2e85", "2i8l", "2kml", "3pu6", "5ija", "5ttx", "5zby", "7c4x" ]
10
[ "PUB00011023" ]
[ "10331925" ]
[ "Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacillus phage G", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 822, 1, 15784, 7, 285 ]
5
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Homologous_superfamily
Peptidase HybD-like domain superfamily
Peptidase HybD-like domain superfamily
Pept_HybD-like_dom_sf
3
IPR023431
23,431
Photosystem II PsbX, type 1 subfamily
PSII_PsbX_type_1_subfam
Family
755
false
false
The protein family of PsbX, also known as Photosystem II reaction center protein X, can be divided into two subfamilies; this one and a longer one found in most but not all Prochlorococcus. This entry represents type 1 subfamily, whose members are mainly found in cyanobacteria, red algae and diatoms, including members ...
[]
[]
[]
0
[ "HAMAP" ]
[ "MF_01386" ]
[ "PSII_PsbX_1" ]
[ 755 ]
1
[]
[]
[]
0
[ "1s5l", "3kzi", "3wu2", "4fby", "4il6", "4ixq", "4ixr", "4pbu", "4pj0", "4rvy", "4tnh", "4tni", "4tnj", "4tnk", "4ub6", "4ub8", "4v62", "4v82", "4yuu", "5b5e", "5b66", "5e79", "5e7c", "5gth", "5gti", "5kaf", "5kai", "5mx2", "5tis", "5v2c", "5ws5", "5ws6"...
129
[ "PUB00014965", "PUB00015357", "PUB00015358", "PUB00015359", "PUB00015378", "PUB00097583", "PUB00152828", "PUB00153318", "PUB00153319" ]
[ "11230572", "12518057", "15100025", "14871485", "11202442", "30076221", "33846594", "34216574", "34937700" ]
[ "Targeted disruption of psbX and biochemical characterization of photosystem II complex in the thermophilic cyanobacterium Synechococcus elongatus.", "Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.", "The evolutionary development of the protein complem...
[ 2001, 2003, 2004, 2004, 2000, 2018, 2021, 2021, 2022 ]
9
[ "IPR009518" ]
[]
1
0
1
[ "Cyanobacteriota", "Eukaryota" ]
[ 311, 444 ]
2
[]
[]
0
true
Family
Photosystem II PsbX, type 1 subfamily
Photosystem II PsbX, type 1 subfamily
PSII_PsbX_type_1_subfam
3
IPR023432
23,432
Acetyl-CoA decarbonylase/synthase complex subunit beta, archaeal
CO_DH/Ac-CoA_synth_bsu_arc
Family
196
false
false
The carbon monoxide dehydrogenase alpha subunit ( ) catalyses the interconversion of CO and CO2 and the synthesis of acteyl-coA from the methylated corrinoid/iron sulphur protein, CO and CoA. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha(2)epsilon (2...
[ "GO:0043885", "GO:0006084" ]
[ "anaerobic carbon-monoxide dehydrogenase activity", "acetyl-CoA metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP" ]
[ "MF_01138" ]
[ "CdhC" ]
[ 196 ]
1
[ "EC" ]
[ "2.3.1.169" ]
[ "EC:2.3.1.169" ]
1
[ "9c0s", "9c0t" ]
2
[]
[]
[]
[]
0
[ "IPR004461" ]
[]
1
0
1
[ "Archaea", "ecological metagenomes" ]
[ 192, 4 ]
2
[]
[]
0
true
Family
Acetyl-CoA decarbonylase/synthase complex subunit beta, archaeal
Acetyl-CoA decarbonylase/synthase complex subunit beta, archaeal
CO_DH/Ac-CoA_synth_bsu_arc
5
IPR023434
23,434
Argininosuccinate synthase, type 1 subfamily
Arginosuc_synth_type_1_subfam
Family
27,794
false
false
This entry represents argininosuccinate synthase, type 1 subfamily. Argininosuccinate synthase ( ) (AS) is a urea cycle enzyme that catalyses the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate [ , ]. In humans, a defect i...
