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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR010996 | 10,996 | Crossover junction endonuclease MUS81-like, HHH domain | HHH_MUS81 | Domain | 19,687 | false | false | This helix-hairpin-helix (HHH) domain is found in Crossover junction endonuclease MUS81, DNA polymerase beta, as well as in other polymerases and DNA nucleotidylexotransferase (TdT). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF14716"
] | [
"HHH_8"
] | [
19687
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7",
"R-BTA-110362",
"R-BTA-110373",
"R-BTA-110381",
"R-BTA-5649702",
"R-BTA-5651801",
"R-BTA-5689880",
"R-BTA-73930",
"R-DRE-110362",
"R-DRE-110373",
"R-DRE-5649702",
"R-DRE-5693568",
"R-DRE-73930",
"R-HSA-110362",
"R-HSA-110373",
"R-HSA-110381",
"R-HSA-5649702",
"R-HSA-565180... | [
"EC:2.7.7",
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-110373",
"REACTOME:R-BTA-110381",
"REACTOME:R-BTA-5649702",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-73930",
"REACTOME:R-DRE-110362",
"REACTOME:R-DRE-110373",
"REACTOME:R-DRE-5649702",
"REACTOME:R-DRE-5693568",
"... | 46 | [
"1bno",
"1bnp",
"1bpd",
"1bpe",
"1bpx",
"1bpy",
"1bpz",
"1dk2",
"1dk3",
"1huo",
"1huz",
"1jms",
"1kdh",
"1kej",
"1mq2",
"1mq3",
"1nzp",
"1rzt",
"1tv9",
"1tva",
"1xsl",
"1xsn",
"1xsp",
"1zjm",
"1zjn",
"1zqa",
"1zqb",
"1zqc",
"1zqd",
"1zqe",
"1zqf",
"1zqg"... | 706 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
521,
7834,
11007,
60,
265
] | 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,
14,
1,
20,
12,
3,
2,
20,
2,
2,
8
] | 11 | true | Domain | Crossover junction endonuclease MUS81-like, HHH domain | Crossover junction endonuclease MUS81-like, HHH domain | HHH_MUS81 | 2 |
IPR010997 | 10,997 | HRDC-like superfamily | HRDC-like_sf | Homologous_superfamily | 63,018 | false | false | This superfamily represents the HRDC (helicase and RNaseD C-terminal) domain, which comprises two orthogonally packed α-hairpin subdomains, and is involved in interactions with DNA and protein. The HRDC (helicase and RNaseD C-terminal) domain is found at the C terminus of many RecQ helicases, including the human Bifunc... | [
"GO:0000166"
] | [
"nucleotide binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF47819"
] | [
""
] | [
63018
] | 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-112382",
"R-BTA-113418",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-759... | [
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-72086",
"REACTOME:R-B... | 217 | [
"1d8b",
"1go3",
"1nt9",
"1pqv",
"1wcm",
"1wud",
"1y14",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"1yt3",
"2b63",
"2b8k",
"2c35",
"2ckz",
"2cpr",
"2dgz",
"2e1e",
"2e1f",
"2hbj",
"2hbk",
"2hbl",
"2hbm",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2kv2",
"2ma1",
"2pmz",
"2r7z"... | 436 | [
"PUB00007873",
"PUB00014060",
"PUB00032236"
] | [
"11741548",
"10647186",
"15591044"
] | [
"Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex.",
"The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins.",
"Structures of complete RNA polymerase II and its subcomplex, Rpb4/7."
] | [
2001,
1999,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1048,
39143,
22021,
806
] | 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",... | [
69,
5,
11,
8,
2,
21,
17,
4,
24,
19,
4,
4,
61
] | 13 | true | Homologous_superfamily | HRDC-like superfamily | HRDC-like superfamily | HRDC-like_sf | 4 |
IPR010998 | 10,998 | Integrase/recombinase, N-terminal | Integrase_recombinase_N | Homologous_superfamily | 230,525 | false | false | Phage integrases are enzymes that mediate unidirectional site-specific recombination between two DNA recognition sequences, the phage attachment site, attP, and the bacterial attachment site, attB [ ]. Integrases may be grouped into two major families, the tyrosine recombinases and the serine recombinases, based on the... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.150.130"
] | [
""
] | [
230525
] | 1 | [] | [] | [] | 0 | [
"1a0p",
"1crx",
"1drg",
"1f44",
"1kbu",
"1ma7",
"1nzb",
"1ouq",
"1p7d",
"1pvp",
"1pvq",
"1pvr",
"1q3u",
"1q3v",
"1xns",
"1xo0",
"1z19",
"1z1b",
"1z1g",
"2a3v",
"2crx",
"2hof",
"2hoi",
"2kd1",
"2key",
"2khq",
"2khv",
"2kiw",
"2kj5",
"2kj8",
"2kj9",
"2kkp"... | 61 | [
"PUB00014061",
"PUB00014062",
"PUB00034645"
] | [
"14687564",
"12560475",
"16139195"
] | [
"Phage integrases: biology and applications.",
"Conservation of structure and function among tyrosine recombinases: homology-based modeling of the lambda integrase core-binding domain.",
"Lambda integrase: armed for recombination."
] | [
2004,
2003,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
3185,
212051,
9299,
2259,
6,
3725
] | 6 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
19,
10,
1,
1,
1
] | 5 | true | Homologous_superfamily | Integrase/recombinase, N-terminal | Integrase/recombinase, N-terminal | Integrase_recombinase_N | 5 |
IPR010999 | 10,999 | Retroviral matrix protein | Retrovr_matrix | Homologous_superfamily | 67,074 | false | false | Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [ ]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF47836"
] | [
""
] | [
67074
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1169408",
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-174490",
"R-HSA-174495",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-198933"
] | [
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-174495",
"REACTOME:R-HSA-17... | 17 | [
"1a6s",
"1bax",
"1ecw",
"1ed1",
"1hek",
"1hiw",
"1jvr",
"1l6n",
"1mn8",
"1tam",
"1uhu",
"1uph",
"2f76",
"2f77",
"2gol",
"2h3f",
"2h3i",
"2h3q",
"2h3v",
"2h3z",
"2hmx",
"2jmg",
"2k4e",
"2k4h",
"2k4i",
"2lya",
"2lyb",
"2mgu",
"2mv4",
"2nv3",
"4jmu",
"4zv5"... | 66 | [
"PUB00014063",
"PUB00016320",
"PUB00055853"
] | [
"9657938",
"12876457",
"18647839"
] | [
"Retroviral matrix proteins: a structural perspective.",
"The evolution, distribution and diversity of endogenous retroviruses.",
"D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein."
] | [
1998,
2003,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Thalassovita mangrovi",
"Viruses"
] | [
1851,
1,
65222
] | 3 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
19,
35,
10
] | 3 | true | Homologous_superfamily | Retroviral matrix protein | Retroviral matrix protein | Retrovr_matrix | 3 |
IPR011001 | 11,001 | Saposin-like | Saposin-like | Homologous_superfamily | 16,776 | false | false | The lysosomal degradation of several sphingolipids requires the presence of four small glycoproteins called saposins, generated by proteolytic processing of a common precursor, prosaposin [ ]. Saposins have three conserved disulphide bridges, and display a 5-helical, closed, folded leaf topology. Other proteins have be... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF47862"
] | [
""
] | [
16776
] | 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-5683826",
"R-BTA-9840310",
"R-CEL-9840310",
"R-DDI-9840310",
"R-HSA-114608",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-5683826",
"R-HSA-5688031",
"R-HSA-5688849",
"R-HSA-5688890",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-9840310",
"R-MMU-114608",
"R-MMU-375276",
"R-MMU-418594",
... | [
"REACTOME:R-BTA-5683826",
"REACTOME:R-BTA-9840310",
"REACTOME:R-CEL-9840310",
"REACTOME:R-DDI-9840310",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-5683826",
"REACTOME:R-HSA-5688031",
"REACTOME:R-HSA-5688849",
"REACTOME:R-HSA-5688890",
"REACTOME:R... | 26 | [
"1l9l",
"1m12",
"1n69",
"1nkl",
"1of9",
"1qdm",
"1sn6",
"2dob",
"2gtg",
"2js9",
"2jsa",
"2qyp",
"2r0r",
"2r1q",
"2rb3",
"2z9a",
"3bqp",
"3bqq",
"3rfi",
"3s63",
"3s64",
"4ddj",
"4uex",
"4v2o",
"5fi9",
"5fib",
"5fic",
"5i81",
"5i85",
"5i8r",
"5jg8",
"5nxb"... | 52 | [
"PUB00014080",
"PUB00014081",
"PUB00014082",
"PUB00014083",
"PUB00014084"
] | [
"9972880",
"8988855",
"14499265",
"10406799",
"11675486"
] | [
"Saposins and their interaction with lipids.",
"NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells.",
"Granulysin.",
"Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.",
"J3-crystallin of the jellyfish lens: similarity to s... | [
1999,
1996,
2003,
1999,
2001
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Orpheovirus IHUMI-LCC2",
"metagenomes"
] | [
8,
16762,
1,
5
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
27,
36,
15,
9,
31,
39,
25,
25,
119
] | 9 | true | Homologous_superfamily | Saposin-like | Saposin-like | Saposin-like | 7 |
IPR011002 | 11,002 | Flagellar motor switch protein FliG, alpha-helical | FliG_a-hlx | Homologous_superfamily | 14,187 | false | false | This superfamily represents an α-α superhelical domain found in the flagellar motor switch protein FliG. The flagellar motor switch regulates the direction of flagellar rotation and swimming behaviour in certain bacteria [ ]. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensor... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF48029"
] | [
""
] | [
14187
] | 1 | [] | [] | [] | 0 | [
"1lkv",
"1qc7",
"3ajc",
"3hjl",
"3soh",
"3usw",
"3usy",
"4fhr",
"4fq0",
"4qrm",
"5tdy",
"5wuj",
"8ucs",
"8umd",
"8umx",
"8uox",
"8upl",
"8vib",
"8vid",
"8vkq",
"8vkr",
"8wiw",
"8wo5",
"8woe",
"8xp0",
"8xp1",
"8yjt",
"8z4d",
"8z4g",
"9n49",
"9n4z"
] | 31 | [
"PUB00001834",
"PUB00014064"
] | [
"8224881",
"12736245"
] | [
"Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.",
"Binding of the chemotaxis response regulator CheY to the isolated, intact switch complex of the bacterial flagellar motor: lack of cooperativity."
] | [
1993,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Sulfolobaceae",
"unclassified sequences"
] | [
13883,
54,
4,
246
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Flagellar motor switch protein FliG, alpha-helical | Flagellar motor switch protein FliG, alpha-helical | FliG_a-hlx | 1 |
IPR011004 | 11,004 | Trimeric LpxA-like superfamily | Trimer_LpxA-like_sf | Homologous_superfamily | 284,988 | false | false | This domain superfamily is characterised by trimeric LpxA-like enzymes that display a single-stranded left-handed β-helix fold, composed of tandem repeats of a hexapeptide, as represented by the Bacterial transferase hexapeptide repeat, where the hexapeptide repeats correspond to individual strands. Many bacterial tran... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51161"
] | [
""
] | [
284988
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1",
"R-BTA-2132295",
"R-BTA-3371497",
"R-BTA-6807878",
"R-BTA-6811436",
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-72731",
"R-DDI-6807878",
"R-HSA-2132295",
"R-HSA-3371497",
"R-HSA-6787639",
"R-HSA-6807878",
"R-HSA-6811436",
"R-HSA-72731",
"R-MMU-2132295",
"R-MMU-3371497",
"R-MM... | [
"EC:2.3.1",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811436",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-72731",
"REACTOME:R-DDI-6807878",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-3371497",
"REACTOME:R-HSA-6787639"... | 29 | [
"1fwy",
"1fxj",
"1g95",
"1g97",
"1hm0",
"1hm8",
"1hm9",
"1hv9",
"1j2z",
"1kgq",
"1kgt",
"1khr",
"1kk4",
"1kk5",
"1kk6",
"1kqa",
"1krr",
"1kru",
"1krv",
"1lxa",
"1mr7",
"1mr9",
"1mrl",
"1ocx",
"1qq0",
"1qre",
"1qrf",
"1qrg",
"1qrl",
"1qrm",
"1s80",
"1ssm"... | 428 | [
"PUB00005215",
"PUB00007906",
"PUB00013969",
"PUB00013970",
"PUB00013971"
] | [
"7481807",
"11329257",
"11937062",
"10924115",
"11910040"
] | [
"A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.",
"Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.",
"Structure of the lac operon galactoside acetyltransferase.",
"A closer look at the active site of gamma-class carbo... | [
1995,
2001,
2002,
2000,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
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IPR011005 | 11,005 | Dihydropteroate synthase-like superfamily | Dihydropteroate_synth-like_sf | Homologous_superfamily | 86,259 | false | false | All organisms require reduced folate cofactors for the synthesis of a variety of metabolites. The enzyme 7,8-dihydropteroate synthase (DHPS) ( ) catalyses the condensation of para-aminobenzoic acid (pABA) with 6-hydroxymethyl-7, 8-dihydropterin-pyrophosphate to form 7,8-dihydropteroate and pyrophosphate. DHPS is essent... | [] | [] | [] | 0 | [
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2000
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2229
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15
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IPR011008 | 11,008 | Dimeric alpha-beta barrel | Dimeric_a/b-barrel | Homologous_superfamily | 392,087 | false | false | Dimeric α-β barrel domains exhibit an α+β sandwich fold with an antiparallel β-sheet that forms a closed barrel. These domains dimerise through the β-sheet, and in some cases these dimers may assemble into higher oligomers. Domains with this structure are found in proteins from several different families, including bac... | [] | [] | [] | 0 | [
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"Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus."
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2003,
1989,
2001
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8209,
339848,
40052,
6,
13,
3959
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18,
18,
9,
21,
34,
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27
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IPR011009 | 11,009 | Protein kinase-like domain superfamily | Kinase-like_dom_sf | Homologous_superfamily | 2,730,699 | false | false | Protein kinases ( ) modify other proteins by chemically adding phosphate groups to them. This process is fundamental to most signalling and regulatory processes in the eukaryotic cell [ ]. | [] | [] | [] | 0 | [
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"Structu... | [
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2000,
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400362,
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6062
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162,
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134,
127,
8577
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IPR011010 | 11,010 | DNA breaking-rejoining enzyme, catalytic core | DNA_brk_join_enz | Homologous_superfamily | 352,186 | false | false | Phage integrases are enzymes that mediate unidirectional site-specific recombination between two DNA recognition sequences, the phage attachment site, attP, and the bacterial attachment site, attB [ ]. Integrases may be grouped into two major families, the tyrosine recombinases and the serine recombinases, based on the... | [
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] | [
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301296,
34798,
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6625
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15,
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IPR011011 | 11,011 | Zinc finger, FYVE/PHD-type | Znf_FYVE_PHD | Homologous_superfamily | 375,681 | false | false | The FYVE zinc finger domain is conserved from yeast to man, and is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is found mainly on endosomes [ , ]. The... | [] | [] | [] | 0 | [
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2002,
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2007,
2005,
2005,
1999,
2001
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374827,
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102,
1105,
184,
667,
438,
28,
296,
621,
21,
25,
1336
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IPR011012 | 11,012 | Longin-like domain superfamily | Longin-like_dom_sf | Homologous_superfamily | 101,190 | false | false | VAMPs (and its homologue synaptobrevins) define a group of SNARE proteins that contain a C-terminal coiled-coil/SNARE motif, in combination with variable N-terminal domains that are used to classify VAMPs: those containing longin N-terminal domains (~150 aa) are referred to as longins, while those with shorter N-termin... | [] | [] | [] | 0 | [
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] | [
"Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins.",
"Molecular architecture and functional model of the endocytic AP2 complex.",
"Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda."
