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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR016156 | 16,156 | FAD/NAD-linked reductase, dimerisation domain superfamily | FAD/NAD-linked_Rdtase_dimer_sf | Homologous_superfamily | 177,396 | false | false | This superfamily represents a dimerisation domain that is usually found at the C-terminal of FAD and NAD-linked reductases. This domain has a core α+β sandwich structure consisting of beta(3,4)-alpha(3). The first two domains are of the same β/β/α fold. This domain can be found in the following proteins: Glutathione re... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.390.30",
"SSF55424"
] | [
"",
""
] | [
162366,
155382
] | 2 | [
"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-204174",
"R-BTA-3299685",
"R-BTA-499943",
"R-BTA-5263617",
"R-BTA-5362517",
"R-BTA-5628897",
"R-BTA-6783984",
"R-BTA-70895",
"R-BTA-9837999",
"R-BTA-9853506",
"R-BTA-9858328",
"R-BTA-9859138",
"R-BTA-9861559",
"R-CEL-204174",
"R-CEL-3299685",
"R-CEL-499943",
"R-CEL-5263617",
... | [
"REACTOME:R-BTA-204174",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-499943",
"REACTOME:R-BTA-5263617",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-6783984",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9853506",
"REACTOME:R-BTA-9858328",
"REACTOME:R-... | 102 | [
"1alg",
"1aog",
"1bhy",
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"1bzl",
"1d7y",
"1dnc",
"1dxl",
"1ebd",
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"1ger",
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"1grf",
"1grg",
"1grh",
"1grt",
"1gsn",
"1gv4",
"1gxf",
"1h6v",
"1jeh",
"1joa"... | 398 | [
"PUB00019486",
"PUB00020217",
"PUB00024128",
"PUB00024255",
"PUB00025549",
"PUB00027231",
"PUB00027392",
"PUB00030078",
"PUB00035398",
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] | [
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"11090282",
"9546215",
"11481439",
"12198487",
"12390015",
"15095867",
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"7766608"
] | [
"Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.",
"The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution.",
"Crystal s... | [
1996,
1996,
2000,
1998,
2001,
2002,
2002,
2004,
1994,
1995
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
2962,
140825,
31708,
3,
5,
1893
] | 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",... | [
46,
10,
27,
15,
6,
47,
28,
3,
35,
33,
3,
3,
63
] | 13 | true | Homologous_superfamily | FAD/NAD-linked reductase, dimerisation domain superfamily | FAD/NAD-linked reductase, dimerisation domain superfamily | FAD/NAD-linked_Rdtase_dimer_sf | 9 |
IPR016157 | 16,157 | Cullin, conserved site | Cullin_CS | Conserved_site | 17,347 | false | false | Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express several cullins (Cul1, 2, 3, 4A, 4B, 5, 7 and 9), each forming part of a multi-subunit ubiquitin complex [ , ]. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) ... | [
"GO:0031625",
"GO:0006511",
"GO:0031461"
] | [
"ubiquitin protein ligase binding",
"ubiquitin-dependent protein catabolic process",
"cullin-RING ubiquitin ligase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS01256"
] | [
"CULLIN_1"
] | [
17347
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00967",
"R-CEL-110314",
"R-CEL-1234176",
"R-CEL-187577",
"R-CEL-195253",
"R-CEL-2565942",
"R-CEL-4641258",
"R-CEL-5632684",
"R-CEL-5696394",
"R-CEL-5696395",
"R-CEL-5696400",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-68949",
"R-CEL-69231",
"R-CEL-69601",
"R-CEL... | [
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"REACTOME:R-CEL-110314",
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"REACTOME:R-CEL-187577",
"REACTOME:R-CEL-195253",
"REACTOME:R-CEL-2565942",
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-5632684",
"REACTOME:R-CEL-5696394",
"REACTOME:R-CEL-5696395",
"REACTOME:R-CEL-5696400",
"REACTOME:R-C... | 196 | [
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"7okq",
"7oni"... | 103 | [
"PUB00000937",
"PUB00010627",
"PUB00031678",
"PUB00042618",
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"8681378",
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"15537541",
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] | [
"cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.",
"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.",
"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.",... | [
1996,
2002,
2004,
2005,
2014,
2023
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"viral metagenome"
] | [
17345,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
9,
26,
10,
43,
26,
1,
10,
34,
2,
3,
40
] | 12 | true | Conserved_site | Cullin, conserved site | Cullin, conserved site | Cullin_CS | 3 |
IPR016159 | 16,159 | Cullin repeat-like-containing domain superfamily | Cullin_repeat-like_dom_sf | Homologous_superfamily | 61,964 | false | false | This superfamily represents the N-terminal cullin repeat-containing domain; these repeats form a domain with a multi-helical 2-layered α/α structure, which in turn is folded into a right-handed superhelix. A similar structural domain is found in exocyst complex components such as EXO70 and EXO84. Cullins are a family o... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF74788"
] | [
""
] | [
61964
] | 1 | [
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-264876",
"R-BTA-5620916",
"R-CEL-110314",
"R-CEL-1234176",
"R-CEL-187577",
"R-CEL-195253",
"R-CEL-2565942",
"R-CEL-4641258",
"R-CEL-5632684",
"R-CEL-5696394",
"R-CEL-5696395",
"R-CEL-5696400",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6807878",
"R-CEL-6811438",... | [
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"REACTOME:R-BTA-5620916",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-1234176",
"REACTOME:R-CEL-187577",
"REACTOME:R-CEL-195253",
"REACTOME:R-CEL-2565942",
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-5632684",
"REACTOME:R-CEL-5696394",
"REACTOME:R-CEL-5696395",
"REACTOME:R-... | 231 | [
"1ldj",
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"1u6g",
"2b1e",
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"2pft",
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"4a0c",
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"4a0l",
"4a64",
"4ap2",
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"4rl5",
"4wqo",
"5n4w",
"5nlb",
"5yfp",
"6i2m",
"6r6h",
"6r7f",
"6r7h",
"6r7i",
"6r7n",
"6ttu"... | 122 | [
"PUB00000937",
"PUB00010627",
"PUB00031678",
"PUB00042618",
"PUB00075111",
"PUB00103546"
] | [
"8681378",
"11961546",
"15537541",
"15688063",
"24793696",
"36041947"
] | [
"cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.",
"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.",
"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.",... | [
1996,
2002,
2004,
2005,
2014,
2023
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
18,
61939,
2,
5
] | 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... | [
183,
10,
60,
20,
100,
50,
5,
193,
53,
4,
6,
254
] | 12 | true | Homologous_superfamily | Cullin repeat-like-containing domain superfamily | Cullin repeat-like-containing domain superfamily | Cullin_repeat-like_dom_sf | 2 |
IPR016161 | 16,161 | Aldehyde/histidinol dehydrogenase | Ald_DH/histidinol_DH | Homologous_superfamily | 442,330 | false | false | This entry represents a structural domain found in aldehyde dehydrogenases [ ] and histidinol dehydrogenases [ ]. These proteins contain two similar domains, each with a 3-layer α/β/α structure, which probably arose from a duplication. These enzymes bind NAD differently from other NAD(P)-dependent oxidoreductases. Alde... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF53720"
] | [
""
] | [
442330
] | 1 | [
"EC",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
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"R-BTA-380612",
"R-BTA-389661",
"R-BTA-5365859",
"R-BTA-6798695",
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"R-CEL-8964539",
"R-CEL-9837999",
"R-CFA-211945",
"R-DDI-211945",
"R-DDI-389599",... | [
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"REACTOME:R-BTA-380612",
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"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-6798695",
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"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9845614",
"REACTOME:R-CEL-6798163",
"REACTOME:R-CEL-70895",
"REA... | 127 | [
"1a4s",
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"1qi1",
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"1t90",
"1uxn",
"1uxp",
"1uxq"... | 548 | [
"PUB00000285",
"PUB00000303",
"PUB00004740",
"PUB00016238",
"PUB00022295",
"PUB00151182",
"PUB00151183",
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"3533140",
"2713359",
"2034659",
"11842181",
"12795606",
"29240402",
"8797830",
"33565183"
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"A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.",
"Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitoc... | [
1986,
1989,
1991,
2002,
2003,
2018,
1996,
2021
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
4446,
332701,
99586,
3,
6,
5588
] | 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",... | [
82,
24,
49,
60,
15,
140,
80,
16,
85,
112,
11,
9,
250
] | 13 | true | Homologous_superfamily | Aldehyde/histidinol dehydrogenase | Aldehyde/histidinol dehydrogenase | Ald_DH/histidinol_DH | 3 |
IPR016162 | 16,162 | Aldehyde dehydrogenase, N-terminal | Ald_DH_N | Homologous_superfamily | 404,869 | false | false | This superfamily represents a structural domain found at the N-terminal of aldehyde dehydrogenases [ ]. These proteins contain two similar domains, each with a 3-layer α/β/α structure, which probably arose from a duplication; this entry covers the N-terminal a/b/a domain. These enzymes binds NAD differently from other ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.605.10"
] | [
""
] | [
404869
] | 1 | [
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"R-CEL-71064",
"R-CEL-8964539",
"R-CEL-9837999",
"R-CFA-211945",
"R-DDI-211945",
"R-DDI-389599",... | [
"EC:1.2.1",
"REACTOME:R-BTA-380612",
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"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-6798695",
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"REACTOME:R-BTA-9845614",
"REACTOME:R-CEL-6798163",
"REACTOME:R-CEL-70895",
"REA... | 127 | [
"1a4s",
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"1o00",
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"1o20",
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"1qi1",
"1qi6",
"1t90",
"1uxn",
"1uxp",
"1uxq",
"1uxr",
"1uxt",
"1uxu",
"1uxv"... | 527 | [
"PUB00000303",
"PUB00022295"
] | [
"2713359",
"12795606"
] | [
"Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.",
"Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase."
] | [
1989,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3540,
302465,
94159,
3,
6,
4696
] | 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",... | [
79,
24,
49,
48,
14,
132,
79,
15,
82,
112,
10,
8,
227
] | 13 | true | Homologous_superfamily | Aldehyde dehydrogenase, N-terminal | Aldehyde dehydrogenase, N-terminal | Ald_DH_N | 7 |
IPR016163 | 16,163 | Aldehyde dehydrogenase, C-terminal | Ald_DH_C | Homologous_superfamily | 392,984 | false | false | This superfamily represents a structural domain found at the C-terminal of aldehyde dehydrogenases [ ]. These proteins contain two similar domains, each with a 3-layer α/β/α structure, which probably arose from a duplication; this entry covers the C-terminal a/b/a domain. These enzymes bind NAD differently from other N... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.309.10"
] | [
""
] | [
392984
] | 1 | [
"EC",
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"1.2.1",
"R-BTA-380612",
"R-BTA-389661",
"R-BTA-5365859",
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"R-BTA-70350",
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"R-CEL-8964539",
"R-CEL-9837999",
"R-CFA-211945",
"R-DDI-211945",
"R-DDI-389599",... | [
"EC:1.2.1",
"REACTOME:R-BTA-380612",
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"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-6798695",
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"REACTOME:R-BTA-9845614",
"REACTOME:R-CEL-6798163",
"REACTOME:R-CEL-70895",
"REA... | 127 | [
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"1uxn",
"1uxp",
"1uxq",
"1uxr",
"1uxt",
"1uxu",
"1uxv"... | 526 | [
"PUB00000303",
"PUB00022295"
] | [
"2713359",
"12795606"
] | [
"Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.",
"Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase."
] | [
1989,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3487,
295047,
90285,
3,
6,
4156
] | 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",... | [
75,
23,
49,
58,
14,
104,
67,
15,
70,
103,
10,
8,
201
] | 13 | true | Homologous_superfamily | Aldehyde dehydrogenase, C-terminal | Aldehyde dehydrogenase, C-terminal | Ald_DH_C | 9 |
IPR016164 | 16,164 | FAD-linked oxidase-like, C-terminal | FAD-linked_Oxase-like_C | Homologous_superfamily | 101,132 | false | false | This superfamily represents a structural domain found at the C-terminal of several FAD-linked oxidases. This domain consists of two structural subdomains: subdomain 1 is a 2-layer a/b or 3-layer a/b/a sandwich, and subdomain 2 is either an orthogonal α-bundle or a second 2-layer a/b sandwich. It can be found in the fol... | [
"GO:0003824",
"GO:0050660"
] | [
"catalytic activity",
"flavin adenine dinucleotide binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SSF"
] | [
"SSF55103"
] | [
""
] | [
101132
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"REACTOME:R-HSA-880009",
"REACTOME:R-HSA-9033241",
"REACTOME:R-HSA-9033500",
"REACTOME:R-HSA-9... | 23 | [
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"2qkn"... | 129 | [
"PUB00024738",
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"The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.",
"Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair.",
"Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.",
"Str... | [
2000,
2001,
1999,
2004,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
1746,
75852,
22254,
3,
8,
1269
] | 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",... | [
45,
5,
6,
5,
5,
18,
11,
4,
33,
17,
3,
1,
95
] | 13 | true | Homologous_superfamily | FAD-linked oxidase-like, C-terminal | FAD-linked oxidase-like, C-terminal | FAD-linked_Oxase-like_C | 9 |
IPR016166 | 16,166 | FAD-binding domain, PCMH-type | FAD-bd_PCMH | Domain | 261,212 | false | false | Flavoenzymes have the ability to catalyse a wide range of biochemical reactions. They are involved in the dehydrogenation of a variety of metabolites, in electron transfer from and to redox centres, in light emission, in the activation of oxygen for oxidation and hydroxylation reactions [ ]. About 1% of all eukaryotic ... | [
"GO:0071949"
] | [
"FAD binding"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS51387"
] | [
"FAD_PCMH"
] | [
261212
] | 1 | [
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"R-DME-9748787",
"R-DRE-1268020",
"R-DRE-880009",
"R-GGA-421178",... | [
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"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-74259",
"REACTOME:R-DME-75896",
"REACT... | 56 | [
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"1n62",
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"1t3q"... | 340 | [
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"PUB00032326",
"PUB00036706",
"PUB00043766",
"PUB00043767",
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"15321719",
"15723539",
"10966817",
"10694883",
"16600599",
"7248267"
] | [
"Sequence-structure analysis of FAD-containing proteins.",
"Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.",
"The crystal structure of D-lactate dehydrogenase, a peripheral membrane ... | [
2001,
2000,
2000,
2001,
2002,
1999,
2004,
2004,
1997,
2004,
2004,
2005,
2000,
2000,
2006,
1981
] | 16 | [] | [
"IPR002346",
"IPR006094"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
2627,
162993,
92856,
3,
39,
2694
] | 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",... | [
230,
11,
12,
12,
9,
32,
28,
22,
103,
48,
4,
2,
197
] | 13 | true | Domain | FAD-binding domain, PCMH-type | FAD-binding domain, PCMH-type | FAD-bd_PCMH | 8 |
IPR016167 | 16,167 | FAD-binding, type PCMH, subdomain 1 | FAD-bd_PCMH_sub1 | Homologous_superfamily | 157,027 | false | false | According to structural similarities and conserved sequence motifs, FAD-binding domains have been grouped in three main families: (i) the ferredoxin reductase (FR)-type FAD-binding domain, (ii) the FAD-binding domains that adopt a Rossmann fold and (iii) the p-cresol methylhydroxylase (PCMH)-type FAD-binding domain [ ]... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.43.10"
] | [
""
] | [
157027
] | 1 | [
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"R-HSA-75896",
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"R-HSA-885... | [
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"REACTOME:R-DME-9748787",
"REACTOME:R-DRE-88... | 42 | [
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"1n62",
"1n63",
"1qlt",
"1qlu",
"1rm6",
"1sb3",
"1t3q"... | 280 | [
"PUB00019097",
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"9020778",
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] | [
"Sequence-structure analysis of FAD-containing proteins.",
"Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism.",
"The crystal structure of D-lactate dehydrogenase, a peripheral membrane ... | [
2001,
2000,
2000,
2001,
1999,
1997,
2004,
2005,
2000,
2000
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1329,
105800,
48239,
23,
1636
] | 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",... | [
223,
4,
8,
6,
6,
26,
27,
8,
65,
42,
3,
2,
112
] | 13 | true | Homologous_superfamily | FAD-binding, type PCMH, subdomain 1 | FAD-binding, type PCMH, subdomain 1 | FAD-bd_PCMH_sub1 | 9 |
IPR016170 | 16,170 | Cytokinin dehydrogenase, C-terminal domain superfamily | Cytok_DH_C_sf | Homologous_superfamily | 10,492 | false | false | This domain superfamily is found towards the C terminus of cytokinin dehydrogenase and vanillyl-alcohol oxidase. | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.462.10"
] | [
""
] | [
10492
] | 1 | [
"EC"
] | [
"1.5.99.12"
] | [
"EC:1.5.99.12"
] | 1 | [
"1ahu",
"1ahv",
"1ahz",
"1dii",
"1diq",
"1dzn",
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"2qpm",
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"3bw7",
"3c0p"... | 86 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Edafosvirus sp.",
"Eukaryota",
"ecological metagenomes"
] | [
5,
3794,
1,
6663,
29
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
37,
21,
49
] | 3 | true | Homologous_superfamily | Cytokinin dehydrogenase, C-terminal domain superfamily | Cytokinin dehydrogenase, C-terminal domain superfamily | Cytok_DH_C_sf | 9 |
IPR016172 | 16,172 | D-lactate dehydrogenase, cap domain, subdomain 1 | D-lactate_DH_C-sub1 | Homologous_superfamily | 3,330 | false | false | The D-lactate dehydrogenase (d-LDH) structure is composed of three discontinuous domains: the FAD-binding domain (residues 1-268 and 520-571), the cap domain (residues 269-310, 388-425, and 450-519), and the membrane-binding domain (residues 311-387 and 426-449, of which residues 329-376 are in the disordered region) [... | [
"GO:0050660",
"GO:0006089",
"GO:0055085"
] | [
"flavin adenine dinucleotide binding",
"lactate metabolic process",
"transmembrane transport"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.70.610"
] | [
""
] | [
3330
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.5.12",
"PWY-5386",
"PWY-7425"
] | [
"EC:1.1.5.12",
"METACYC:PWY-5386",
"METACYC:PWY-7425"
] | 3 | [
"1f0x"
] | 1 | [
"PUB00024738",
"PUB00025871"
] | [
"10944213",
"11397813"
] | [
"The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.",
"Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair."