[ "GO:0004055" ]
[ "argininosuccinate synthase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "CDD" ]
[ "MF_00005", "cd01999" ]
[ "Arg_succ_synth_type1", "ASS" ]
[ 20117, 27794 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.4.5", "PWY-4983", "PWY-4984", "PWY-5", "PWY-5154", "PWY-7400", "R-BTA-70635", "R-HSA-70635", "R-MMU-70635" ]
[ "EC:6.3.4.5", "METACYC:PWY-4983", "METACYC:PWY-4984", "METACYC:PWY-5", "METACYC:PWY-5154", "METACYC:PWY-7400", "REACTOME:R-BTA-70635", "REACTOME:R-HSA-70635", "REACTOME:R-MMU-70635" ]
9
[ "1j1z", "1j20", "1j21", "1k92", "1k97", "1kh1", "1kh2", "1kh3", "1kor", "1kp2", "1kp3", "1vl2", "2nz2", "4nzp", "4u7j", "4xfj", "5us8", "6e5y", "6xnq", "7k5z" ]
20
[ "PUB00001799", "PUB00002066" ]
[ "2123815", "3133361" ]
[ "Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals.", "Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina bark...
[ 1990, 1988 ]
2
[ "IPR001518" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 814, 22234, 4290, 1, 455 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...
[ 4, 1, 1, 1, 4, 3, 2, 3, 3, 1, 1, 10 ]
12
true
Family
Argininosuccinate synthase, type 1 subfamily
Argininosuccinate synthase, type 1 subfamily
Arginosuc_synth_type_1_subfam
5
IPR023435
23,435
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit KbaZ
TagBP_ald_KbaZ
Family
347
false
false
Escherichia coli and other enteric bacteria contain two closely related D-tagatose 1,6-bisphosphate (TagBP)-specific aldolases involved in catabolism of galactitol (genes gatY gatZ) and of N-acetyl-galactosamine and D-galactosamine (genes kbaY, kbaZ, also called agaY, agaZ). The catalytic subunits GatY/KbaY alone are s...
[]
[]
[]
0
[ "HAMAP" ]
[ "MF_01295" ]
[ "Tagatose_aldol_KbaZ" ]
[ 347 ]
1
[]
[]
[]
0
[]
0
[ "PUB00003595", "PUB00014682", "PUB00014683", "PUB00014684", "PUB00092978" ]
[ "8932697", "10931310", "11976750", "8955298", "30879203" ]
[ "Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli.", "Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli.", "Two class II D-tagatose-bisphosphate aldola...
[ 1996, 2000, 2002, 1996, 2019 ]
5
[ "IPR012062" ]
[]
1
0
1
[ "Enterobacterales" ]
[ 347 ]
1
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit KbaZ
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit KbaZ
TagBP_ald_KbaZ
2
IPR023436
23,436
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit GatZ
TagBP_ald_GatZ
Family
914
false
false
Escherichia coli and other enteric bacteria contain two closely related D-tagatose 1,6-bisphosphate (TagBP)-specific aldolases involved in catabolism of galactitol (genes gatY gatZ) and of N-acetyl-galactosamine and D-galactosamine (genes kbaY, kbaZ, also called agaY, agaZ). The catalytic subunits GatY/KbaY alone are s...
[ "GO:0019402" ]
[ "galactitol metabolic process" ]
[ "biological_process" ]
1
[ "HAMAP", "NCBIFAM" ]
[ "MF_01296", "NF011626" ]
[ "Tagatose_aldol_GatZ", "PRK15052.1" ]
[ 795, 913 ]
2
[]
[]
[]
0
[ "2fiq" ]
1
[ "PUB00003595", "PUB00014682", "PUB00014683", "PUB00014684", "PUB00092978" ]
[ "8932697", "10931310", "11976750", "8955298", "30879203" ]
[ "Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli.", "Pathways for the utilization of N-acetyl-galactosamine and galactosamine in Escherichia coli.", "Two class II D-tagatose-bisphosphate aldola...