] | [
2003,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
11,
4,
101137,
6,
32
] | 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... | [
141,
16,
68,
33,
208,
104,
17,
121,
132,
15,
15,
290
] | 12 | true | Homologous_superfamily | Longin-like domain superfamily | Longin-like domain superfamily | Longin-like_dom_sf | 3 |
IPR011013 | 11,013 | Galactose mutarotase-like domain superfamily | Gal_mutarotase_sf_dom | Homologous_superfamily | 198,656 | false | false | Proteins with this domain belong to the galactose mutarotase-like structural superfamily. The domain has a distorted supersandwich structure consisting of 18 strands in two sheets, and probably functions to bind carbohydrates in enzymes that act on sugars. Domains with this structure occur in several protein families, ... | [
"GO:0030246",
"GO:0005975"
] | [
"carbohydrate binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF74650"
] | [
""
] | [
198656
] | 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-6798695",
"R-BTA-70221",
"R-BTA-70370",
"R-BTA-8853383",
"R-DDI-6798695",
"R-DDI-8853383",
"R-DME-975578",
"R-HSA-189085",
"R-HSA-532668",
"R-HSA-5357609",
"R-HSA-5659898",
"R-HSA-6798695",
"R-HSA-6811438",
"R-HSA-70221",
"R-HSA-70370",
"R-HSA-8853383",
"R-HSA-901042",
"R-HS... | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70221",
"REACTOME:R-BTA-70370",
"REACTOME:R-BTA-8853383",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-8853383",
"REACTOME:R-DME-975578",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-532668",
"REACTOME:R-HSA-5357609",
"REACTOME:R-HSA-5659898",
"REACTOME:R-HSA... | 42 | [
"1c82",
"1cb8",
"1dp0",
"1egu",
"1f1s",
"1f4a",
"1f4h",
"1f9g",
"1h54",
"1hm2",
"1hm3",
"1hmu",
"1hmw",
"1hn0",
"1hn1",
"1hty",
"1hww",
"1hxk",
"1i8q",
"1j0m",
"1j0n",
"1jov",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7"... | 527 | [
"PUB00008368",
"PUB00010717",
"PUB00014072",
"PUB00014073",
"PUB00014074"
] | [
"11587643",
"11907040",
"12829379",
"12501412",
"12618437"
] | [
"Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases.",
"High resolution X-ray structure of galactose mutarotase from Lactococcus lactis.",
"Purification and characterization of hyaluronic acid from the mollusc bivalve Mytilus galloprovin... | [
2001,
2002,
2003,
1998,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
898,
125645,
70722,
8,
1383
] | 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",... | [
176,
10,
47,
40,
13,
65,
44,
14,
101,
72,
7,
6,
228
] | 13 | true | Homologous_superfamily | Galactose mutarotase-like domain superfamily | Galactose mutarotase-like domain superfamily | Gal_mutarotase_sf_dom | 8 |
IPR011014 | 11,014 | Mechanosensitive ion channel MscS, transmembrane-2 | MscS_channel_TM-2 | Homologous_superfamily | 61,015 | false | false | MscS is a mechanosensitive channel present in the membrane of bacteria, archaea and eukarya that responds both to stretching of the cell membrane and to membrane depolarisation [ , , , ]. MscS folds as a homo-heptamer with a cylindrical shape, and can be divided into transmembrane and extramembrane regions: an N-termin... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"SSF"
] | [
"SSF82861"
] | [
""
] | [
61015
] | 1 | [] | [] | [] | 0 | [
"2oau",
"2vv5",
"3t9n",
"3udc",
"4age",
"4agf",
"4hw9",
"4hwa",
"5aji",
"5y4o",
"6lyp",
"6pwn",
"6pwo",
"6pwp",
"6rld",
"6urt",
"6uzh",
"6vxm",
"6vxn",
"6vxp",
"6vyk",
"6vyl",
"6vym",
"6zyd",
"6zye",
"7a46",
"7dlu",
"7n4t",
"7onj",
"7onl",
"7oo0",
"7oo6"... | 54 | [
"PUB00013956",
"PUB00064132",
"PUB00101036",
"PUB00101037"
] | [
"12446901",
"23074248",
"34376558",
"23339071"
] | [
"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel.",
"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.",
"Mechanosensitive channel gating by delipidation.",
"Open and shut: crystal structures of the dodecylmaltos... | [
2002,
2012,
2021,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sylvanvirus sp.",
"unclassified sequences"
] | [
2257,
56873,
1130,
1,
754
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
5,
6,
9
] | 4 | true | Homologous_superfamily | Mechanosensitive ion channel MscS, transmembrane-2 | Mechanosensitive ion channel MscS, transmembrane-2 | MscS_channel_TM-2 | 7 |
IPR011015 | 11,015 | LEM/LEM-like domain superfamily | LEM/LEM-like_dom_sf | Homologous_superfamily | 8,623 | false | false | The LEM domain is a ~40-residue motif found in nuclear membrane-associated proteins, including lamino-associated polypeptide 2 (LAP2), emerin, MAN1, otefin and Lem-3 [ ]. Defects in the emerin gene are a cause of Emery-Dreifuss muscular dystrophy, an X-linked disorder characterised by early contractures, muscle wasting... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.720.40",
"SSF63451"
] | [
"",
""
] | [
8562,
7815
] | 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-HSA-2980766",
"R-HSA-2995383",
"R-HSA-4419969",
"R-HSA-8980692",
"R-HSA-9013106",
"R-HSA-9013148",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013405",
"R-HSA-9013408",
"R-HSA-9013409",
"R-HSA-9013423",
"R-HSA-9035034",
"R-HSA-9609523",
"R-HSA-9668328",
"R-HSA-9696264",
"R-HSA-96962... | [
"REACTOME:R-HSA-2980766",
"REACTOME:R-HSA-2995383",
"REACTOME:R-HSA-4419969",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013106",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013149",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9013409",
"REACTOM... | 35 | [
"1gjj",
"1h9e",
"1h9f",
"1jei",
"2odc",
"2odg",
"6ghd",
"6rpr",
"7ndy"
] | 9 | [
"PUB00014170",
"PUB00017332",
"PUB00017333",
"PUB00018424"
] | [
"11792821",
"10671519",
"11435115",
"11500367"
] | [
"Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF.",
"MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin.",
"Structural characterization of the LEM motif common to three human inner nuclear membrane proteins.",
"Sol... | [
2001,
2000,
2001,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Bacillaceae",
"Eukaryota"
] | [
83,
8540
] | 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)"
] | [
3,
54,
6,
21,
24,
2,
32,
1
] | 8 | true | Homologous_superfamily | LEM/LEM-like domain superfamily | LEM/LEM-like domain superfamily | LEM/LEM-like_dom_sf | 3 |
IPR011016 | 11,016 | Zinc finger, RING-CH-type | Znf_RING-CH | Domain | 57,348 | false | false | The RING finger is a well characterised zinc finger which coordinates two zinc atoms in a cross-braced manner (see ). According to the pattern of cysteines and histidines three different subfamilies of RING finger can be defined. The classical RING finger (RING-HC) has a histidine at the fourth coordinating position an... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF12906",
"PS51292",
"SM00744"
] | [
"RINGv",
"ZF_RING_CH",
"RINGv"
] | [
38863,
39492,
56275
] | 3 | [
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.27",
"GenProp1754",
"PWY-7511",
"R-HSA-901032",
"R-HSA-983168",
"R-MMU-983168",
"R-SCE-983168"
] | [
"EC:2.3.2.27",
"GP:GenProp1754",
"METACYC:PWY-7511",
"REACTOME:R-HSA-901032",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-983168",
"REACTOME:R-SCE-983168"
] | 7 | [
"1vyx",
"2d8s",
"2ep4",
"2m6m",
"3j92",
"5d0i",
"5d0k",
"5d0m",
"5ulh",
"5ulk",
"7r70",
"7r71",
"8aaf",
"8agt",
"8agu",
"8agv",
"8agw",
"8agx",
"8agz",
"8pd0",
"8pda",
"8tqm",
"9gy4",
"9n1f",
"9ofv"
] | 25 | [
"PUB00014077",
"PUB00032129",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00043776",
"PUB00043777",
"PUB00043778",
"PUB00043779"
] | [
"12665246",
"15465811",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"11641273",
"12695663",
"16873052",
"17051211"
] | [
"Zinc fingers--folds for many occasions.",
"Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
... | [
2002,
2004,
2007,
2005,
2005,
1999,
2001,
2001,
2003,
2006,
2006
] | 11 | [] | [
"IPR047904",
"IPR047905",
"IPR047906"
] | 0 | 3 | 0 | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"metagenomes"
] | [
57095,
5,
190,
58
] | 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... | [
202,
8,
74,
19,
37,
42,
5,
100,
61,
2,
5,
217
] | 12 | true | Domain | Zinc finger, RING-CH-type | Zinc finger, RING-CH-type | Znf_RING-CH | 5 |
IPR011017 | 11,017 | TRASH domain | TRASH_dom | Domain | 22,222 | false | false | TRASH domain contains a well-conserved cysteine motif that may be involved in metal coordination. TRASH is encoded by multiple prokaryotic genomes and is present in transcriptional regulators, cation-transporting ATPases and hydrogenases, and is also present as a stand-alone module. The observed domain associations and... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00746"
] | [
"TRASH"
] | [
22222
] | 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-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
"R-DME-975957",
"R-DRE-156827",
"R-DRE-1799339",
"R-DRE-72689",
"R-DRE-975956",
"R-DRE-9759... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-DME-156827",
"REACTOME:R-DME-1799339",
"REACTOME:R-DME-72689",
"REACTOME:R-DME-72706",
"REACTOME:R-DME-9759... | 50 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp"... | 422 | [
"PUB00014222"
] | [
"12713899"
] | [
"TRASH: a novel metal-binding domain predicted to be involved in heavy-metal sensing, trafficking and resistance."
] | [
2003
] | 1 | [] | [
"IPR056526"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2236,
5818,
8,
13893,
267
] | 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... | [
9,
1,
37,
10,
28,
29,
1,
11,
31,
1,
1,
18
] | 12 | true | Domain | TRASH domain | TRASH domain | TRASH_dom | 6 |
IPR011019 | 11,019 | KIND domain | KIND_dom | Domain | 7,690 | false | false | The KIND (kinase non-catalytic C-lobe domain) is a putative protein interaction domain, which has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe) (see ). The presence of the KIND domain at the N terminus of signalling proteins and the absence of the active site residues in the ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF16474",
"PS51377",
"SM00750"
] | [
"KIND",
"KIND",
"KIND"
] | [
4883,
7570,
6724
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1660499",
"R-HSA-9008059",
"R-HSA-9696264",
"R-HSA-9696270",
"R-HSA-9696273",
"R-MMU-1660499",
"R-MMU-9696264",
"R-MMU-9696270",
"R-MMU-9696273"
] | [
"REACTOME:R-HSA-1660499",
"REACTOME:R-HSA-9008059",
"REACTOME:R-HSA-9696264",
"REACTOME:R-HSA-9696270",
"REACTOME:R-HSA-9696273",
"REACTOME:R-MMU-1660499",
"REACTOME:R-MMU-9696264",
"REACTOME:R-MMU-9696270",
"REACTOME:R-MMU-9696273"
] | 9 | [
"2yle",
"2ylf",
"3r7g",
"3rbw"
] | 4 | [
"PUB00014223",
"PUB00043706",
"PUB00071258",
"PUB00076396"
] | [
"12877999",
"16099729",
"21730168",
"21705804"
] | [
"The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold.",
"Very-KIND is a novel nervous system specific guanine nucleotide exchange factor for Ras GTPases.",
"Structure and function of the interacting domains of Spire and Fmn-family formins.",
"Molecular basis of act... | [
2003,
2005,
2011,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
7,
7683
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
65,
8,
29,
15,
23
] | 6 | true | Domain | KIND domain | KIND domain | KIND_dom | 7 |
IPR011020 | 11,020 | HTTM-like | HTTM-like | Domain | 7,170 | false | false | Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane). In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal g... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00752"
] | [
"HTTM"
] | [
7170
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.90",
"PWY-7999",
"R-BTA-159740",
"R-HSA-159740",
"R-HSA-9673240",
"R-MMU-159740",
"R-RNO-159740"
] | [
"EC:4.1.1.90",
"METACYC:PWY-7999",
"REACTOME:R-BTA-159740",
"REACTOME:R-HSA-159740",
"REACTOME:R-HSA-9673240",
"REACTOME:R-MMU-159740",
"REACTOME:R-RNO-159740"
] | 7 | [
"9bum",
"9bur",
"9bux",
"9bvk",
"9bvl",
"9bvm",
"9bvo",
"9bvp",
"9bvq",
"9bvr",
"9l1y",
"9l20",
"9l21",
"9l23",
"9l24",
"9l25",
"9l54",
"9l6q",
"9l6r",
"9l6s",
"9mqb",
"9mqc",
"9mqe"
] | 23 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"ecological metagenomes"
] | [
358,
5136,
1643,
3,
30
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
9,
3,
6
] | 5 | true | Domain | HTTM-like | HTTM-like | HTTM-like | 9 |
IPR011021 | 11,021 | Arrestin-like, N-terminal | Arrestin-like_N | Domain | 30,864 | false | false | G protein-coupled receptors are a large family of signalling molecules that respond to a wide variety of extracellular stimuli. The receptors relay the information encoded by the ligand through the activation of heterotrimeric G proteins and intracellular effector molecules. To ensure the appropriate regulation of the ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00339"
] | [
"Arrestin_N"
] | [
30864
] | 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-2514859",
"R-BTA-418555",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-456926",
"R-BTA-5635838",
"R-BTA-5674135",
"R-BTA-5689880",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-9839389",
"R-CEL-2514859",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-456926",
"R-CEL-5099900",
"R-CEL-5674135",
... | [
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-456926",
"REACTOME:R-BTA-5635838",
"REACTOME:R-BTA-5674135",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9839389",
"REACTOME:R-... | 82 | [
"1ayr",
"1cf1",
"1g4m",
"1g4r",
"1jsy",
"1suj",
"1zsh",
"2wtr",
"3gc3",
"3gd1",
"3p2d",
"3ugu",
"3ugx",
"4gei",
"4gej",
"4gfx",
"4j2q",
"4jqi",
"4ll1",
"4ll4",
"4r7v",
"4r7x",
"4zrg",
"4zwj",
"5dgy",
"5tv1",
"5w0p",
"6bk9",
"6k3f",
"6kl7",
"6ni2",
"6pwc"... | 104 | [
"PUB00000986",
"PUB00001029",
"PUB00001684",
"PUB00002739",
"PUB00004275",
"PUB00005126",
"PUB00075595",
"PUB00075596"
] | [
"8452755",
"15335861",
"7720881",
"1517224",
"9495348",
"2158671",
"18664266",
"23519408"
] | [
"Arrestin-subtypes in insect antennae.",
"Arresting G-protein coupled receptor activity.",
"The arrestin superfamily: cone arrestins are a fourth family.",
"Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.",
"X-ray crystal structure of arrestin from bovine rod outer segments.",
"A... | [
1993,
1993,
1995,
1992,
1998,
1990,
2008,
2013
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Avipoxvirus",
"Bacteria",
"Eukaryota"
] | [
5,
4,
24,
30831
] | 4 | [
"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... | [
30,
35,
36,
27,
35,
3,
42,
5,
4
] | 9 | true | Domain | Arrestin-like, N-terminal | Arrestin-like, N-terminal | Arrestin-like_N | 1 |
IPR011023 | 11,023 | Nop2p | Nop2p | Domain | 10,249 | false | false | This domain is found in archaeal, bacterial and eukaryotic proteins. It is found in the homologues of human 28S rRNA (cytosine(4447)-C(5))-methyltransferase that specifically methylates the C5 position of cytosine 4447 in 28S rRNA and is required for efficient rRNA processing and 60S ribosomal subunit biogenesis [ , , ... | [
"GO:0003723",
"GO:0008757",
"GO:0006396"
] | [
"RNA binding",
"S-adenosylmethionine-dependent methyltransferase activity",
"RNA processing"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00446"
] | [
"nop2p"
] | [
10249
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"2.1.1.178",
"R-HSA-6790901",
"R-HSA-8869496"
] | [
"EC:2.1.1.178",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-8869496"
] | 3 | [
"1ixk",
"2frx",
"2yxl",
"3a4t",
"3ajd",
"3m4x",
"5zvd",
"5zve",
"5zvg",
"5zvh",
"6elz",
"6em5",
"7nac",
"7ohr",
"7r6k",
"7r7a",
"7r7c",
"8esq",
"8esr",
"8fkt",
"8fku",
"8fkv",
"8fkw",
"8fkx",
"8fky",
"8i9r",
"8i9t",
"8i9v",
"8i9w",
"8i9x",
"8i9y",
"8i9z"... | 36 | [
"PUB00014204",
"PUB00014212",
"PUB00014217",
"PUB00014219",
"PUB00014224",
"PUB00036064",
"PUB00097261",
"PUB00154576",
"PUB00154577"
] | [
"14656444",
"12872006",
"7806561",
"8972218",
"2576976",
"16793063",
"24120868",
"26196125",
"36161484"
] | [
"The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.",
"Automated identification of putative methyltransferases from genomic open reading frames.",
"Yeast NOP2 encodes an essential nucleolar protein with homology to a human p... | [
2003,
2003,
1994,
1997,
1989,
2006,
2013,
2015,
2022
] | 9 | [
"IPR001678"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
674,
3751,
5801,
23
] | 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",... | [
15,
1,
3,
1,
1,
1,
3,
1,
7,
1,
1,
1,
12
] | 13 | true | Domain | Nop2p | Nop2p | Nop2p | 3 |
IPR011024 | 11,024 | Gamma-crystallin-like | G_crystallin-like | Homologous_superfamily | 27,789 | false | false | This entry contains proteins which have a Greek key motif [ ]. They are all structurally related to the beta/gamma crystallin superfamily. This superfamily of proteins includes: Beta and gamma crystallins Yeast killer toxin Killer toxin-like protein SKLP Antifungal protein, AFP1 Plant antimicrobial protein, MIAMP1 Stre... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF49695"
] | [
""
] | [
27789
] | 1 | [] | [] | [] | 0 | [
"1a45",
"1a5d",
"1a7h",
"1ag4",
"1amm",
"1bd7",
"1bhu",
"1blb",
"1c01",
"1dsl",
"1e7n",
"1elp",
"1f53",
"1g6e",
"1gam",
"1gcs",
"1gh5",
"1h4a",
"1ha4",
"1hdf",
"1hk0",
"1i5i",
"1m8u",
"1nps",
"1oki",
"1prr",
"1prs",
"1wkt",
"1yhp",
"1ytq",
"1zgt",
"1zie"... | 107 | [
"PUB00014340",
"PUB00014341"
] | [
"8506258",
"9735297"
] | [
"The Greek key motif: extraction, classification and analysis.",
"NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure."
] | [
1993,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
8,
4517,
23212,
20,
32
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Zea mays"
] | [
89,
51,
47,
1,
52,
4
] | 6 | true | Homologous_superfamily | Gamma-crystallin-like | Gamma-crystallin-like | G_crystallin-like | 5 |
IPR011025 | 11,025 | G protein alpha subunit, helical insertion | GproteinA_insert | Homologous_superfamily | 38,710 | false | false | Guanine nucleotide binding proteins (G proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins act as signal transducers, relaying a signal from a ligand-activated GPCR (G protein-coupled receptor) to an enzyme or ion channel effector. The... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.400.10",
"SSF47895"
] | [
"",
""
] | [
36490,
38156
] | 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-112043",
"R-BTA-170670",
"R-BTA-202040",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-381771",
"R-BTA-392170",
"R-BTA-399997",
"R-BTA-400042",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418592",
"R-BTA-418594",
"R-BTA-428930",
"R-BTA-434316",
"R-BTA-456926",
"R-BTA-6814122",
"R-BTA... | [
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-170670",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-381771",
"REACTOME:R-BTA-392170",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-400042",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-... | 226 | [
"1agr",
"1as0",
"1as2",
"1as3",
"1azs",
"1azt",
"1bh2",
"1bof",
"1cip",
"1cjk",
"1cjt",
"1cju",
"1cjv",
"1cs4",
"1cul",
"1fqj",
"1fqk",
"1gdd",
"1gfi",
"1gg2",
"1gia",
"1gil",
"1git",
"1got",
"1gp2",
"1kjy",
"1shz",
"1svk",
"1svs",
"1tad",
"1tag",
"1tl7"... | 1,021 | [
"PUB00015168",
"PUB00015232"
] | [
"15119945",
"12517447"
] | [
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"Activation of G-protein Galpha subunits by receptors through Galpha-Gbeta and Galpha-Ggamma interactions."
] | [
2004,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Orpheovirus IHUMI-LCC2",
"viral metagenome"
] | [
3,
38703,
2,
2
] | 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... | [
18,
27,
53,
11,
69,
49,
3,
24,
69,
2,
2,
20
] | 12 | true | Homologous_superfamily | G protein alpha subunit, helical insertion | G protein alpha subunit, helical insertion | GproteinA_insert | 5 |
IPR011026 | 11,026 | Actin nucleation-promoting factor WAS, C-terminal | WAS_C | Homologous_superfamily | 3,522 | false | false | The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through activation of Actin nucleation-promoting factor WAS protein (WASP) family members [ ]. Mutations in WASP lead to the Wiskott-Aldrich syndrome, a paediatric disorder characterised by actin cytoskeletal defects in haematopoietic cells, leading clin... | [
"GO:0007015"
] | [
"actin filament organization"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF47912"
] | [
""
] | [
3522
] | 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-2029482",
"R-BTA-203641",
"R-BTA-373753",
"R-BTA-3928662",
"R-BTA-418885",
"R-BTA-5663213",
"R-BTA-8856828",
"R-BTA-9013406",
"R-BTA-9013424",
"R-HSA-202433",
"R-HSA-2029482",
"R-HSA-203641",
"R-HSA-373753",
"R-HSA-3928662",
"R-HSA-418885",
"R-HSA-5663213",
"R-HSA-8856828",
... | [
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-203641",
"REACTOME:R-BTA-373753",
"REACTOME:R-BTA-3928662",
"REACTOME:R-BTA-418885",
"REACTOME:R-BTA-5663213",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9013406",
"REACTOME:R-BTA-9013424",
"REACTOME:R-HSA-202433",
"REACTOME:R-HSA-2029482",
"REACTOME:R-... | 31 | [
"1cee",
"1ej5",
"1t84",
"2k42",
"2lnh",
"2vcp",
"3m3n",
"6uhc",
"7t5q",
"8s5t",
"9dlx",
"9dlz",
"9r3y",
"9r4v"
] | 14 | [
"PUB00014097"
] | [
"10724160"
] | [
"Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3522
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
16,
3,
7,
9,
11,
1
] | 6 | true | Homologous_superfamily | Actin nucleation-promoting factor WAS, C-terminal | Actin nucleation-promoting factor WAS, C-terminal | WAS_C | 4 |
IPR011029 | 11,029 | Death-like domain superfamily | DEATH-like_dom_sf | Homologous_superfamily | 118,610 | false | false | This superfamily represents the death domain and other structurally similar domains, including DED, CARD and the DAPIN domain. The death domain (DD) is a conserved region of about 80 residues found on death receptors, and which is required for death signalling, as well as a variety of non-apoptotic functions [ , ]. Pro... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.10.533.10",
"SSF47986"
] | [
"",
""
] | [
117167,
107390
] | 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-1257604",
"R-BTA-140534",
"R-BTA-168638",
"R-BTA-202424",
"R-BTA-209543",
"R-BTA-209560",
"R-BTA-2562578",
"R-BTA-3371378",
"R-BTA-450302",
"R-BTA-450321",
"R-BTA-5218900",
"R-BTA-5357786",
"R-BTA-5357905",
"R-BTA-5357956",
"R-BTA-5620971",
"R-BTA-5669034",
"R-BTA-5675482",
... | [
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-140534",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-209543",
"REACTOME:R-BTA-209560",
"REACTOME:R-BTA-2562578",
"REACTOME:R-BTA-3371378",
"REACTOME:R-BTA-450302",
"REACTOME:R-BTA-450321",
"REACTOME:R-BTA-5218900",
"REACTOME:R-BTA... | 456 | [
"1a1w",
"1a1z",
"1c15",
"1cww",
"1cy5",
"1d2z",
"1ddf",
"1dgn",
"1e3y",
"1e41",
"1fad",
"1ich",
"1ik7",
"1n3k",
"1ngr",
"1pn5",
"1ucp",
"1wh4",
"1wmg",
"1wxp",
"1ygo",
"1z6t",
"2a5y",
"2a9i",
"2b1w",
"2bbr",
"2bbz",
"2d96",
"2dbd",
"2dbf",
"2dbg",
"2dbh"... | 299 | [
"PUB00014106",
"PUB00014107",
"PUB00014108",
"PUB00014109",
"PUB00015057"
] | [
"11828422",
"12655292",
"12719729",
"12101092",
"15226512"
] | [
"Molecular mechanisms of death-receptor-mediated apoptosis.",
"All in the family: evolutionary and functional relationships among death receptors.",
"The death effector domain protein family: regulators of cellular homeostasis.",
"CARD games in apoptosis and immunity.",
"The domains of apoptosis: a genomics... | [
2001,
2003,
2003,
2002,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
71,
118384,
147,
8
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
5,
23,
680,
35,
523,
353,
363,
2
] | 8 | true | Homologous_superfamily | Death-like domain superfamily | Death-like domain superfamily | DEATH-like_dom_sf | 6 |
IPR011030 | 11,030 | Lipovitellin-phosvitin complex, superhelical domain | Lipovitellin_superhlx_dom | Homologous_superfamily | 12,669 | false | false | Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients in the yolk of egg-laying animals. Vitellogenin is a large multidomain protein. In vertebrates, a complete vitellinogen is composed of an N-terminal signal peptide for export, followed by four regions that can be cleaved into yol... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:1.25.10.20",
"SSF48431"
] | [
"",
""
] | [
11562,
12255
] | 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-DME-8964041",
"R-DRE-8964041",
"R-GGA-204626",
"R-HSA-202733",
"R-HSA-3000471",
"R-HSA-3000480",
"R-HSA-3000484",
"R-HSA-3000497",
"R-HSA-381426",
"R-HSA-432142",
"R-HSA-5686938",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-8866423",
"R-HSA-8957275",
"R-HSA-8963888",
"R-HSA-8963901",... | [
"REACTOME:R-DME-8964041",
"REACTOME:R-DRE-8964041",
"REACTOME:R-GGA-204626",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-3000471",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-3000497",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-432142",
"REACTOME:R-HSA-5686938",
"REACTOME:R-... | 64 | [
"1lsh",
"6i7s",
"8eoj",
"9bd1",
"9bd8",
"9bde",
"9bdt",
"9coo",
"9e9r",
"9ea7",
"9eag",
"9enr",
"9ens"
] | 13 | [
"PUB00007158",
"PUB00035546",
"PUB00087300"
] | [
"12135361",
"17314313",
"15278911"
] | [
"Lipid-protein interactions in lipovitellin.",
"Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.",
"Vertebrate yolk proteins: a review."