] | [
2000,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3308,
7,
15
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | D-lactate dehydrogenase, cap domain, subdomain 1 | D-lactate dehydrogenase, cap domain, subdomain 1 | D-lactate_DH_C-sub1 | 7 |
IPR016173 | 16,173 | D-lactate dehydrogenase, cap domain, subdomain 2 | D-lactate_DH_C-sub2 | Homologous_superfamily | 3,313 | false | false | The D-lactate dehydrogenase (d-LDH) structure is composed of three discontinuous domains: the FAD-binding domain (residues 1-268 and 520-571), the cap domain (residues 269-310, 388-425, and 450-519), and the membrane-binding domain (residues 311-387 and 426-449, of which residues 329-376 are in the disordered region) [... | [
"GO:0050660",
"GO:0006089",
"GO:0055085"
] | [
"flavin adenine dinucleotide binding",
"lactate metabolic process",
"transmembrane transport"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.1370.20"
] | [
""
] | [
3313
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.5.12",
"PWY-5386",
"PWY-7425"
] | [
"EC:1.1.5.12",
"METACYC:PWY-5386",
"METACYC:PWY-7425"
] | 3 | [
"1f0x"
] | 1 | [
"PUB00024738"
] | [
"10944213"
] | [
"The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3291,
10,
12
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | D-lactate dehydrogenase, cap domain, subdomain 2 | D-lactate dehydrogenase, cap domain, subdomain 2 | D-lactate_DH_C-sub2 | 8 |
IPR016174 | 16,174 | Di-haem cytochrome, transmembrane | Di-haem_cyt_TM | Homologous_superfamily | 331,895 | false | false | This entry represents a haem-binding domain with a 4-helical bundle structure that is found in transmembrane di-haem cytochromes. The domain contains four transmembrane helices in an up-and-down bundle, and binds two haem groups in between the helices; three of the four haem-binding residues is conserved between family... | [
"GO:0022904",
"GO:0016020"
] | [
"respiratory electron transport chain",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"SSF"
] | [
"SSF81342"
] | [
""
] | [
331895
] | 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-5419276",
"R-BTA-611105",
"R-BTA-9865881",
"R-CEL-5419276",
"R-CEL-611105",
"R-CEL-9865881",
"R-DDI-611105",
"R-DME-5419276",
"R-DME-611105",
"R-DME-9865881",
"R-DRE-611105",
"R-DRE-9865881",
"R-GGA-5419276",
"R-GGA-611105",
"R-GGA-9865881",
"R-HSA-5419276",
"R-HSA-611105",
... | [
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-9865881",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-611105",
"REACTOME:R-CEL-9865881",
"REACTOME:R-DDI-611105",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-9865881",
"REACTOME:R-DRE-611105",
"REACTOME:R-D... | 27 | [
"1bcc",
"1be3",
"1bgy",
"1ezv",
"1kb9",
"1kqf",
"1kqg",
"1kyo",
"1l0l",
"1l0n",
"1ntk",
"1ntm",
"1ntz",
"1nu1",
"1p84",
"1pp9",
"1ppj",
"1q90",
"1qcr",
"1sqb",
"1sqp",
"1sqq",
"1sqv",
"1sqx",
"1vf5",
"1zrt",
"2a06",
"2bcc",
"2d2c",
"2e74",
"2e75",
"2e76"... | 252 | [
"PUB00009871",
"PUB00032072",
"PUB00037404"
] | [
"11884747",
"14526088",
"16024040"
] | [
"Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.",
"Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity.",
"Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered... | [
2002,
2003,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctGBP5",
"unclassified sequences"
] | [
1003,
62407,
267429,
1,
1055
] | 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",... | [
10,
3,
2,
16,
7,
1984,
127,
3,
6,
94,
4,
1,
5
] | 13 | true | Homologous_superfamily | Di-haem cytochrome, transmembrane | Di-haem cytochrome, transmembrane | Di-haem_cyt_TM | 8 |
IPR016176 | 16,176 | Cobalamin (vitamin B12)-dependent enzyme, catalytic | Cbl-dep_enz_cat | Homologous_superfamily | 37,466 | false | false | This superfamily represents a structural domain with a TIM β/α barrel fold found in cobalamin (vitamin B12)-dependent enzymes, including: N-terminal coenzyme A-binding domain of both the alpha and beta subunits of methylmalonyl-CoA mutase ( ) (only the alpha subunit is active) [ ]. The large subunit of glutamate mutase... | [
"GO:0003824",
"GO:0031419"
] | [
"catalytic activity",
"cobalamin binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SSF"
] | [
"SSF51703"
] | [
""
] | [
37466
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.4.99",
"R-CEL-71032",
"R-CEL-9759218",
"R-HSA-3359475",
"R-HSA-3359478",
"R-HSA-71032",
"R-HSA-9759218",
"R-MMU-71032",
"R-MMU-9759218"
] | [
"EC:5.4.99",
"REACTOME:R-CEL-71032",
"REACTOME:R-CEL-9759218",
"REACTOME:R-HSA-3359475",
"REACTOME:R-HSA-3359478",
"REACTOME:R-HSA-71032",
"REACTOME:R-HSA-9759218",
"REACTOME:R-MMU-71032",
"REACTOME:R-MMU-9759218"
] | 9 | [
"1cb7",
"1ccw",
"1dio",
"1e1c",
"1eex",
"1egm",
"1egv",
"1i9c",
"1iwb",
"1iwp",
"1mmf",
"1req",
"1uc4",
"1uc5",
"1xrs",
"2req",
"2xij",
"2xiq",
"3auj",
"3bic",
"3kow",
"3kox",
"3koy",
"3koz",
"3kp0",
"3kp1",
"3req",
"4r3u",
"4req",
"4xc6",
"4xc7",
"4xc8"... | 55 | [
"PUB00016228",
"PUB00024521",
"PUB00033105",
"PUB00042625",
"PUB00042626"
] | [
"10467146",
"10903944",
"10387043",
"10985746",
"5514022"
] | [
"Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.",
"How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex.",
"Crystal structure of substrate complex... | [
1999,
2000,
1999,
2000,
1970
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1088,
33189,
2112,
1077
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
21,
2,
3
] | 6 | true | Homologous_superfamily | Cobalamin (vitamin B12)-dependent enzyme, catalytic | Cobalamin (vitamin B12)-dependent enzyme, catalytic | Cbl-dep_enz_cat | 9 |
IPR016177 | 16,177 | DNA-binding domain superfamily | DNA-bd_dom_sf | Homologous_superfamily | 120,667 | false | false | This superfamily represents a DNA-binding domain with a 2-layer β(3)-α fold that is found in several DNA-binding proteins, including: DNA-binding domain of tn916 integrase [ ]. N-terminal DNA-binding domain of lambda integrase [ ]. GCC-box DNA-binding domains of certain transcription factors [ ]. Methyl-CpG DNA-binding... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF54171"
] | [
""
] | [
120667
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-3214841",
"R-DME-3214841",
"R-DME-3214847",
"R-DME-5689603",
"R-DME-6804759",
"R-DME-9772755",
"R-DME-9843940",
"R-DRE-3214841",
"R-DRE-9843940",
"R-DRE-9843970",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110357",
"R-HSA-3214815",
"R-HSA-3214841",
"R-HSA-3899300",
"R-HSA-427389",... | [
"REACTOME:R-CEL-3214841",
"REACTOME:R-DME-3214841",
"REACTOME:R-DME-3214847",
"REACTOME:R-DME-5689603",
"REACTOME:R-DME-6804759",
"REACTOME:R-DME-9772755",
"REACTOME:R-DME-9843940",
"REACTOME:R-DRE-3214841",
"REACTOME:R-DRE-9843940",
"REACTOME:R-DRE-9843970",
"REACTOME:R-HSA-110328",
"REACTOME... | 51 | [
"1b69",
"1bb8",
"1d9n",
"1gcc",
"1ig4",
"1kjk",
"1qk9",
"1tn9",
"1ub1",
"1z1b",
"1z1g",
"2bb8",
"2gcc",
"2ky8",
"2mb7",
"2moe",
"2wcc",
"3c2i",
"3gcc",
"3vxv",
"3vxx",
"3vyb",
"3vyq",
"4lg7",
"5agq",
"5bt2",
"5j0n",
"5wx9",
"6acv",
"6c1a",
"6c1t",
"6c1u"... | 57 | [
"PUB00007416",
"PUB00015392",
"PUB00018484",
"PUB00030284",
"PUB00038703"
] | [
"9665166",
"11371345",
"9736626",
"10518942",
"15973401"
] | [
"Site-specific DNA binding using a variation of the double stranded RNA binding motif.",
"Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.",
"A novel mode of DNA recognition by a beta-sheet revealed by the solution structure of the GCC-box binding domain in compl... | [
1998,
2001,
1998,
1999,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
4948,
114274,
6,
1273,
166
] | 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"
] | [
678,
2,
125,
14,
1,
56,
50,
509,
51,
816
] | 10 | true | Homologous_superfamily | DNA-binding domain superfamily | DNA-binding domain superfamily | DNA-bd_dom_sf | 7 |
IPR016179 | 16,179 | Insulin-like | Insulin-like | Domain | 9,287 | false | false | This entry represents a disulphide-rich α-helical domain found in insulin [ ], as well as in related proteins, such as insulin-like growth factor [ ], relaxin [ ] and bombyxin [ ]. Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00049",
"SM00078"
] | [
"Insulin",
"IlGF"
] | [
8477,
8852
] | 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-114608",
"R-BTA-2404192",
"R-BTA-2428928",
"R-BTA-2428933",
"R-BTA-381426",
"R-BTA-418555",
"R-BTA-422085",
"R-BTA-444821",
"R-CFA-114608",
"R-CFA-2404192",
"R-CFA-2428928",
"R-CFA-2428933",
"R-CFA-264876",
"R-CFA-381426",
"R-CFA-422085",
"R-CFA-444821",
"R-CFA-6807878",
"R-... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-2404192",
"REACTOME:R-BTA-2428928",
"REACTOME:R-BTA-2428933",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-444821",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-2404192",
"REACTOME:R-CFA-2428928",
"REACTOME:R-CF... | 116 | [
"1a7f",
"1ai0",
"1aiy",
"1aph",
"1b17",
"1b18",
"1b19",
"1b2a",
"1b2b",
"1b2c",
"1b2d",
"1b2e",
"1b2f",
"1b2g",
"1b9e",
"1b9g",
"1ben",
"1bom",
"1bon",
"1bph",
"1bqt",
"1bzv",
"1cph",
"1dei",
"1dph",
"1efe",
"1ev3",
"1ev6",
"1evr",
"1fu2",
"1fub",
"1g7a"... | 503 | [
"PUB00003970",
"PUB00003972",
"PUB00003973",
"PUB00023078",
"PUB00027447",
"PUB00032303",
"PUB00036456",
"PUB00037375",
"PUB00042627",
"PUB00053639",
"PUB00053640",
"PUB00053641",
"PUB00053642",
"PUB00096674"
] | [
"503234",
"6243748",
"6107857",
"2036417",
"12595704",
"15642270",
"7473749",
"9141131",
"1656049",
"10601981",
"8735594",
"8683595",
"1319992",
"30747102"
] | [
"Nucleotide sequence of a cDNA clone encoding human preproinsulin.",
"Sequence of the human insulin gene.",
"Hormone families: pancreatic hormones and homologous growth factors.",
"Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study.",... | [
1979,
1980,
1980,
1991,
2003,
2005,
1995,
1997,
1991,
1999,
1996,
1996,
1992,
2019
] | 14 | [] | [] | 0 | 0 | null | [
"Alphairidovirinae",
"Brevibacillus brevis",
"Eukaryota",
"viral metagenome"
] | [
6,
1,
9279,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
21,
17,
24,
31,
39
] | 6 | true | Domain | Insulin-like | Insulin-like | Insulin-like | 5 |
IPR016180 | 16,180 | Large ribosomal subunit protein uL16 domain | Ribosomal_uL16_dom | Domain | 52,855 | false | false | This entry represents a structural domain with an α/β-hammerhead fold, where the β-hammerhead motif is similar to that in barrel-sandwich hybrids. Domains of this structure can be found in ribosomal proteins uL16. uL16 is an essential protein in the large ribosomal subunit of bacteria, mitochondria, and chloroplasts. L... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CDD"
] | [
"cd01433"
] | [
"Ribosomal_L16_L10e"
] | [
52855
] | 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-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-... | 89 | [
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1njm",
"1njp",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql"... | 1,763 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00032317",
"PUB00045451",
"PUB00070812",
"PUB00079547",
"PUB00079548",
"PUB00079549",
"PUB00079550",
"PUB00079551"
] | [
"11297922",
"11290319",
"11114498",
"15561149",
"17613524",
"16390447",
"16997968",
"16431913",
"11259679",
"12384386",
"9988728"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Solution structure of ribosomal protein L16 from Thermus thermophilus HB8.",
"Isolation and characterization of a dominant negative mutant of Bacillus subtili... | [
2001,
2001,
2000,
2004,
2007,
2006,
2006,
2006,
2001,
2002,
1999
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Picornavirales sp.",
"unclassified sequences"
] | [
694,
23376,
28329,
1,
455
] | 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",... | [
24,
2,
6,
4,
1,
12,
10,
2,
15,
11,
2,
3,
23
] | 13 | true | Domain | Large ribosomal subunit protein uL16 domain | Large ribosomal subunit protein uL16 domain | Ribosomal_uL16_dom | 7 |
IPR016181 | 16,181 | Acyl-CoA N-acyltransferase | Acyl_CoA_acyltransferase | Homologous_superfamily | 1,127,881 | false | false | This entry represents a structural domain found in several acyl-CoA acyltransferase enzymes. This domain has a 3-layer α/β/α structure that contains mixed β-sheets, and can be found in the following proteins: N-acetyl transferase (NAT) family members, including aminoglycoside N-acetyltransferases [ ], the histone acety... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF55729"
] | [
""
] | [
1127881
] | 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-351200",
"R-BTA-5617833",
"R-CEL-3214847",
"R-CEL-350562",
"R-CEL-351200",
"R-CEL-5693607",
"R-DDI-2514859",
"R-DDI-3214847",
"R-DDI-446210",
"R-DME-201722",
"R-DME-2468052",
"R-DME-2559586",
"R-DME-3214847",
"R-DME-350562",
"R-DME-446210",
"R-DME-5693548",
... | [
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-351200",
"REACTOME:R-BTA-5617833",
"REACTOME:R-CEL-3214847",
"REACTOME:R-CEL-350562",
"REACTOME:R-CEL-351200",
"REACTOME:R-CEL-5693607",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DDI-3214847",
"REACTOME:R-DDI-446210",
"REACTOME:R-DME-201722",
"REACTOME:R-D... | 185 | [
"1b6b",
"1b87",
"1bo4",
"1bob",
"1cjw",
"1cm0",
"1fy7",
"1ghe",
"1i12",
"1i1d",
"1i21",
"1ib1",
"1iic",
"1iid",
"1iyk",
"1iyl",
"1j4j",
"1k4j",
"1kuv",
"1kux",
"1kuy",
"1kzf",
"1l0c",
"1lrz",
"1m1d",
"1m36",
"1m44",
"1m4d",
"1m4g",
"1m4i",
"1mj9",
"1mja"... | 1,003 | [
"PUB00006453",
"PUB00014008",
"PUB00023984",
"PUB00026039",
"PUB00026875",
"PUB00027579",
"PUB00029031",
"PUB00030742",
"PUB00039506",
"PUB00040115"
] | [
"10430873",
"12176388",
"10393169",
"11371195",
"11931774",
"12592013",
"14962386",
"15306017",
"16455797",
"17242373"
] | [
"Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.",
"X-ray crystal structure of Staphylococcus aureus FemA.",
"Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.",
"Structures of Saccha... | [
1999,
2002,
1999,
2001,
2002,
2003,
2004,
2004,
2006,
2007
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
15346,
897080,
204421,
1234,
6,
9794
] | 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",... | [
264,
77,
136,
119,
27,
222,
152,
46,
153,
199,
21,
26,
369
] | 13 | true | Homologous_superfamily | Acyl-CoA N-acyltransferase | Acyl-CoA N-acyltransferase | Acyl_CoA_acyltransferase | 4 |
IPR016182 | 16,182 | Copper amine oxidase, N-terminal | Cu_amine_oxidase_N-reg | Homologous_superfamily | 17,801 | false | false | This entry represents the N-terminal region of copper amine oxidases, and has a core structure consisting of α-β(4), where the helix packs against the coiled antiparallel β-sheet [ ]. A domain with a similar structural fold can be found as the first and second domains in lysyl oxidase PplO [ ]. Amine oxidases (AO) are ... | [
"GO:0005507",
"GO:0008131",
"GO:0048038",
"GO:0009308"
] | [
"copper ion binding",
"primary methylamine oxidase activity",
"quinone binding",
"amine metabolic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"SSF"
] | [
"SSF54416"
] | [
""
] | [
17801
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3",
"1.4.3.21",
"R-BTA-211945",
"R-HSA-211945",
"R-HSA-6798695",
"R-MMU-211945",
"R-MMU-6798695",
"R-RNO-211945",
"R-RNO-6798695",
"R-SSC-211945",
"R-SSC-6798695"
] | [
"EC:1.4.3",
"EC:1.4.3.21",
"REACTOME:R-BTA-211945",
"REACTOME:R-HSA-211945",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-211945",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-211945",
"REACTOME:R-RNO-6798695",
"REACTOME:R-SSC-211945",
"REACTOME:R-SSC-6798695"
] | 11 | [
"1a2v",
"1av4",
"1avk",
"1avl",
"1d6u",
"1d6y",
"1d6z",
"1dyu",
"1ekm",
"1iqx",
"1iqy",
"1iu7",
"1ivu",
"1ivv",
"1ivw",
"1ivx",
"1jrq",
"1ksi",
"1lvn",
"1n9e",
"1oac",
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"1qaf",
"1qak",
"1qal",
"1rjo",
"1rky",
"1sih",
"1sii",
"1spu",
"1tu5",
"1ui7"... | 151 | [
"PUB00005251",
"PUB00010699",
"PUB00010700",
"PUB00010701",
"PUB00016565",
"PUB00027613"
] | [
"8591028",
"9048544",
"9405045",
"8805580",
"10576737",
"14690425"
] | [
"Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.",
"Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.",
"Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the... | [
1995,
1997,
1997,
1996,
1999,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"metagenomes"
] | [
56,
3233,
14451,
2,
59
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe... | [
44,
1,
6,
1,
8,
15,
2,
22,
13,
2,
11
] | 11 | true | Homologous_superfamily | Copper amine oxidase, N-terminal | Copper amine oxidase, N-terminal | Cu_amine_oxidase_N-reg | 8 |
IPR016183 | 16,183 | Leukocidin/Hemolysin toxin | Leukocidin/Hemolysin_toxin | Domain | 1,110 | false | false | This entry represents a structural domain consisting of a β-sandwich fold with an immunoglobulin-like Greek-key topology, and a β-ribbon arm that forms an oligomeric transmembrane barrel. Haemolysins attack blood cell membranes and cause cell rupture by forming water-filled homoheptameric transmembrane pores. Leukocidi... | [
"GO:0051715",
"GO:0005576"
] | [
"cytolysis in another organism",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF07968"
] | [
"Leukocidin"
] | [
1110
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-844456",
"R-HSA-9660826"
] | [
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-9660826"
] | 2 | [
"1lkf",
"1pvl",
"1t5r",
"1xez",
"2lkf",
"2qk7",
"2ygt",
"3anz",
"3b07",
"3lkf",
"3m2l",
"3m3r",
"3m4d",
"3m4e",
"3o44",
"3roh",
"4h56",
"4i0n",
"4idj",
"4iya",
"4iyc",
"4iyt",
"4izl",
"4j0o",
"4p1x",
"4p1y",
"4p24",
"4q7g",
"4tw1",
"4u6v",
"4yhd",
"5k59"... | 71 | [
"PUB00042629"
] | [
"16195546"
] | [
"The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
1048,
2,
60
] | 3 | [] | [] | 0 | true | Domain | Leukocidin/Hemolysin toxin | Leukocidin/Hemolysin toxin | Leukocidin/Hemolysin_toxin | 1 |
IPR016184 | 16,184 | Capsid/spike protein, ssDNA virus | Capsid/spike_ssDNA_virus | Homologous_superfamily | 13,456 | false | false | This entry represents a coat protein found in ssDNA viruses, such as the capsid protein F and the spike protein G in Microviridae [ ], the Parvovirus capsid protein [ ], the Dependovirus capsid protein [ ] and the Densovirus capsid protein [ ]. These proteins share a β-sandwich structure consisting of 8 β-strands in tw... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF88645"
] | [
""
] | [
13456
] | 1 | [] | [] | [] | 0 | [
"1al0",
"1c8d",
"1c8e",
"1c8f",
"1c8g",
"1c8h",
"1cd3",
"1dnv",
"1fpv",
"1gff",
"1ijs",
"1k3v",
"1kvp",
"1lp3",
"1m06",
"1m0f",
"1mvm",
"1p5w",
"1p5y",
"1rb8",
"1s58",
"1z14",
"1z1c",
"2bpa",
"2cas",
"2g8g",
"2qa0",
"2xgk",
"3j1q",
"3j1s",
"3j4p",
"3jcx"... | 234 | [
"PUB00019406",
"PUB00027172",
"PUB00028896",
"PUB00037580"
] | [
"9817847",
"12473449",
"12136130",
"15289612"
] | [
"The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 A resolution.",
"Structural studies of bacteriophage alpha3 assembly.",
"The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy.",
"The structure of human parvovirus B19."