[ 1996, 2000, 2002, 1996, 2019 ]
5
[ "IPR012062" ]
[]
1
0
1
[ "Pseudomonadota" ]
[ 914 ]
1
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit GatZ
D-tagatose-bisphosphate aldolase, class II, non-catalytic subunit GatZ
TagBP_ald_GatZ
7
IPR023437
23,437
Argininosuccinate synthase, type 2 subfamily
Arg_succ_synth_type2_subfam
Family
4,770
false
false
Argininosuccinate synthase ( ) (AS) is a urea cycle enzyme that catalyses the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate [ , ]. In humans, a defect in the AS gene causes citrullinemia, a genetic disease characterised ...
[ "GO:0004055" ]
[ "argininosuccinate synthase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "NCBIFAM" ]
[ "MF_00581", "NF003779" ]
[ "Arg_succ_synth_type2", "PRK05370.1" ]
[ 4494, 4767 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "6.3.4.5", "PWY-4983", "PWY-4984", "PWY-5", "PWY-5154", "PWY-7400" ]
[ "EC:6.3.4.5", "METACYC:PWY-4983", "METACYC:PWY-4984", "METACYC:PWY-5", "METACYC:PWY-5154", "METACYC:PWY-7400" ]
6
[ "1k92", "1k97", "1kp2", "1kp3", "5us8", "6e5y" ]
6
[ "PUB00001799", "PUB00002066", "PUB00028813", "PUB00104182" ]
[ "2123815", "3133361", "11738042", "10666579" ]
[ "Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals.", "Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina bark...
[ 1990, 1988, 2001, 1999 ]
4
[ "IPR001518" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 4634, 2, 134 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Argininosuccinate synthase, type 2 subfamily
Argininosuccinate synthase, type 2 subfamily
Arg_succ_synth_type2_subfam
8
IPR023444
23,444
L-rhamnonate dehydratase
L-Rhamnon_dehydrat
Family
2,938
false
false
L-rhamnonate dehydratase belongs to the mandelate racemase/muconate lactonizing enzyme family, specifically the RhamD subfamily. L-rhamnonate dehydratase ( ) catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR) L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate+ H(2)O. This reaction proceeds via a ...
[ "GO:0050032" ]
[ "L-rhamnonate dehydratase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "NCBIFAM", "SFLD", "CDD" ]
[ "MF_01288", "NF011968", "SFLDF00006", "cd03327" ]
[ "Rhamnon_dehydrat", "PRK15440.1", "rhamnonate_dehydratase", "MR_like_2" ]
[ 1161, 2406, 2214, 2588 ]
4
[ "EC", "METACYC", "METACYC" ]
[ "4.2.1.90", "PWY-6713", "PWY-6714" ]
[ "EC:4.2.1.90", "METACYC:PWY-6713", "METACYC:PWY-6714" ]
3
[ "2gsh", "2i5q", "2oz3", "2p0i", "2p3z", "3box", "3cxo", "3d46", "3d47", "3ekg", "3fxg", "3sqs", "3ssz", "3stp" ]
14
[]
[]
[]
[]
0
[ "IPR046945" ]
[ "IPR034619" ]
1
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 23, 1727, 1170, 18 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1, 1 ]
2
true
Family
L-rhamnonate dehydratase
L-rhamnonate dehydratase
L-Rhamnon_dehydrat
8
IPR023445
23,445
Arginine exporter protein ArgO, enterobacteria
Arg_export_ArgO_enterobac
Family
1,270
false
false
The arginine exporter protein ArgO is involved in the export of arginine and is important to control the intracellular level of arginine and the correct balance between arginine and lysine [ ].