] | [
2002,
2007,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Citrobacter phage HCF1",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes"
] | [
756,
1,
11888,
15,
9
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
6,
28,
7,
14,
4,
5,
1
] | 7 | true | Homologous_superfamily | Lipovitellin-phosvitin complex, superhelical domain | Lipovitellin-phosvitin complex, superhelical domain | Lipovitellin_superhlx_dom | 1 |
IPR011033 | 11,033 | PRC-barrel-like superfamily | PRC_barrel-like_sf | Homologous_superfamily | 63,902 | false | false | The PRC-barrel is an all β-barrel domain found in photosystem reaction centre subunit H of the purple bacteria and RNA metabolism proteins of the RimM group. PRC-barrels are approximately 80 residues long, and found widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50346"
] | [
""
] | [
63902
] | 1 | [] | [] | [] | 0 | [
"1aig",
"1aij",
"1ds8",
"1dv3",
"1dv6",
"1dxr",
"1e14",
"1e6d",
"1eys",
"1f6n",
"1fnp",
"1fnq",
"1jgw",
"1jgx",
"1jgy",
"1jgz",
"1jh0",
"1k6l",
"1k6n",
"1kby",
"1l9b",
"1l9j",
"1m3x",
"1mps",
"1ogv",
"1pcr",
"1pm3",
"1prc",
"1pss",
"1pst",
"1qov",
"1r2c"... | 238 | [
"PUB00010437",
"PUB00153712"
] | [
"12429060",
"38443575"
] | [
"The PRC-barrel: a widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism.",
"Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division."
] | [
2002,
2024
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Escherichia phage vB_EcoM-613R3",
"Eukaryota",
"unclassified sequences"
] | [
2016,
52594,
1,
8492,
799
] | 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"
] | [
9,
1,
44,
14,
1,
9,
8,
8,
15,
14
] | 10 | true | Homologous_superfamily | PRC-barrel-like superfamily | PRC-barrel-like superfamily | PRC_barrel-like_sf | 5 |
IPR011034 | 11,034 | Formyl transferase-like, C-terminal domain superfamily | Formyl_transferase-like_C_sf | Homologous_superfamily | 53,899 | false | false | Methionyl-tRNA formyltransferase (FMT) ( ) transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. T... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF50486"
] | [
""
] | [
53899
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.2.9",
"R-HSA-110330",
"R-HSA-110331",
"R-HSA-110357",
"R-HSA-196757",
"R-HSA-5368286",
"R-MMU-110331",
"R-MMU-110357",
"R-MMU-196757",
"R-RNO-110331",
"R-RNO-110357",
"R-RNO-196757",
"R-XTR-196757"
] | [
"EC:2.1.2.9",
"REACTOME:R-HSA-110330",
"REACTOME:R-HSA-110331",
"REACTOME:R-HSA-110357",
"REACTOME:R-HSA-196757",
"REACTOME:R-HSA-5368286",
"REACTOME:R-MMU-110331",
"REACTOME:R-MMU-110357",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-110331",
"REACTOME:R-RNO-110357",
"REACTOME:R-RNO-196757",
"R... | 13 | [
"1bnk",
"1ewn",
"1f4r",
"1f6o",
"1fmt",
"1s3i",
"1yrw",
"1z7e",
"1zgh",
"2bln",
"2bw0",
"2cfi",
"2fmt",
"3q0i",
"3qi5",
"3r8x",
"3tqq",
"3uby",
"4iqf",
"4qpc",
"4qpd",
"4r8v",
"4ts4",
"4tt8",
"4tts",
"4wkg",
"4xcz",
"4xd0",
"4xd1",
"5j63",
"5uai",
"5uij"... | 52 | [
"PUB00014118",
"PUB00014119"
] | [
"8887566",
"11106395"
] | [
"Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.",
"Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG."
] | [
1996,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
219,
45282,
7505,
26,
867
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
13,
1,
4,
5,
2,
15,
8,
6,
15,
1,
11
] | 11 | true | Homologous_superfamily | Formyl transferase-like, C-terminal domain superfamily | Formyl transferase-like, C-terminal domain superfamily | Formyl_transferase-like_C_sf | 6 |
IPR011035 | 11,035 | Large ribosomal subunit protein bL25/Gln-tRNA synthetase, anti-codon-binding domain superfamily | Ribosomal_bL25/Gln-tRNA_synth | Homologous_superfamily | 49,802 | false | false | The bacterial large ribosomal subunit protein bL25, previously known as ribosomal protein L25, is bound to 5S rRNA along with uL5 and uL18, forming a separate domain of the ribosome [ , ]. The solution structure of protein bL25 uncomplexed with RNA shows two significantly disordered loops and a closed β-barrel domain w... | [
"GO:0006412"
] | [
"translation"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF50715"
] | [
""
] | [
49802
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9856649",
"R-DDI-9856649",
"R-DME-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-6782315",
"R-HSA-9856649",
"R-MMU-9856649",
"R-RNO-9856649"
] | [
"REACTOME:R-BTA-9856649",
"REACTOME:R-DDI-9856649",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649",
"REACTOME:R-RNO-9856649"
] | 10 | [
"1b75",
"1d6k",
"1dfu",
"1euq",
"1euy",
"1exd",
"1feu",
"1gsg",
"1gtr",
"1gts",
"1ml5",
"1njm",
"1njp",
"1nkw",
"1nwx",
"1nwy",
"1nyl",
"1o0b",
"1o0c",
"1qrs",
"1qrt",
"1qru",
"1qtq",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"1zjw",
"2hz7"... | 1,075 | [
"PUB00014120",
"PUB00014121",
"PUB00014122",
"PUB00080279"
] | [
"11418764",
"12737824",
"10696113",
"24524803"
] | [
"Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.",
"tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase.",
"Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution.",
"A... | [
2001,
2003,
2000,
2014
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
948,
34749,
13173,
26,
906
] | 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",... | [
29,
5,
3,
2,
2,
20,
12,
2,
22,
11,
2,
2,
44
] | 13 | true | Homologous_superfamily | Large ribosomal subunit protein bL25/Gln-tRNA synthetase, anti-codon-binding domain superfamily | Large ribosomal subunit protein bL25/Gln-tRNA synthetase, anti-codon-binding domain superfamily | Ribosomal_bL25/Gln-tRNA_synth | 8 |
IPR011037 | 11,037 | Pyruvate kinase-like, insert domain superfamily | Pyrv_Knase-like_insert_dom_sf | Homologous_superfamily | 89,722 | false | false | Pyruvate kinase ( ) (PK) catalyses the final step in glycolysis [ , ], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP: ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50800"
] | [
""
] | [
89722
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"2.7.1.40",
"PWY-1042",
"PWY-2221",
"PWY-5484",
"PWY-5723",
"PWY-6886",
"PWY-6901",
"PWY-7003",
"PWY-7218",
"PWY-7383",
"PWY-8004",
"PWY-8404",
"R-BTA-211945",
"R-BTA-947581",
"R-CEL-947581",
"R-CFA-70171",
"R-CFA-70268",
"R-DDI-6798695",
"R-DDI-70171",
"R-DDI-70268",
"R-DDI-... | [
"EC:2.7.1.40",
"METACYC:PWY-1042",
"METACYC:PWY-2221",
"METACYC:PWY-5484",
"METACYC:PWY-5723",
"METACYC:PWY-6886",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-7218",
"METACYC:PWY-7383",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-BTA-211945",
"REACTOME:R-BTA-947581",
"RE... | 60 | [
"1a3w",
"1a3x",
"1a49",
"1a5u",
"1aqf",
"1e0t",
"1e0u",
"1f3w",
"1f3x",
"1o65",
"1o67",
"1oru",
"1pkl",
"1pkm",
"1pkn",
"1pky",
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"1zjh",
"2e28",
"2g50",
"2vgb",
"2vgf",
"2vgg",
"2vgi",
"3bjf",
"3bjt",
"3e0v",
"3e0w",
"3eoe",
"3g2g",
"3gg8",
"3gqy"... | 177 | [
"PUB00000569",
"PUB00014134",
"PUB00014243",
"PUB00019067",
"PUB00024392",
"PUB00100069"
] | [
"2379684",
"11960989",
"12798932",
"11886751",
"10751408",
"29748232"
] | [
"Isoenzymes of pyruvate kinase.",
"Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.",
"Pyruvate kinase: current status of regulatory and functional properties.",
"MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal-s... | [
1990,
2002,
2003,
2002,
2000,
2018
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1255,
61823,
25694,
6,
944
] | 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",... | [
67,
13,
15,
12,
4,
24,
16,
3,
39,
26,
2,
1,
89
] | 13 | true | Homologous_superfamily | Pyruvate kinase-like, insert domain superfamily | Pyruvate kinase-like, insert domain superfamily | Pyrv_Knase-like_insert_dom_sf | 7 |
IPR011039 | 11,039 | Transcription Factor IIF, Rap30/Rap74, interaction | TFIIF_interaction | Homologous_superfamily | 9,383 | false | false | Transcription factor IIF (TFIIF), which is essential for eukaryotic transcription by RNA polymerase II. (PolII), consists of a heterodimer of Rap30 (beta) ( ) and Rap74 (alpha) ( ) subunits [ ]. Rap30 and Rap74 have multiple domains that bind to PolII, TFIIB, TAF250 and DNA in interactions that are essential for transc... | [
"GO:0006367"
] | [
"transcription initiation at RNA polymerase II promoter"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF50916"
] | [
""
] | [
9383
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-674695",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-75955",
"R-BTA-76042",
"R-BTA-77075",
"R-BTA-9018519",
"R-DDI-113418",
... | [
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-72086",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72165",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-73776",
"REACTOME:R-BTA-73779... | 137 | [
"1f3u",
"4v1n",
"4v1o",
"5fmf",
"5fyw",
"5fz5",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5oqj",
"5oqm",
"5sva",
"6gyk",
"6gyl",
"6gym",
"6o9l",
"7edx",
"7eg7",
"7eg8",
"7eg9",
"7ega",
"7egb",
"7egc",
"7ena",
"7enc",
"7lbm",
"7mei"... | 90 | [
"PUB00011486",
"PUB00014142"
] | [
"12354769",
"11183778"
] | [
"A key role for the alpha 1 helix of human RAP74 in the initiation and elongation of RNA chains.",
"Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution."
] | [
2002,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Dorea longicatena DSM 13814",
"Eukaryota",
"metagenomes"
] | [
1,
9380,
2
] | 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... | [
12,
2,
12,
2,
9,
5,
2,
17,
10,
2,
2,
25
] | 12 | true | Homologous_superfamily | Transcription Factor IIF, Rap30/Rap74, interaction | Transcription Factor IIF, Rap30/Rap74, interaction | TFIIF_interaction | 2 |
IPR011040 | 11,040 | Sialidase | Sialidase | Domain | 24,147 | false | false | Sialidases (neuraminidases) hydrolyse the non-reducing, terminal sialic acid linkage in various natural substrates, such as glycoproteins, glycolipids, gangliosides, and polysaccharides [ ]. In mammals, sialidases occur in the lysosome, the cytosol, and associated with the plasma membrane. Sialidases have also been imp... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF13088",
"PF13859"
] | [
"BNR_2",
"BNR_3"
] | [
19174,
4977
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
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"R-BTA-4085001",
"R-BTA-6798695",
"R-BTA-9840310",
"R-HSA-4085001",
"R-HSA-4341670",
"R-HSA-6798695",
"R-HSA-9840310",
"R-MMU-4085001",
"R-MMU-6798695",
"R-MMU-9840310",
"R-RNO-4085001",
"R-RNO-6798695",
"R-RNO-9840310",
"R-SSC-4085001",
"R-SSC-6798695",
"R-SSC-9840310"
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"REACTOME:R-BTA-4085001",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9840310",
"REACTOME:R-HSA-4085001",
"REACTOME:R-HSA-4341670",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9840310",
"REACTOME:R-MMU-4085001",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-9840310",
"REACTOME:R-RNO-408... | 17 | [
"1dil",
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"1eur",
"1eus",
"1eut",
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"1sli",
"1sll",
"1snt",
"1so7",
"1vcu",
"1w0o",
"1w0p",
"1w8n",
"1w8o"... | 216 | [
"PUB00014144",
"PUB00014145",
"PUB00014146",
"PUB00014147",
"PUB00031976"
] | [
"12374200",
"14561719",
"8591030",
"9878409",
"14729348"
] | [
"Recent development in mammalian sialidase molecular biology.",
"Variation in the divalent cation requirements of influenza a virus N2 neuraminidases.",
"The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll.",
"The 1.8 A structures of leech ... | [
2002,
2003,
1995,
1999,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
33,
13723,
10160,
25,
206
] | 5 | [
"Arabidopsis thaliana",
"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",
"Zea mays"
] | [
10,
16,
19,
15,
1,
5,
16,
10
] | 8 | true | Domain | Sialidase | Sialidase | Sialidase | 4 |
IPR011041 | 11,041 | Soluble quinoprotein glucose/sorbosone dehydrogenase, beta-propeller domain superfamily | Quinoprot_gluc/sorb_DH_b-prop | Homologous_superfamily | 61,949 | false | false | This superfamily represents the β-propeller domain found in dehydrogenases from all cellular organisms. Quinoproteins form a class of dehydrogenases distinct from the NAD(P)- and flavin-dependent enzymes, using one of four different quinone cofactors for the oxidation of a variety of compounds. Soluble glucose dehydrog... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50952"
] | [
""
] | [
61949
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME"
] | [
"R-DDI-6791226",
"R-HSA-1989781",
"R-HSA-212436",
"R-HSA-381340",
"R-HSA-5632681",
"R-HSA-5682910",
"R-HSA-6798695",
"R-HSA-9833110",
"R-HSA-9841922",
"R-MMU-5632681",
"R-MMU-5682910",
"R-MMU-8951664",
"R-MMU-983168"
] | [
"REACTOME:R-DDI-6791226",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-212436",
"REACTOME:R-HSA-381340",
"REACTOME:R-HSA-5632681",
"REACTOME:R-HSA-5682910",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9833110",
"REACTOME:R-HSA-9841922",
"REACTOME:R-MMU-5632681",
"REACTOME:R-MMU-5682910",
"REACTOME:... | 13 | [
"1c9u",
"1cq1",
"1cru",
"1qbi",
"2g8s",
"2ism",
"2wft",
"2wfx",
"2wg3",
"2wg4",
"3a9g",
"3a9h",
"3das",
"3ho3",
"3ho4",
"3ho5",
"4zoz",
"5min",
"6h7t",
"6i1q",
"6i1t",
"6jt5",
"6jwf",
"6w1s",
"7emf",
"7ena",
"7enc",
"7enj",
"7lbm",
"7pgm",
"7pgn",
"8gxq"... | 41 | [
"PUB00014148"
] | [
"10518528"
] | [
"Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
921,
48918,
11446,
6,
658
] | 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",... | [
14,
2,
53,
4,
1,
14,
10,
3,
13,
24,
16
] | 11 | true | Homologous_superfamily | Soluble quinoprotein glucose/sorbosone dehydrogenase, beta-propeller domain superfamily | Soluble quinoprotein glucose/sorbosone dehydrogenase, beta-propeller domain superfamily | Quinoprot_gluc/sorb_DH_b-prop | 6 |
IPR011042 | 11,042 | Six-bladed beta-propeller, TolB-like | 6-blade_b-propeller_TolB-like | Homologous_superfamily | 383,743 | false | false | This superfamily represents a six-bladed β-propeller domain consisting of six 4-stranded β-sheet motifs. This domain can be found in TolB proteins (C-terminal), in soluble quinoprotein glucose dehydrogenase, in calcium-dependent phosphotriesterases, in the low density lipoprotein (LDL) receptor YWTD domain, in nidogen,... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.120.10.30"
] | [
""
] | [
383743
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-2142688",
"R-BTA-6798695",
"R-BTA-72764",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8964026",
"R-BTA-8964038",
"R-CEL-156827",
"R-CEL-2142688",
"R-CEL-6798695",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-8863795",
"R-CEL-9754706",
"R-DM... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-2142688",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-72764",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-8964026",
"REACTOME:R-BTA-8964038",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-2142688",
"REACTOME:R-CEL-6798695",
"REACTOME:R-... | 184 | [
"1c5k",
"1c9u",
"1cq1",
"1cru",
"1crz",
"1cvm",
"1e1a",
"1h6l",
"1ijq",
"1n7d",
"1npe",
"1pjx",
"1poo",
"1q7f",
"1qbi",
"1qlg",
"1rwi",
"1rwl",
"1v04",
"2dg0",
"2dg1",
"2dso",
"2fp8",
"2fp9",
"2fpb",
"2fpc",
"2g8s",
"2ghs",
"2gop",
"2gvu",
"2gvv",
"2gvw"... | 332 | [
"PUB00014149",
"PUB00014150"
] | [
"10545334",
"10673426"
] | [
"Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution.",
"The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9."