] | [
1998,
2003,
2002,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"Viruses",
"organismal metagenomes"
] | [
419,
385,
4,
12643,
5
] | 5 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
10
] | 2 | true | Homologous_superfamily | Capsid/spike protein, ssDNA virus | Capsid/spike protein, ssDNA virus | Capsid/spike_ssDNA_virus | 8 |
IPR016185 | 16,185 | Pre-ATP-grasp domain superfamily | PreATP-grasp_dom_sf | Homologous_superfamily | 280,692 | false | false | The pre-ATP-grasp domain is a structural component found in many ATP-grasp enzymes. It is an N-terminal domain that precedes the core ATP-grasp fold in these proteins [ ]. While not directly involved in ATP binding, the pre-ATP-grasp domain likely plays a role in substrate recognition and binding, contributing to the o... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF52440"
] | [
""
] | [
280692
] | 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-70263",
"R-BTA-70268",
"R-BTA-73817",
"R-CEL-196780",
"R-CEL-500753",
"R-CEL-70263",
"R-CEL-70268",
"R-CEL-71032",
"R-DDI-174403",
"R-DDI-196780",
"R-DDI-200425",
"R-DDI-500753",
"R-DDI-70895",
"R-DDI-73817",
"R-DDI-75105",
"R-DME-181429",
"R-DME-212676",
"... | [
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-73817",
"REACTOME:R-CEL-196780",
"REACTOME:R-CEL-500753",
"REACTOME:R-CEL-70263",
"REACTOME:R-CEL-70268",
"REACTOME:R-CEL-71032",
"REACTOME:R-DDI-174403",
"REACTOME:R-DDI-196780",
"REACTOME:R-DDI-200425",
... | 84 | [
"1a9x",
"1auv",
"1aux",
"1b6r",
"1b6s",
"1bnc",
"1bxr",
"1c30",
"1c3o",
"1ce8",
"1cs0",
"1dv1",
"1dv2",
"1e4e",
"1ehi",
"1eyz",
"1ez1",
"1glv",
"1gsa",
"1gsh",
"1gso",
"1i7l",
"1i7n",
"1iov",
"1iow",
"1jdb",
"1kee",
"1kj8",
"1kj9",
"1kji",
"1kjj",
"1kjq"... | 325 | [
"PUB00020972",
"PUB00028114",
"PUB00057486"
] | [
"9416615",
"12392708",
"20023723"
] | [
"A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.",
"Mutational analysis of ATP-grasp residues in the two ATP sites of Saccharomyces cerevisiae carbamoyl phosphate synthetase.",
"Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains... | [
1997,
2002,
2009
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4889,
200237,
71998,
51,
3517
] | 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",... | [
64,
13,
73,
23,
11,
66,
48,
10,
32,
76,
10,
7,
119
] | 13 | true | Homologous_superfamily | Pre-ATP-grasp domain superfamily | Pre-ATP-grasp domain superfamily | PreATP-grasp_dom_sf | 9 |
IPR016186 | 16,186 | C-type lectin-like/link domain superfamily | C-type_lectin-like/link_sf | Homologous_superfamily | 163,790 | false | false | Lectins occur in plants, animals, bacteria and viruses. Initially described for their carbohydrate-binding activity [ ], they are now recognised as a more diverse group of proteins, some of which are involved in protein-protein, protein-lipid or protein-nucleic acid interactions [ ]. There are at least twelve structura... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.10.100.10"
] | [
""
] | [
163790
] | 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-1482788",
"R-BTA-1482801",
"R-BTA-1482839",
"R-BTA-1482922",
"R-BTA-1482925",
"R-BTA-1483166",
"R-BTA-166016",
"R-BTA-166662",
"R-BTA-166663",
"R-BTA-1971475",
"R-BTA-198933",
"R-BTA-2022870",
"R-BTA-2022923",
"R-BTA-2024101",
"R-BTA-202733",
"R-BTA-2142845",
"R-BTA-2160916",
... | [
"REACTOME:R-BTA-1482788",
"REACTOME:R-BTA-1482801",
"REACTOME:R-BTA-1482839",
"REACTOME:R-BTA-1482922",
"REACTOME:R-BTA-1482925",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-166662",
"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-1971475",
"REACTOME:R-BTA-198933",
"REACTOME:R-... | 228 | [
"1afa",
"1afb",
"1afd",
"1b08",
"1b6e",
"1bch",
"1bcj",
"1bj3",
"1bnl",
"1buu",
"1bv4",
"1byf",
"1c3a",
"1cwv",
"1dv8",
"1dy0",
"1dy1",
"1dy2",
"1e5u",
"1e87",
"1e8i",
"1egg",
"1egi",
"1esl",
"1f00",
"1f02",
"1fif",
"1fih",
"1fm5",
"1fvu",
"1g1q",
"1g1r"... | 538 | [
"PUB00001702",
"PUB00006623",
"PUB00018560",
"PUB00021244",
"PUB00022318",
"PUB00022805",
"PUB00024352",
"PUB00042634",
"PUB00042635",
"PUB00042644",
"PUB00081335"
] | [
"8690089",
"10890451",
"10514372",
"9724722",
"12972412",
"14992719",
"10966814",
"14533786",
"12223269",
"15476922",
"16336259"
] | [
"The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily.",
"Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.",
"Crystal structure of invasin: a bacterial integrin-binding... | [
1996,
2000,
1999,
1998,
2003,
2004,
2000,
2001,
2002,
2004,
2005
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
25,
4581,
158305,
563,
316
] | 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"
] | [
6,
279,
517,
132,
1,
336,
449,
4,
505,
2
] | 10 | true | Homologous_superfamily | C-type lectin-like/link domain superfamily | C-type lectin-like/link domain superfamily | C-type_lectin-like/link_sf | 9 |
IPR016187 | 16,187 | C-type lectin fold | CTDL_fold | Homologous_superfamily | 227,196 | false | false | Lectins occur in plants, animals, bacteria and viruses. Initially described for their carbohydrate-binding activity [ ], they are now recognised as a more diverse group of proteins, some of which are involved in protein-protein, protein-lipid or protein-nucleic acid interactions [ ]. There are at least twelve structura... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF56436"
] | [
""
] | [
227196
] | 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-1442490",
"R-BTA-1482788",
"R-BTA-1482801",
"R-BTA-1482839",
"R-BTA-1482922",
"R-BTA-1482925",
"R-BTA-1483166",
"R-BTA-1566977",
"R-BTA-1650814",
"R-BTA-166016",
"R-BTA-1663150",
"R-BTA-166662",
"R-BTA-166663",
"R-BTA-186797",
"R-BTA-1971475",
"R-BTA-198933",
"R-BTA-2022090",
... | [
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1482788",
"REACTOME:R-BTA-1482801",
"REACTOME:R-BTA-1482839",
"REACTOME:R-BTA-1482922",
"REACTOME:R-BTA-1482925",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-1566977",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-1663150",
"REACTOME... | 268 | [
"1afa",
"1afb",
"1afd",
"1b08",
"1b6e",
"1bch",
"1bcj",
"1bcp",
"1bj3",
"1bnl",
"1buu",
"1bv4",
"1byf",
"1c3a",
"1cwv",
"1dv8",
"1dy0",
"1dy1",
"1dy2",
"1e5u",
"1e87",
"1e8i",
"1egg",
"1egi",
"1esl",
"1f00",
"1f02",
"1fif",
"1fih",
"1fm5",
"1fvu",
"1g1q"... | 646 | [
"PUB00004166",
"PUB00006623",
"PUB00018560",
"PUB00020076",
"PUB00021244",
"PUB00022318",
"PUB00022805",
"PUB00027036",
"PUB00032580",
"PUB00035615",
"PUB00038630",
"PUB00042634",
"PUB00042635",
"PUB00042644",
"PUB00042646"
] | [
"7510043",
"10890451",
"10514372",
"8637000",
"9724722",
"12972412",
"14992719",
"12011424",
"15687489",
"16041070",
"16170324",
"14533786",
"12223269",
"15476922",
"966814"
] | [
"Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states.",
"Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.",
"Crystal structure of invasin: a bacterial integrin-binding protein.",
"Crystal structure of the pertussis toxin-ATP complex: a... | [
1994,
2000,
1999,
1996,
1998,
2003,
2004,
2002,
2005,
2005,
2005,
2001,
2002,
2004,
1976
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
289,
48141,
176883,
602,
1281
] | 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",
"Schizosaccharomyces pombe (stra... | [
6,
303,
535,
139,
405,
479,
1,
4,
540,
1,
2
] | 11 | true | Homologous_superfamily | C-type lectin fold | C-type lectin fold | CTDL_fold | 7 |
IPR016188 | 16,188 | PurM-like, N-terminal domain | PurM-like_N | Domain | 89,085 | false | false | This entry represents a structural domain with a core structure consisting of β-α-β-α-β(2), which is found in two enzymes of the purine biosynthetic pathway: at the N-terminal of aminoimidazole ribonucleotide (AIR) synthetase (PurM) [ ], as well as the N1 and N2 domains of formylglycinamide ribonucleotide (FGAR) amidot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00586"
] | [
"AIRS"
] | [
89085
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-73817",
"R-CEL-2408557",
"R-DDI-2408557",
"R-DDI-73817",
"R-DME-2408557",
"R-DME-73817",
"R-DRE-2408557",
"R-GGA-419140",
"R-HSA-2408557",
"R-HSA-73817",
"R-MMU-2408557",
"R-MMU-73817",
"R-SCE-73817",
"R-SPO-73817",
"R-SSC-2408557"
] | [
"REACTOME:R-BTA-73817",
"REACTOME:R-CEL-2408557",
"REACTOME:R-DDI-2408557",
"REACTOME:R-DDI-73817",
"REACTOME:R-DME-2408557",
"REACTOME:R-DME-73817",
"REACTOME:R-DRE-2408557",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-2408557",
"REACTOME:R-HSA-73817",
"REACTOME:R-MMU-2408557",
"REACTOME:R-MMU-7... | 15 | [
"1cli",
"1vk3",
"1vqv",
"2btu",
"2hru",
"2hry",
"2hs0",
"2hs3",
"2hs4",
"2i6r",
"2rb9",
"2v9y",
"2yxz",
"2yye",
"2z01",
"2z1e",
"2z1f",
"2z1t",
"2z1u",
"2zau",
"2zod",
"3c9r",
"3c9s",
"3c9t",
"3c9u",
"3d54",
"3fd5",
"3fd6",
"3kiz",
"3m84",
"3mcq",
"3mdo"... | 67 | [
"PUB00014643",
"PUB00016093",
"PUB00016818",
"PUB00037958"
] | [
"10508786",
"9188462",
"15301531",
"16544324"
] | [
"X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.",
"Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium.",
"Domain organization of Salmonella typhimurium formylglycinamid... | [
1999,
1997,
2004,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4482,
74810,
7835,
60,
1898
] | 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",... | [
5,
2,
7,
10,
4,
13,
7,
1,
3,
6,
1,
1,
15
] | 13 | true | Domain | PurM-like, N-terminal domain | PurM-like, N-terminal domain | PurM-like_N | 2 |
IPR016190 | 16,190 | Translation initiation factor IF2/IF5, zinc-binding | Transl_init_fac_IF2/IF5_Zn-bd | Homologous_superfamily | 11,524 | false | false | The beta subunit of archaeal and eukaryotic translation initiation factor 2 (IF2beta) and the N-terminal domain of translation initiation factor 5 (IF5) show significant sequence homology [ ]. Archaeal IF2beta contains two independent structural domains: an N-terminal mixed α/β core domain (topological similarity to th... | [
"GO:0003743",
"GO:0006413"
] | [
"translation initiation factor activity",
"translational initiation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SSF"
] | [
"SSF75689"
] | [
""
] | [
11524
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-156827",
"R-CEL-381042",
"R-CEL-382556",
"R-CEL-72649",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72731",
"R-CEL-9840373",
"R-DDI-156827",
"R-DDI-382556",
"R-DDI-72695",
"R-DDI-72702",
"R-DDI-72731",
"R-DDI-9840373",
"R-DME-156827",
"R-DME-381042",
"R-DME-382556",
"R-DME-72649",
... | [
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-381042",
"REACTOME:R-CEL-382556",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL-72702",
"REACTOME:R-CEL-72731",
"REACTOME:R-CEL-9840373",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-382556",
"REACTOME:R-DDI-72695",
"REACTOME:R-DDI-72702",... | 59 | [
"1k81",
"1nee",
"2d74",
"2dcu",
"2e9h",
"2g2k",
"2nxu",
"2qmu",
"3cw2",
"3j81",
"3jap",
"3v11",
"5jb3",
"5jbh",
"6fyx",
"6fyy",
"6gsm",
"6gsn",
"6i3m",
"6i7t",
"6k71",
"6k72",
"6qg0",
"6qg1",
"6qg2",
"6qg3",
"6qg5",
"6qg6",
"6sw9",
"6swc",
"6ybv",
"6zmw"... | 53 | [
"PUB00017012",
"PUB00017014",
"PUB00041778",
"PUB00042630"
] | [
"11980477",
"14978306",
"16781736",
"17608795"
] | [
"Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins.",
"Structure of the archaeal translation initiation factor aIF2 beta from Methanobacterium thermoautotrophicum: implications for translation initi... | [
2002,
2004,
2006,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1077,
63,
10288,
38,
58
] | 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... | [
18,
2,
4,
3,
10,
14,
3,
12,
4,
2,
2,
22
] | 12 | true | Homologous_superfamily | Translation initiation factor IF2/IF5, zinc-binding | Translation initiation factor IF2/IF5, zinc-binding | Transl_init_fac_IF2/IF5_Zn-bd | 5 |
IPR016191 | 16,191 | Ribonuclease/ribotoxin | Ribonuclease/ribotoxin | Homologous_superfamily | 9,652 | false | false | This entry represents a structural domain consisting of a single helix packed against anti-parallel β-sheet, which is found in both bacterial and fungal ribonucleases, as well as in ribotoxins such as restrictocin and alpha-sarcin. | [
"GO:0003723",
"GO:0004540"
] | [
"RNA binding",
"RNA nuclease activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SSF"
] | [
"SSF53933"
] | [
""
] | [
9652
] | 1 | [] | [] | [] | 0 | [
"1a2p",
"1aqz",
"1ay7",
"1b20",
"1b21",
"1b27",
"1b2m",
"1b2s",
"1b2u",
"1b2x",
"1b2z",
"1b3s",
"1ban",
"1bao",
"1bgs",
"1bir",
"1bne",
"1bnf",
"1bng",
"1bni",
"1bnj",
"1bnr",
"1bns",
"1box",
"1brg",
"1brh",
"1bri",
"1brj",
"1brk",
"1brn",
"1brs",
"1bsa"... | 187 | [
"PUB00020267",
"PUB00022627",
"PUB00024182",
"PUB00025037",
"PUB00025316",
"PUB00027066",
"PUB00027328",
"PUB00030035",
"PUB00036210",
"PUB00036933",
"PUB00037535"
] | [
"8805570",
"7492561",
"10843858",
"8386773",
"11976484",
"12136142",
"12228255",
"15213380",
"7078632",
"11453993",
"8218254"
] | [
"Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin.",
"Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8 A resolution.",
"The highly refined solution structure of the cytotoxic ribonuclease alpha... | [
1996,
1995,
2000,
1993,
2002,
2002,
2002,
2004,
1982,
2001,
1993
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Pithovirus LCPAC304",
"metagenomes"
] | [
6064,
3550,
17,
1,
20
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Homologous_superfamily | Ribonuclease/ribotoxin | Ribonuclease/ribotoxin | Ribonuclease/ribotoxin | 8 |
IPR016193 | 16,193 | Cytidine deaminase-like | Cytidine_deaminase-like | Homologous_superfamily | 184,809 | false | false | This superfamily represents a structural domain with a core fold consisting of α-β(2)-(α-β)2 that folds into three layers (α/β/α); some members may contain an extra C-terminal strand. This domain is found in several types of proteins, including: Cytidine deaminase ( ), including both mono-domain enzymes [ ] and two-dom... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF53927"
] | [
""
] | [
184809
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.5.4",
"R-BTA-73817",
"R-DDI-6798695",
"R-DDI-73614",
"R-DDI-73817",
"R-GGA-419140",
"R-HSA-180585",
"R-HSA-180689",
"R-HSA-499943",
"R-HSA-6782315",
"R-HSA-6798695",
"R-HSA-72200",
"R-HSA-73614",
"R-HSA-73817",
"R-HSA-75094",
"R-HSA-9725370",
"R-HSA-9821002",
"R-MMU-499943",
"... | [
"EC:3.5.4",
"REACTOME:R-BTA-73817",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-73614",
"REACTOME:R-DDI-73817",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-180585",
"REACTOME:R-HSA-180689",
"REACTOME:R-HSA-499943",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-72200",
"REACT... | 33 | [
"1af2",
"1aln",
"1ctt",
"1ctu",
"1g8m",
"1jtk",
"1m9n",
"1mq0",
"1ox7",
"1oz0",
"1p4r",
"1p6o",
"1pkx",
"1pl0",
"1r5t",
"1rb7",
"1thz",
"1tiy",
"1uaq",
"1uwz",
"1ux0",
"1ux1",
"1vk9",
"1vq2",
"1wkq",
"1wn5",
"1wn6",
"1wwr",
"1ysb",
"1ysd",
"1z3a",
"1zab"... | 252 | [
"PUB00025174",
"PUB00027416",
"PUB00028183",
"PUB00032117",
"PUB00032259",
"PUB00042648"
] | [
"11323713",
"15689149",
"8634261",
"15504034",
"15180998",
"2906827"
] | [
"Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis.",
"Structure of human cytidine deaminase bound to a potent inhibitor.",
"Cytidine deaminase complexed to 3-deazacytidine: a \"valence buffer\" in zinc enzyme catalysis.",
"Three-dimensional structure of the R... | [
2001,
2005,
1996,
2004,
2004,
1988
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2306,
139325,
38626,
1356,
3196
] | 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",... | [
87,
11,
19,
10,
5,
76,
45,
10,
42,
48,
8,
7,
94
] | 13 | true | Homologous_superfamily | Cytidine deaminase-like | Cytidine deaminase-like | Cytidine_deaminase-like | 5 |
IPR016195 | 16,195 | Polymerase/histidinol phosphatase-like | Pol/histidinol_Pase-like | Homologous_superfamily | 110,452 | false | false | This entry represents a PHP-like (Polymerase and Histidinol Phosphatase) domain, the catalytic site of which has four motifs with conserved histidine residues. This domain has a 7-stranded β/α barrel fold; this structure shows some similarity to the TIM-barrel fold metallohydrolases. PHP-like domains are found in alpha... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF89550"
] | [
""
] | [
110452
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6791226",
"R-HSA-6784531",
"R-HSA-6791226",
"R-MMU-6791226"
] | [
"REACTOME:R-BTA-6791226",
"REACTOME:R-HSA-6784531",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226"
] | 4 | [
"1m65",
"1m68",
"1pb0",
"1v77",
"2anu",
"2czv",
"2hnh",
"2hpi",
"2hpm",
"2hqa",
"2w9m",
"2yb1",
"2yb4",
"2yxo",
"2yz5",
"2z4g",
"3au2",
"3au6",
"3auo",
"3b0x",
"3b0y",
"3dcp",
"3e0d",
"3e0f",
"3e38",
"3f2b",
"3f2c",
"3f2d",
"3o0f",
"3qy6",
"3qy7",
"3wyz"... | 67 | [
"PUB00027226",
"PUB00032011",
"PUB00042649"