[ "GO:0061459", "GO:1903826" ]
[ "L-arginine transmembrane transporter activity", "L-arginine transmembrane transport" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "NCBIFAM" ]
[ "MF_01901", "NF006801" ]
[ "ArgO", "PRK09304.1" ]
[ 1240, 1269 ]
2
[]
[]
[]
0
[]
0
[ "PUB00042858" ]
[ "15150242" ]
[ "Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli." ]
[ 2004 ]
1
[ "IPR004777" ]
[]
1
0
1
[ "Bacteria", "human gut metagenome" ]
[ 1269, 1 ]
2
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Arginine exporter protein ArgO, enterobacteria
Arginine exporter protein ArgO, enterobacteria
Arg_export_ArgO_enterobac
3
IPR023447
23,447
Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, ferredoxin-like superfamily
ForMFR_H4MPT_ForTrfase_fd-like
Homologous_superfamily
1,189
false
false
This superfamily represents two ferredoxin-like domains found in Ftr. Formylmethanofuran:tetrahyromethanopterin formyltransferase (Ftr) is involved in C1 metabolism in methanogenic archaea, sulphate-reducing archaea and methylotrophic bacteria. It catalyses the following reversible reaction: N-formylmethanofuran + 5,6,...
[]
[]
[]
0
[ "CATHGENE3D", "SSF" ]
[ "G3DSA:3.30.70.520", "SSF55112" ]
[ "", "" ]
[ 1183, 1188 ]
2
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "2.3.1.101", "PWY-5209", "PWY-7784", "PWY-8305" ]
[ "EC:2.3.1.101", "METACYC:PWY-5209", "METACYC:PWY-7784", "METACYC:PWY-8305" ]
4
[ "1ftr", "1m5h", "1m5s", "2fhj", "2fhk", "6s6y" ]
6
[ "PUB00005787", "PUB00016939", "PUB00016940" ]
[ "9195883", "12192072", "12123819" ]
[ "Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.", "Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.", "Generation of for...
[ 1997, 2002, 2002 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Cladocopium goreaui", "unclassified sequences" ]
[ 356, 775, 2, 56 ]
4
[]
[]
0
true
Homologous_superfamily
Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, ferredoxin-like superfamily
Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, ferredoxin-like superfamily
ForMFR_H4MPT_ForTrfase_fd-like
2
IPR023449
23,449
L-carnitine/gamma-butyrobetaine antiporter CaiT
BCCT_transptr_CaiT
Family
575
false
false
CaiT is a membrane antiporter that catalyses the exchange of L-carnitine for gamma-butyrobetaine, which is the excreted end product of the carnitine pathway [ , ]. CaiT belongs to a family known as BCCT (for Betaine / Carnitine / Choline Transporters) [ ], which are specific for compounds containing a quaternary nitrog...
[ "GO:0044667", "GO:1900749", "GO:1900751", "GO:0016020" ]
[ "(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity", "(R)-carnitine transport", "4-(trimethylammonio)butanoate transport", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "HAMAP" ]
[ "MF_01049" ]
[ "CaiT" ]
[ 575 ]
1
[]
[]
[]
0
[ "2wsw", "2wsx", "3hfx", "4m8j" ]
4
[ "PUB00002302", "PUB00003866", "PUB00053911", "PUB00054251", "PUB00054253", "PUB00061640", "PUB00061643" ]
[ "8752321", "7815937", "9037756", "12163501", "12081978", "20923416", "20357772" ]
[ "Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD.", "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.", "Bacterial carnitine metabolism.", "CaiT of Escherichia coli, a new transporter cata...
[ 1996, 1994, 1997, 2002, 2002, 2010, 2010 ]
7
[ "IPR000060" ]
[]
1
0
1
[ "Enterobacterales" ]
[ 575 ]
1
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
L-carnitine/gamma-butyrobetaine antiporter CaiT
L-carnitine/gamma-butyrobetaine antiporter CaiT
BCCT_transptr_CaiT
5
IPR023450
23,450
Crotonobetainyl-CoA reductase CaiA
CaiA
Family
579
false
false
Many enterobacteria are able to convert carnitine, via crotonobetaine, to gamma-butyrobetaine in the presence of carbon and nitrogen sources under anaerobic conditions [ ]. In Escherichia coli the enzymes involved in this pathway are encoded by the caiTABCDE operon [ ]. The adjacent but divergent fixABCD operon also ap...