] | [
1999,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3949,
204487,
170439,
81,
4787
] | 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",... | [
156,
60,
315,
134,
4,
202,
124,
12,
128,
180,
1,
187
] | 12 | true | Homologous_superfamily | Six-bladed beta-propeller, TolB-like | Six-bladed beta-propeller, TolB-like | 6-blade_b-propeller_TolB-like | 7 |
IPR011043 | 11,043 | Galactose oxidase/kelch, beta-propeller | Gal_Oxase/kelch_b-propeller | Homologous_superfamily | 82,779 | false | false | This entry represents a β-propeller domain found in galactose oxidase and in Kelch repeat-containing proteins. The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; neuram... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50965"
] | [
""
] | [
82779
] | 1 | [
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-8951664",
"R-DME-983168",
"R-DRE-8951664",
"R-DRE-983168",
"R-HSA-1266695",
"R-HSA-5687128",
"R-HSA-9013420",
"R-HSA-9013424",
"R-HSA-9696264",
"R-HSA-9696270",
"R-HSA-9696273",
"R-HSA-9772755",
"R-HSA-9861718",
"R-MMU-4641258",
"R-MMU-8951664",
"R-MMU-983168",
"R-MMU-9861718"... | [
"REACTOME:R-DME-8951664",
"REACTOME:R-DME-983168",
"REACTOME:R-DRE-8951664",
"REACTOME:R-DRE-983168",
"REACTOME:R-HSA-1266695",
"REACTOME:R-HSA-5687128",
"REACTOME:R-HSA-9013420",
"REACTOME:R-HSA-9013424",
"REACTOME:R-HSA-9696264",
"REACTOME:R-HSA-9696270",
"REACTOME:R-HSA-9696273",
"REACTOME:... | 20 | [
"1gof",
"1gog",
"1goh",
"1k3i",
"1t2x",
"2eib",
"2eic",
"2eid",
"2eie",
"2jkx",
"2vz1",
"2vz3",
"2wq8",
"2zw9",
"2zwa",
"2zzk",
"3jbw",
"3jbx",
"3jby",
"4ch9",
"4unm",
"4wwx",
"5c86",
"5c92",
"5lqi",
"5lxz",
"5nkp",
"5yq4",
"5zdz",
"5ze0",
"5ze1",
"5ze2"... | 94 | [
"PUB00003094",
"PUB00003318",
"PUB00014151",
"PUB00014152"
] | [
"7593276",
"8126718",
"11698678",
"12418174"
] | [
"beta-Scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm.",
"Drosophila kelch motif is derived from a common enzyme fold.",
"Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.",
"Galactose oxidase."
] | [
1995,
1994,
2001,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
116,
8806,
73556,
79,
222
] | 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... | [
381,
4,
34,
5,
27,
27,
10,
116,
53,
2,
2,
140
] | 12 | true | Homologous_superfamily | Galactose oxidase/kelch, beta-propeller | Galactose oxidase/kelch, beta-propeller | Gal_Oxase/kelch_b-propeller | 9 |
IPR011044 | 11,044 | Quinoprotein amine dehydrogenase, beta chain-like | Quino_amine_DH_bsu | Homologous_superfamily | 65,672 | false | false | Quinohemoprotein amine dehydrogenase (QHNDH) from Paracoccus denitrificans is a heterotrimer consisting of alpha, beta and gamma chains [ ]. The alpha chain has a four-domain structure that includes a dihaem cytochrome c, the beta chain forms a 7-bladed β-propeller that is part of the enzyme active site, and the gamma ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50969"
] | [
""
] | [
65672
] | 1 | [
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-6791226",
"R-DME-525793",
"R-HSA-6790901",
"R-HSA-6791226",
"R-HSA-6811434",
"R-HSA-8951664",
"R-HSA-983168",
"R-MMU-6811438",
"R-MMU-6811440",
"R-MMU-8876198",
"R-SCE-6807878",
"R-SCE-6811434",
"R-SPO-6791226"
] | [
"REACTOME:R-CEL-6791226",
"REACTOME:R-DME-525793",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-HSA-6811434",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-6811438",
"REACTOME:R-MMU-6811440",
"REACTOME:R-MMU-8876198",
"REACTOME:R-SCE-6807878",
"REACTOME:... | 13 | [
"1jju",
"1jmx",
"1jmz",
"1mae",
"1maf",
"1mda",
"1mg2",
"1mg3",
"1pby",
"2agl",
"2agw",
"2agx",
"2agy",
"2agz",
"2ah0",
"2ah1",
"2bbk",
"2faw",
"2gc4",
"2gc7",
"2h3x",
"2h47",
"2hj4",
"2hjb",
"2hkm",
"2hkr",
"2hxc",
"2i0r",
"2i0s",
"2i0t",
"2iaa",
"2iup"... | 115 | [
"PUB00012384",
"PUB00013278",
"PUB00014157"
] | [
"9514722",
"11717396",
"12377130"
] | [
"Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution.",
"Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking.",
"Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domai... | [
1998,
2001,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
532,
36816,
27720,
54,
550
] | 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... | [
33,
3,
41,
15,
33,
18,
4,
36,
29,
3,
3,
60
] | 12 | true | Homologous_superfamily | Quinoprotein amine dehydrogenase, beta chain-like | Quinoprotein amine dehydrogenase, beta chain-like | Quino_amine_DH_bsu | 7 |
IPR011045 | 11,045 | Nitrous oxide reductase, N-terminal | N2O_reductase_N | Homologous_superfamily | 27,443 | false | false | This entry represents the 7-bladed β-propeller domain found in YbhE 6-phosphogluconolactonase, nitrous oxide reductase, and WD repeat-containing proteins. Nitrous oxide (N2O) reductase ( ) is a copper-containing enzyme that catalyses the two-electron reduction of the greenhouse gas N2O to N2 [ ]. N2O reductase has two ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50974"
] | [
""
] | [
27443
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1.31",
"PWY-8004",
"R-DRE-8951664",
"R-DRE-983168",
"R-HSA-114608",
"R-MMU-114608",
"R-RNO-114608",
"R-XTR-114608"
] | [
"EC:3.1.1.31",
"METACYC:PWY-8004",
"REACTOME:R-DRE-8951664",
"REACTOME:R-DRE-983168",
"REACTOME:R-HSA-114608",
"REACTOME:R-MMU-114608",
"REACTOME:R-RNO-114608",
"REACTOME:R-XTR-114608"
] | 8 | [
"1fwx",
"1qni",
"1ri6",
"2iwf",
"2iwk",
"3bws",
"3sbp",
"3sbq",
"3sbr",
"5c2v",
"5c2w",
"5i5i",
"5i5j",
"5i5m",
"6cmk",
"6igb",
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"6nau",
"6rkz",
"6rl0",
"6y6y",
"6y71",
"6y72",
"6y77",
"6y7d",
"6y7e",
"7apy",
"7aq0",
"7aq2",
"7aq3",
"7aq4",
"7aq5"... | 41 | [
"PUB00014158",
"PUB00051612",
"PUB00053730",
"PUB00158686"
] | [
"10700275",
"19345229",
"15576773",
"25613812"
] | [
"A novel type of catalytic copper cluster in nitrous oxide reductase.",
"Insights into the enzymatic mechanism of 6-phosphogluconolactonase from Trypanosoma brucei using structural data and molecular dynamics simulation.",
"Identification of the Escherichia coli K-12 ybhE gene as pgl, encoding 6-phosphogluconol... | [
2000,
2009,
2004,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
596,
22658,
3021,
11,
1157
] | 5 | [
"Arabidopsis thaliana",
"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",
"Zea mays"
] | [
3,
3,
1,
12,
8,
1,
2,
3,
6
] | 9 | true | Homologous_superfamily | Nitrous oxide reductase, N-terminal | Nitrous oxide reductase, N-terminal | N2O_reductase_N | 7 |
IPR011047 | 11,047 | Quinoprotein alcohol dehydrogenase-like superfamily | Quinoprotein_ADH-like_sf | Homologous_superfamily | 207,957 | false | false | Quinoprotein alcohol dehydrogenases are a family of proteins found in methylotrophic or autotrophic bacteria. These quinoproteins use pyrroloquinoline quinone as their prosthetic group. There are three types of alcohol dehydrogenases: type I includes methanol dehydrogenase and ethanol dehydrogenase, type II includes so... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50998"
] | [
""
] | [
207957
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1632852",
"R-BTA-165159",
"R-BTA-166208",
"R-BTA-3371571",
"R-BTA-380972",
"R-BTA-381042",
"R-BTA-5628897",
"R-BTA-8943724",
"R-BTA-9639288",
"R-BTA-9909505",
"R-CEL-110314",
"R-CEL-1169408",
"R-CEL-193648",
"R-CEL-381042",
"R-CEL-381070",
"R-CEL-416482",
"R-CEL-5620922",
"R... | [
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-165159",
"REACTOME:R-BTA-166208",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-380972",
"REACTOME:R-BTA-381042",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-8943724",
"REACTOME:R-BTA-9639288",
"REACTOME:R-BTA-9909505",
"REACTOME:R-CEL-110314",
"REACTOME:R-C... | 205 | [
"1flg",
"1g72",
"1h4i",
"1h4j",
"1kb0",
"1kv9",
"1lrw",
"1w6s",
"1yiq",
"2ad6",
"2ad7",
"2ad8",
"2b5l",
"2b5m",
"2be1",
"2d0v",
"2hye",
"2hz6",
"2yh3",
"2yms",
"2ymu",
"3ei4",
"3hx6",
"3hxj",
"3i7h",
"3i7k",
"3i7l",
"3i7n",
"3i7o",
"3i7p",
"3i89",
"3i8c"... | 437 | [
"PUB00014161",
"PUB00014162",
"PUB00014163",
"PUB00014164"
] | [
"12686102",
"12686116",
"11714714",
"11761326"
] | [
"The structure and mechanism of methanol dehydrogenase.",
"The ethanol oxidation system and its regulation in Pseudomonas aeruginosa.",
"Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.",
"Pyrroloquinoline ... | [
2003,
2003,
2002,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4873,
92186,
108250,
151,
2497
] | 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",... | [
115,
26,
174,
53,
2,
134,
89,
12,
79,
149,
7,
7,
248
] | 13 | true | Homologous_superfamily | Quinoprotein alcohol dehydrogenase-like superfamily | Quinoprotein alcohol dehydrogenase-like superfamily | Quinoprotein_ADH-like_sf | 6 |
IPR011048 | 11,048 | Cytochrome cd1-nitrite reductase-like, haem d1 domain superfamily | Haem_d1_sf | Homologous_superfamily | 44,736 | false | false | Cytochrome cd1 (cyt cd1) nitrite reductase is a dimeric enzyme of the bacterial periplasm that plays a key role in denitrification, the respiratory reduction of nitrite to nitric oxide in the nitrogen cycle. Each subunit of the cyt cd1 dimer contains one cytochrome c and one d1 haem group [ ]. The active site contains ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51004"
] | [
""
] | [
44736
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6807878",
"R-HSA-6811434",
"R-MMU-6807878",
"R-MMU-6811434"
] | [
"REACTOME:R-HSA-6807878",
"REACTOME:R-HSA-6811434",
"REACTOME:R-MMU-6807878",
"REACTOME:R-MMU-6811434"
] | 4 | [
"1aof",
"1aom",
"1aoq",
"1bl9",
"1dy7",
"1e2r",
"1gjq",
"1gq1",
"1h9x",
"1h9y",
"1hcm",
"1hj3",
"1hj4",
"1hj5",
"1hzu",
"1hzv",
"1l0q",
"1n15",
"1n50",
"1n90",
"1nir",
"1nno",
"1qks",
"3dsm",
"3fgb",
"3hfq",
"3scy",
"3vgz",
"3vh0",
"4qrj",
"5f75",
"5guw"... | 62 | [
"PUB00014166"
] | [
"12556530"
] | [
"Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
512,
33536,
6786,
12,
3890
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
2,
1,
5,
2,
5,
11,
2,
15
] | 9 | true | Homologous_superfamily | Cytochrome cd1-nitrite reductase-like, haem d1 domain superfamily | Cytochrome cd1-nitrite reductase-like, haem d1 domain superfamily | Haem_d1_sf | 8 |
IPR011049 | 11,049 | Serralysin-like metalloprotease, C-terminal | Serralysin-like_metalloprot_C | Homologous_superfamily | 73,491 | false | false | This entry represents the C-terminal domain of serralysins. The serralysin precursor does not possess a signal peptide, instead the C-terminal domain is required for secretion [ , ]. This domain is a 21-strand β sandwich known as a "parallel β roll" with the β strands arranged in a right-handed spiral. There are tandem... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF",
"SSF"
] | [
"G3DSA:2.150.10.10",
"SSF101967",
"SSF51120"
] | [
"",
"",
""
] | [
61664,
18310,
51701
] | 3 | [
"REACTOME"
] | [
"R-HSA-9760173"
] | [
"REACTOME:R-HSA-9760173"
] | 1 | [
"1af0",
"1akl",
"1g9k",
"1go7",
"1go8",
"1h71",
"1jiw",
"1k7g",
"1k7i",
"1k7q",
"1kap",
"1o0q",
"1o0t",
"1om6",
"1om7",
"1om8",
"1omj",
"1p9h",
"1sat",
"1smp",
"1srp",
"2agm",
"2ml1",
"2ml2",
"2ml3",
"2qua",
"2qub",
"2xqh",
"2ynz",
"2yo0",
"2yo1",
"2yo2"... | 95 | [
"PUB00001820",
"PUB00014467",
"PUB00030971",
"PUB00088141"
] | [
"1427098",
"12072965",
"8089845",
"2211614"
] | [
"Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways.",
"Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: highly active (>2000%) Co(II) and Cu(II) derivatives for further corro... | [
1992,
2002,
1994,
1990
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
120,
66775,
5592,
344,
660
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Oryza sativa subsp. japonica",
"Rattus norvegicus"
] | [
5,
3,
7,
4
] | 4 | true | Homologous_superfamily | Serralysin-like metalloprotease, C-terminal | Serralysin-like metalloprotease, C-terminal | Serralysin-like_metalloprot_C | 5 |
IPR011050 | 11,050 | Pectin lyase fold/virulence factor | Pectin_lyase_fold/virulence | Homologous_superfamily | 319,373 | false | false | Microbial pectin and pectate lyases are virulence factors that degrade the pectic components of the plant cell wall [ ]. When the backbone of pectin is methylated it is known as pectin and is cleaved by pectin lyase, and when it is demethylated it is known as pectate and is cleaved by pectate lyase. Pectin lyase from A... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51126"
] | [
""
] | [
319373
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-8951664",
"R-CEL-983168",
"R-DDI-418594",
"R-DDI-420499",
"R-DDI-977444",
"R-HSA-2160916",
"R-HSA-8951664",
"R-HSA-9760173",
"R-HSA-983168",
"R-HSA-9927020",
"R-MMU-2160916",
"R-MMU-8951664",
"R-MMU-983168",
"R-RNO-8951664",
"R-RNO-983168"
] | [
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-418594",
"REACTOME:R-DDI-420499",
"REACTOME:R-DDI-977444",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-8951664",
"REACTOME:R-HSA-9760173",
"REACTOME:R-HSA-983168",
"REACTOME:R-HSA-9927020",
"REACTOME:R-MMU-2160916",
"REACTOME:R-M... | 15 | [
"1air",
"1bhe",
"1bn8",
"1clw",
"1czf",
"1dab",
"1dbg",
"1dbo",
"1ee6",
"1gq8",
"1h80",
"1hg8",
"1ia5",
"1ib4",
"1idj",
"1idk",
"1jrg",
"1jta",
"1k5c",
"1kcc",
"1kcd",
"1ktw",
"1nhc",
"1o88",
"1o8d",
"1o8e",
"1o8f",
"1o8g",
"1o8h",
"1o8i",
"1o8j",
"1o8k"... | 380 | [
"PUB00009696",
"PUB00014172"
] | [
"9724625",
"9195887"
] | [
"Structure and evolution of parallel beta-helix proteins.",
"Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases."
] | [
1998,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7048,
163276,
141793,
3215,
4041
] | 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",... | [
783,
6,
21,
9,
13,
20,
18,
12,
332,
31,
1,
614
] | 12 | true | Homologous_superfamily | Pectin lyase fold/virulence factor | Pectin lyase fold/virulence factor | Pectin_lyase_fold/virulence | 4 |
IPR011051 | 11,051 | RmlC-like cupin domain superfamily | RmlC_Cupin_sf | Homologous_superfamily | 552,888 | false | false | RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase; ) is a dTDP-sugar isomerase enzyme involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria [ ]. RmlC is a dimer, each monomer being formed from two β-sheets arranged in a β-sandwich, where the ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51182"
] | [
""
] | [
552888
] | 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-1237112",
"R-BTA-159740",
"R-BTA-446205",
"R-CEL-1614558",
"R-CEL-446205",
"R-CEL-71240",
"R-CEL-8963684",
"R-DDI-1237112",
"R-DDI-1614558",
"R-DDI-446205",
"R-DDI-71240",
"R-DDI-8963684",
"R-DME-1237112",
"R-DME-8963684",
"R-DRE-1237112",
"R-DRE-71240",
"R-GGA-1237112",
"R-... | [
"REACTOME:R-BTA-1237112",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-446205",
"REACTOME:R-CEL-1614558",
"REACTOME:R-CEL-446205",
"REACTOME:R-CEL-71240",
"REACTOME:R-CEL-8963684",
"REACTOME:R-DDI-1237112",
"REACTOME:R-DDI-1614558",
"REACTOME:R-DDI-446205",
"REACTOME:R-DDI-71240",
"REACTOME:R-DDI-... | 59 | [
"1cau",
"1cav",
"1caw",
"1cax",
"1dgr",
"1dgw",
"1dzr",
"1dzt",
"1ep0",
"1epz",
"1ey2",
"1eyb",
"1fi2",
"1fxz",
"1gqg",
"1gqh",
"1h1i",
"1h1m",
"1ipj",
"1ipk",
"1j1l",
"1j3p",
"1j3q",
"1j3r",
"1j58",
"1juh",
"1l3j",
"1lkn",
"1lr5",
"1lrh",
"1nxm",
"1nyw"... | 667 | [
"PUB00003929",
"PUB00009903",
"PUB00009949",
"PUB00014173",
"PUB00014174",
"PUB00014175",
"PUB00014176",
"PUB00014177"
] | [
"8612079",
"10876237",
"10802738",
"11062559",
"12065401",
"11124907",
"12402029",
"11839311"
] | [
"The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.",
"Crystal structure of human homogentisate dioxygenase.",
"RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase.",
"Germin is a manganese containing homohexamer with oxalate ox... | [
1996,
2000,
2000,
2000,
2002,
2001,
2002,
2002
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
7465,
431537,
107642,
309,
2,
5933
] | 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",... | [
331,
11,
21,
7,
30,
45,
26,
16,
253,
50,
5,
4,
469
] | 13 | true | Homologous_superfamily | RmlC-like cupin domain superfamily | RmlC-like cupin domain superfamily | RmlC_Cupin_sf | 5 |
IPR011052 | 11,052 | Proteinase/amylase inhibitor domain superfamily | Proteinase_amylase_inhib_sf | Homologous_superfamily | 113 | false | false | This superfamily includes inhibitors of proteinases and amylases, such as trypsin inhibitors ( ) [ ], carboxypeptidase A inhibitors ( ) [ ], and alpha-amylase inhibitors (AAI) [ ]. The proteins display a knottins-like (small inhibitors, toxins, lectins) disulphide-bound fold, containing a β-hairpin with two adjacent di... | [
"GO:0004866"
] | [
"endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF57027"
] | [
""
] | [
113
] | 1 | [] | [] | [] | 0 | [
"1clv",
"1cti",
"1f2s",
"1h20",
"1h9h",
"1h9i",
"1ha9",
"1htx",
"1ib9",
"1lu0",
"1mct",
"1mcv",
"1ppe",
"1qfd",
"1w7z",
"2btc",
"2c4b",
"2cti",
"2eti",
"2hlg",
"2it7",
"2it8",
"2let",
"2ljs",
"2m7t",
"2m86",
"2mt8",
"2n8b",
"2n8c",
"2po8",
"2sta",
"2stb"... | 56 | [
"PUB00014182",
"PUB00014184",
"PUB00014185"
] | [
"12198301",
"11298757",
"12557184"
] | [
"Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination.",
"Solution structure of the main alpha-amylase inhibitor from amaranth seeds.",
"Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR."