] | [
"12661000",
"15184052",
"17929834"
] | [
"Crystal structure of the Escherichia coli YcdX protein reveals a trinuclear zinc active site.",
"Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3.",
"Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus H... | [
2003,
2004,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4449,
95354,
7898,
359,
2392
] | 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",... | [
13,
2,
4,
1,
3,
4,
4,
2,
11,
5,
2,
3,
12
] | 13 | true | Homologous_superfamily | Polymerase/histidinol phosphatase-like | Polymerase/histidinol phosphatase-like | Pol/histidinol_Pase-like | 2 |
IPR016197 | 16,197 | Chromo-like domain superfamily | Chromo-like_dom_sf | Homologous_superfamily | 124,253 | false | false | This entry represents a chromo (CHRromatin Organization MOdifier) structural domain, which consists of an SH3-like β-barrel capped by a C-terminal helix. Chromo domains are conserved modules of around 60 amino acids that are implicated in the recognition of lysine-methylated histone tails and nucleic acids. Chromo doma... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF54160"
] | [
""
] | [
124253
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-4551638",
"R-CEL-5693607",
"R-CEL-6804758",
"R-CEL-73772",
"R-CEL-9031628",
"R-CEL-983231",
"R-DME-201722",
"R-DME-2559580",
"R-DME-2559586",
"R-DME-3108214",
"R-DME-3214815",
"R-DME-3214847",
"R-DME-3899300",
"R-DME-427359",
"R-DME-4570464",
"R-DME-5693548",
"R-DME-5693565",
... | [
"REACTOME:R-CEL-4551638",
"REACTOME:R-CEL-5693607",
"REACTOME:R-CEL-6804758",
"REACTOME:R-CEL-73772",
"REACTOME:R-CEL-9031628",
"REACTOME:R-CEL-983231",
"REACTOME:R-DME-201722",
"REACTOME:R-DME-2559580",
"REACTOME:R-DME-2559586",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3214815",
"REACTOME:R-... | 151 | [
"1ap0",
"1azp",
"1azq",
"1b4o",
"1bbx",
"1bf4",
"1bnz",
"1c8c",
"1ca5",
"1ca6",
"1dz1",
"1e0b",
"1g6z",
"1guw",
"1jic",
"1kna",
"1kne",
"1pdq",
"1pfb",
"1q3l",
"1s4z",
"1sap",
"1sso",
"1wd0",
"1wd1",
"1wgs",
"1wto",
"1wtp",
"1wtq",
"1wtr",
"1wtv",
"1wtw"... | 270 | [
"PUB00023596",
"PUB00026774",
"PUB00028545",
"PUB00029833",
"PUB00039496",
"PUB00039764"
] | [
"9731772",
"11859155",
"11273706",
"12897052",
"16372014",
"15964847"
] | [
"The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.",
"Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail.",
"Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransfe... | [
1998,
2002,
2001,
2003,
2005,
2005
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"Viruses",
"metagenomes"
] | [
229,
123893,
88,
18,
25
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
84,
25,
130,
84,
136,
97,
14,
622,
128,
3,
9,
223
] | 12 | true | Homologous_superfamily | Chromo-like domain superfamily | Chromo-like domain superfamily | Chromo-like_dom_sf | 9 |
IPR016201 | 16,201 | PSI domain | PSI | Domain | 56,575 | false | false | This domain is found in several different extracellular receptors, including plexins, which are involved in the development of neural and epithelial tissues [ ]; in semaphorins, which regulate axon guidance, immune function and angiogenesis [ ]; in integrins, which are important Metazoan adhesion receptors that transmi... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00423"
] | [
"PSI"
] | [
56575
] | 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-1566948",
"R-BTA-166016",
"R-BTA-198933",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-3000178",
"R-BTA-6798695",
"R-CEL-399954",
"R-CEL-399955",
"R-CEL-399956",
"R-CEL-416482",
"R-CEL-416550",
"R-CEL-416572",
"R-CEL-416700",
"R-CEL-9013405",
"R-D... | [
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-3000178",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-399954",
"REACTOME:R-CEL-399955",
"REACTOME:R-CE... | 228 | [
"1jv2",
"1l5g",
"1m1x",
"1olz",
"1shy",
"1ssl",
"1tye",
"1u8c",
"1yuk",
"2p26",
"2p28",
"2uzx",
"2uzy",
"2vc2",
"2vdk",
"2vdl",
"2vdm",
"2vdn",
"2vdo",
"2vdp",
"2vdq",
"2vdr",
"3al8",
"3al9",
"3fcs",
"3fcu",
"3ije",
"3k6s",
"3k71",
"3k72",
"3nid",
"3nif"... | 211 | [
"PUB00015415",
"PUB00015416",
"PUB00037805",
"PUB00042651"
] | [
"12958590",
"15167892",
"15378069",
"17855350"
] | [
"The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D.",
"Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor.",
"Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics.",
"Plexin-B1 u... | [
2003,
2004,
2004,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Sandaracinus amylolyticus",
"Viruses",
"viral metagenome"
] | [
56549,
1,
21,
4
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
216,
22,
164,
86,
130
] | 6 | true | Domain | PSI domain | PSI domain | PSI | 2 |
IPR016202 | 16,202 | Deoxyribonuclease I | DNase_I | Family | 5,912 | false | false | This entry represents DNaseI and related proteins such as DNase gamma. Deoxyribonuclease I (DNase I) ( ) [ ] is a vertebrate enzyme which catalyzes the endonucleolytic cleavage of double-stranded DNA to 5'- phosphodinucleotide and 5'-phosphooligonucleotide end-products. DNase I is an enzyme involved in DNA degradation;... | [
"GO:0004536",
"GO:0006308"
] | [
"DNA nuclease activity",
"DNA catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PRINTS",
"SMART"
] | [
"PIRSF000988",
"PR00130",
"SM00476"
] | [
"DNase_I_euk",
"DNASEI",
"DNaseIc"
] | [
3720,
5059,
5859
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.21",
"R-HSA-6798695",
"R-MMU-6798695",
"R-RNO-6798695"
] | [
"EC:3.1.21",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-6798695"
] | 4 | [
"1atn",
"1dnk",
"2a3z",
"2a40",
"2a41",
"2a42",
"2d1k",
"2dnj",
"3cjc",
"3dni",
"3w3d",
"4awn",
"7kiu",
"7nxv",
"7nzm",
"9fju",
"9fjy",
"9nb9"
] | 18 | [
"PUB00001239",
"PUB00003994",
"PUB00004018",
"PUB00004077",
"PUB00004719"
] | [
"8428592",
"3713845",
"3352748",
"2395459",
"2251263"
] | [
"Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death).",
"Structure of DNase I at 2.0 A resolution suggests a mechanism for binding to and cutting DNA.",
"Structure refined to 2A of a nicked DNA octanucleotide complex with DNase I.",
... | [
1993,
1986,
1988,
1990,
1990
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"Scale drop disease virus",
"ecological metagenomes"
] | [
744,
5106,
51,
2,
9
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
21,
16,
17
] | 4 | true | Family | Deoxyribonuclease I | Deoxyribonuclease I | DNase_I | 8 |
IPR016204 | 16,204 | Homoserine dehydrogenase | HDH | Family | 17,450 | false | false | This entry represents a family of homoserine dehydrogenases mainly found in bacteria. Homoserine dehydrogenase ( ) catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta-semialdehyde into homoserine [ , ]. Homoserine is an intermediate in the biosynthesis of threonine, isole... | [
"GO:0004412",
"GO:0006520"
] | [
"homoserine dehydrogenase activity",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000098"
] | [
"Homoser_dehydrog"
] | [
17450
] | 1 | [
"EC"
] | [
"1.1.1.3"
] | [
"EC:1.1.1.3"
] | 1 | [
"3mtj",
"6dzs"
] | 2 | [
"PUB00000699",
"PUB00001656",
"PUB00021481",
"PUB00034672"
] | [
"8395899",
"8500624",
"10700284",
"11352712"
] | [
"Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.",
"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.",
"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.",
"T... | [
1993,
1993,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriaceae",
"unclassified sequences"
] | [
16958,
125,
26,
341
] | 4 | [] | [] | 0 | true | Family | Homoserine dehydrogenase | Homoserine dehydrogenase | HDH | 4 |
IPR016205 | 16,205 | Glycerol dehydrogenase | Glycerol_DH | Family | 13,560 | false | false | This entry represents two distinct enzymes: bacterial NAD-linked glycerol dehydrogenase and archaeal glycerol-1-phosphate dehydrogenase. NAD-linked glycerol dehydrogenase converts glycerol to glycerone and s NADH during glycerol metabolism [ , ]. Glycerol-1-phosphate dehydrogenase is responsible for the formation of th... | [
"GO:0016614",
"GO:0046872"
] | [
"oxidoreductase activity, acting on CH-OH group of donors",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000112",
"PTHR43616"
] | [
"Glycerol_dehydrogenase",
""
] | [
11346,
13560
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.261",
"PWY-6349",
"PWY-8365"
] | [
"EC:1.1.1.261",
"METACYC:PWY-6349",
"METACYC:PWY-8365"
] | 3 | [
"1jpu",
"1jq5",
"1jqa",
"1kq3",
"1ta9",
"3ce9",
"3uhj",
"4mca",
"4rfl",
"4rgq",
"4rgv",
"5fb3",
"5xn8",
"5zxl",
"6csj",
"8goa",
"8gob",
"8k1g",
"8k1h",
"8x6m"
] | 20 | [
"PUB00002240",
"PUB00043530",
"PUB00043531",
"PUB00043532",
"PUB00081219"
] | [
"8132480",
"1339360",
"9348086",
"9419225",
"15876564"
] | [
"Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase.",
"Cloning and characterization of a gene from Bacillus stearothermophilus var. non-diastaticus encoding a glycerol dehydrogenase.",
"Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methan... | [
1994,
1992,
1997,
1998,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
983,
12257,
182,
138
] | 4 | [
"Escherichia coli (strain K12)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
1
] | 2 | true | Family | Glycerol dehydrogenase | Glycerol dehydrogenase | Glycerol_DH | 4 |
IPR016206 | 16,206 | Ketol-acid reductoisomerase, plant | KetolA_reductoisomerase_plant | Family | 522 | false | false | Ketol-acid reductoisomerases (KARI) catalyses two steps in the biosynthesis of branched-chain amino acids. The reaction involves an Mg2+ dependent alkyl migration followed by an NADPH-dependent reduction of the 2-keto group. There are two groups of KARI enzymes: class I is a short form found in fungi and most bacteria,... | [
"GO:0004455"
] | [
"ketol-acid reductoisomerase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000118"
] | [
"Ilv5_plant"
] | [
522
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.86",
"PWY-5103",
"PWY-7111"
] | [
"EC:1.1.1.86",
"METACYC:PWY-5103",
"METACYC:PWY-7111"
] | 3 | [] | 0 | [
"PUB00034453",
"PUB00036035"
] | [
"16322583",
"15272168"
] | [
"The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution.",
"Facile crystallization of Escherichia coli ketol-acid reductoisomerase."
] | [
2005,
2004
] | 2 | [
"IPR013023"
] | [] | 1 | 0 | 1 | [
"Mesangiospermae"
] | [
522
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
4,
6
] | 3 | true | Family | Ketol-acid reductoisomerase, plant | Ketol-acid reductoisomerase, plant | KetolA_reductoisomerase_plant | 7 |
IPR016207 | 16,207 | Ketol-acid reductoisomerase, fungi | KetolA_reductoisomerase_fun | Family | 1,421 | false | false | Ketol-acid reductoisomerases (KARI) catalyses two steps in the biosynthesis of branched-chain amino acids. The reaction involves an Mg2+ dependent alkyl migration followed by an NADPH-dependent reduction of the 2-keto group. There are two groups of KARI enzymes: class I is a short form found in fungi and most bacteria,... | [
"GO:0004455"
] | [
"ketol-acid reductoisomerase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000119"
] | [
"Ilv5_fungal"
] | [
1421
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.86",
"PWY-5103",
"PWY-7111"
] | [
"EC:1.1.1.86",
"METACYC:PWY-5103",
"METACYC:PWY-7111"
] | 3 | [
"7toc"
] | 1 | [
"PUB00034453",
"PUB00036035"
] | [
"16322583",
"15272168"
] | [
"The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution.",
"Facile crystallization of Escherichia coli ketol-acid reductoisomerase."
] | [
2005,
2004
] | 2 | [
"IPR013023"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1421
] | 1 | [
"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)",
"Zea mays"
] | [
1,
1,
1,
1
] | 4 | true | Family | Ketol-acid reductoisomerase, fungi | Ketol-acid reductoisomerase, fungi | KetolA_reductoisomerase_fun | 3 |
IPR016208 | 16,208 | Aldehyde oxidase/xanthine dehydrogenase-like | Ald_Oxase/xanthine_DH-like | Family | 65,370 | false | false | This entry includes aldehyde oxidases (AOXs) and xanthine dehydrogenases (XDHs). They are both molybdenum cofactor (Moco) containing enzymes [ ]. AOX catalyses the reaction: aldehyde + H(2)O + O(2) = a carboxylic acid + H2O2 It binds 2 2Fe-2S clusters uses FAD and molybdopterin as cofactors. XDH has the same cofactors ... | [
"GO:0005506",
"GO:0016491"
] | [
"iron ion binding",
"oxidoreductase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF",
"PANTHER",
"PANTHER"
] | [
"PIRSF000127",
"PTHR11908",
"PTHR45444"
] | [
"Xanthine_DH",
"",
""
] | [
11306,
46584,
18786
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-964975",
"R-DDI-74259",
"R-DDI-964975",
"R-DDI-9748787",
"R-DME-74259",
"R-DME-964975",
"R-DME-9748787",
"R-GGA-421178",
"R-HSA-74259",
"R-HSA-8851680",
"R-HSA-964975",
"R-HSA-9748787",
"R-MMU-74259",
"R-MMU-8851680",
"R-MMU-964975",
"R-MMU-9748787",
"R-RNO-74259",
"R-RNO-88... | [
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-74259",
"REACTOME:R-DDI-964975",
"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-74259",
"REACTOME:R-DME-964975",
"REACTOME:R-DME-9748787",
"REACTOME:R-GGA-421178",
"REACTOME:R-HSA-74259",
"REACTOME:R-HSA-8851680",
"REACTOME:R-HSA-964975",
"REACTOME:R-HSA-974... | 20 | [
"1dgj",
"1ffu",
"1ffv",
"1fiq",
"1fo4",
"1jro",
"1jrp",
"1n5w",
"1n5x",
"1n60",
"1n61",
"1n62",
"1n63",
"1rm6",
"1sb3",
"1sij",
"1t3q",
"1v97",
"1vdv",
"1vlb",
"1wyg",
"1zxi",
"2ckj",
"2e1q",
"2e3t",
"2w3r",
"2w3s",
"2w54",
"2w55",
"3am9",
"3amz",
"3an1"... | 85 | [
"PUB00043467",
"PUB00043468",
"PUB00100884"
] | [
"17649978",
"18258600",
"27537049"
] | [
"Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase.",
"Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mech... | [
2007,
2008,
2016
] | 3 | [] | [
"IPR012175",
"IPR012780",
"IPR014313",
"IPR017607",
"IPR017609",
"IPR017697",
"IPR017699",
"IPR049648",
"IPR050028",
"IPR054705"
] | 0 | 10 | 0 | [
"Archaea",
"Bacteria",
"Caudovirales sp. ctU7I6",
"Eukaryota",
"unclassified sequences"
] | [
1022,
45583,
1,
17332,
1432
] | 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",... | [
48,
3,
4,
8,
3,
9,
23,
1,
39,
27,
104
] | 11 | true | Family | Aldehyde oxidase/xanthine dehydrogenase-like | Aldehyde oxidase/xanthine dehydrogenase-like | Ald_Oxase/xanthine_DH-like | 9 |
IPR016209 | 16,209 | Protochlorophyllide reductase, ChlB, light independent | Protochlorophyllide_Rdtase | Family | 3,643 | false | false | This group represents a light independent protochlorophyllide reductase (DPOR) chain ChlB. DPOR is important for chlorophyll synthesis in the dark for some algae, lower plants, and gymnosperms, but not for angiosperms. The enzyme consists of three subunits encoded by the chlB, chlL, and chlN genes in the plastid genome... | [
"GO:0016730",
"GO:0046148"
] | [
"oxidoreductase activity, acting on iron-sulfur proteins as donors",
"pigment biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000163"
] | [
"PCP_ChlB"
] | [
3643
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.3.7.7",
"PWY-5531",
"PWY-7159"
] | [
"EC:1.3.7.7",
"METACYC:PWY-5531",
"METACYC:PWY-7159"
] | 3 | [
"2xdq",
"2ynm",
"3aek",
"3aeq",
"3aer",
"3aes",
"3aet",
"3aeu",
"8vqi",
"8vqj",
"9buo",
"9e7h"
] | 12 | [
"PUB00043361"
] | [
"16428257"
] | [
"Proceedings of the SMBE Tri-National Young Investigators' Workshop 2005. Relaxation of functional constraint on light-independent protochlorophyllide oxidoreductase in Thuja."
] | [
2006
] | 1 | [] | [
"IPR005969",
"IPR010244",
"IPR010245"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"freshwater sediment metagenome"
] | [
2344,
1296,
3
] | 3 | [] | [] | 0 | true | Family | Protochlorophyllide reductase, ChlB, light independent | Protochlorophyllide reductase, ChlB, light independent | Protochlorophyllide_Rdtase | 9 |
IPR016210 | 16,210 | NAD-dependent glutamate dehydrogenase, eukaryotes | NAD-GDH_euk | Family | 1,753 | false | false | This protein family represents fungal NAD-dependent glutamate dehydrogenases, including the NAD-specific glutamate dehydrogenases from Neurospora crassa and Saccharomyces cerevisiae (DHE2) [ , ]. These enzymes catalyse the reversible oxidative deamination of glutamate to ketoglutarate and ammonia. | [
"GO:0004352",
"GO:0006538"
] | [
"glutamate dehydrogenase (NAD+) activity",
"L-glutamate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000184"
] | [
"GDH_NAD"
] | [
1753
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.4.1.2",
"PWY-5022",
"PWY-6728",
"PWY-7126",
"PWY-8190"
] | [
"EC:1.4.1.2",
"METACYC:PWY-5022",
"METACYC:PWY-6728",
"METACYC:PWY-7126",
"METACYC:PWY-8190"
] | 5 | [] | 0 | [
"PUB00016745",
"PUB00042874"
] | [
"7901008",
"8398079"
] | [
"The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant.",
"NAD(+)-specific glutamate dehydrogenase of Neurospora crassa: cloning, complete nucleotide sequence, and gene mapping."