[ "GO:0016627", "GO:0009437" ]
[ "oxidoreductase activity, acting on the CH-CH group of donors", "carnitine metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP" ]
[ "MF_01052" ]
[ "CaiA" ]
[ 579 ]
1
[ "EC" ]
[ "1.3.8.13" ]
[ "EC:1.3.8.13" ]
1
[]
0
[ "PUB00003866", "PUB00053911", "PUB00054252", "PUB00054253" ]
[ "7815937", "9037756", "15731894", "12081978" ]
[ "Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.", "Bacterial carnitine metabolism.", "Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp.", "The fixA and fixB genes are necessary...
[ 1994, 1997, 2005, 2002 ]
4
[]
[]
0
0
null
[ "Enterobacterales" ]
[ 579 ]
1
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Crotonobetainyl-CoA reductase CaiA
Crotonobetainyl-CoA reductase CaiA
CaiA
9
IPR023451
23,451
Thymidylate synthase/dCMP hydroxymethylase domain
Thymidate_synth/dCMP_Mease_dom
Domain
29,925
false
false
Thymidylate synthase ( ) [ , ] catalyzes the reductive methylation of dUMP to dTMP with concomitant conversion of 5,10-methylenetetrahydrofolate to dihydrofolate: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP This provides the sole de novo pathway for production of dTMP and is the only enzyme in folate m...
[]
[]
[]
0
[ "PFAM", "CDD" ]
[ "PF00303", "cd00351" ]
[ "Thymidylat_synt", "TS_Pyrimidine_HMase" ]
[ 29924, 27484 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1.45", "PWY-3841", "PWY-7184", "PWY-7187", "PWY-7198", "PWY-7199", "PWY-7210", "R-DME-499943", "R-HSA-499943", "R-HSA-69205", "R-MMU-499943", "R-RNO-499943", "R-SCE-499943", "R-SPO-499943" ]
[ "EC:2.1.1.45", "METACYC:PWY-3841", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7198", "METACYC:PWY-7199", "METACYC:PWY-7210", "REACTOME:R-DME-499943", "REACTOME:R-HSA-499943", "REACTOME:R-HSA-69205", "REACTOME:R-MMU-499943", "REACTOME:R-RNO-499943", "REACTOME:R-SCE-499943", "REACT...
14
[ "1aiq", "1ajm", "1an5", "1aob", "1axw", "1b02", "1b49", "1b5d", "1b5e", "1bdu", "1bid", "1bjg", "1bko", "1bkp", "1bo7", "1bo8", "1bp0", "1bp6", "1bpj", "1bq1", "1bq2", "1bsf", "1bsp", "1ci7", "1ddu", "1dna", "1ev5", "1ev8", "1evf", "1evg", "1f28", "1f4b"...
347
[ "PUB00000031", "PUB00000137", "PUB00002591", "PUB00005100", "PUB00023500", "PUB00030463", "PUB00036705", "PUB00037605", "PUB00081476", "PUB00081477", "PUB00081481" ]
[ "6996564", "2117882", "2243092", "3099389", "10064578", "14555647", "16615077", "16511011", "16162288", "16178783", "7574499" ]
[ "On the mechanism of action of folate- and biopterin-requiring enzymes.", "Cloning and characterization of the thymidylate synthase gene from Lactococcus lactis subsp. lactis.", "Structural and functional analysis of the human thymidylate synthase gene.", "Atomic structure of thymidylate synthase: target for ...