] | [
2002,
2001,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Xanthomonas citri pv. citri"
] | [
112,
1
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Proteinase/amylase inhibitor domain superfamily | Proteinase/amylase inhibitor domain superfamily | Proteinase_amylase_inhib_sf | 5 |
IPR011053 | 11,053 | Single hybrid motif | Single_hybrid_motif | Homologous_superfamily | 234,901 | false | false | The single hybrid motif has a β-barrel sandwich hybrid fold, consisting of a sandwich of half-barrel shaped β-sheets. This motif is found in biotinyl/lipoyl-carrier proteins and domains, where the biotin and lipoic acid moieties act as covalently attached coenzyme cofactors in enzymes that catalyse metabolic reactions.... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51230"
] | [
""
] | [
234901
] | 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-196780",
"R-BTA-204174",
"R-BTA-5362517",
"R-BTA-6783984",
"R-BTA-70263",
"R-BTA-70268",
"R-BTA-70895",
"R-BTA-9013407",
"R-BTA-9837999",
"R-BTA-9857492",
"R-BTA-9859138",
"R-BTA-9861559",
"R-CEL-196780",
"R-CEL-204174",
"R-CEL-5362517",
"R-CEL-70263",
"R-CEL-70268",
"R-CEL-... | [
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-204174",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-6783984",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-9013407",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9857492",
"REACTOME:R-BTA-9859138",
"REACTOME:R-BTA-... | 121 | [
"1a6x",
"1bdo",
"1dcz",
"1dd2",
"1dxm",
"1fyc",
"1ghj",
"1ghk",
"1gjx",
"1hpc",
"1htp",
"1iyu",
"1iyv",
"1k8m",
"1k8o",
"1lab",
"1lac",
"1o78",
"1onl",
"1pmr",
"1qjo",
"1y8n",
"1y8o",
"1y8p",
"1z6h",
"1z7t",
"1zko",
"1zy8",
"2b8f",
"2b8g",
"2bdo",
"2d5d"... | 203 | [
"PUB00005256",
"PUB00014188",
"PUB00014189",
"PUB00014190"
] | [
"8747466",
"10806386",
"10913250",
"8950276"
] | [
"Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.",
"Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins.",
"Restricted motion of ... | [
1995,
2000,
2000,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2506,
173902,
55465,
7,
3021
] | 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",... | [
85,
15,
68,
18,
4,
63,
26,
8,
45,
64,
9,
6,
194
] | 13 | true | Homologous_superfamily | Single hybrid motif | Single hybrid motif | Single_hybrid_motif | 3 |
IPR011054 | 11,054 | Rudiment single hybrid motif | Rudment_hybrid_motif | Homologous_superfamily | 167,172 | false | false | The rudiment single hybrid motif has a β-barrel sandwich hybrid motif, consisting of a sandwich of half-barrel shaped β-sheets. This motif is found in the small domain of cytochrome f [ ], as well as in the C-terminal domain of the biotin carboxylase subunit of acetyl-CoA carboxylase [ ], and its family members, such a... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51246"
] | [
""
] | [
167172
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-196780",
"R-BTA-70263",
"R-BTA-70268",
"R-BTA-73817",
"R-CEL-196780",
"R-CEL-70263",
"R-CEL-70268",
"R-CEL-71032",
"R-DDI-196780",
"R-DDI-200425",
"R-DDI-70895",
"R-DDI-73817",
"R-DDI-75105",
"R-DME-73817",
"R-GGA-419140",
"R-HSA-163765",
"R-HSA-196780",
"R-HSA-200425",
"R... | [
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-73817",
"REACTOME:R-CEL-196780",
"REACTOME:R-CEL-70263",
"REACTOME:R-CEL-70268",
"REACTOME:R-CEL-71032",
"REACTOME:R-DDI-196780",
"REACTOME:R-DDI-200425",
"REACTOME:R-DDI-70895",
"REACTOME:R-DDI-73817",
... | 56 | [
"1b6r",
"1b6s",
"1bnc",
"1cfm",
"1ci3",
"1ctm",
"1dv1",
"1dv2",
"1e2v",
"1e2w",
"1e2z",
"1ewh",
"1eyz",
"1ez1",
"1gso",
"1hcz",
"1kj8",
"1kj9",
"1kji",
"1kjj",
"1kjq",
"1q90",
"1tkw",
"1tu2",
"1ulz",
"1vf5",
"1vkz",
"1w93",
"1w96",
"2c00",
"2czg",
"2d2c"... | 226 | [
"PUB00007904",
"PUB00014226",
"PUB00014227",
"PUB00014228",
"PUB00014229"
] | [
"10569930",
"10821865",
"10423236",
"9843369",
"11953435"
] | [
"Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.",
"Movement of the biotin carboxylase B-domain as a result of ATP binding.",
"Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum.",
"X-ra... | [
1999,
2000,
1999,
1998,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2484,
116743,
46072,
14,
1859
] | 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",... | [
37,
9,
58,
13,
4,
24,
18,
5,
21,
44,
7,
4,
123
] | 13 | true | Homologous_superfamily | Rudiment single hybrid motif | Rudiment single hybrid motif | Rudment_hybrid_motif | 1 |
IPR011055 | 11,055 | Duplicated hybrid motif | Dup_hybrid_motif | Homologous_superfamily | 156,110 | false | false | The duplicated hybrid motif is a structural motif that is found in certain glucose-permease-like enzymes, and consists of a half-barrel β-sheet of eight strands that is sandwiched with two 3-stranded β-sheets. Enzymes displaying this motif include domain IIa of the glucose-specific permease from bacteria ( ) ( ), which... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.70.70.10",
"SSF51261"
] | [
"",
""
] | [
155891,
152612
] | 2 | [] | [] | [] | 0 | [
"1ax3",
"1f3g",
"1f3z",
"1ggr",
"1gla",
"1glb",
"1glc",
"1gld",
"1gle",
"1gpr",
"1o2f",
"1qwy",
"2b0p",
"2b13",
"2b44",
"2f3g",
"2gpr",
"2gu1",
"2hsi",
"2mp0",
"3csq",
"3it5",
"3it7",
"3nyy",
"3our",
"3slu",
"3tuf",
"3uz0",
"4bh5",
"4jbw",
"4lxc",
"4qp5"... | 85 | [
"PUB00014245",
"PUB00160315"
] | [
"9705652",
"34281200"
] | [
"A promiscuous binding surface: crystal structure of the IIA domain of the glucose-specific permease from Mycoplasma capricolum.",
"Structural Characterization of EnpA D,L-Endopeptidase from <i>Enterococcus faecalis</i> Prophage Provides Insights into Substrate Specificity of M23 Peptidases."
] | [
1998,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
497,
150430,
2117,
858,
2208
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
7,
7,
4,
3,
3
] | 6 | true | Homologous_superfamily | Duplicated hybrid motif | Duplicated hybrid motif | Dup_hybrid_motif | 2 |
IPR011057 | 11,057 | Mss4-like superfamily | Mss4-like_sf | Homologous_superfamily | 100,056 | false | false | This superfamily represents a structural domain with a complex fold consisting of several coiled β-sheets. This domain exists as a duplication, consisting of a tandem repeat of two similar structural motifs. These domains can be found in: Mss4, which contains a zinc-binding site. Translationally controlled tumour-assoc... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51316"
] | [
""
] | [
100056
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.8.4",
"1.8.4.12",
"R-CEL-5676934",
"R-DME-5676934",
"R-DRE-5676934",
"R-HSA-5676934",
"R-MMU-5676934",
"R-RNO-5676934",
"R-SSC-5676934"
] | [
"EC:1.8.4",
"EC:1.8.4.12",
"REACTOME:R-CEL-5676934",
"REACTOME:R-DME-5676934",
"REACTOME:R-DRE-5676934",
"REACTOME:R-HSA-5676934",
"REACTOME:R-MMU-5676934",
"REACTOME:R-RNO-5676934",
"REACTOME:R-SSC-5676934"
] | 9 | [
"1fwq",
"1h6q",
"1h7y",
"1hxr",
"1l1d",
"1txj",
"1x6m",
"1xa8",
"1yz1",
"2fu5",
"2hr9",
"2k8d",
"2kv1",
"2kwb",
"2kzn",
"2l1u",
"2loy",
"3cez",
"3cxk",
"3e0m",
"3e0o",
"3ebm",
"3fac",
"3hcg",
"3hch",
"3hci",
"3hcj",
"3mao",
"3p3k",
"5fa9",
"5o9k",
"5o9l"... | 44 | [
"PUB00007168",
"PUB00014250",
"PUB00014251"
] | [
"11473261",
"11258916",
"11938352"
] | [
"Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.",
"A helical turn motif in Mss4 is a critical determinant of Rab binding and nucleotide release.",
"The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB."
] | [
2001,
2001,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
629,
61064,
37458,
8,
897
] | 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",... | [
49,
8,
15,
10,
1,
35,
13,
11,
13,
24,
3,
4,
47
] | 13 | true | Homologous_superfamily | Mss4-like superfamily | Mss4-like superfamily | Mss4-like_sf | 5 |
IPR011058 | 11,058 | Cyanovirin-N | Cyanovirin-N | Domain | 4,986 | false | false | Cyanovirin-N (CV-N) is an 11kDa protein from the cyanobacterium Nostoc ellipsosporum that displays virucidal activity against several viruses, including human immunodeficiency virus (AIDS). The virucidal activity of CV-N is mediated through specific high-affinity interactions with the viral surface envelope glycoprotei... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08881",
"SM01111"
] | [
"CVNH",
"CVNH"
] | [
4950,
3496
] | 2 | [] | [] | [] | 0 | [
"1iiy",
"1j4v",
"1l5b",
"1l5e",
"1lom",
"1n02",
"2ezm",
"2ezn",
"2jzj",
"2jzk",
"2jzl",
"2kjl",
"2l2f",
"2l9y",
"2pys",
"2rdk",
"2rp3",
"2y1s",
"2yhh",
"2z21",
"3czz",
"3ezm",
"3gxy",
"3gxz",
"3hnu",
"3hnx",
"3hp8",
"3lhc",
"3s3y",
"3s3z",
"4j4c",
"4j4d"... | 40 | [
"PUB00014252",
"PUB00014253",
"PUB00014254",
"PUB00044941"
] | [
"12678493",
"12878514",
"12110688",
"16003744"
] | [
"Cyanovirin-N: a sugar-binding antiviral protein with a new twist.",
"Potent anti-influenza activity of cyanovirin-N and interactions with viral hemagglutinin.",
"Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides.",
"The anti-HIV cyanovirin-N domain is evo... | [
2003,
2003,
2002,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Megamimivirinae",
"hydrothermal vent metagenome"
] | [
196,
4774,
15,
1
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
8
] | 1 | true | Domain | Cyanovirin-N | Cyanovirin-N | Cyanovirin-N | 9 |
IPR011059 | 11,059 | Metal-dependent hydrolase, composite domain superfamily | Metal-dep_hydrolase_composite | Homologous_superfamily | 314,099 | false | false | The composite domain of metal-dependent hydrolases has a pseudo-barrel fold that is interrupted by the catalytic β/α barrel domain. This domain is found in a variety of bacterial and fungal enzymes, including: cytosine deaminase, an enzyme that is important in the pyrimidine salvage pathway [ ]; the alpha-subunit of ur... | [
"GO:0016810"
] | [
"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.30.40.10",
"SSF51338"
] | [
"",
""
] | [
283606,
296890
] | 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-399956",
"R-BTA-446210",
"R-BTA-70921",
"R-CEL-399956",
"R-CEL-446210",
"R-CEL-500753",
"R-CEL-70921",
"R-CEL-73621",
"R-DDI-500753",
"R-DDI-70921",
"R-DDI-73621",
"R-DDI-74259",
"R-DME-446210",
"R-DME-500753",
"R-DME-74259",
"R-DRE-399956",
"R-DRE-446210",
"R-DRE-70921",
... | [
"REACTOME:R-BTA-399956",
"REACTOME:R-BTA-446210",
"REACTOME:R-BTA-70921",
"REACTOME:R-CEL-399956",
"REACTOME:R-CEL-446210",
"REACTOME:R-CEL-500753",
"REACTOME:R-CEL-70921",
"REACTOME:R-CEL-73621",
"REACTOME:R-DDI-500753",
"REACTOME:R-DDI-70921",
"REACTOME:R-DDI-73621",
"REACTOME:R-DDI-74259",
... | 43 | [
"1a5k",
"1a5l",
"1a5m",
"1a5n",
"1a5o",
"1e9y",
"1e9z",
"1ef2",
"1ejr",
"1ejs",
"1ejt",
"1eju",
"1ejv",
"1ejw",
"1ejx",
"1fwa",
"1fwb",
"1fwc",
"1fwd",
"1fwe",
"1fwf",
"1fwg",
"1fwh",
"1fwi",
"1fwj",
"1gkp",
"1gkq",
"1gkr",
"1ie7",
"1j6p",
"1k1d",
"1k6w"... | 367 | [
"PUB00014255",
"PUB00014256",
"PUB00014257",
"PUB00014258",
"PUB00014260",
"PUB00014261"
] | [
"11812140",
"12127484",
"12837777",
"12718528",
"14557261",
"12454005"
] | [
"The structure of Escherichia coli cytosine deaminase.",
"Transcriptional and mutational analysis of the Helicobacter pylori urease promoter.",
"Crystal structure of D-Hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability.",
"Hig... | [
2002,
2002,
2003,
2003,
2004,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6687,
247788,
47008,
13,
12603
] | 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",... | [
25,
8,
31,
16,
10,
52,
37,
12,
12,
45,
3,
4,
56
] | 13 | true | Homologous_superfamily | Metal-dependent hydrolase, composite domain superfamily | Metal-dependent hydrolase, composite domain superfamily | Metal-dep_hydrolase_composite | 3 |
IPR011060 | 11,060 | Ribulose-phosphate binding barrel | RibuloseP-bd_barrel | Homologous_superfamily | 236,127 | false | false | The ribulose-phosphate binding barrel consists of a parallel β-sheet barrel fold containing a phosphate-binding site. Several proteins display this fold, including histidine biosynthesis enzymes, tryptophan biosynthesis enzymes, D-ribulose-5-phosphate 3-epimerase, and decarboxylases [ ]. | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF51366"
] | [
""
] | [
236127
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-HSA-500753",
"R-HSA-71336",
"R-MMU-500753",
"R-MMU-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-HSA-500753",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-500753",
"REACTOME:R-MMU-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 9 | [
"1a50",
"1a53",
"1a5a",
"1a5b",
"1a5s",
"1beu",
"1bks",
"1c29",
"1c8v",
"1c9d",
"1cw2",
"1cx9",
"1dbt",
"1dl3",
"1dqw",
"1dqx",
"1dv7",
"1dvj",
"1eix",
"1fuy",
"1geq",
"1gpw",
"1h1y",
"1h1z",
"1h5y",
"1i4n",
"1igs",
"1j5t",
"1jcm",
"1jjk",
"1juk",
"1jul"... | 714 | [
"PUB00014262"
] | [
"11688714"
] | [
"Divergent evolution of (betaalpha)8-barrel enzymes."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"minichromosomes",
"unclassified sequences"
] | [
7299,
193066,
30789,
19,
4,
4950
] | 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",... | [
87,
3,
4,
5,
12,
19,
11,
8,
60,
11,
10,
7,
163
] | 13 | true | Homologous_superfamily | Ribulose-phosphate binding barrel | Ribulose-phosphate binding barrel | RibuloseP-bd_barrel | 4 |
IPR011061 | 11,061 | Hirudin/antistatin | Hirudin/antistatin | Homologous_superfamily | 3,247 | false | false | Leeches, such as Hirudo medicinalis (Medicinal leech), produce a variety of antihaemostatic proteins that act as proteinase inhibitors. These inhibitors are used to aid the leech in feeding upon its host by blocking blood coagulation [ , ]. Examples of these proteins include hirustasin (inhibitor of tissue kallikrein, ... | [
"GO:0004857"
] | [
"enzyme inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF57262"
] | [
""
] | [
3247
] | 1 | [] | [] | [] | 0 | [
"1bx7",
"1bx8",
"1c9p",
"1c9t",
"1dec",
"1e0f",
"1eja",
"1hia",
"1hic",
"1hrt",
"1skz",
"2hir",
"2joo",
"2pw8",
"3bg4",
"3htc",
"4hir",
"4htc",
"4mlf",
"5hir",
"5ubm",
"6hir",
"7a0d",
"7a0e",
"7a0f"
] | 25 | [
"PUB00010320",
"PUB00014230",
"PUB00014231",
"PUB00014232",
"PUB00014233",
"PUB00014234",
"PUB00014235"
] | [
"9311976",
"11563948",
"10512718",
"10368273",
"11257492",
"8607116",
"11851400"
] | [
"X-ray structure of antistasin at 1.9 A resolution and its modelled complex with blood coagulation factor Xa.",
"Proteinase inhibitors from the medicinal leech Hirudo medicinalis.",
"Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of the bdellastasin-microplasmi... | [
1997,
2001,
1999,
1999,
2001,
1995,
2002
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"viral metagenome"
] | [
19,
3223,
5
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
7,
3,
2,
2,
4
] | 6 | true | Homologous_superfamily | Hirudin/antistatin | Hirudin/antistatin | Hirudin/antistatin | 9 |
IPR011063 | 11,063 | tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal | TilS/TtcA_N | Domain | 47,647 | false | false | The structure of tRNA(Ile)-lysidine synthetase consists of an N-terminal dinucleotide-binding fold domain (NTD), and a C-terminal globular domain (CTD). The structure of the NTD closely resembles that of a P-loop "N-type" ATP pyrophosphatase [ ]. tRNA(Ile)-lysidine and 2-thiocytidine synthase both belong to the PP-loop... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01171"
] | [
"ATP_bind_3"
] | [
47647
] | 1 | [
"REACTOME"
] | [
"R-HSA-6782315"
] | [
"REACTOME:R-HSA-6782315"
] | 1 | [
"1ni5",
"1wy5",
"2e21",
"2e89",
"3a2k",
"3vrh",
"5b4e",
"5b4f",
"5gha",
"5mko",
"5mkp",
"5mkq",
"5ztb",
"6scy"
] | 14 | [
"PUB00014303",
"PUB00034489"
] | [
"7731953",
"15894617"
] | [
"A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.",
"Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain."