] | [
1993,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1753
] | 1 | [
"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,
1,
1
] | 3 | true | Family | NAD-dependent glutamate dehydrogenase, eukaryotes | NAD-dependent glutamate dehydrogenase, eukaryotes | NAD-GDH_euk | 5 |
IPR016211 | 16,211 | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, bacterial/archaeal | Glu/Phe/Leu/Val/Trp_DH_bac/arc | Family | 9,649 | false | false | Glutamate, leucine, phenylalanine, valine and tryptophan dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases ( ... | [
"GO:0016639"
] | [
"oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000188",
"PTHR42722"
] | [
"Phe_leu_dh",
""
] | [
9183,
9649
] | 2 | [
"EC"
] | [
"1.4.1"
] | [
"EC:1.4.1"
] | 1 | [
"1bw9",
"1bxg",
"1c1d",
"1c1x",
"1leh",
"3vpx",
"5b37",
"6acf",
"6ach",
"7vid",
"8gxd",
"8hpe",
"8hr6"
] | 13 | [
"PUB00000302",
"PUB00001430",
"PUB00002221",
"PUB00002347",
"PUB00002418",
"PUB00003424",
"PUB00004656",
"PUB00101895",
"PUB00101896"
] | [
"3069133",
"1358610",
"8320231",
"1880121",
"2989290",
"8315654",
"3368458",
"27815281",
"24835098"
] | [
"Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.",
"Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.",
"Sequence, transcriptional, and function... | [
1988,
1992,
1993,
1991,
1985,
1993,
1988,
2017,
2014
] | 9 | [
"IPR006095"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
45,
9341,
158,
105
] | 4 | [] | [] | 0 | true | Family | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, bacterial/archaeal | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, bacterial/archaeal | Glu/Phe/Leu/Val/Trp_DH_bac/arc | 5 |
IPR016212 | 16,212 | Methyl coenzyme M reductase, alpha subunit | Me_CoM_Rdtase_asu | Family | 337 | false | false | Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-... | [
"GO:0050524",
"GO:0015948"
] | [
"coenzyme-B sulfoethylthiotransferase activity",
"methanogenesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF000262",
"TIGR03256"
] | [
"MCR_alpha",
"met_CoM_red_alp"
] | [
307,
330
] | 2 | [
"EC",
"GP",
"GP"
] | [
"2.8.4.1",
"GenProp0719",
"GenProp0722"
] | [
"EC:2.8.4.1",
"GP:GenProp0719",
"GP:GenProp0722"
] | 3 | [
"1e6v",
"1e6y",
"1hbm",
"1hbn",
"1hbo",
"1hbu",
"1mro",
"3m1v",
"3m2r",
"3m2u",
"3m2v",
"3m30",
"3m32",
"3pot",
"3sqg",
"5a0y",
"5a8k",
"5a8r",
"5a8w",
"5g0r",
"5n1q",
"5n28",
"5n2a",
"7b2h",
"7nkg",
"7suc",
"7sxm",
"8gf5",
"8gf6",
"8s7v",
"8s7x",
"9ecn"... | 37 | [
"PUB00006391",
"PUB00010614",
"PUB00035993",
"PUB00035994"
] | [
"9367957",
"11491299",
"16260307",
"16234924"
] | [
"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.",
"On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.",
"Methyl-coenzyme M reductase genes: unique functional ma... | [
1997,
2001,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
332,
5
] | 2 | [] | [] | 0 | true | Family | Methyl coenzyme M reductase, alpha subunit | Methyl coenzyme M reductase, alpha subunit | Me_CoM_Rdtase_asu | 6 |
IPR016213 | 16,213 | Polyphenol oxidase | Polyphenol_oxidase | Family | 1,885 | false | false | This group represents a polyphenol oxidase, plant type. | [
"GO:0004097",
"GO:0046148"
] | [
"catechol oxidase activity",
"pigment biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000290"
] | [
"PPO_plant"
] | [
1885
] | 1 | [
"EC",
"METACYC"
] | [
"1.10.3.1",
"PWY-6752"
] | [
"EC:1.10.3.1",
"METACYC:PWY-6752"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Euphyllophyta"
] | [
1885
] | 1 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
11
] | 2 | true | Family | Polyphenol oxidase | Polyphenol oxidase | Polyphenol_oxidase | 6 |
IPR016214 | 16,214 | NAD-reducing hydrogenase, HoxS gamma subunit | NAD-red_Hydgase_HoxS_gsu | Family | 789 | false | false | This entry represents the NAD-reducing hydrogenase HoxS gamma subunit (also known as HoxU). Subunits alpha and gamma of HoxS constitute a diaphorase sub-complex that binds a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters [ , , [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000309"
] | [
"NAD_red_hyd_HoxU"
] | [
789
] | 1 | [] | [] | [] | 0 | [
"5xf9",
"5xfa"
] | 2 | [
"PUB00060766",
"PUB00060767",
"PUB00060933"
] | [
"9541559",
"12034472",
"22016788"
] | [
"Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium anacystis nidulans",
"HoxE--a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria.",
"Catalytic propert... | [
1998,
2002,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
660,
109,
20
] | 3 | [] | [] | 0 | true | Family | NAD-reducing hydrogenase, HoxS gamma subunit | NAD-reducing hydrogenase, HoxS gamma subunit | NAD-red_Hydgase_HoxS_gsu | 2 |
IPR016216 | 16,216 | Monophenol monooxygenase, fungi | Monophenol_mOase_fun | Family | 174 | false | false | This entry includes tyrosinases and polyphenol oxidases from fungi [ , ]. | [
"GO:0004503"
] | [
"tyrosinase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000340"
] | [
"MPO_fungal"
] | [
174
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.14.18.1",
"PWY-6481",
"PWY-7913",
"PWY-7917"
] | [
"EC:1.14.18.1",
"METACYC:PWY-6481",
"METACYC:PWY-7913",
"METACYC:PWY-7917"
] | 4 | [
"4oua",
"5m6b"
] | 2 | [
"PUB00075304",
"PUB00075305"
] | [
"7893753",
"12743763"
] | [
"Molecular cloning and nucleotide sequence of the protyrosinase gene, melO, from Aspergillus oryzae and expression of the gene in yeast cells.",
"Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus."
] | [
1995,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Dikarya"
] | [
174
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Monophenol monooxygenase, fungi | Monophenol monooxygenase, fungi | Monophenol_mOase_fun | 1 |
IPR016217 | 16,217 | Nitrogen fixation, NifU | N_fixation_NifU | Family | 1,288 | false | false | The nitrogen fixation protein NifU is required for full activation of the metalloenzyme nitrogenase, the catalytic component of biological nitrogen fixation. In Azotobacter vinelandii, it is a homodimer; each subunit contains one 2Fe-2S cluster [ ], which is proposed to have a redox function involving the release of Fe... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000375"
] | [
"NifU"
] | [
1288
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016779",
"PUB00016841"
] | [
"7947754",
"10819462"
] | [
"nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters.",
"Modular organization and identification of a mononuclear iron-binding site within the NifU protein."
] | [
1994,
2000
] | 2 | [] | [
"IPR010238"
] | 0 | 1 | 0 | [
"Bacteria",
"Mastigamoebida",
"Methanosarcina siciliae",
"ecological metagenomes"
] | [
1237,
13,
3,
35
] | 4 | [] | [] | 0 | true | Family | Nitrogen fixation, NifU | Nitrogen fixation, NifU | N_fixation_NifU | 7 |
IPR016218 | 16,218 | Acetyl-CoA decarbonylase/synthase complex, gamma subunit | AcylCoA_decarb/synth_gsu | Family | 523 | false | false | This group represents the gamma subunit of acetyl-CoA decarbonylase/synthase (ACDS), a complex catalysing the reversible cleavage of acetyl-CoA. Depending on the direction of the reaction this complex allows either growth on acetate as sole carbon and energy source, or autotrophic growth from carbon dioxide/carbon mono... | [
"GO:0005506",
"GO:0008168",
"GO:0046356"
] | [
"iron ion binding",
"methyltransferase activity",
"acetyl-CoA catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000376"
] | [
"AcCoA_decarb_gamma"
] | [
523
] | 1 | [
"EC"
] | [
"2.1.1.245"
] | [
"EC:2.1.1.245"
] | 1 | [
"2h9a",
"2ycl",
"4c1n",
"4djd",
"4dje",
"4djf"
] | 6 | [
"PUB00043434",
"PUB00043435",
"PUB00043436"
] | [
"14709073",
"14664578",
"18442256"
] | [
"Chemically distinct Ni sites in the A-cluster in subunit beta of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila: Ni L-edge absorption and X-ray magnetic circular dichroism analyses.",
"The A-cluster in subunit beta of the acetyl-CoA decarbonylase/synthase complex from Methanosarcin... | [
2004,
2003,
2008
] | 3 | [] | [
"IPR023427"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
247,
260,
16
] | 3 | [] | [] | 0 | true | Family | Acetyl-CoA decarbonylase/synthase complex, gamma subunit | Acetyl-CoA decarbonylase/synthase complex, gamma subunit | AcylCoA_decarb/synth_gsu | 8 |
IPR016219 | 16,219 | Phosphatidylethanolamine N-methyltransferase, fungi | Phosphatid-EA_MeTrfase_fun | Family | 1,728 | false | false | This family consists of phosphatidylethanolamine N-methyltransferases from Fungi. Phosphatidylethanolamine N-methyltransferase (CHO2) catalyses the first step in the conversion of phosphatidylethanolamine to phosphatidylcholine during the methylation pathway of phosphatidylcholine biosynthesis [ ]. Methyltransferases (... | [
"GO:0004608",
"GO:0006644"
] | [
"phosphatidylethanolamine N-methyltransferase activity",
"phospholipid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PROFILE"
] | [
"MF_03217",
"PIRSF000383",
"PS51598"
] | [
"PEMT",
"PEAMT",
"SAM_CHO2"
] | [
1515,
1566,
1706
] | 3 | [
"EC",
"METACYC"
] | [
"2.1.1.17",
"PWY-6825"
] | [
"EC:2.1.1.17",
"METACYC:PWY-6825"
] | 2 | [] | 0 | [
"PUB00006319",
"PUB00054125",
"PUB00057256",
"PUB00057957",
"PUB00057958"
] | [
"7897657",
"12826405",
"15258140",
"16225687",
"21858014"
] | [
"Universal catalytic domain structure of AdoMet-dependent methyltransferases.",
"Many paths to methyltransfer: a chronicle of convergence.",
"The yeast phospholipid N-methyltransferases catalyzing the synthesis of phosphatidylcholine preferentially convert di-C16:1 substrates both in vivo and in vitro.",
"Nat... | [
1995,
2003,
2004,
2005,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1728
] | 1 | [
"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,
1,
1
] | 3 | true | Family | Phosphatidylethanolamine N-methyltransferase, fungi | Phosphatidylethanolamine N-methyltransferase, fungi | Phosphatid-EA_MeTrfase_fun | 3 |
IPR016220 | 16,220 | Methylphosphotriester-DNA alkyltransferase, AdaA | Me-P-triester_DNA_alkyl-Trfase | Family | 1,622 | false | false | Methylphosphotriester-DNA alkyltransferase AdaA is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. It repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues [ , ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000408"
] | [
"Alkyltransferas_AdaA"
] | [
1622
] | 1 | [] | [] | [] | 0 | [
"1wpk"
] | 1 | [
"PUB00060922",
"PUB00060923"
] | [
"2120677",
"8376346"
] | [
"Bacillus subtilis ada operon encodes two DNA alkyltransferases.",
"Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA glycosylase is adjacent to the ada operon."
] | [
1990,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Fungi",
"Promethearchaeaceae",
"ecological metagenomes"
] | [
1600,
10,
2,
10
] | 4 | [] | [] | 0 | true | Family | Methylphosphotriester-DNA alkyltransferase, AdaA | Methylphosphotriester-DNA alkyltransferase, AdaA | Me-P-triester_DNA_alkyl-Trfase | 9 |
IPR016221 | 16,221 | Bifunctional regulatory protein Ada | Bifunct_regulatory_prot_Ada | Family | 5,933 | false | false | This group represents the bifunctional regulatory protein Ada. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000409"
] | [
"Ada"
] | [
5933
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrososphaera",
"metagenomes"
] | [
5905,
4,
3,
21
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Bifunctional regulatory protein Ada | Bifunctional regulatory protein Ada | Bifunct_regulatory_prot_Ada | 5 |
IPR016222 | 16,222 | Glycerol-3-phosphate O-acyltransferase, chloroplast | G3P_O-acylTrfase_chlp | Family | 1,389 | false | false | Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate [ ]. Glycerol-3-phosphate (G3P) plays an important role in carbohydrate and lipid... | [
"GO:0004366",
"GO:0006650"
] | [
"glycerol-3-phosphate O-acyltransferase activity",
"glycerophospholipid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000431",
"PTHR35695"
] | [
"Glycerol-3-P_O-acyltransfrase",
""
] | [
884,
1389
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.15",
"PWY-5667",
"PWY-6453",
"PWY-7411",
"PWY-7587",
"PWY-8051",
"PWY-8053",
"PWY-8055"
] | [
"EC:2.3.1.15",
"METACYC:PWY-5667",
"METACYC:PWY-6453",
"METACYC:PWY-7411",
"METACYC:PWY-7587",
"METACYC:PWY-8051",
"METACYC:PWY-8053",
"METACYC:PWY-8055"
] | 8 | [
"1iuq",
"1k30",
"8ia1"
] | 3 | [
"PUB00021962",
"PUB00084353"
] | [
"11377195",
"18567828"
] | [
"Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.",
"Glycerol-3-phosphate levels are associated with basal resistance to the hemibiotrophic fungus Colletotrichum higginsianum in Arabidopsis."
] | [
2001,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
43,
1345,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
3,
25
] | 3 | true | Family | Glycerol-3-phosphate O-acyltransferase, chloroplast | Glycerol-3-phosphate O-acyltransferase, chloroplast | G3P_O-acylTrfase_chlp | 8 |
IPR016224 | 16,224 | Ecdysteroid UDP-glucosyltransferase | Ecdysteroid_UDP-Glc_Trfase | Family | 170 | false | false | Ecdysteroid UDP-glucosyltransferase catalyses the transfer of glucose from UDP-glucose to ecdysteroids [ ]. | [
"GO:0016740"
] | [
"transferase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000476"
] | [
"Ecdystd_UDP_glucosyltfrase"
] | [
170
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.4.1.-",
"PWY-1901",
"PWY-1961",
"PWY-1981",
"PWY-2021",
"PWY-2881",
"PWY-2901",
"PWY-2902",
"PWY-4421",
"PWY-4801",
"PWY-5094",
"PWY-5105",
"PWY-5129",
"PWY-5139",
"PWY-5160",
"PWY-5161",
"PWY-5268",
"PWY-5284",
"PWY-5286",
"PWY-5310",
"PWY-5312",
"PWY-5313",
"PWY-5317... | [
"EC:2.4.1.-",
"METACYC:PWY-1901",
"METACYC:PWY-1961",
"METACYC:PWY-1981",
"METACYC:PWY-2021",
"METACYC:PWY-2881",
"METACYC:PWY-2901",
"METACYC:PWY-2902",
"METACYC:PWY-4421",
"METACYC:PWY-4801",
"METACYC:PWY-5094",
"METACYC:PWY-5105",
"METACYC:PWY-5129",
"METACYC:PWY-5139",
"METACYC:PWY-5... | 200 | [] | 0 | [
"PUB00005121"
] | [
"2505387"
] | [
"A baculovirus blocks insect molting by producing ecdysteroid UDP-glucosyl transferase."
] | [
1989
] | 1 | [
"IPR002213"
] | [] | 1 | 0 | 1 | [
"Baculoviridae"
] | [
170
] | 1 | [] | [] | 0 | true | Family | Ecdysteroid UDP-glucosyltransferase | Ecdysteroid UDP-glucosyltransferase | Ecdysteroid_UDP-Glc_Trfase | 1 |
IPR016227 | 16,227 | Dihydropteroate synthase, predicted | Dihydropteroate_synthase_prd | Family | 416 | false | false | This group represents a group of predicted dihydropteroate synthases found mostly in the Campylobacterales. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000501"
] | [
"DHPS_Campy_prd"
] | [
416
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR045031"
] | [] | 1 | 0 | 1 | [
"Epsilonproteobacteria",
"ecological metagenomes"
] | [
408,
8
] | 2 | [] | [] | 0 | true | Family | Dihydropteroate synthase, predicted | Dihydropteroate synthase, predicted | Dihydropteroate_synthase_prd | 8 |
IPR016229 | 16,229 | Thiamine-phosphate synthase, cyanobacterial/bacterial | TMP_synthase_cyanobac_bac | Family | 574 | false | false | This group represents a predicted thiamine-phosphate synthase from cyanobacteria and bacteria. Thiamine phosphate synthase (TPS) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate i... | [
"GO:0004789",
"GO:0009228"
] | [
"thiamine-phosphate diphosphorylase activity",
"thiamine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PIRSF"
] | [
"MF_01327",
"NF002727",
"PIRSF000512"
] | [
"TMP_synthase_cyanobact",
"PRK02615.1",
"TMP_PPase_Cyanobac_prd"
] | [
346,
536,
522
] | 3 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.5.1.3",
"PWY-6893",
"PWY-6894",
"PWY-6897",
"PWY-6907",
"PWY-6908",
"PWY-7356",
"PWY-8457"
] | [
"EC:2.5.1.3",
"METACYC:PWY-6893",
"METACYC:PWY-6894",
"METACYC:PWY-6897",
"METACYC:PWY-6907",
"METACYC:PWY-6908",
"METACYC:PWY-7356",
"METACYC:PWY-8457"
] | 8 | [] | 0 | [
"PUB00005784"
] | [
"9139923"
] | [
"Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis."