[ 1980, 1990, 1990, 1987, 1999, 2003, 2006, 2005, 2005, 2005, 1995 ]
11
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 536, 21027, 5944, 1901, 517 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 20, 2, 1, 2, 1, 4, 11, 1, 9, 3, 1, 1, 22 ]
13
true
Domain
Thymidylate synthase/dCMP hydroxymethylase domain
Thymidylate synthase/dCMP hydroxymethylase domain
Thymidate_synth/dCMP_Mease_dom
1
IPR023453
23,453
Methionine repressor MetJ domain superfamily
Met_repressor_MetJ_dom_sf
Homologous_superfamily
1,997
false
false
Binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the Escherichia coli methionine repressor (MetJ) leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformatio...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:1.10.140.10" ]
[ "" ]
[ 1997 ]
1
[]
[]
[]
0
[ "1cma", "1cmb", "1cmc", "1mj2", "1mjk", "1mjl", "1mjm", "1mjo", "1mjp", "1mjq" ]
10
[ "PUB00000028", "PUB00006686", "PUB00008039", "PUB00013999", "PUB00037197" ]
[ "8092669", "8026581", "1406951", "1943695", "10986458" ]
[ "The Met repressor-operator complex: DNA recognition by beta-strands.", "Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system.", "Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands.",...
[ 1994, 1994, 1992, 1991, 2000 ]
5
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 1989, 3, 5 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Homologous_superfamily
Methionine repressor MetJ domain superfamily
Methionine repressor MetJ domain superfamily
Met_repressor_MetJ_dom_sf
2
IPR023454
23,454
Small ribosomal subunit protein uS2, archaea
Ribosomal_uS2_arc
Family
845
false
false
This entry represents the archaeal ribosomal protein uS2 family. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in acco...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP" ]
[ "MF_00291_A" ]
[ "Ribosomal_uS2_A" ]
[ 845 ]
1
[]
[]
[]
0
[ "1vi5", "1vi6", "4v4n", "4v6u", "5jb3", "5jbh", "6skf", "6skg", "6sw9", "6swc", "6swd", "6th6", "6tmf", "7zag", "7zah", "7zai", "7zhg", "8hkx", "8hky", "8hkz", "8hl1", "8hl2", "8hl3", "8hl4", "8hl5", "8wkp", "8wq2", "8wq4", "9e71", "9e7f", "9fhl", "9fny"...
45
[ "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "11297922", "11290319", "11114498" ]
[ "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: structural studies of ribosomal proteins." ]
[ 2001, 2001, 2000 ]
3
[ "IPR005707" ]
[]
1
0
1
[ "Archaea", "Candidatus Nomurabacteria bacterium GW2011_GWA2_40_9", "Geodia barretti", "unclassified sequences" ]
[ 830, 1, 1, 13 ]
4
[]
[]
0
true
Family
Small ribosomal subunit protein uS2, archaea
Small ribosomal subunit protein uS2, archaea
Ribosomal_uS2_arc
6
IPR023455
23,455
Dihydroorotate dehydrogenase electron transfer subunit
Dihydroorotate_DHASE_ETsu
Family
4,219
false
false
Dihydroorotate dehydrogenase ( ) (DHOdehase) catalyzes the fourth step in the de novo biosynthesis of pyrimidine, the conversion of dihydroorotate into orotate. DHOdehase is a ubiquitous FAD flavoprotein. In bacteria (gene pyrD), DHOdease is located on the inner side of the cytosolic membrane. In some yeasts, such as i...
[]
[]
[]
0
[ "HAMAP" ]
[ "MF_01211" ]
[ "DHODB_Fe_S_bind" ]
[ 4219 ]
1
[]
[]
[]
0
[ "1ep1", "1ep2", "1ep3", "5ksw", "5ue9" ]
5
[ "PUB00004801", "PUB00033241" ]
[ "1409592", "8910599" ]
[ "Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts.", "The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers." ]
[ 1992, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 196, 3989, 34 ]
3
[]
[]
0
true
Family
Dihydroorotate dehydrogenase electron transfer subunit
Dihydroorotate dehydrogenase electron transfer subunit
Dihydroorotate_DHASE_ETsu
8