] | [
1994,
2005
] | 2 | [] | [
"IPR012795",
"IPR056369"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1213,
37867,
7691,
25,
851
] | 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",... | [
18,
2,
3,
1,
2,
1,
1,
2,
6,
1,
1,
2,
11
] | 13 | true | Domain | tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal | tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal | TilS/TtcA_N | 8 |
IPR011064 | 11,064 | Allophycocyanin linker chain | Allophyco_linker_chain | Homologous_superfamily | 457 | false | false | This superfamily represents the Allophycocyanin linker chain domain. | [
"GO:0015979",
"GO:0030089"
] | [
"photosynthesis",
"phycobilisome"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.1490.170",
"SSF54580"
] | [
"",
""
] | [
385,
457
] | 2 | [] | [] | [] | 0 | [
"1b33",
"5y6p",
"6kgx",
"7ext",
"7eyd",
"7ezx",
"7sc7",
"7sc9",
"7scb",
"7scc",
"7vea",
"7y4l",
"7y5e",
"7y7a",
"8to2",
"8tpj",
"8uhe",
"8wql",
"9i1r",
"9v7j",
"9v7k"
] | 21 | [
"PUB00014263"
] | [
"9990029"
] | [
"Structural analysis at 2.2 A of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex, AP.LC7.8, from phycobilisomes of Mastigocladus laminosus."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota",
"Eukaryota"
] | [
432,
25
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Allophycocyanin linker chain | Allophycocyanin linker chain | Allophyco_linker_chain | 9 |
IPR011065 | 11,065 | Kunitz inhibitor STI-like superfamily | Kunitz_inhibitor_STI-like_sf | Homologous_superfamily | 6,175 | false | false | The Kunitz-type soybean trypsin inhibitor (STI) family consists mainly of proteinase inhibitors from Leguminosae seeds [ ]. They belong to MEROPS inhibitor family I3, clan IC. They exhibit proteinase inhibitory activity against serine proteinases; trypsin (MEROPS peptidase family S1, ) and subtilisin (MEROPS peptidase ... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF50386"
] | [
""
] | [
6175
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5250955",
"R-HSA-5250958",
"R-HSA-5250968",
"R-HSA-5250971",
"R-HSA-5250981",
"R-HSA-5250982",
"R-HSA-5250989",
"R-HSA-5250992"
] | [
"REACTOME:R-HSA-5250955",
"REACTOME:R-HSA-5250958",
"REACTOME:R-HSA-5250968",
"REACTOME:R-HSA-5250971",
"REACTOME:R-HSA-5250981",
"REACTOME:R-HSA-5250982",
"REACTOME:R-HSA-5250989",
"REACTOME:R-HSA-5250992"
] | 8 | [
"1a8d",
"1af9",
"1ava",
"1avu",
"1avw",
"1avx",
"1ba7",
"1d0h",
"1dfq",
"1diw",
"1dll",
"1epw",
"1eyl",
"1f31",
"1fmz",
"1fn0",
"1fv2",
"1fv3",
"1g9a",
"1g9b",
"1g9c",
"1g9d",
"1i1e",
"1r8n",
"1r8o",
"1s0b",
"1s0c",
"1s0d",
"1s0e",
"1s0f",
"1s0g",
"1tie"... | 228 | [
"PUB00014133",
"PUB00014264"
] | [
"14705960",
"11418600"
] | [
"Evolutionary families of peptidase inhibitors.",
"The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin."
] | [
2004,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes"
] | [
299,
5871,
5
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
26,
5,
3
] | 3 | true | Homologous_superfamily | Kunitz inhibitor STI-like superfamily | Kunitz inhibitor STI-like superfamily | Kunitz_inhibitor_STI-like_sf | 4 |
IPR011066 | 11,066 | Mechanosensitive ion channel MscS, C-terminal domain superfamily | MscS_channel_C_sf | Homologous_superfamily | 63,578 | false | false | MscS is a mechanosensitive channel present in the membrane of bacteria, archaea and eukaryote thsat responds both to stretching of the cell membrane and to membrane depolarisation [ ]. MscS folds as a homo-heptamer with a cylindrical shape, and can be divided into transmembrane and extra membrane regions: an N-terminal... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"SSF"
] | [
"SSF82689"
] | [
""
] | [
63578
] | 1 | [] | [] | [] | 0 | [
"2oau",
"2vv5",
"3t9n",
"3udc",
"4age",
"4agf",
"4hw9",
"4hwa",
"5aji",
"5y4o",
"6pwn",
"6pwo",
"6pwp",
"6rld",
"6urt",
"6uzh",
"6vyk",
"6vyl",
"6vym",
"6zyd",
"6zye",
"7a46",
"7dlu",
"7n4t",
"7onj",
"7onl",
"7oo0",
"7oo6",
"7oo8",
"7ooa",
"7raz",
"7uw5"... | 46 | [
"PUB00013956",
"PUB00064132",
"PUB00101036",
"PUB00101037"
] | [
"12446901",
"23074248",
"34376558",
"23339071"
] | [
"Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel.",
"Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.",
"Mechanosensitive channel gating by delipidation.",
"Open and shut: crystal structures of the dodecylmaltos... | [
2002,
2012,
2021,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
2769,
59878,
184,
1,
746
] | 5 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Homologous_superfamily | Mechanosensitive ion channel MscS, C-terminal domain superfamily | Mechanosensitive ion channel MscS, C-terminal domain superfamily | MscS_channel_C_sf | 1 |
IPR011067 | 11,067 | Plasmid maintenance toxin/Cell growth inhibitor | Plasmid_toxin/cell-grow_inhib | Homologous_superfamily | 27,693 | false | false | Bacterial cells remove plasmid-free segregants by the use of toxin/antitoxin systems, where cells that lack plasmids cannot produce the antitoxin required for survival. Several of the toxin components have similar structures, which consists of an SH3-like barrel fold, and contains an inserted β-sheet subdomain and a C-... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.30.30.110"
] | [
""
] | [
27693
] | 1 | [] | [] | [] | 0 | [
"1m1f",
"1ne8",
"1ub4",
"1vub",
"1x75",
"2c06",
"2kmt",
"2mf2",
"2vub",
"3g7z",
"3hpw",
"3jrz",
"3jsc",
"3nfc",
"3tcj",
"3vub",
"4ely",
"4elz",
"4hke",
"4mdx",
"4me7",
"4mzm",
"4mzp",
"4mzt",
"4of1",
"4vub",
"5cca",
"5ck9",
"5ckb",
"5ckd",
"5cke",
"5ckf"... | 77 | [
"PUB00005844",
"PUB00014266",
"PUB00014267"
] | [
"9917404",
"12377128",
"12718874"
] | [
"Crystal structure of CcdB, a topoisomerase poison from E. coli.",
"Structural and functional analysis of the kid toxin protein from E. coli plasmid R1.",
"Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition."
] | [
1999,
2002,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
567,
26274,
238,
118,
2,
494
] | 6 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Homologous_superfamily | Plasmid maintenance toxin/Cell growth inhibitor | Plasmid maintenance toxin/Cell growth inhibitor | Plasmid_toxin/cell-grow_inhib | 8 |
IPR011068 | 11,068 | Nucleotidyltransferase, class I-like, C-terminal | NuclTrfase_I-like_C | Homologous_superfamily | 12,012 | false | false | Nucleotidytransferases can be divided into two classes based on highly conserved features of the nucleotidyltransferase motif [ ]. Class I enzymes include eukaryotic poly(A) polymerase (PAP), archaeal tRNA CCA-adding enzyme and possibly DNA polymerase beta, while class II enzymes include eukaryotic and eubacterial tRNA... | [
"GO:0003723",
"GO:0016779",
"GO:0031123"
] | [
"RNA binding",
"nucleotidyltransferase activity",
"RNA 3'-end processing"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"SSF"
] | [
"SSF55003"
] | [
""
] | [
12012
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.72",
"R-BTA-72187",
"R-BTA-72203",
"R-BTA-73856",
"R-BTA-77595",
"R-HSA-72187",
"R-HSA-72203",
"R-HSA-73856",
"R-HSA-77595",
"R-HSA-9930044",
"R-MMU-72187",
"R-MMU-72203",
"R-MMU-73856",
"R-MMU-77595",
"R-MMU-9930044"
] | [
"EC:2.7.7.72",
"REACTOME:R-BTA-72187",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-73856",
"REACTOME:R-BTA-77595",
"REACTOME:R-HSA-72187",
"REACTOME:R-HSA-72203",
"REACTOME:R-HSA-73856",
"REACTOME:R-HSA-77595",
"REACTOME:R-HSA-9930044",
"REACTOME:R-MMU-72187",
"REACTOME:R-MMU-72203",
"REACTOME:R... | 15 | [
"1f5a",
"1fa0",
"1q78",
"1q79",
"1r89",
"1r8a",
"1r8b",
"1r8c",
"1sz1",
"1tfw",
"1tfy",
"1uet",
"1ueu",
"1uev",
"2dr5",
"2dr7",
"2dr8",
"2dr9",
"2dra",
"2drb",
"2dvi",
"2hhp",
"2o1p",
"2q66",
"2zh1",
"2zh2",
"2zh3",
"2zh4",
"2zh5",
"2zh6",
"2zh7",
"2zh8"... | 54 | [
"PUB00008708",
"PUB00010740",
"PUB00035662"
] | [
"10944102",
"8809016",
"15590678"
] | [
"Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP.",
"CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae.",
"Archaeal CCA-add... | [
2000,
1996,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
957,
3,
11020,
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... | [
21,
3,
6,
4,
15,
11,
2,
21,
12,
1,
1,
78
] | 12 | true | Homologous_superfamily | Nucleotidyltransferase, class I-like, C-terminal | Nucleotidyltransferase, class I-like, C-terminal | NuclTrfase_I-like_C | 6 |
IPR011072 | 11,072 | HR1 rho-binding domain | HR1_rho-bd | Domain | 25,091 | false | false | This entry also includes Transducer of Cdc42-dependent actin assembly protein (TOCA) family proteins which contains a central HR1 (also known as Rho effector motif class 1, REM-1) which is closely related to Cdc42-interacting protein 4 (CIP4), effectors of the Rho family small G protein Cdc2 [ ]. HR1 was first describe... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF02185",
"PS51860",
"SM00742"
] | [
"HR1",
"REM_1",
"Hr1"
] | [
11673,
23784,
13629
] | 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-5625740",
"R-BTA-5625886",
"R-BTA-5666185",
"R-BTA-8980692",
"R-BTA-9013106",
"R-BTA-9013149",
"R-CEL-8856828",
"R-CEL-9013406",
"R-DME-5625740",
"R-DME-5625886",
"R-DME-8980692",
"R-DME-9013026",
"R-DME-9013149",
"R-DME-9856530",
"R-DRE-5625740",
"R-DRE-5666185",
"R-DRE-89806... | [
"REACTOME:R-BTA-5625740",
"REACTOME:R-BTA-5625886",
"REACTOME:R-BTA-5666185",
"REACTOME:R-BTA-8980692",
"REACTOME:R-BTA-9013106",
"REACTOME:R-BTA-9013149",
"REACTOME:R-CEL-8856828",
"REACTOME:R-CEL-9013406",
"REACTOME:R-DME-5625740",
"REACTOME:R-DME-5625886",
"REACTOME:R-DME-8980692",
"REACTOM... | 146 | [
"1cxz",
"1urf",
"2ke4",
"2rmk",
"4nkg",
"5frg",
"8p0s"
] | 7 | [
"PUB00006204",
"PUB00006205",
"PUB00006206",
"PUB00006207",
"PUB00031871",
"PUB00094802"
] | [
"7851406",
"8647255",
"9446575",
"10619026",
"14514689",
"27129201"
] | [
"Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family.",
"Characterization of the interaction between RhoA and the amino-terminal region of PKN.",
"Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif.",
"The structural basis of Rho... | [
1995,
1996,
1998,
1999,
2003,
2016
] | 6 | [] | [
"IPR037312",
"IPR037313",
"IPR037317",
"IPR049603",
"IPR057870"
] | 0 | 5 | 0 | [
"Eukaryota"
] | [
25091
] | 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... | [
6,
97,
27,
46,
46,
2,
70,
1,
3
] | 9 | true | Domain | HR1 rho-binding domain | HR1 rho-binding domain | HR1_rho-bd | 2 |
IPR011075 | 11,075 | Tetracyclin repressor-like, C-terminal domain | TetR_C | Domain | 66,273 | false | false | This entry represents the C-terminal domain found in a number of different TetR transcription regulator proteins. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit pr... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM"
] | [
"PF14514",
"PF16859",
"PF16914",
"PF16925",
"PF19352"
] | [
"TetR_C_9",
"TetR_C_11",
"TetR_C_12",
"TetR_C_13",
"TetR_C_38"
] | [
381,
26966,
294,
37549,
1084
] | 5 | [] | [] | [] | 0 | [
"2fq4",
"2g7s",
"2hku",
"2hyj",
"2i10",
"2id3",
"2qtq",
"2rha",
"2zb9",
"3bru",
"3eup",
"3knw",
"3qbm",
"3rd3",
"4jkz",
"4jl3",
"4l62",
"4yze",
"6nsm",
"6nsn",
"6nsr",
"6zui"
] | 22 | [
"PUB00003347",
"PUB00014320",
"PUB00031338",
"PUB00031782",
"PUB00035982",
"PUB00035983",
"PUB00035984",
"PUB00035985"
] | [
"7707374",
"11739955",
"15236969",
"14757054",
"16887689",
"15837373",
"1423217",
"15944459"
] | [
"The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance.",
"Structural mechanisms of QacR induction and multidrug recognition.",
"Crystal structure of the TetR/CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance.",
"Crys... | [
1995,
2001,
2004,
2004,
2003,
2005,
1992,
2005
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"unclassified sequences"
] | [
65928,
40,
8,
297
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Tetracyclin repressor-like, C-terminal domain | Tetracyclin repressor-like, C-terminal domain | TetR_C | 5 |
IPR011076 | 11,076 | Malate synthase superfamily | Malate_synth_sf | Homologous_superfamily | 22,360 | false | false | Malate synthase (MS) ( ) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. There have been identified two isoforms, A and G (MSA and MSG, respectively) that d... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF51645"
] | [
""
] | [
22360
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.3.9",
"PWY-7118",
"PWY-7294",
"PWY-7295",
"PWY-7854"
] | [
"EC:2.3.3.9",
"METACYC:PWY-7118",
"METACYC:PWY-7294",
"METACYC:PWY-7295",
"METACYC:PWY-7854"
] | 5 | [
"1d8c",
"1n8i",
"1n8w",
"1p7t",
"1y8b",
"2gq3",
"2jqx",
"3cux",
"3cuz",
"3cv1",
"3cv2",
"3s9i",
"3s9z",
"3sad",
"3saz",
"3sb0",
"4ex4",
"5c7v",
"5c9r",
"5c9u",
"5c9w",
"5c9x",
"5cah",
"5cak",
"5cbb",
"5cbi",
"5cbj",
"5cc3",
"5cc5",
"5cc6",
"5cc7",
"5ccz"... | 64 | [
"PUB00014321",
"PUB00029759",
"PUB00051135",
"PUB00163367"
] | [
"10715138",
"12930982",
"18714089",
"37043529"
] | [
"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications.",
"Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution.",
"Atomic resolution structures of Esch... | [
2000,
2003,
2008,
2023
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
53,
17192,
4923,
192
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
6,
1,
1,
2,
1,
2,
2,
5
] | 8 | true | Homologous_superfamily | Malate synthase superfamily | Malate synthase superfamily | Malate_synth_sf | 1 |
IPR011078 | 11,078 | Pyridoxal phosphate homeostasis protein | PyrdxlP_homeostasis | Family | 30,862 | false | false | Pyridoxal 5'-phosphate (PLP), the active form of vitamin B6, is an essential cofactor for nearly 60 Escherichia coli enzymes and 140 human enzymes. It is a highly reactive molecule that is toxic in its free form. The E. coli PROSC, known as yggS, binds to PLP and is involved in PLP homeostasis, supplying this cofactor ... | [
"GO:0030170"
] | [
"pyridoxal phosphate binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PIRSF",
"PROSITE",
"PANTHER",
"NCBIFAM"
] | [
"MF_02087",
"PIRSF004848",
"PS01211",
"PTHR10146",
"TIGR00044"
] | [
"PLP_homeostasis",
"YBL036c_PLPDEIII",
"UPF0001",
"",
""
] | [
29246,
28602,
16416,
30764,
29807
] | 5 | [
"PROSITEDOC"
] | [
"PDOC00931"
] | [
"PROSITEDOC:PDOC00931"
] | 1 | [
"1b54",
"1ct5",
"1w8g",
"3cpg",
"3r79",
"3sy1",
"5nlc",
"5nm8",
"6kzw",
"7f8e",
"7u9c",
"7u9h",
"7uat",
"7uau",
"7uax",
"7ub4",
"7ub8",
"7ubp",
"7ubq",
"7ygf"
] | 20 | [
"PUB00016839",
"PUB00016894",
"PUB00083213",
"PUB00083214"
] | [
"10496079",
"12499548",
"26872910",
"27912044"
] | [
"Cloning and characterization of human and mouse PROSC (proline synthetase co-transcribed) genes.",
"Structure of a yeast hypothetical protein selected by a structural genomics approach.",
"Evidence That COG0325 Proteins are involved in PLP Homeostasis.",
"Mutations in PROSC Disrupt Cellular Pyridoxal Phospha... | [
1999,
2003,
2016,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
75,
24768,
5331,
688
] | 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",... | [
9,
1,
1,
1,
1,
7,
10,
1,
7,
6,
1,
1,
12
] | 13 | true | Family | Pyridoxal phosphate homeostasis protein | Pyridoxal phosphate homeostasis protein | PyrdxlP_homeostasis | 2 |
IPR011079 | 11,079 | Alanine racemase, C-terminal | Ala_racemase_C | Domain | 32,755 | false | false | Alanine racemase ( ) plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. The molecular structure of alanine racemase from Bacillus stearothermophilus (Geobacillus stearothermophilus) was determined by X-ray crystallography to a resolution of 1.9 A [ ]. The ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00842",
"SM01005"
] | [
"Ala_racemase_C",
"Ala_racemase_C"
] | [
32702,
32691
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.1.1",
"5.1.1.1",
"PWY-7383",
"PWY-8040",
"PWY-8072",
"PWY-8443"
] | [
"EC:5.1.1",
"EC:5.1.1.1",
"METACYC:PWY-7383",
"METACYC:PWY-8040",
"METACYC:PWY-8072",
"METACYC:PWY-8443"
] | 6 | [
"1bd0",
"1epv",
"1ftx",
"1l6f",
"1l6g",
"1niu",
"1rcq",
"1sft",
"1vfh",
"1vfs",
"1vft",
"1xfc",
"1xqk",
"1xql",
"2dy3",
"2odo",
"2rjg",
"2rjh",
"2sfp",
"2vd8",
"2vd9",
"3b8t",
"3b8u",
"3b8v",
"3b8w",
"3co8",
"3e5p",
"3e6e",
"3ha1",
"3hur",
"3kw3",
"3oo2"... | 74 | [
"PUB00000440"
] | [
"9063881"
] | [
"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
31835,
278,
21,
2,
619
] | 5 | [
"Escherichia coli (strain K12)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2
] | 2 | true | Domain | Alanine racemase, C-terminal | Alanine racemase, C-terminal | Ala_racemase_C | 7 |
IPR011081 | 11,081 | Bacterial Ig-like domain | Big_4 | Domain | 4,968 | false | false | This entry represents a bacterial domain with an Ig-like fold. These domains are found in a variety of bacterial surface proteins such as Beta-L-arabinobiosidase and Exo-beta-1,6-galactobiohydrolase. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07532"
] | [
"Big_4"
] | [
4968
] | 1 | [] | [] | [] | 0 | [
"7nit",
"8q2h",
"8q4y",
"8q51",
"9fli"
] | 5 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Daphnia sinensis",
"Desulfurococcaceae",
"unclassified sequences"
] | [
4951,
1,
4,
12
] | 4 | [] | [] | 0 | true | Domain | Bacterial Ig-like domain | Bacterial Ig-like domain | Big_4 | 6 |
IPR011082 | 11,082 | Exosome-associated factor Rrp47/DNA strand repair C1D | Exosome-assoc_fac/DNA_repair | Family | 4,072 | false | false | The CD1 family of proteins includes exosome-associated cofactor Rrp47, and DNA double-strand repair protein C1D. Both of these proteins are implicated in DNA double-strand repair and in nuclear exosome activity. Rrp47 functions in nuclear RNA processing. Rrp47 is associated with nuclear exosomes, and with the nuclear e... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR15341"
] | [
""
] | [
4072
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6791226",
"R-BTA-9930044",
"R-HSA-6791226",
"R-HSA-9930044",
"R-MMU-6791226",
"R-MMU-9930044",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-9930044",
"REACTOME:R-HSA-6791226",
"REACTOME:R-HSA-9930044",
"REACTOME:R-MMU-6791226",
"REACTOME:R-MMU-9930044",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 8 | [
"4wfc",
"4wfd",
"5c0w",
"6fsz",
"6ft6",
"6lqs",
"7d4i"
] | 7 | [
"PUB00014272",
"PUB00035574",
"PUB00035575",
"PUB00035576"
] | [
"12972615",
"12421302",
"17412707",
"15148393"
] | [
"Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs.",
"Saccharomyces cerevisiae C1D is implicated in both non-homologous DNA end joining and homologous recombination.",
"C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing... | [
2003,
2002,
2007,
2004
] | 4 | [
"IPR007146"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4072
] | 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... | [
2,
1,
6,
1,
2,
2,
1,
3,
4,
1,
1,
5
] | 12 | true | Family | Exosome-associated factor Rrp47/DNA strand repair C1D | Exosome-associated factor Rrp47/DNA strand repair C1D | Exosome-assoc_fac/DNA_repair | 3 |
IPR011083 | 11,083 | Phage tail collar domain | Phage_tail_collar_dom | Domain | 14,265 | false | false | This entry is represented by a domain found in Bacteriophage T4, Gp12. The characteristics of the protein distribution suggest prophage matches in addition to the phage matches. This region is occasionally found in conjunction with . Most of the proteins appear to be phage tail proteins; however some appear to be invol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07484"
] | [
"Collar"
] | [
14265
] | 1 | [] | [] | [] | 0 | [
"1ocy",
"1pdi",
"2xgf",
"5iv5",
"5lye",
"8kec",
"9cuy",
"9mjn",
"9qgo"
] | 9 | [
"PUB00014273",
"PUB00014295"
] | [
"12888344",
"1597418"
] | [
"The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold.",
"Molecular characterization and regulation of the rhizosphere-expressed genes rhiABCR that can influence nodulation by Rhizobium leguminosarum biovar viciae."