] | [
1997
] | 1 | [
"IPR034291"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"ecological metagenomes"
] | [
567,
2,
5
] | 3 | [] | [] | 0 | true | Family | Thiamine-phosphate synthase, cyanobacterial/bacterial | Thiamine-phosphate synthase, cyanobacterial/bacterial | TMP_synthase_cyanobac_bac | 5 |
IPR016230 | 16,230 | Serine-protein kinase PrkA/YeaG | PrkA/YeaG | Family | 6,564 | false | false | This entry represents YeaG, PrkA and similar proteins in bacteria. ATP-dependent protease PrkA proteins are bacterial and archaeal serine kinases, approximately 630 residues in length. They possesses the A-motif of nucleotide-binding proteins and exhibit distant homology to eukaryotic protein kinases [ ]. Serine/threon... | [
"GO:0004672"
] | [
"protein kinase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000549"
] | [
"Ser_prot_kin"
] | [
6564
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [] | 0 | [
"PUB00012839",
"PUB00160792",
"PUB00160793",
"PUB00160794"
] | [
"8626065",
"18276156",
"26621053",
"33889145"
] | [
"Cloning and characterization of the Bacillus subtilis prkA gene encoding a novel serine protein kinase.",
"Cloning, expression, purification and characterization of the stress kinase YeaG from Escherichia coli.",
"Adaptation to sustained nitrogen starvation by Escherichia coli requires the eukaryote-like serin... | [
1996,
2008,
2015,
2021
] | 4 | [] | [
"IPR057741"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacterium",
"metagenomes",
"uncultured marine phage"
] | [
6532,
2,
7,
22,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Serine-protein kinase PrkA/YeaG | Serine-protein kinase PrkA/YeaG | PrkA/YeaG | 3 |
IPR016231 | 16,231 | Mitogen-activated protein (MAP) kinase kinase kinase, MLK1-4 | MLK1-4 | Family | 2,062 | false | false | This entry represents mitogen-activated protein kinase kinase kinase MAP3K9 (MLK1), MAP3K10 (MLK2), MAP3K11 (MLK3) and MAP3K21 (MLK4), which form part of the mixed lineage kinase (MLK) family [ ]. | [
"GO:0004709"
] | [
"MAP kinase kinase kinase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000556"
] | [
"MAPKKK9_11"
] | [
2062
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.11.25",
"R-HSA-5673000",
"R-HSA-6802946",
"R-HSA-6802955",
"R-HSA-9013148",
"R-HSA-9013408",
"R-HSA-9013424",
"R-HSA-9649948",
"R-MMU-5673000",
"R-MMU-9013408",
"R-MMU-9013424",
"R-RNO-5673000",
"R-RNO-9013408",
"R-RNO-9013424"
] | [
"EC:2.7.11.25",
"REACTOME:R-HSA-5673000",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802955",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9013424",
"REACTOME:R-HSA-9649948",
"REACTOME:R-MMU-5673000",
"REACTOME:R-MMU-9013408",
"REACTOME:R-MMU-9013424",
"REACTOME:R-RNO-56... | 14 | [] | 0 | [
"PUB00073511"
] | [
"12209126"
] | [
"Mixed-lineage kinase control of JNK and p38 MAPK pathways."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
2062
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
7,
6,
7
] | 4 | true | Family | Mitogen-activated protein (MAP) kinase kinase kinase, MLK1-4 | Mitogen-activated protein (MAP) kinase kinase kinase, MLK1-4 | MLK1-4 | 1 |
IPR016233 | 16,233 | Homeobox protein Pitx/unc30 | Homeobox_Pitx/unc30 | Family | 3,025 | false | false | This entry represents the Pitx/unc30 homeobox proteins, which act as transcriptional regulators. | [
"GO:0003700"
] | [
"DNA-binding transcription factor activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000563"
] | [
"Homeobox_protein_Pitx/Unc30"
] | [
3025
] | 1 | [
"REACTOME"
] | [
"R-HSA-8866906"
] | [
"REACTOME:R-HSA-8866906"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
3025
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
8,
6,
7,
10
] | 5 | true | Family | Homeobox protein Pitx/unc30 | Homeobox protein Pitx/unc30 | Homeobox_Pitx/unc30 | 6 |
IPR016234 | 16,234 | Serine/threonine-protein kinase, Sbk1 | Ser/Thr_kinase_Sbk1 | Family | 1,087 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004674",
"GO:0005524",
"GO:0006468"
] | [
"protein serine/threonine kinase activity",
"ATP binding",
"protein phosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000566"
] | [
"Ser/Thr_PK_Sbk1"
] | [
1087
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1087
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
1,
2,
3
] | 4 | true | Family | Serine/threonine-protein kinase, Sbk1 | Serine/threonine-protein kinase, Sbk1 | Ser/Thr_kinase_Sbk1 | 1 |
IPR016235 | 16,235 | Tyrosine/threonine-protein kinase, Cdc2 inhibitor | Tyr/Thr_kinase_Cdc2_inhib | Family | 30 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004674",
"GO:0006468",
"GO:0016020"
] | [
"protein serine/threonine kinase activity",
"protein phosphorylation",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF000567"
] | [
"TYPK_Myt1"
] | [
30
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.11.1",
"R-DME-156711",
"R-DME-69273",
"R-DME-69478",
"R-HSA-156711",
"R-HSA-69273",
"R-HSA-69478",
"R-MMU-156711",
"R-MMU-69273",
"R-MMU-69478"
] | [
"EC:2.7.11.1",
"REACTOME:R-DME-156711",
"REACTOME:R-DME-69273",
"REACTOME:R-DME-69478",
"REACTOME:R-HSA-156711",
"REACTOME:R-HSA-69273",
"REACTOME:R-HSA-69478",
"REACTOME:R-MMU-156711",
"REACTOME:R-MMU-69273",
"REACTOME:R-MMU-69478"
] | 10 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 8 | [
"IPR050339"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
30
] | 1 | [
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus"
] | [
1,
1,
1
] | 3 | true | Family | Tyrosine/threonine-protein kinase, Cdc2 inhibitor | Tyrosine/threonine-protein kinase, Cdc2 inhibitor | Tyr/Thr_kinase_Cdc2_inhib | 7 |
IPR016236 | 16,236 | Serine/threonine-protein kinase PknK, predicted | Ser/Thr_kinase_PknK_prd | Family | 413 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000574"
] | [
"Ser/Thr_PK_PknK_prd"
] | [
413
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Mycobacteriales"
] | [
413
] | 1 | [] | [] | 0 | true | Family | Serine/threonine-protein kinase PknK, predicted | Serine/threonine-protein kinase PknK, predicted | Ser/Thr_kinase_PknK_prd | 1 |
IPR016239 | 16,239 | Ribosomal protein S6 kinase II | Ribosomal_S6_kinase_II | Family | 10,360 | false | false | This entry represents ribosomal protein S6 kinase II [ ]. This enzyme acts as a serine/threonine kinase required for the mitogen or stress-induced phosphorylation of the transcription factors CREB (cAMP response element-binding protein) and ATF1 (activating transcription factor-1). It plays an essential role in the con... | [
"GO:0000287",
"GO:0004674",
"GO:0006468",
"GO:0035556"
] | [
"magnesium ion binding",
"protein serine/threonine kinase activity",
"protein phosphorylation",
"intracellular signal transduction"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF000606"
] | [
"Ribsml_S6_kin_2"
] | [
10360
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.1",
"R-CEL-198753",
"R-CEL-199920",
"R-CEL-2559582",
"R-CEL-375165",
"R-CEL-442742",
"R-CEL-444257",
"R-CEL-881907",
"R-CEL-9856649",
"R-GGA-198753",
"R-GGA-199920",
"R-GGA-2559582",
"R-GGA-375165",
"R-GGA-442742",
"R-GGA-444257",
"R-GGA-5621575",
"R-GGA-881907",
"R-GGA-985... | [
"EC:2.7.11.1",
"REACTOME:R-CEL-198753",
"REACTOME:R-CEL-199920",
"REACTOME:R-CEL-2559582",
"REACTOME:R-CEL-375165",
"REACTOME:R-CEL-442742",
"REACTOME:R-CEL-444257",
"REACTOME:R-CEL-881907",
"REACTOME:R-CEL-9856649",
"REACTOME:R-GGA-198753",
"REACTOME:R-GGA-199920",
"REACTOME:R-GGA-2559582",
... | 44 | [] | 0 | [
"PUB00042703"
] | [
"17804722"
] | [
"Ribosomal S6 kinase 2 is a key regulator in tumor promoter induced cell transformation."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
10360
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
32,
2,
40,
27,
40
] | 6 | true | Family | Ribosomal protein S6 kinase II | Ribosomal protein S6 kinase II | Ribosomal_S6_kinase_II | 8 |
IPR016240 | 16,240 | Serine/threonine-protein kinase YKL116C, predicted | Ser/Thr_kin_YKL116c_prd | Family | 6 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000609"
] | [
"Ser/Thr_PK_YKL116c_prd"
] | [
6
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Saccharomycetaceae"
] | [
6
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Serine/threonine-protein kinase YKL116C, predicted | Serine/threonine-protein kinase YKL116C, predicted | Ser/Thr_kin_YKL116c_prd | 7 |
IPR016241 | 16,241 | Nitrogen network kinase 1 | Nnk1 | Family | 35 | false | false | Nitrogen network kinase 1 (Nnk1) is a protein kinase involved in the phosphorylation of the NAD+-dependent glutamate dehydrogenase Gdh2. When overexpressed, confers hypersensitivity to rapamycin and induces rapid nuclear accumulation of GLN3 to activate the transcription of nitrogen-regulated genes [ ]. | [
"GO:0004672",
"GO:0006468"
] | [
"protein kinase activity",
"protein phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000610"
] | [
"Ser/Thr_PK_YKL171w_prd"
] | [
35
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074992"
] | [
"20489023"
] | [
"A global protein kinase and phosphatase interaction network in yeast."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
35
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Nitrogen network kinase 1 | Nitrogen network kinase 1 | Nnk1 | 1 |
IPR016242 | 16,242 | Serine/threonine-protein kinase Mps1 | Mps1 | Family | 15 | false | false | Mps1 is a serine/threonine-protein kinase involved in the phosphorylation of many mitotic regulators. It is required for spindle pole body (SPB) duplication and spindle checkpoint function [ , ]. It is involved in sister chromatid biorientation in mitosis and meiosis [ ]. The expression of Mps1 is regulated in a cell c... | [
"GO:0004674",
"GO:0004712",
"GO:0006468",
"GO:0007094",
"GO:0030474"
] | [
"protein serine/threonine kinase activity",
"protein serine/threonine/tyrosine kinase activity",
"protein phosphorylation",
"mitotic spindle assembly checkpoint signaling",
"spindle pole body duplication"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"biological_process"
] | 5 | [
"PIRSF"
] | [
"PIRSF000611"
] | [
"Ser/Thr_PK_MPS1"
] | [
15
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042756",
"PUB00073466",
"PUB00073467",
"PUB00074938"
] | [
"17728254",
"7737118",
"8567717",
"23371552"
] | [
"Mps1 activation loop autophosphorylation enhances kinase activity.",
"Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase.",
"The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint.",
"Mps1 and Ipl1/Aurora B act sequ... | [
2007,
1995,
1996,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
15
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Serine/threonine-protein kinase Mps1 | Serine/threonine-protein kinase Mps1 | Mps1 | 7 |
IPR016244 | 16,244 | Tyrosine-protein kinase, HGF/MSP receptor | Tyr_kinase_HGF/MSP_rcpt | Family | 1,833 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004714",
"GO:0005524",
"GO:0007169",
"GO:0016020"
] | [
"transmembrane receptor protein tyrosine kinase activity",
"ATP binding",
"cell surface receptor protein tyrosine kinase signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF000617"
] | [
"TyrPK_HGF-R"
] | [
1833
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"R-HSA-1257604",
"R-HSA-2219530",
"R-HSA-416550",
"R-HSA-5673001",
"R-HSA-6806942",
"R-HSA-6807004",
"R-HSA-6811558",
"R-HSA-8851805",
"R-HSA-8851907",
"R-HSA-8852405",
"R-HSA-8865999",
"R-HSA-8874081",
"R-HSA-8875360",
"R-HSA-8875513",
"R-HSA-8875555",
"R-HSA-8875656",
... | [
"EC:2.7.10.1",
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-2219530",
"REACTOME:R-HSA-416550",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-6806942",
"REACTOME:R-HSA-6807004",
"REACTOME:R-HSA-6811558",
"REACTOME:R-HSA-8851805",
"REACTOME:R-HSA-8851907",
"REACTOME:R-HSA-8852405",
"REACTOME:R-HSA-8865... | 67 | [
"7mo7",
"7mo8",
"7mo9",
"7moa",
"7mob"
] | 5 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052448",
"PUB00052449",
"PUB00052485"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350",
"1846706",
"15314156",
"7939629"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005,
1991,
2004,
1994
] | 11 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
1833
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
2,
6,
6
] | 4 | true | Family | Tyrosine-protein kinase, HGF/MSP receptor | Tyrosine-protein kinase, HGF/MSP receptor | Tyr_kinase_HGF/MSP_rcpt | 2 |
IPR016245 | 16,245 | Tyrosine protein kinase, EGF/ERB/XmrK receptor | Tyr_kinase_EGF/ERB/XmrK_rcpt | Family | 6,167 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004713",
"GO:0005524",
"GO:0006468",
"GO:0007169",
"GO:0016020"
] | [
"protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"cell surface receptor protein tyrosine kinase signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF"
] | [
"PIRSF000619"
] | [
"TyrPK_EGF-R"
] | [
6167
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"R-DME-1227986",
"R-DME-1236394",
"R-DME-1250196",
"R-DME-1250342",
"R-DME-1250347",
"R-DME-1251985",
"R-DME-1253288",
"R-DME-1257604",
"R-DME-1358803",
"R-DME-177929",
"R-DME-179812",
"R-DME-180292",
"R-DME-180336",
"R-DME-182971",
"R-DME-1963640",
"R-DME-1963642",
"R-... | [
"EC:2.7.10.1",
"REACTOME:R-DME-1227986",
"REACTOME:R-DME-1236394",
"REACTOME:R-DME-1250196",
"REACTOME:R-DME-1250342",
"REACTOME:R-DME-1250347",
"REACTOME:R-DME-1251985",
"REACTOME:R-DME-1253288",
"REACTOME:R-DME-1257604",
"REACTOME:R-DME-1358803",
"REACTOME:R-DME-177929",
"REACTOME:R-DME-1798... | 139 | [
"7mn5",
"7mn6",
"7mn8",
"7syd",
"7sye",
"7sz0",
"7sz1",
"7sz5",
"7sz7"
] | 9 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
] | [
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"12368087",
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"15320712",
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"16700535",
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] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 8 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
6167
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
94,
15,
5,
32
] | 5 | true | Family | Tyrosine protein kinase, EGF/ERB/XmrK receptor | Tyrosine protein kinase, EGF/ERB/XmrK receptor | Tyr_kinase_EGF/ERB/XmrK_rcpt | 5 |
IPR016246 | 16,246 | Tyrosine-protein kinase, insulin-like receptor | Tyr_kinase_insulin-like_rcpt | Family | 4,072 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004714",
"GO:0005524",
"GO:0043548",
"GO:0043560",
"GO:0007169",
"GO:0046777",
"GO:0016020"
] | [
"transmembrane receptor protein tyrosine kinase activity",
"ATP binding",
"phosphatidylinositol 3-kinase binding",
"insulin receptor substrate binding",
"cell surface receptor protein tyrosine kinase signaling pathway",
"protein autophosphorylation",
"membrane"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 7 | [
"PIRSF"
] | [
"PIRSF000620"
] | [
"Insulin_receptor"
] | [
4072
] | 1 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"GenProp2088",
"GenProp2090",
"R-HSA-2404192",
"R-HSA-2428928",
"R-HSA-2428933",
"R-HSA-6811558",
"R-HSA-74713",
"R-HSA-74749",
"R-HSA-74751",
"R-HSA-74752",
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"R-HSA-9009391",
"R-HSA-9820960",
"R-MMU-2404192",
"R-MMU-2428928",
"R-MMU-2428933",
"R-MMU-68115... | [
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"REACTOME:R-HSA-6811558",
"REACTOME:R-HSA-74713",
"REACTOME:R-HSA-74749",
"REACTOME:R-HSA-74751",
"REACTOME:R-HSA-74752",
"REACTOME:R-HSA-77387",
"REACTOME:R-HSA-9... | 34 | [
"6jk8",
"6pxv",
"6pxw",
"6pyh",
"7bw7",
"7bw8",
"7bwa",
"7pg0",
"7pg2",
"7pg3",
"7pg4",
"7sl1",
"7sl2",
"7sl3",
"7sl4",
"7sl6",
"7sl7",
"7sth",
"7sti",
"7stj",
"7stk",
"7tyj",
"7tyk",
"7tym",
"8dtl",
"8dtm",
"8eyr",
"8eyx",
"8eyy",
"8ez0",
"8u4b",
"8u4c"... | 48 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052450",
"PUB00052451",
"PUB00052452"
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"12471243",
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"19275641",
"16700535",
"15845350",
"12138094",
"16831875",
"8276809"
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"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005,
2002,
2006,
1994
] | 11 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
4072
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
4,
5,
11
] | 4 | true | Family | Tyrosine-protein kinase, insulin-like receptor | Tyrosine-protein kinase, insulin-like receptor | Tyr_kinase_insulin-like_rcpt | 6 |
IPR016247 | 16,247 | Tyrosine-protein kinase, receptor ROR | Tyr_kinase_rcpt_ROR | Family | 1,688 | false | false | The Ror family of receptor tyrosine kinases consists of two structurally related proteins, Ror1 and Ror2. Ror1 is a pseudokinase that acts as a substrate for the oncogenic tyrosine kinase Met [ ]. It is expressed during development [ ]. It shows no significant expression in normal adult tissues, but it is selectively o... | [
"GO:0007169"
] | [
"cell surface receptor protein tyrosine kinase signaling pathway"
] | [
"biological_process"
] | 1 | [
"PIRSF"
] | [
"PIRSF000624"
] | [
"TyrPK_TMrec_ROR"
] | [
1688
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.10.1",
"R-CEL-5140745",
"R-HSA-4086400",
"R-HSA-5140745",
"R-MMU-5140745"
] | [
"EC:2.7.10.1",
"REACTOME:R-CEL-5140745",
"REACTOME:R-HSA-4086400",
"REACTOME:R-HSA-5140745",
"REACTOME:R-MMU-5140745"
] | 5 | [] | 0 | [
"PUB00076689",
"PUB00076690",
"PUB00076691",
"PUB00076692",
"PUB00076693"
] | [
"25835638",
"25825749",
"11713269",
"21487037",
"18667433"
] | [
"Receptor tyrosine kinase-like orphan receptor 1: a novel target for cancer immunotherapy.",
"RoR2 functions as a noncanonical Wnt receptor that regulates NMDAR-mediated synaptic transmission.",
"Loss of mRor1 enhances the heart and skeletal abnormalities in mRor2-deficient mice: redundant and pleiotropic funct... | [
2015,
2015,
2001,
2011,
2008
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1688
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
1,
5,
8,
11
] | 6 | true | Family | Tyrosine-protein kinase, receptor ROR | Tyrosine-protein kinase, receptor ROR | Tyr_kinase_rcpt_ROR | 8 |
IPR016248 | 16,248 | Fibroblast growth factor receptor family | FGF_rcpt_fam | Family | 8,006 | false | false | Fibroblast growth factors (FGFs) [ , ] are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [ , ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGF... | [
"GO:0005007",
"GO:0005524",
"GO:0006468",
"GO:0008284",
"GO:0008543",
"GO:0016020"
] | [
"fibroblast growth factor receptor activity",
"ATP binding",
"protein phosphorylation",
"positive regulation of cell population proliferation",
"fibroblast growth factor receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PIRSF"
] | [
"PIRSF000628"
] | [
"FGFR"
] | [
8006
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"R-DME-109704",
"R-DME-1257604",
"R-DME-1307965",
"R-DME-190322",
"R-DME-190371",
"R-DME-190372",
"R-DME-190375",
"R-DME-190377",
"R-DME-5654221",
"R-DME-5654227",
"R-DME-5654228",
"R-DME-5654695",
"R-DME-5654699",
"R-DME-5654700",
"R-DME-5654704",
"R-DME-5654706",
"R-D... | [
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"REACTOME:R-DME-190322",
"REACTOME:R-DME-190371",
"REACTOME:R-DME-190372",
"REACTOME:R-DME-190375",
"REACTOME:R-DME-190377",
"REACTOME:R-DME-5654221",
"REACTOME:R-DME-5654227",
"REACTOME:R-DME-5654228",... | 185 | [
"8jqi"
] | 1 | [
"PUB00000068",
"PUB00001036",
"PUB00005334",
"PUB00021048",
"PUB00024683",
"PUB00039267",
"PUB00067611",
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"PUB00067613",
"PUB00067626",
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"PUB00067628",
"PUB00067629",
"PUB00067630",
"PUB00067631",
"PUB00067632",
"PUB00067633",
"PUB00067634",
"PUB000676... | [
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"7583099",
"3072709",
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"8652550",
"8663044",
"16829530",
"15781473",
"1705486",
"8760337",
"23000357",
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"23016864",
"1649700",
"11746231",
"14745970",
"8978613",
"16597617",
"9212826",
"18216218"
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"The heparin-binding (fibroblast) growth factor family of proteins.",
"Functions of fibroblast growth factors and their receptors.",
"Transforming potential of fibroblast growth factor genes.",
"Fibroblast growth factors.",
"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-rece... | [
1989,
1995,
1988,
2001,
2000,
1996,
1996,
2006,
2005,
1990,
1996,
2012,
2005,
1999,
2013,
2013,
1991,
2001,
2003,
1996,
2006,
1997,
2008
] | 23 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
8006
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
45,
1,
35,
46,
18
] | 5 | true | Family | Fibroblast growth factor receptor family | Fibroblast growth factor receptor family | FGF_rcpt_fam | 5 |
IPR016249 | 16,249 | Tyrosine-protein kinase, Ret receptor | Tyr_kinase_Ret_rcpt | Family | 846 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000631"
] | [
"TyrPK_receptor_Ret"
] | [
846
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"R-MMU-5673001",
"R-MMU-8853659",
"R-RNO-5673001",
"R-RNO-8853659"
] | [
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"REACTOME:R-HSA-8853659",
"REACTOME:R-HSA-9768919",
"REACTOME:R-HSA-9830364",
"REACTOME:R-HSA-9830674",
"REACTOME:R-MMU-5673001",
"REACTOME:R-MMU-8853659",
"REACTOME:R-RNO-5673001",
"REACTOME:R-RNO-8853659"
] | 10 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
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"12471243",
"15078142",
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"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 8 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
846
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
1,
3
] | 4 | true | Family | Tyrosine-protein kinase, Ret receptor | Tyrosine-protein kinase, Ret receptor | Tyr_kinase_Ret_rcpt | 9 |
IPR016250 | 16,250 | Tyrosine-protein kinase, Fes/Fps type | Tyr-prot_kinase_Fes/Fps | Family | 2,295 | false | false | Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups [ ]: Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhes... | [
"GO:0004715",
"GO:0018108"
] | [
"non-membrane spanning protein tyrosine kinase activity",
"peptidyl-tyrosine phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000632"
] | [
"TyrPK_fps"
] | [
2295
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
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"R-HSA-1433557",
"R-HSA-399954",
"R-HSA-399955",
"R-HSA-399956",
"R-MMU-1433557",
"R-MMU-399954",
"R-MMU-399956",
"R-RNO-1433557"
] | [
"EC:2.7.10.2",
"REACTOME:R-HSA-1433557",
"REACTOME:R-HSA-399954",
"REACTOME:R-HSA-399955",
"REACTOME:R-HSA-399956",
"REACTOME:R-MMU-1433557",
"REACTOME:R-MMU-399954",
"REACTOME:R-MMU-399956",
"REACTOME:R-RNO-1433557"
] | 9 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
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"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 8 | [] | [] | 0 | 0 | null | [
"Fujinami sarcoma virus",
"Metazoa"
] | [
1,
2294
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
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8,
2,
6,
3,
6
] | 5 | true | Family | Tyrosine-protein kinase, Fes/Fps type | Tyrosine-protein kinase, Fes/Fps type | Tyr-prot_kinase_Fes/Fps | 4 |
IPR016251 | 16,251 | Tyrosine-protein kinase, non-receptor Jak/Tyk2 | Tyr_kinase_non-rcpt_Jak/Tyk2 | Family | 5,802 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004715",
"GO:0005524",
"GO:0006468",
"GO:0035556",
"GO:0016020"
] | [
"non-membrane spanning protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"intracellular signal transduction",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF000636",
"PR01823"
] | [
"TyrPK_Jak",
"JANUSKINASE"
] | [
4696,
5722
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"R-HSA-1170546",
"R-HSA-1266695",
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"REACTOME:R-DRE-6783783",
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"REACTOME:R-DRE-877300",
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"REACTOME:R-DRE-8854691",
"REACTOME:R-DRE-8985947",
"REACTOME:R-DRE-9020958",
"REACTOME:R-HSA-1059683... | 159 | [
"4oli",
"7t6f",
"8ewy"
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"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052425",
"PUB00052523",
"PUB00052524",
"PUB00052525",
"PUB00052526"
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"9096349",
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"19596999",
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"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005,
2009,
1997,
2009,
2009,
1994
] | 13 | [] | [
"IPR020693",
"IPR020775",
"IPR020776"
] | 0 | 3 | 0 | [
"Bilateria"
] | [
5802
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
25,
15,
13
] | 4 | true | Family | Tyrosine-protein kinase, non-receptor Jak/Tyk2 | Tyrosine-protein kinase, non-receptor Jak/Tyk2 | Tyr_kinase_non-rcpt_Jak/Tyk2 | 2 |
IPR016252 | 16,252 | Serine/threonine-protein kinase SpkB | Ser/Thr_kinase_SpkB | Family | 302 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000647"
] | [
"Ser/Thr_PK_SpkB"
] | [
302
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00042771"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"12168951"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2002
] | 6 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota"
] | [
302
] | 1 | [] | [] | 0 | true | Family | Serine/threonine-protein kinase SpkB | Serine/threonine-protein kinase SpkB | Ser/Thr_kinase_SpkB | 3 |
IPR016254 | 16,254 | Serine/threonine-protein kinase, asfivirus | Ser/Thr_kinase_asfivir | Family | 6 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004674",
"GO:0005524",
"GO:0006468",
"GO:0016032"
] | [
"protein serine/threonine kinase activity",
"ATP binding",
"protein phosphorylation",
"viral process"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF000657"
] | [
"Ser/Thr_PK_ASFV"
] | [
6
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00042772"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"8331722"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
1993
] | 6 | [] | [] | 0 | 0 | null | [
"African swine fever virus"
] | [
6
] | 1 | [] | [] | 0 | true | Family | Serine/threonine-protein kinase, asfivirus | Serine/threonine-protein kinase, asfivirus | Ser/Thr_kinase_asfivir | 1 |
IPR016255 | 16,255 | eIF-2-alpha kinase Gcn2 | Gcn2 | Family | 3,175 | false | false | This entry represents Gcn2, a protein kinase that regulates the G1/S cell cycle checkpoint in response to DNA damage [ , ]. It stimulates Gcn4 translation in amino acid-starved cells by phosphorylating the alpha subunit of eIF-2 (SUI2) on 'Ser-52' [ ]. This entry also includes the probable serine/threonine-protein kina... | [
"GO:0004694",
"GO:0000077",
"GO:0006468",
"GO:0010998"
] | [
"eukaryotic translation initiation factor 2alpha kinase activity",
"DNA damage checkpoint signaling",
"protein phosphorylation",
"regulation of translational initiation by eIF2 alpha phosphorylation"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF000660"
] | [
"Ser/Thr_PK_GCN2"
] | [
3175
] | 1 | [
"EC",
"REACTOME"
] | [
"2.7.11.1",
"R-HSA-9633012"
] | [
"EC:2.7.11.1",
"REACTOME:R-HSA-9633012"
] | 2 | [
"8t7t",
"9bf3",
"9f58"
] | 3 | [
"PUB00042773",
"PUB00042774",
"PUB00042775"
] | [
"17890903",
"17369398",
"11350982"
] | [
"Gcn2p regulates a G1/S cell cycle checkpoint in response to DNA damage.",
"A novel checkpoint mechanism regulating the G1/S transition.",
"Budding yeast GCN1 binds the GI domain to activate the eIF2alpha kinase GCN2."
] | [
2007,
2007,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3175
] | 1 | [
"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 (strain 972 / ATCC 24843)"
] | [
2,
4,
1,
3,
1,
6,
1,
1
] | 8 | true | Family | eIF-2-alpha kinase Gcn2 | eIF-2-alpha kinase Gcn2 | Gcn2 | 5 |
IPR016256 | 16,256 | Serine/threonine-protein kinase Rad53 | Ser/Thr_kinase_Rad53 | Family | 158 | false | false | Rad53 is a protein kinase required for cell-cycle arrest in response to DNA damage. Rad53 controls the S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. It prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase Cdc5 [ ]. Rad53 also seems to be involved in the phos... | [
"GO:0003688",
"GO:0004712",
"GO:0000077",
"GO:0006270",
"GO:0006281",
"GO:0009202",
"GO:0005634"
] | [
"DNA replication origin binding",
"protein serine/threonine/tyrosine kinase activity",
"DNA damage checkpoint signaling",
"DNA replication initiation",
"DNA repair",
"deoxyribonucleoside triphosphate biosynthetic process",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 7 | [
"PIRSF"
] | [
"PIRSF000661"
] | [
"Ser/Thr_PK_RAD53"
] | [
158
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042765",
"PUB00042766",
"PUB00042767"
] | [
"10550056",
"11809875",
"17325030"
] | [
"Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms.",
"Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase.",
"Mechanisms of checkpoint kinase Rad53 inactivation after a double-strand break in... | [
1999,
2002,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Dikarya"
] | [
158
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Serine/threonine-protein kinase Rad53 | Serine/threonine-protein kinase Rad53 | Ser/Thr_kinase_Rad53 | 3 |
IPR016257 | 16,257 | Ephrin receptor type-A /type-B | EPH | Family | 16,905 | false | false | This entry represents type A and type B ephrin receptors. There are 10 EphA receptors and six EphB receptors, distinguished on sequence difference and binding preferences. They interact with the six glycosylphosphatidylinositol-linked ephrin-A ligands and the three transmembrane ephrin-B ligands, respectively [ ]. The ... | [
"GO:0005003",
"GO:0005524",
"GO:0006468",
"GO:0007169",
"GO:0005886"
] | [
"ephrin receptor activity",
"ATP binding",
"protein phosphorylation",
"cell surface receptor protein tyrosine kinase signaling pathway",
"plasma membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF"
] | [
"PIRSF000666"
] | [
"TyrPK_ephrin_receptor"
] | [
16905
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"R-DRE-2682334",
"R-DRE-3928662",
"R-DRE-3928663",
"R-DRE-3928664",
"R-DRE-3928665",
"R-GGA-2682334",
"R-GGA-3928663",
"R-GGA-3928665",
"R-HSA-2682334",
"R-HSA-2892247",
"R-HSA-373760",
"R-HSA-3928662",
"R-HSA-3928663",
"R-HSA-3928664",
"R-HSA-3928665",
"R-HSA-9013149",
... | [
"EC:2.7.10.1",
"REACTOME:R-DRE-2682334",
"REACTOME:R-DRE-3928662",
"REACTOME:R-DRE-3928663",
"REACTOME:R-DRE-3928664",
"REACTOME:R-DRE-3928665",
"REACTOME:R-GGA-2682334",
"REACTOME:R-GGA-3928663",
"REACTOME:R-GGA-3928665",
"REACTOME:R-HSA-2682334",
"REACTOME:R-HSA-2892247",
"REACTOME:R-HSA-373... | 45 | [] | 0 | [
"PUB00004289",
"PUB00006523",
"PUB00010665",
"PUB00052266",
"PUB00055943",
"PUB00055944",
"PUB00067418",
"PUB00073291"
] | [
"9853759",
"10730216",
"11780069",
"19525919",
"11750881",
"11256076",
"12094214",
"23021982"
] | [
"Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.",
"Eph receptors and ephrins: regulators of guidance and assembly.",
"Crystal structure of an Eph receptor-ephrin complex.",
"Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domai... | [
1998,
2000,
2001,
2009,
2002,
2001,
2002,
2012
] | 8 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
16905
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
83,
8,
37,
32,
46
] | 5 | true | Family | Ephrin receptor type-A /type-B | Ephrin receptor type-A /type-B | EPH | 9 |
IPR016258 | 16,258 | Multiphosphoryl transfer protein FruB | FruB | Family | 116 | false | false | This group represents multiphosphoryl transfer protein fruB. It is part of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyses the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membr... | [] | [] | [] | 0 | [
"NCBIFAM",
"PIRSF"
] | [
"NF010351",
"PIRSF000690"
] | [
"PRK13779.1",
"Fruc_PTS_diPryltransf"
] | [
103,
116
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pasteurellaceae"
] | [
116
] | 1 | [] | [] | 0 | true | Family | Multiphosphoryl transfer protein FruB | Multiphosphoryl transfer protein FruB | FruB | 6 |
IPR016259 | 16,259 | Hygromycin-B kinase | Hygromycin-B_Kinase | Family | 866 | false | false | This entry represents a group of hygromycin-B kinases, including hygromycin-B 7''-O-kinase from Streptomyces hygroscopicus [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000707"
] | [
"Hygromycin-B_kinase"
] | [
866
] | 1 | [] | [] | [] | 0 | [
"6iy9"
] | 1 | [
"PUB00073580"
] | [
"3005976"
] | [
"Nucleotide sequence of the hygromycin B phosphotransferase gene from Streptomyces hygroscopicus."
] | [
1986
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"marine sediment metagenome"
] | [
833,
29,
3,
1
] | 4 | [] | [] | 0 | true | Family | Hygromycin-B kinase | Hygromycin-B kinase | Hygromycin-B_Kinase | 5 |
IPR016261 | 16,261 | Folic acid synthesis protein FOL1 | Folic_acid_synth | Family | 116 | false | false | FOL1 catalyses three sequential steps of the tetrahydrofolate biosynthetic pathway and is therefore the central enzyme of this pathway [ ]. | [
"GO:0003848",
"GO:0004150",
"GO:0004156",
"GO:0046654"
] | [
"2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity",
"dihydroneopterin aldolase activity",
"dihydropteroate synthase activity",
"tetrahydrofolate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF000741"
] | [
"Folic_acid_synth"
] | [
116
] | 1 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.5.1.15",
"2.7.6.3",
"4.1.2.25",
"PWY-6147",
"PWY-6148",
"PWY-6614",
"PWY-6797",
"PWY-7539",
"PWY-7852",
"PWY-7853"
] | [
"EC:2.5.1.15",
"EC:2.7.6.3",
"EC:4.1.2.25",
"METACYC:PWY-6147",
"METACYC:PWY-6148",
"METACYC:PWY-6614",
"METACYC:PWY-6797",
"METACYC:PWY-7539",
"METACYC:PWY-7852",
"METACYC:PWY-7853"
] | 10 | [] | 0 | [
"PUB00073622"
] | [
"15169867"
] | [
"Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth."
] | [
2004
] | 1 | [
"IPR045031"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
116
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1
] | 2 | true | Family | Folic acid synthesis protein FOL1 | Folic acid synthesis protein FOL1 | Folic_acid_synth | 5 |
IPR016262 | 16,262 | RNA polymerase sigma factor, SigB/C/D/F, plastid | RNA_pol_sigma_SigB/C/D/F | Family | 1,196 | false | false | This entry represents certain plastid RNA polymerase sigma factors, including SigB, SigC, SigD and sigF [ , ]. Development of plastids into chloroplasts is triggered by light. The coordination of light-induced plastid gene expression is directed by both nuclear and plastid genomes. Plastid DNA is transcribed by at leas... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000767"
] | [
"RNA_pol_sigma_SigB/C/D"
] | [
1196
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042712",
"PUB00042713",
"PUB00042714"
] | [
"10555304",
"10984613",
"11094163"
] | [
"Plastidic RNA polymerase sigma factors in Arabidopsis.",
"Three new nuclear genes, sigD, sigE and sigF, encoding putative plastid RNA polymerase sigma factors in Aarabidopsis thaliana.",
"Chloroplast development in Arabidopsis thaliana requires the nuclear-encoded transcription factor sigma B."
] | [
1999,
2000,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1196
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
12,
11,
20
] | 3 | true | Family | RNA polymerase sigma factor, SigB/C/D/F, plastid | RNA polymerase sigma factor, SigB/C/D/F, plastid | RNA_pol_sigma_SigB/C/D/F | 8 |
IPR016266 | 16,266 | DNA polymerase epsilon, subunit B | POLE2 | Family | 4,955 | false | false | DNA polymerase epsilon is essential for cell viability and chromosomal DNA replication in budding yeast. In addition, DNA polymerase epsilon may be involved in DNA repair and cell-cycle checkpoint control. The enzyme consists of at least four subunits in mammalian cells as well as in yeast. The largest subunit of DNA p... | [
"GO:0003677",
"GO:0006261",
"GO:0008622"
] | [
"DNA binding",
"DNA-templated DNA replication",
"epsilon DNA polymerase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000799",
"PTHR12708"
] | [
"DNA_pol_eps_2",
""
] | [
2243,
4955
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-110314",
"R-CEL-5651801",
"R-CEL-5656169",
"R-CEL-5696397",
"R-CEL-5696400",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-68952",
"R-CEL-68962",
"R-DDI-110314",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6782210",
"R-DDI-68952",
"R-DDI-68962",
"R-... | [
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-5651801",
"REACTOME:R-CEL-5656169",
"REACTOME:R-CEL-5696397",
"REACTOME:R-CEL-5696400",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-68952",
"REACTOME:R-CEL-68962",
"REACTOME:R-DDI-110314",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DD... | 65 | [
"5vbn",
"6hv8",
"6hv9",
"6wjv",
"7pfo",
"7plo",
"7pmk",
"7pmn",
"7qhs",
"7z13",
"8kg6",
"8kg8",
"8kg9",
"8p5e",
"8p62",
"8p63",
"8w7m",
"8w7s",
"8xgc"
] | 19 | [
"PUB00010584"
] | [
"11872158"
] | [
"The second largest subunit of mouse DNA polymerase epsilon, DPE2, interacts with SAP18 and recruits the Sin3 co-repressor protein to DNA."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4955
] | 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... | [
6,
1,
4,
1,
4,
4,
1,
7,
4,
1,
1,
6
] | 12 | true | Family | DNA polymerase epsilon, subunit B | DNA polymerase epsilon, subunit B | POLE2 | 1 |
IPR016267 | 16,267 | UTP--glucose-1-phosphate uridylyltransferase | UDPGP_trans | Family | 9,728 | false | false | UDP-glucose is the universal activated form of glucose, employed in all organisms for glucosyl transfer reactions and as precursor for various activated carbohydrates [ ]. It is formed by the enzyme UDP-glucose pyrophosphorylase (UGPase, UDPGP), also known as UTP--glucose-1-phosphate uridylyltransferase, ( ), which cat... | [
"GO:0003983",
"GO:0006011"
] | [
"UTP:glucose-1-phosphate uridylyltransferase activity",
"UDP-alpha-D-glucose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER",
"CDD"
] | [
"PIRSF000806",
"PTHR43511",
"cd00897"
] | [
"UDPGP",
"",
"UGPase_euk"
] | [
6931,
9628,
6414
] | 3 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.9",
"PWY-3801",
"PWY-6527",
"PWY-7238",
"PWY-7343",
"PWY-7817",
"R-BTA-173599",
"R-BTA-3322077",
"R-DDI-173599",
"R-DDI-3322077",
"R-HSA-173599",
"R-HSA-3322077",
"R-MMU-173599",
"R-MMU-3322077",
"R-SCE-173599",
"R-SCE-3322077",
"R-SPO-173599",
"R-SPO-3322077"
] | [
"EC:2.7.7.9",
"METACYC:PWY-3801",
"METACYC:PWY-6527",
"METACYC:PWY-7238",
"METACYC:PWY-7343",
"METACYC:PWY-7817",
"REACTOME:R-BTA-173599",
"REACTOME:R-BTA-3322077",
"REACTOME:R-DDI-173599",
"REACTOME:R-DDI-3322077",
"REACTOME:R-HSA-173599",
"REACTOME:R-HSA-3322077",
"REACTOME:R-MMU-173599",
... | 18 | [
"1z90",
"2i5k",
"2icx",
"2icy",
"2oef",
"2oeg",
"2q4j",
"3gue",
"3r2w",
"3r3i",
"4j18",
"4m28",
"4m2a",
"4m2b",
"4r7p",
"5nzg",
"5nzh",
"5nzi",
"5nzj",
"5nzk",
"5nzl",
"5nzm",
"5weg",
"7ppr",
"8c0b"
] | 25 | [
"PUB00041612"
] | [
"17010990"
] | [
"Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae."