] | [
2003,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
8,
13096,
394,
664,
103
] | 5 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Phage tail collar domain | Phage tail collar domain | Phage_tail_collar_dom | 7 |
IPR011084 | 11,084 | DNA repair metallo-beta-lactamase | DRMBL | Domain | 9,883 | false | false | The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07522"
] | [
"DRMBL"
] | [
9883
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-353248",
"R-GGA-353303",
"R-GGA-5693571",
"R-HSA-5693571",
"R-HSA-6783310",
"R-MMU-5693571",
"R-MMU-6783310",
"R-RNO-5693571",
"R-RNO-6783310"
] | [
"REACTOME:R-GGA-353248",
"REACTOME:R-GGA-353303",
"REACTOME:R-GGA-5693571",
"REACTOME:R-HSA-5693571",
"REACTOME:R-HSA-6783310",
"REACTOME:R-MMU-5693571",
"REACTOME:R-MMU-6783310",
"REACTOME:R-RNO-5693571",
"REACTOME:R-RNO-6783310"
] | 9 | [
"4b87",
"5aho",
"5ahr",
"5nzw",
"5nzx",
"5nzy",
"5q1j",
"5q1k",
"5q1l",
"5q1m",
"5q1n",
"5q1o",
"5q1p",
"5q1q",
"5q1r",
"5q1s",
"5q1t",
"5q1u",
"5q1v",
"5q1w",
"5q1x",
"5q1y",
"5q1z",
"5q20",
"5q22",
"5q23",
"5q24",
"5q25",
"5q26",
"5q27",
"5q28",
"5q29"... | 333 | [
"PUB00014290"
] | [
"12177301"
] | [
"Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Caldicellulosiruptor acetigenus",
"Eukaryota",
"Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)",
"marine sediment metagenome"
] | [
2,
9879,
1,
1
] | 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... | [
30,
1,
12,
1,
11,
7,
2,
17,
12,
1,
1,
46
] | 12 | true | Domain | DNA repair metallo-beta-lactamase | DNA repair metallo-beta-lactamase | DRMBL | 1 |
IPR011086 | 11,086 | Domain of unknown function DUF1521 | DUF1521 | Domain | 252 | false | false | This domain of unknown function is found in a limited set of Bradyrhizobium proteins. There appears to be a periodic -DG- motif in the domain. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07481"
] | [
"DUF1521"
] | [
252
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ditylenchus destructor"
] | [
251,
1
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1521 | Domain of unknown function DUF1521 | DUF1521 | 8 |
IPR011087 | 11,087 | Domain of unknown function DUF1522 | DUF1522 | Domain | 283 | false | false | The function of these proteins is unknown. They are mainly found in Bradyrhizobium. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07482"
] | [
"DUF1522"
] | [
283
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Hyphomicrobiales"
] | [
283
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1522 | Domain of unknown function DUF1522 | DUF1522 | 9 |
IPR011088 | 11,088 | Bacteriophage phiNM3, A0EWY4 | Phage_phiNM3_A0EWY4 | Family | 1,330 | false | false | This entry is represented by Bacteriophage phiNM3, . The characteristics of the protein distribution suggest prophage matches in addition to the phage matches. Members of this family are mainly found in Proteobacteria. The function of these proteins is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07509"
] | [
"DUF1523"
] | [
1330
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bastillevirinae",
"Methanobrevibacter arboriphilus JCM 13429 = DSM 1125",
"Symbiodinium necroappetens",
"metagenomes"
] | [
1312,
9,
1,
1,
7
] | 5 | [] | [] | 0 | true | Family | Bacteriophage phiNM3, A0EWY4 | Bacteriophage phiNM3, A0EWY4 | Phage_phiNM3_A0EWY4 | 1 |
IPR011089 | 11,089 | GmrSD restriction endonucleases, C-terminal domain | GmrSD_C | Domain | 17,975 | false | false | This entry (previously known as DUF1524) represents a domain found C-terminal in the GmrSD family of modification-dependent restriction endonucleases including SspE proteins [ ]. SspE is a dual-function protein that exerts both N-terminal NTPase and C-terminal DNA nicking nuclease activities to defend against phage inf... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07510"
] | [
"GmrSD_C"
] | [
17975
] | 1 | [] | [] | [] | 0 | [
"6jiv",
"7dri",
"7drr",
"7drs",
"9jfl"
] | 5 | [
"PUB00097591",
"PUB00097592",
"PUB00155272"
] | [
"29040665",
"17188711",
"36351933"
] | [
"Systematic classification of the His-Me finger superfamily.",
"Exclusion of glucosyl-hydroxymethylcytosine DNA containing bacteriophages is overcome by the injected protein inhibitor IPI*.",
"Nicking mechanism underlying the DNA phosphorothioate-sensing antiphage defense by SspE."
] | [
2017,
2007,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
272,
16300,
1134,
10,
259
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1,
1
] | 2 | true | Domain | GmrSD restriction endonucleases, C-terminal domain | GmrSD restriction endonucleases, C-terminal domain | GmrSD_C | 6 |
IPR011090 | 11,090 | Integrating conjugative element protein, PFL4709 | Integr_conj_element_PFL4709 | Family | 1,579 | false | false | This entry represents a group of proteins predominantly found in Gammaproteobacteria. Members belong to extended genomic regions that appear to be spread by conjugative transfer [ ]. | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF07511",
"TIGR03757"
] | [
"DUF1525",
"conj_TIGR03757"
] | [
1579,
1479
] | 2 | [
"GP"
] | [
"GenProp0855"
] | [
"GP:GenProp0855"
] | 1 | [] | 0 | [
"PUB00100049"
] | [
"32108566"
] | [
"Comparative genomics of the fish pathogens Edwardsiella ictaluri 93-146 and Edwardsiella piscicida C07-087."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"metagenomes"
] | [
4,
1555,
20
] | 3 | [] | [] | 0 | true | Family | Integrating conjugative element protein, PFL4709 | Integrating conjugative element protein, PFL4709 | Integr_conj_element_PFL4709 | 7 |
IPR011093 | 11,093 | Putative conjugal transfer nickase/helicase TraI, C-terminal | TraI_2_C | Domain | 2,225 | false | false | This entry contains proteins some of which are from pathogenic strains of Gammaproteobacteria. Though the function of these proteins is unknown, they could be involved in pathogenesis. This domain is found at the C terminus of proteins that contain a N-terminal metal-dependent phosphohydrolase (HD) region and are consi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07515"
] | [
"TraI_2_C"
] | [
2225
] | 1 | [] | [] | [] | 0 | [
"2ipq",
"3kq5"
] | 2 | [
"PUB00019457"
] | [
"12426355"
] | [
"Gene islands integrated into tRNA(Gly) genes confer genome diversity on a Pseudomonas aeruginosa clone."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2192,
6,
27
] | 3 | [] | [] | 0 | true | Domain | Putative conjugal transfer nickase/helicase TraI, C-terminal | Putative conjugal transfer nickase/helicase TraI, C-terminal | TraI_2_C | 7 |
IPR011094 | 11,094 | Uncharacterised protein family, LppY/LpqO | Uncharacterised_LppY/LpqO | Family | 1,975 | false | false | This family is the lppY/lpqO homologue family. They are related to 'probable conserved lipoproteins' LppY and LpqO from Mycobacterium bovis. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07485"
] | [
"DUF1529"
] | [
1975
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Pandoravirus",
"Sordariomycetes",
"ecological metagenomes"
] | [
8,
1948,
8,
4,
7
] | 5 | [] | [] | 0 | true | Family | Uncharacterised protein family, LppY/LpqO | Uncharacterised protein family, LppY/LpqO | Uncharacterised_LppY/LpqO | 9 |
IPR011095 | 11,095 | D-alanine--D-alanine ligase, C-terminal | Dala_Dala_lig_C | Domain | 40,012 | false | false | This entry represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme . D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-al... | [
"GO:0008716"
] | [
"D-alanine-D-alanine ligase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07478"
] | [
"Dala_Dala_lig_C"
] | [
40012
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.3.2.4",
"PWY-6386",
"PWY-6387",
"PWY-7953"
] | [
"EC:6.3.2.4",
"METACYC:PWY-6386",
"METACYC:PWY-6387",
"METACYC:PWY-7953"
] | 4 | [
"1e4e",
"1ehi",
"1iov",
"1iow",
"2dln",
"2fb9",
"2i80",
"2i87",
"2i8c",
"2pvp",
"2yzg",
"2yzm",
"2yzn",
"2zdg",
"2zdh",
"2zdq",
"3e5n",
"3i12",
"3k3p",
"3ln7",
"3lwb",
"3n8d",
"3q1k",
"3r23",
"3r5f",
"3r5x",
"3rfc",
"3se7",
"3tqt",
"3v4z",
"4c5a",
"4c5b"... | 67 | [
"PUB00014287"
] | [
"12499203"
] | [
"Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine."
] | [
2003
] | 1 | [
"IPR011761"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"unclassified sequences"
] | [
96,
36935,
2185,
3,
793
] | 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",
"Zea mays"
] | [
17,
2,
1,
4,
7
] | 5 | true | Domain | D-alanine--D-alanine ligase, C-terminal | D-alanine--D-alanine ligase, C-terminal | Dala_Dala_lig_C | 4 |
IPR011096 | 11,096 | FTP domain | FTP_domain | Domain | 13,607 | false | false | The fungalysin/thermolysin propeptide (FTP) domain is found in both the bacterial M4 peptidase propeptide and the fungal M36 propeptide. Its exact function is not clear, but it is likely to either inhibit the peptidase, so as to prevent its premature activation, or to have a chaperone activity. Both of these roles have... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07504"
] | [
"FTP"
] | [
13607
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"3.4.24",
"3.4.24.-",
"PWY-8119"
] | [
"EC:3.4.24",
"EC:3.4.24.-",
"METACYC:PWY-8119"
] | 3 | [
"3nqy",
"3nqz",
"4k90",
"5a3y",
"8cr3",
"8cr4",
"8cr7",
"8r1b",
"9gm4"
] | 9 | [
"PUB00014268",
"PUB00014293"
] | [
"12589825",
"8636020"
] | [
"General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease.",
"Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides."
] | [
2003,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"metagenomes"
] | [
11407,
2135,
19,
46
] | 4 | [] | [] | 0 | true | Domain | FTP domain | FTP domain | FTP_domain | 2 |
IPR011099 | 11,099 | Glycosyl hydrolase family 67, C-terminal | Glyco_hydro_67_C | Domain | 3,941 | false | false | Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C-terminal region of alpha-glucuronidase, which is mainly α-helical. It wraps around the catalytic domain ( ), mak... | [
"GO:0046559",
"GO:0045493",
"GO:0005576"
] | [
"alpha-glucuronidase activity",
"xylan catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07477"
] | [
"Glyco_hydro_67C"
] | [
3941
] | 1 | [
"EC"
] | [
"3.2.1.139"
] | [
"EC:3.2.1.139"
] | 1 | [
"1gqi",
"1gqj",
"1gqk",
"1gql",
"1h41",
"1k9d",
"1k9e",
"1k9f",
"1l8n",
"1mqp",
"1mqq",
"1mqr"
] | 12 | [
"PUB00014285"
] | [
"11937059"
] | [
"The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
2974,
901,
43,
23
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Glycosyl hydrolase family 67, C-terminal | Glycosyl hydrolase family 67, C-terminal | Glyco_hydro_67_C | 3 |
IPR011100 | 11,100 | Glycosyl hydrolase family 67, catalytic domain | Glyco_hydro_67_cat | Domain | 3,865 | false | false | Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuronidase [ ]. | [
"GO:0046559",
"GO:0045493",
"GO:0005576"
] | [
"alpha-glucuronidase activity",
"xylan catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07488"
] | [
"Glyco_hydro_67M"
] | [
3865
] | 1 | [
"EC"
] | [
"3.2.1.139"
] | [
"EC:3.2.1.139"
] | 1 | [
"1gqi",
"1gqj",
"1gqk",
"1gql",
"1h41",
"1k9d",
"1k9e",
"1k9f",
"1l8n",
"1mqp",
"1mqq",
"1mqr"
] | 12 | [
"PUB00014285"
] | [
"11937059"
] | [
"The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
2884,
914,
43,
24
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Glycosyl hydrolase family 67, catalytic domain | Glycosyl hydrolase family 67, catalytic domain | Glyco_hydro_67_cat | 3 |
IPR011101 | 11,101 | Protein of unknown function DUF5131 | DUF5131 | Family | 4,495 | false | false | This is a family of bacterial and phage proteins of unknown function. There are three highly conserved cysteine residues in the disposition Cx6Cxxc, amongst many highly conserved residues. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07505"
] | [
"DUF5131"
] | [
4495
] | 1 | [
"GP"
] | [
"GenProp1100"
] | [
"GP:GenProp1100"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [
"IPR031010"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
33,
3964,
12,
63,
423
] | 5 | [] | [] | 0 | true | Family | Protein of unknown function DUF5131 | Protein of unknown function DUF5131 | DUF5131 | 3 |
IPR011104 | 11,104 | HPr kinase/phosphorylase, C-terminal | Hpr_kin/Pase_C | Domain | 10,568 | false | false | This entry represents the C-terminal kinase domain of Hpr Serine/threonine kinase (HprK/P). HprK/P is a bifunctional histidine-containing protein kinase/phosphatase, which controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by Gram-positive bacteria. It c... | [
"GO:0000155",
"GO:0004672",
"GO:0005524",
"GO:0000160",
"GO:0006109"
] | [
"phosphorelay sensor kinase activity",
"protein kinase activity",
"ATP binding",
"phosphorelay signal transduction system",
"regulation of carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"PFAM",
"CDD"
] | [
"PF07475",
"cd01918"
] | [
"Hpr_kinase_C",
"HprK_C"
] | [
10561,
9701
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC"
] | [
"2.7.11.-",
"2.7.4.-",
"PWY-5107",
"PWY-7039"
] | [
"EC:2.7.11.-",
"EC:2.7.4.-",
"METACYC:PWY-5107",
"METACYC:PWY-7039"
] | 4 | [
"1jb1",
"1kkl",
"1kkm",
"1knx",
"1ko7",
"2qmh",
"3tqf"
] | 7 | [
"PUB00008233",
"PUB00014276",
"PUB00021974"
] | [
"9570401",
"11904409",
"15317796"
] | [
"A novel protein kinase that controls carbon catabolite repression in bacteria.",
"Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.",
"High-resolution structure of the histidine-containing pho... | [
1998,
2002,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
10433,
18,
3,
114
] | 4 | [] | [] | 0 | true | Domain | HPr kinase/phosphorylase, C-terminal | HPr kinase/phosphorylase, C-terminal | Hpr_kin/Pase_C | 6 |
IPR011105 | 11,105 | Cell wall hydrolase, SleB | Cell_wall_hydrolase_SleB | Domain | 15,051 | false | false | These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance is expressed during sporulation in an inactive form and deposited on the cell outer cortex. During germination the enzyme is activated and hydrolyses the cortex [ ]. A similar role is carried out by the parti... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07486"
] | [
"Hydrolase_2"
] | [
15051
] | 1 | [] | [] | [] | 0 | [
"4f55",
"4fet"
] | 2 | [
"PUB00014269",
"PUB00014275",
"PUB00014339",
"PUB00065266"
] | [
"9515903",
"10658652",
"10197998",
"22777830"
] | [
"Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores.",
"Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB.",
"Expression of a germination-specific amidase, SleB, of Bacilli in ... | [
1998,
2000,
1999,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
2,
14117,
180,
586,
166
] | 5 | [] | [] | 0 | true | Domain | Cell wall hydrolase, SleB | Cell wall hydrolase, SleB | Cell_wall_hydrolase_SleB | 4 |
IPR011106 | 11,106 | Seven cysteines, N-terminal | MANSC_N | Domain | 5,298 | false | false | The MANSC (motif at N terminus with seven cysteines) domain is a module with a well-conserved seven cysteine motif that is present at the N terminus of higher multicellular animal membrane and extracellular proteins. It is possible that some of the cysteine residues in the MANSC domain form structurally important disul... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00765"
] | [
"MANEC"
] | [
5298
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6806942",
"R-HSA-8852405",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-6806942",
"R-MMU-8852405",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-8856825",
"R-RNO-8856828"
] | [
"REACTOME:R-HSA-6806942",
"REACTOME:R-HSA-8852405",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-6806942",
"REACTOME:R-MMU-8852405",
"REACTOME:R-MMU-8856825",
"REACTOME:R-MMU-8856828",
"REACTOME:R-RNO-8856825",
"REACTOME:R-RNO-8856828"
] | 10 | [
"2msx",
"5h7v"
] | 2 | [
"PUB00015396"
] | [
"15124631"
] | [
"MANSC: a seven-cysteine-containing domain present in animal membrane and extracellular proteins."
] | [
2004
] | 1 | [
"IPR013980"
] | [] | 1 | 0 | 1 | [
"Metazoa"
] | [
5298
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
20,
3,
12,
13,
15
] | 5 | true | Domain | Seven cysteines, N-terminal | Seven cysteines, N-terminal | MANSC_N | 7 |
IPR011107 | 11,107 | Type 1 protein phosphatase inhibitor | PPI_Ypi1 | Family | 3,901 | false | false | This family includes Saccharomyces cerevisiae type 1 protein phosphatase inhibitor Ypi1 [ ] and human protein phosphatase 1 regulatory subunit 11 (Ppp1r11/hcgv), an atypical E3 ubiquitin-protein ligase also known to be a PP1 inhibitor [ , ]. | [
"GO:0004865"
] | [
"protein serine/threonine phosphatase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF07491",
"PTHR20835"
] | [
"PPI_Ypi1",
""
] | [
3901,
3661
] | 2 | [] | [] | [] | 0 | [
"8dwk",
"8dwl",
"8u5g"
] | 3 | [
"PUB00014282",
"PUB00086883",
"PUB00088167"
] | [
"14506263",
"9843442",
"27805901"
] | [
"Molecular characterization of Ypi1, a novel Saccharomyces cerevisiae type 1 protein phosphatase inhibitor.",
"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1.",
"RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate immunity."
] | [
2003,
1998,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3901
] | 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... | [
4,
3,
2,
8,
3,
6,
1,
6,
2,
1,
1,
1
] | 12 | true | Family | Type 1 protein phosphatase inhibitor | Type 1 protein phosphatase inhibitor | PPI_Ypi1 | 2 |
IPR011109 | 11,109 | DNA-binding recombinase domain | DNA_bind_recombinase_dom | Domain | 36,033 | false | false | The large serine recombinases (LSRs) are DNA-rearranging enzymes that are members of the serine recombinase or resolvase/invertase superfamily. Most resolvases/invertases have a catalytic domain of ~150 residues at their amino terminus, followed by a small, helix-turn-helix (HTH) DNA-binding domain. The LSRs share a si... | [
"GO:0000150",
"GO:0003677"
] | [
"DNA strand exchange activity",
"DNA binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF07508",
"PS51737"
] | [
"Recombinase",
"RECOMBINASE_DNA_BIND"
] | [
35248,
32038
] | 2 | [] | [] | [] | 0 | [
"4bqq",
"4kis",
"5udo",
"6dnw"
] | 4 | [
"PUB00074825",
"PUB00074826"
] | [
"23821671",
"23980849"
] | [
"Attachment site recognition and regulation of directionality by the serine integrases.",
"Large serine recombinase domain structure and attachment site binding."
] | [
2013,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
96,
34560,
136,
682,
559
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DNA-binding recombinase domain | DNA-binding recombinase domain | DNA_bind_recombinase_dom | 8 |
IPR011110 | 11,110 | Two component regulator propeller | Reg_prop | Repeat | 27,498 | false | false | A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to members of and indicating that they are likely to form a β-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other β-pro... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07494"
] | [
"Reg_prop"
] | [
27498
] | 1 | [] | [] | [] | 0 | [
"3ott",
"3v9f",
"3va6",
"4a2l",
"4a2m"
] | 5 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
8,
27077,
34,
1,
378
] | 5 | [] | [] | 0 | true | Repeat | Two component regulator propeller | Two component regulator propeller | Reg_prop | 3 |
IPR011111 | 11,111 | RepB plasmid partition | Plasmid_RepB | Domain | 4,315 | false | false | This family includes proteins with sequence similarity to the RepB partitioning protein of the large Ti (tumour-inducing) plasmids of Agrobacterium tumefaciens [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07506"
] | [
"RepB"
] | [
4315
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014279",
"PUB00014506"
] | [
"10613878",
"9524202"
] | [
"The replicator of the nopaline-type Ti plasmid pTiC58 is a member of the repABC family and is influenced by the TraR-dependent quorum-sensing regulatory system.",
"Novel structural difference between nopaline- and octopine-type trbJ genes: construction of genetic and physical map and sequencing of trb/traI and r... | [
2000,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Ochrobactrum phage POI1126",
"Plasmid pTiB6S3",
"ecological metagenomes"
] | [
4294,
6,
1,
1,
13
] | 5 | [] | [] | 0 | true | Domain | RepB plasmid partition | RepB plasmid partition | Plasmid_RepB | 7 |
IPR011112 | 11,112 | Rho termination factor-like, N-terminal | Rho-like_N | Domain | 26,918 | false | false | The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It is thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers [ ]. This domain is found to the N terminus of the RNA binding domain ( ). | [
"GO:0006353"
] | [
"DNA-templated transcription termination"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF07498",
"SM00959"
] | [
"Rho_N",
"Rho_N"
] | [
26286,
22744
] | 2 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"1a62",
"1a63",
"1a8v",
"1pv4",
"1pvo",
"1xpo",
"1xpr",
"1xpu",
"2a8v",
"2ht1",
"3ice",
"3l0o",
"5jji",
"5jjk",
"5jjl",
"6duq",
"6wa8",
"6xas",
"6xav",
"6z9p",
"6z9q",
"6z9r",
"6z9s",
"6z9t",
"7adb",
"7adc",
"7add",
"7ade",
"7oqh",
"7x2r",
"8e3h",
"8e5l"... | 56 | [
"PUB00014277"
] | [
"10230401"
] | [
"The structural basis for terminator recognition by the Rho transcription termination factor."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
37,
24492,
1658,
223,
508
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
23,
1,
8,
5
] | 4 | true | Domain | Rho termination factor-like, N-terminal | Rho termination factor-like, N-terminal | Rho-like_N | 4 |
IPR011113 | 11,113 | Rho termination factor, RNA-binding domain | Rho_RNA-bd | Domain | 23,533 | false | false | The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It is thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers [ ]. The Rho N-terminal domain consists of two subdomains: a three-helix bundle followed by a β-barrel. Th... | [
"GO:0003723",
"GO:0006353"
] | [
"RNA binding",
"DNA-templated transcription termination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF07497",
"PS51856",
"cd04459"
] | [
"Rho_RNA_bind",
"RHO_RNA_BD",
"Rho_CSD"
] | [
23346,
23513,
18564
] | 3 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"1a62",
"1a63",
"1a8v",
"1pv4",
"1pvo",
"1xpo",
"1xpr",
"1xpu",
"2a8v",
"2ht1",
"3ice",
"3l0o",
"5jji",
"5jjk",
"5jjl",
"6duq",
"6wa8",
"6xas",
"6xav",
"6z9p",
"6z9q",
"6z9r",
"6z9s",
"6z9t",
"7adb",
"7adc",
"7add",
"7ade",
"7oqh",
"7x2r",
"8e3h",
"8e5l"... | 56 | [
"PUB00014277",
"PUB00029986"
] | [
"10230401",
"12859904"
] | [
"The structural basis for terminator recognition by the Rho transcription termination factor.",
"Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading."
] | [
1999,
2003
] | 2 | [
"IPR011129"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
22901,
91,
541
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Rho termination factor, RNA-binding domain | Rho termination factor, RNA-binding domain | Rho_RNA-bd | 5 |
IPR011114 | 11,114 | Holliday junction DNA helicase RuvA, C-terminal | RuvA_C | Domain | 24,559 | false | false | In prokaryotes, RuvA, RuvB, and RuvC process the universal DNA intermediate of homologous recombination, termed Holliday junction. The tetrameric DNA helicase RuvA specifically binds to the Holliday junction and facilitates the isomerization of the junction from the stacked folded configuration to the square-planar str... | [
"GO:0005524",
"GO:0009378",
"GO:0006281",
"GO:0006310",
"GO:0009379"
] | [
"ATP binding",
"four-way junction helicase activity",
"DNA repair",
"DNA recombination",
"Holliday junction helicase complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM",
"CDD"
] | [
"PF07499",
"cd14332"
] | [
"RuvA_C",
"UBA_RuvA_C"
] | [
24001,
21315
] | 2 | [] | [] | [] | 0 | [
"1bdx",
"1c7y",
"1cuk",
"1hjp",
"1ixr",
"1ixs",
"2h5x",
"2ztc",
"2ztd",
"2zte",
"7oa5",
"7pbl",
"7pbm",
"7pbn",
"7pbo",
"7pbp",
"7pbq",
"7pbs",
"7pbt",
"7x7p",
"7x7q"
] | 21 | [
"PUB00013198",
"PUB00014281"
] | [
"12408833",
"10890893"
] | [
"Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.",
"Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer."
] | [
2002,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
23888,
2,
71,
44,
554
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Holliday junction DNA helicase RuvA, C-terminal | Holliday junction DNA helicase RuvA, C-terminal | RuvA_C | 3 |
IPR011115 | 11,115 | SecA DEAD-like, N-terminal | SecA_DEAD | Domain | 36,487 | false | false | SecA protein binds to the plasma membrane where it interacts with proOmpA to support translocation of proOmpA through the membrane. SecA protein achieves this translocation, in association with SecY protein, in an ATP-dependent manner [ , , ]. This domain represents the N-terminal ATP-dependent helicase domain. | [
"GO:0005524",
"GO:0017038",
"GO:0016020"
] | [
"ATP binding",
"protein import",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF07517",
"SM00957"
] | [
"SecA_DEAD",
"SecA_DEAD"
] | [
36198,
35203
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.4.2.8",
"R-HSA-1222387",
"R-HSA-9636383",
"R-HSA-9760173"
] | [
"EC:7.4.2.8",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-9636383",
"REACTOME:R-HSA-9760173"
] | 4 | [
"1m6n",
"1m74",
"1nkt",
"1nl3",
"1tf2",
"1tf5",
"2fsf",
"2fsg",
"2fsh",
"2fsi",
"2ibm",
"2ipc",
"2vda",
"3bxz",
"3din",
"3dl8",
"3iqm",
"3iqy",
"3jux",
"3jv2",
"4uaq",
"4ys0",
"5eul",
"5k94",
"5k9t",
"6gox",
"6itc",
"6s0k",
"6sxh",
"6t4h",
"7xha",
"7xhb"... | 37 | [
"PUB00001183",
"PUB00002363",
"PUB00099958"
] | [
"2542029",
"9644254",
"21051552"
] | [
"SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.",
"Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.",
"Plastids contain a second sec translocase system with ess... | [
1989,
1998,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanogaster sp.",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
31611,
1,
4152,
1,
722
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
3,
1,
8,
12
] | 5 | true | Domain | SecA DEAD-like, N-terminal | SecA DEAD-like, N-terminal | SecA_DEAD | 8 |
IPR011116 | 11,116 | SecA Wing/Scaffold | SecA_Wing/Scaffold | Domain | 32,293 | false | false | SecA protein binds to the plasma membrane where it interacts with proOmpA to support translocation of proOmpA through the membrane. SecA protein achieves this translocation, in association with SecY protein, in an ATP-dependent manner. This domain is composed of two C-terminal α helical subdomains: the wing and scaffol... | [
"GO:0017038",
"GO:0016020"
] | [
"protein import",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF07516"
] | [
"SecA_SW"
] | [
32293
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.4.2.8",
"R-HSA-1222387",
"R-HSA-9636383",
"R-HSA-9760173"
] | [
"EC:7.4.2.8",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-9636383",
"REACTOME:R-HSA-9760173"
] | 4 | [
"1m6n",
"1m74",
"1nkt",
"1nl3",
"1tf2",
"1tf5",
"2fsf",
"2fsg",
"2fsh",
"2fsi",
"2ibm",
"2ipc",
"2vda",
"3din",
"3dl8",
"3iqm",
"3iqy",
"3jux",
"3jv2",
"4uaq",
"4ys0",
"5eul",
"6gox",
"6itc",
"6s0k",
"6sxh",
"6t4h",
"7xha",
"7xhb",
"8y9y",
"8y9z",
"8ya0"... | 34 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanogaster sp.",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
29440,
1,
2157,
1,
694
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
1,
7,
11
] | 4 | true | Domain | SecA Wing/Scaffold | SecA Wing/Scaffold | SecA_Wing/Scaffold | 8 |
IPR011118 | 11,118 | Tannase/feruloyl esterase | Tannase/feruloyl_esterase | Family | 13,246 | false | false | This family includes fungal tannase [ ] and feruloyl esterase [ , ]. It also includes mono(2-hydroxyethyl) terephthalate hydrolase from the bacterium Ideonella sakaiensis [ ] and several bacterial homologues of unknown function. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07519",
"PTHR33938"
] | [
"Tannase",
""
] | [
13158,
12673
] | 2 | [
"EC",
"METACYC"
] | [
"3.1.1.73",
"PWY-6784"
] | [
"EC:3.1.1.73",
"METACYC:PWY-6784"
] | 2 | [
"3wmt",
"6fat",
"6g21",
"6jtt",
"6jtu",
"6qg9",
"6qga",
"6qgb",
"6qz1",
"6qz2",
"6qz3",
"6qz4",
"7k4o",
"8bhh",
"8ekg"
] | 15 | [
"PUB00014271",
"PUB00014296",
"PUB00014507",
"PUB00079212"
] | [
"11931668",
"8917102",
"8679110",
"26965627"
] | [
"The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds.",
"Cloning and sequencing of the gene encoding tannase and a structural study of the tannase subunit from Aspergillus oryzae.",
"Purific... | [
2002,
1996,
1996,
2016
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4745,
8476,
25
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Tannase/feruloyl esterase | Tannase/feruloyl esterase | Tannase/feruloyl_esterase | 4 |
IPR011119 | 11,119 | Uncharacterised domain, helicase/relaxase, putative | Unchr_helicase_relaxase_TraI | Domain | 3,498 | false | false | The members of this family are restricted to the proteobacteria. Some members have been annotated as helicase, conjugative relaxase or nickase. The majority contain an HD domain, which is found in a superfamily of enzymes with a predicted or known phosphohydrolase activity. These enzymes appear to be involved in the nu... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07514"
] | [
"TraI_2"
] | [
3498
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [
"IPR022391"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3453,
13,
32
] | 3 | [] | [] | 0 | true | Domain | Uncharacterised domain, helicase/relaxase, putative | Uncharacterised domain, helicase/relaxase, putative | Unchr_helicase_relaxase_TraI | 4 |
IPR011120 | 11,120 | Neutral trehalase Ca2+ binding | Trehalase_Ca-bd | Domain | 2,041 | false | false | Neutral trehalases mobilise trehalose accumulated by fungal cells as a protective and storage carbohydrate. This family represents a calcium-binding domain similar to EF hand. Residues 97 and 108 in have been implicated in this interaction. It is thought that this domain may provide a general mechanism for regulating n... | [
"GO:0004555",
"GO:0005509",
"GO:0005993",
"GO:0005737"
] | [
"alpha,alpha-trehalase activity",
"calcium ion binding",
"trehalose catabolic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF07492"
] | [
"Trehalase_Ca-bi"
] | [
2041
] | 1 | [
"EC"
] | [
"3.2.1.28"
] | [
"EC:3.2.1.28"
] | 1 | [
"5jta",
"5n6n",
"5nis"
] | 3 | [
"PUB00014291"
] | [
"12943532"
] | [
"A role for calcium in the regulation of neutral trehalase activity in the fission yeast Schizosaccharomyces pombe."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Fungi",
"Pseudomonadati"
] | [
1901,
140
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
1
] | 3 | true | Domain | Neutral trehalase Ca2+ binding | Neutral trehalase Ca2+ binding | Trehalase_Ca-bd | 8 |
IPR011121 | 11,121 | Tryptophan-rich domain | Trp-rich_dom | Domain | 187 | false | false | This entry represents a tryptophan-rich domain found in membrane proteins of Proteobacteria and Cyanobacteria. It is normally found in 2 to 3 copies. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07483"
] | [
"W_rich_C"
] | [
187
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Adineta steineri",
"Bacteria",
"ecological metagenomes"
] | [
2,
180,
5
] | 3 | [] | [] | 0 | true | Domain | Tryptophan-rich domain | Tryptophan-rich domain | Trp-rich_dom | 8 |
IPR011122 | 11,122 | WavE lipopolysaccharide synthesis | WavE | Family | 534 | false | false | These proteins are encoded by putative wav gene clusters, which are responsible for the synthesis of the core oligosaccharide (OS) region of Vibrio cholerae lipopolysaccharide [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07507"
] | [
"WavE"
] | [
534
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014280"
] | [
"11953379"
] | [
"Comparative and genetic analyses of the putative Vibrio cholerae lipopolysaccharide core oligosaccharide biosynthesis (wav) gene cluster."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Menopon gallinae",
"Nitrososphaerota",
"metagenomes"
] | [
526,
1,
3,
4
] | 4 | [] | [] | 0 | true | Family | WavE lipopolysaccharide synthesis | WavE lipopolysaccharide synthesis | WavE | 5 |
IPR011123 | 11,123 | Two component regulator three Y | Y_Y_Y | Domain | 25,767 | false | false | This region is mostly found at the end of the β-propellers ( ) in a family of two component regulators. However they are also found tandemly repeated in without other signal conduction domains being present. It is named after the conserved tyrosines found in the alignment. The exact function is not known. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07495"
] | [
"Y_Y_Y"
] | [
25767
] | 1 | [] | [] | [] | 0 | [
"3ott",
"3v9f",
"3va6",
"4a2l",
"4a2m"
] | 5 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"Stenosarchaea group",
"unclassified sequences"
] | [
25537,
11,
1,
2,
216
] | 5 | [] | [] | 0 | true | Domain | Two component regulator three Y | Two component regulator three Y | Y_Y_Y | 3 |
IPR011124 | 11,124 | Zinc finger, CW-type | Znf_CW | Domain | 16,331 | false | false | This entry represents a CW-type zinc finger motif, named for its conserved cysteine and tryptophan residues. It is predicted to be a highly specialised mononuclear four-cysteine (C4) zinc finger that plays a role in DNA binding and/or promoting protein-protein interactions in complicated eukaryotic processes including ... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF07496",
"PS51050"
] | [
"zf-CW",
"ZF_CW"
] | [
14898,
16159
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51050",
"R-HSA-3214842",
"R-HSA-5689603",
"R-HSA-75105",
"R-HSA-9029569",
"R-HSA-9843970",
"R-MMU-3214842",
"R-MMU-5689603",
"R-MMU-75105"
] | [
"PROSITEDOC:PDOC51050",
"REACTOME:R-HSA-3214842",
"REACTOME:R-HSA-5689603",
"REACTOME:R-HSA-75105",
"REACTOME:R-HSA-9029569",
"REACTOME:R-HSA-9843970",
"REACTOME:R-MMU-3214842",
"REACTOME:R-MMU-5689603",
"REACTOME:R-MMU-75105"
] | 9 | [
"2e61",
"2l7p",
"2rr4",
"4fwe",
"4fwf",
"4fwj",
"4gu0",
"4gu1",
"4gur",
"4gus",
"4gut",
"4guu",
"4hsu",
"4o62",
"4qq4",
"4z0o",
"4z0r",
"5ix1",
"5ix2",
"5of9",
"5ofa",
"5ofb",
"5svi",
"5svx",
"5svy",
"5yvx",
"6o1e",
"6o5w",
"6qxz",
"6r1u",
"6r25",
"7k7t"... | 40 | [
"PUB00014077",
"PUB00014297",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"12665246",
"14607086",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Zinc fingers--folds for many occasions.",
"The CW domain, a structural module shared amongst vertebrates, vertebrate-infecting parasites and higher plants.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: g... | [
2002,
2003,
2007,
2005,
2005,
1999,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mycobacterium ulcerans group"
] | [
16329,
2
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
54,
8,
24,
17,
38,
23,
174
] | 7 | true | Domain | Zinc finger, CW-type | Zinc finger, CW-type | Znf_CW | 1 |
IPR011125 | 11,125 | Zinc finger, HypF-type | Znf_HypF | Domain | 7,631 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07503"
] | [
"zf-HYPF"
] | [
7631
] | 1 | [] | [] | [] | 0 | [
"3tsp",
"3tsq",
"3tsu",
"3ttc",
"3ttd",
"3ttf",
"3vth",
"3vti",
"4g9i"
] | 9 | [
"PUB00011085",
"PUB00014077",
"PUB00014298",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"12206761",
"12665246",
"9492269",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.",
"Zinc fingers--folds for many occasions.",
"Rhodobacter capsulatus HypF is involved in regulation of hydrogenase synthesis through the HupUV proteins.",
"Sticky fingers: zinc-fingers as pr... | [
2002,
2002,
1998,
2007,
2005,
2005,
1999,
2001
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
408,
7080,
13,
130
] | 4 | [
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica"
] | [
1,
4
] | 2 | true | Domain | Zinc finger, HypF-type | Zinc finger, HypF-type | Znf_HypF | 8 |
IPR011126 | 11,126 | HPr(Ser) kinase/phosphorylase, N-terminal | Hpr_kin/Pase_Hpr_N | Domain | 7,660 | false | false | Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt... | [
"GO:0000155",
"GO:0004672",
"GO:0005524",
"GO:0000160",
"GO:0006109"
] | [
"phosphorelay sensor kinase activity",
"protein kinase activity",
"ATP binding",
"phosphorelay signal transduction system",
"regulation of carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"PFAM"
] | [
"PF02603"
] | [
"Hpr_kinase_N"
] | [
7660
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC"
] | [
"2.7.11.-",
"2.7.4.-",
"PWY-5107",
"PWY-7039"
] | [
"EC:2.7.11.-",
"EC:2.7.4.-",
"METACYC:PWY-5107",
"METACYC:PWY-7039"
] | 4 | [
"1knx",
"1ko7"
] | 2 | [
"PUB00008233",
"PUB00010651",
"PUB00011096",
"PUB00014276",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"9570401",
"12372152",
"10966457",
"11904409",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"A novel protein kinase that controls carbon catabolite repression in bacteria.",
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimick... | [
1998,
2002,
2000,
2002,
2005,
2007,
2002,
2001
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
7568,
16,
76
] | 3 | [] | [] | 0 | true | Domain | HPr(Ser) kinase/phosphorylase, N-terminal | HPr(Ser) kinase/phosphorylase, N-terminal | Hpr_kin/Pase_Hpr_N | 4 |
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