] | [
2006
] | 1 | [
"IPR002618"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"metagenomes"
] | [
1261,
8443,
3,
21
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
12,
7,
7,
5,
17,
3,
1,
9,
6,
2,
2,
51
] | 12 | true | Family | UTP--glucose-1-phosphate uridylyltransferase | UTP--glucose-1-phosphate uridylyltransferase | UDPGP_trans | 1 |
IPR016268 | 16,268 | RNA-directed RNA polymerase, hantavirus | RNA-dir_pol_hantavirus | Family | 280 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [
"GO:0003968",
"GO:0019079"
] | [
"RNA-directed RNA polymerase activity",
"viral genome replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000825"
] | [
"L_HantaV"
] | [
280
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [
"8c4s",
"8c4t",
"8c4u",
"8c4v",
"8ci5",
"8p1j",
"8p1k",
"8p1l",
"8p1m",
"8p1n",
"8qe5",
"8qgt",
"8qgu",
"8qh3",
"8qhd"
] | 15 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625",
"PUB00042718"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187",
"15503219"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000,
2005
] | 7 | [] | [] | 0 | 0 | null | [
"Hantaviridae"
] | [
280
] | 1 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, hantavirus | RNA-directed RNA polymerase, hantavirus | RNA-dir_pol_hantavirus | 6 |
IPR016269 | 16,269 | RNA-directed RNA polymerase, paramyxovirus | RNA-dir_pol_paramyxovirus | Family | 2,932 | false | false | This entry represents RNA-directed RNA polymerase (also known as the large structural protein) from Mononegavirales including Paramyxoviruses [ ]. The large structural protein (or L protein) carries four enzymatic activities: RNA-directed RNA polymerase ( ), mRNA (guanine-N(7)-)-methyltransferase ( ), mRNA guanylyltran... | [
"GO:0016740",
"GO:0006139"
] | [
"transferase activity",
"nucleobase-containing compound metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000830"
] | [
"RNA_pol_ParamyxoV"
] | [
2932
] | 1 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"2.7.7.88",
"3.6.1.-",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289"
] | [
"EC:2.7.7.48",
"EC:2.7.7.88",
"EC:3.6.1.-",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289"
] | 13 | [
"6v85",
"6v86",
"7yot",
"7you",
"7yov",
"8izl",
"8izm",
"8kdb",
"8kdc",
"8x01",
"8yxl",
"8yxm",
"8yxp",
"8zpv",
"9bdq",
"9cgi",
"9cok",
"9dus",
"9dut",
"9fux",
"9gjt",
"9gju",
"9ir3",
"9ir4",
"9iva",
"9knq",
"9knt",
"9knv",
"9knz",
"9mzh",
"9oce",
"9ocf"... | 32 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625",
"PUB00042720"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187",
"15177894"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000,
2004
] | 7 | [] | [] | 0 | 0 | null | [
"Protostomia",
"Viruses"
] | [
5,
2927
] | 2 | [] | [] | 0 | true | Family | RNA-directed RNA polymerase, paramyxovirus | RNA-directed RNA polymerase, paramyxovirus | RNA-dir_pol_paramyxovirus | 1 |
IPR016270 | 16,270 | CDP-alcohol phosphatidyltransferase class-II family | PGS1 | Family | 7,402 | false | false | This entry represents the CDP-alcohol phosphatidyltransferase class-II family, whose members include Pgs1 from S. cerevisiae. Pgs1 is a phosphatidylglycerolphosphate synthase that catalyzes the committed step to the synthesis of of cardiolipin [ ]. | [
"GO:0008444",
"GO:0032049"
] | [
"CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity",
"cardiolipin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER"
] | [
"PTHR12586"
] | [
""
] | [
7402
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME"
] | [
"2.7.8.5",
"PWY-5269",
"PWY-5668",
"PWY-7817",
"R-HSA-1483148"
] | [
"EC:2.7.8.5",
"METACYC:PWY-5269",
"METACYC:PWY-5668",
"METACYC:PWY-7817",
"REACTOME:R-HSA-1483148"
] | 5 | [
"3hsi",
"8yr5",
"8yr6"
] | 3 | [
"PUB00085087"
] | [
"9545322"
] | [
"The PEL1 gene (renamed PGS1) encodes the phosphatidylglycero-phosphate synthase of Saccharomyces cerevisiae."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
3101,
4298,
3
] | 3 | [
"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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
2,
2,
1,
1,
8,
5,
1,
5,
1,
1
] | 10 | true | Family | CDP-alcohol phosphatidyltransferase class-II family | CDP-alcohol phosphatidyltransferase class-II family | PGS1 | 7 |
IPR016271 | 16,271 | CDP-diacylglycerol--serine O-phosphatidyltransferase, fungal | CDP-diaglyc--ser_O-PTrfase_fun | Family | 1,014 | false | false | This group represents a CDP-diacylglycerol--serine O-phosphatidyltransferase, fungal type. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000852"
] | [
"Phosphatidylserine_synth_fun"
] | [
1014
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR004533"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1014
] | 1 | [
"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,
1,
1
] | 3 | true | Family | CDP-diacylglycerol--serine O-phosphatidyltransferase, fungal | CDP-diacylglycerol--serine O-phosphatidyltransferase, fungal | CDP-diaglyc--ser_O-PTrfase_fun | 4 |
IPR016272 | 16,272 | Lipase, LIPH-type | Lipase_LIPH | Family | 8,478 | false | false | This group represents LIPH (lipase H)-type lipases [ ]. It includes lipase H, lipoprotein lipase (LPL), and hepatic and pancreatic lipases. LIPH hydrolyses specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid [ , ]. | [
"GO:0052689",
"GO:0006629"
] | [
"carboxylic ester hydrolase activity",
"lipid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000865"
] | [
"Lipoprotein_lipase_LIPH"
] | [
8478
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.1",
"R-BTA-192456",
"R-BTA-8963889",
"R-BTA-8963901",
"R-BTA-8964026",
"R-BTA-975634",
"R-DRE-1482801",
"R-DRE-1483166",
"R-GGA-8963889",
"R-HSA-1482801",
"R-HSA-1483166",
"R-HSA-192456",
"R-HSA-381340",
"R-HSA-8963889",
"R-HSA-8963901",
"R-HSA-8964026",
"R-HSA-8964058",
"R-HS... | [
"EC:3.1.1",
"REACTOME:R-BTA-192456",
"REACTOME:R-BTA-8963889",
"REACTOME:R-BTA-8963901",
"REACTOME:R-BTA-8964026",
"REACTOME:R-BTA-975634",
"REACTOME:R-DRE-1482801",
"REACTOME:R-DRE-1483166",
"REACTOME:R-GGA-8963889",
"REACTOME:R-HSA-1482801",
"REACTOME:R-HSA-1483166",
"REACTOME:R-HSA-192456",... | 37 | [
"1bu8",
"1eth",
"1gpl",
"1hpl",
"1lpa",
"1lpb",
"1n8s",
"1rp1",
"1w52",
"2oxe",
"2ppl",
"2pvs",
"6e7k",
"6oau",
"6oaz",
"6ob0",
"6u7m",
"8erl",
"9nrn"
] | 19 | [
"PUB00071776",
"PUB00071779",
"PUB00071780"
] | [
"12213196",
"12063250",
"12963729"
] | [
"Lipase H, a new member of the triglyceride lipase family synthesized by the intestine.",
"A novel phosphatidic acid-selective phospholipase A1 that produces lysophosphatidic acid.",
"Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta.... | [
2002,
2002,
2003
] | 3 | [
"IPR000734"
] | [
"IPR002330",
"IPR002331",
"IPR002333"
] | 1 | 3 | 0 | [
"Eumetazoa"
] | [
8478
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
2,
29,
30,
35
] | 5 | true | Family | Lipase, LIPH-type | Lipase, LIPH-type | Lipase_LIPH | 5 |
IPR016273 | 16,273 | Erythromycin esterase, proteobacteria | Emycin_Estase_proteobac | Family | 253 | false | false | This group represents an erythromycin esterase. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000880"
] | [
"Eryth_est"
] | [
253
] | 1 | [] | [] | [] | 0 | [
"6xcq",
"6xcs"
] | 2 | [] | [] | [] | [] | 0 | [
"IPR007815"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
253
] | 1 | [] | [] | 0 | true | Family | Erythromycin esterase, proteobacteria | Erythromycin esterase, proteobacteria | Emycin_Estase_proteobac | 7 |
IPR016274 | 16,274 | Histidine acid phosphatase, eukaryotic | Histidine_acid_Pase_euk | Family | 6,616 | false | false | This family represents eukaryotic histidine acid phosphatases, including Phytase A from Aspergillus oryzae (PhyA) and human Multiple inositol polyphosphate phosphatase 1 (MINPP1). PhyA catalyses the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate) with the subsequent formation of myo-inosit... | [
"GO:0016791"
] | [
"phosphatase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000894"
] | [
"Acid_phosphatase"
] | [
6616
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3",
"R-HSA-1855231",
"R-MMU-1855231",
"R-RNO-1855231"
] | [
"EC:3.1.3",
"REACTOME:R-HSA-1855231",
"REACTOME:R-MMU-1855231",
"REACTOME:R-RNO-1855231"
] | 4 | [
"1ihp",
"1qfx",
"1qwo",
"1sk8",
"1sk9",
"1ska",
"1skb",
"2gfi",
"3k4p",
"3k4q"
] | 10 | [
"PUB00153140",
"PUB00153141",
"PUB00153142"
] | [
"33257696",
"36589890",
"36763800"
] | [
"MINPP1 prevents intracellular accumulation of the chelator inositol hexakisphosphate and is mutated in Pontocerebellar Hypoplasia.",
"Stable Isotopomers of <i>myo-</i>Inositol Uncover a Complex MINPP1-Dependent Inositol Phosphate Network.",
"Enhanced production and immobilization of phytase from Aspergillus or... | [
2020,
2022,
2023
] | 3 | [
"IPR000560"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
6616
] | 1 | [
"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)",
"... | [
4,
3,
3,
2,
1,
1,
2,
4,
5,
3,
4
] | 11 | true | Family | Histidine acid phosphatase, eukaryotic | Histidine acid phosphatase, eukaryotic | Histidine_acid_Pase_euk | 7 |
IPR016275 | 16,275 | Glucose-6-phosphatase | Glucose-6-phosphatase | Family | 2,474 | false | false | This family represents glucose-6-phosphatases, hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. It forms, with the glucose-6-phosphate transporter (SLC37A4/G6PT), the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis, being the key enzyme in hom... | [
"GO:0004346"
] | [
"glucose-6-phosphatase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000905"
] | [
"Glucose-6-phosphatase"
] | [
2474
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.9",
"GenProp2089",
"R-BTA-70263",
"R-DRE-70263",
"R-HSA-3274531",
"R-HSA-3282872",
"R-HSA-70263",
"R-HSA-9615017",
"R-MMU-70263",
"R-RNO-70263"
] | [
"EC:3.1.3.9",
"GP:GenProp2089",
"REACTOME:R-BTA-70263",
"REACTOME:R-DRE-70263",
"REACTOME:R-HSA-3274531",
"REACTOME:R-HSA-3282872",
"REACTOME:R-HSA-70263",
"REACTOME:R-HSA-9615017",
"REACTOME:R-MMU-70263",
"REACTOME:R-RNO-70263"
] | 10 | [
"9j7u",
"9j7v"
] | 2 | [
"PUB00097249",
"PUB00097250",
"PUB00097251"
] | [
"15542400",
"9497333",
"13129915"
] | [
"Glycogen storage disease type Ia in Argentina: two novel glucose-6-phosphatase mutations affecting protein stability.",
"Transmembrane topology of glucose-6-phosphatase.",
"A glucose-6-phosphate hydrolase, widely expressed outside the liver, can explain age-dependent resolution of hypoglycemia in glycogen stor... | [
2004,
1998,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2474
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
3,
3,
6
] | 4 | true | Family | Glucose-6-phosphatase | Glucose-6-phosphatase | Glucose-6-phosphatase | 8 |
IPR016276 | 16,276 | Non-receptor tyrosine-protein phosphatase 22 | PTPN22 | Family | 43 | false | false | Tyrosine-protein phosphatase non-receptor type 22 (PTPN22) acts as negative regulator of T-cell receptor (TCR) signalling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signalling molecules [ ]. Variations of the PTPN22 gene aff... | [
"GO:0004725",
"GO:0050856"
] | [
"protein tyrosine phosphatase activity",
"regulation of T cell receptor signaling pathway"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000930"
] | [
"PTPN8_PTPN22"
] | [
43
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-202427",
"R-HSA-202430",
"R-MMU-202427",
"R-MMU-202430"
] | [
"REACTOME:R-HSA-202427",
"REACTOME:R-HSA-202430",
"REACTOME:R-MMU-202427",
"REACTOME:R-MMU-202430"
] | 4 | [] | 0 | [
"PUB00071118",
"PUB00071119"
] | [
"8890164",
"15273934"
] | [
"Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells.",
"Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE."
] | [
1996,
2004
] | 2 | [
"IPR047170"
] | [] | 1 | 0 | 1 | [
"Euarchontoglires"
] | [
43
] | 1 | [
"Homo sapiens",
"Mus musculus"
] | [
7,
1
] | 2 | true | Family | Non-receptor tyrosine-protein phosphatase 22 | Non-receptor tyrosine-protein phosphatase 22 | PTPN22 | 6 |
IPR016277 | 16,277 | Tyrosine-protein phosphatase 1 | Ptp1 | Family | 86 | false | false | In the budding yeast Saccharomyces cerevisiae three protein tyrosine phosphatases (Ptp1 to 3) have been identified to date. This entry represents Ptp1 [ ]. Like Ptp2 and Ptp3, Ptp1 plays a downregulatory role on MAPK pathways [ ]. | [
"GO:0004725",
"GO:0006470"
] | [
"protein tyrosine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000938"
] | [
"PTPN1_yeast"
] | [
86
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-SCE-5675221",
"R-SCE-6798695"
] | [
"REACTOME:R-SCE-5675221",
"REACTOME:R-SCE-6798695"
] | 2 | [] | 0 | [
"PUB00073575",
"PUB00074980"
] | [
"7559654",
"25736922"
] | [
"The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1.",
"Identification of putative negative regulators of yeast signaling through a screening for protein phosphatases acting on cell wall integrity and mating MAPK pathways."
] | [
1995,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomycotina"
] | [
86
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Tyrosine-protein phosphatase 1 | Tyrosine-protein phosphatase 1 | Ptp1 | 8 |
IPR016278 | 16,278 | Dual specificity protein phosphatase 12 | DUSP12 | Family | 2,527 | false | false | Human YVH1, also known as dual specificity phosphatase 12 (DUSP12), is a cell survival phosphatase that prevents both thermal and oxidative stress-induced cell death. Furthermore, it associates with multiple ribonucleoprotein particles and may affect a variety of fundamental cellular processes [ ]. The enzyme is known ... | [
"GO:0008138",
"GO:0006470"
] | [
"protein tyrosine/serine/threonine phosphatase activity",
"protein dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000941"
] | [
"DUSP12"
] | [
2527
] | 1 | [
"EC",
"EC"
] | [
"3.1.3.16",
"3.1.3.48"
] | [
"EC:3.1.3.16",
"EC:3.1.3.48"
] | 2 | [
"6n8m",
"6n8n",
"6n8o",
"6rzz",
"6s05"
] | 5 | [
"PUB00085007",
"PUB00085008",
"PUB00085099"
] | [
"27856639",
"19797079",
"18456458"
] | [
"The Atypical Dual Specificity Phosphatase hYVH1 Associates with Multiple Ribonucleoprotein Particles.",
"Yvh1 is required for a late maturation step in the 60S biogenesis pathway.",
"Molecular identification and functional characterization of a Drosophila dual-specificity phosphatase DMKP-4 which is involved i... | [
2017,
2009,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2527
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
4,
1,
1,
2,
3,
1,
1
] | 8 | true | Family | Dual specificity protein phosphatase 12 | Dual specificity protein phosphatase 12 | DUSP12 | 7 |
IPR016279 | 16,279 | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma | PLC-gamma | Family | 2,922 | false | false | Phospholipase C gamma (PLCg), also known as 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma, is a member of the family of phosphoinositide specific PLCs that convert phosphatidylinositol 4,5-bisphosphate into second messengers 1,2-diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), thereby init... | [
"GO:0004435",
"GO:0007165",
"GO:0009395"
] | [
"phosphatidylinositol-4,5-bisphosphate phospholipase C activity",
"signal transduction",
"phospholipid catabolic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PIRSF"
] | [
"PIRSF000952"
] | [
"PLC-gamma"
] | [
2922
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.4.11",
"PWY-6351",
"PWY-6367",
"PWY-7039",
"PWY-8052",
"R-CEL-1855204",
"R-HSA-114604",
"R-HSA-1169408",
"R-HSA-1236382",
"R-HSA-1251932",
"R-HSA-1489509",
"R-HSA-166016",
"R-HSA-167021",
"R-HSA-1855204",
"R-HSA-186763",
"R-HSA-201556",
"R-HSA-202433",
"R-HSA-2029485",
"R-HS... | [
"EC:3.1.4.11",
"METACYC:PWY-6351",
"METACYC:PWY-6367",
"METACYC:PWY-7039",
"METACYC:PWY-8052",
"REACTOME:R-CEL-1855204",
"REACTOME:R-HSA-114604",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-1236382",
"REACTOME:R-HSA-1251932",
"REACTOME:R-HSA-1489509",
"REACTOME:R-HSA-166016",
"REACTOME:R-HSA-1... | 96 | [
"6pbc",
"7t8t",
"7z3j",
"8jqg",
"8jqh",
"8jqi",
"8qju",
"8t7c",
"9qb7"
] | 9 | [
"PUB00068260",
"PUB00068261",
"PUB00082318"
] | [
"11602179",
"20807769",
"15194811"
] | [
"Regulation of phospholipase C gamma isoforms in haematopoietic cells: why one, not the other?",
"Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.",
"Inositol 1,4,5-trisphosphate signaling regulates rhythmic contractile activity of myoepithelial sheath cells in Caenorhabditis e... | [
2001,
2010,
2004
] | 3 | [
"IPR001192"
] | [] | 1 | 0 | 1 | [
"Metazoa"
] | [
2922
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
6,
2,
5,
5,
11
] | 6 | true | Family | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma | PLC-gamma | 7 |
IPR016280 | 16,280 | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta | PLC-beta | Family | 7,081 | false | false | This group represents phospholipase C-beta, also known as 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta. PLC-beta isoforms mediate the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) to propagate signals for several physiological responses [ , ].... | [
"GO:0004435",
"GO:0005509"
] | [
"phosphatidylinositol-4,5-bisphosphate phospholipase C activity",
"calcium ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF"
] | [
"PIRSF000956"
] | [
"PLC-beta"
] | [
7081
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"3.1.4.11",
"GenProp2096",
"GenProp2098",
"PWY-6351",
"PWY-6367",
"PWY-7039",
"PWY-8052",
"R-BTA-112043",
"R-BTA-1855204",
"R-BTA-399997",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418217",
"R-BTA-434316",
"R-BTA-500657",
"R-CEL-112043",
"R-CEL-1855204",
"R-CEL-416476",
"R-DME-1120... | [
"EC:3.1.4.11",
"GP:GenProp2096",
"GP:GenProp2098",
"METACYC:PWY-6351",
"METACYC:PWY-6367",
"METACYC:PWY-7039",
"METACYC:PWY-8052",
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418217",
"REACTO... | 48 | [
"4gnk",
"7sq2",
"8emv",
"8emw",
"8emx",
"8uqn",
"8uqo"
] | 7 | [
"PUB00068310",
"PUB00074069",
"PUB00074070"
] | [
"2457447",
"11118617",
"25193662"
] | [
"Isolation of a putative phospholipase C gene of Drosophila, norpA, and its role in phototransduction.",
"Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1).",
"Membrane-induced allosteric control of phospholipase C-β isozymes."
] | [
1988,
2000,
2014
] | 3 | [
"IPR001192"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
7081
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
23,
21,
4,
32,
14,
25
] | 6 | true | Family | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta | Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta | PLC-beta | 5 |
IPR016281 | 16,281 | Crossover junction endodeoxyribonuclease, RusA | Endonuclease_RusA | Family | 1,948 | false | false | This group represents a crossover junction endodeoxyribonuclease, RusA type. | [
"GO:0008821"
] | [
"crossover junction DNA endonuclease activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF001007"
] | [
"RusA"
] | [
1948
] | 1 | [
"EC"
] | [
"3.1.21.10"
] | [
"EC:3.1.21.10"
] | 1 | [
"1q8r",
"2h8c",
"2h8e"
] | 3 | [] | [] | [] | [] | 0 | [
"IPR008822"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Panagrolaimus superbus",
"Viruses",
"ecological metagenomes"
] | [
1851,
1,
89,
7
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Crossover junction endodeoxyribonuclease, RusA | Crossover junction endodeoxyribonuclease, RusA | Endonuclease_RusA | 2 |
IPR016282 | 16,282 | Glycoside hydrolase, family 5, endoglucanase B | Glyco_hydro_5_endoGlcnase_B | Family | 759 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0016798"
] | [
"hydrolase activity, acting on glycosyl bonds"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF001043"
] | [
"Endoglucanase_B"
] | [
759
] | 1 | [] | [] | [] | 0 | [
"4v2x",
"4yzp",
"4yzt",
"5e09",
"5e0c",
"5xrc"
] | 6 | [
"PUB00000503",
"PUB00001778",
"PUB00004870",
"PUB00004956",
"PUB00005266"
] | [
"1747104",
"2806912",
"7624375",
"1677466",
"8535779"
] | [
"A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Cellulase families revealed by hydrophobic cluster analysis.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Cellulase EGZ of Erwinia chrysanthemi: struct... | [
1991,
1989,
1995,
1991,
1995
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
472,
287
] | 2 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 5, endoglucanase B | Glycoside hydrolase, family 5, endoglucanase B | Glyco_hydro_5_endoGlcnase_B | 5 |
IPR016284 | 16,284 | Bacteriophage PRD1, P15, lysozyme | Phage_PRD1_P15_lysozyme | Family | 9 | false | false | This group represents one of the lytic enzymes of bacteriophage PRD1 (protein P15): muramidase (lysozyme). Host peptidoglycan is digested after permeabilization of the cytoplasmic membrane by holin, liberating progeny phages. Hydrolysis of the cell wall peptidoglycan occurs at the (1->4)-beta-linkages between N-acetylm... | [
"GO:0044659"
] | [
"viral release from host cell by cytolysis"
] | [
"biological_process"
] | 1 | [
"PIRSF"
] | [
"PIRSF001069"
] | [
"Lytic_enz_p15"
] | [
9
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00056033",
"PUB00056034"
] | [
"7925454",
"11741849"
] | [
"Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase activity.",
"The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane."
] | [
1994,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Alphatectivirus"
] | [
9
] | 1 | [] | [] | 0 | true | Family | Bacteriophage PRD1, P15, lysozyme | Bacteriophage PRD1, P15, lysozyme | Phage_PRD1_P15_lysozyme | 7 |
IPR016285 | 16,285 | Haemagglutinin-neuraminidase | Hemagglutn-neuramid | Family | 3,608 | false | false | This entry represents the haemagglutinin-neuraminidase (HN) glycoprotein found in a variety of paramyxoviruses (negative-stranded RNA viruses), including Mumps virus, Human parainfluenza virus 3, and the avian pathogen Newcastle disease virus. Some paramyxoviruses have two surface glycoproteins, HN and a fusion protein... | [
"GO:0004308",
"GO:0046789",
"GO:0019058",
"GO:0019031"
] | [
"exo-alpha-sialidase activity",
"host cell surface receptor binding",
"viral life cycle",
"viral envelope"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF",
"CDD"
] | [
"PIRSF001072",
"cd15469"
] | [
"Hemagglut-neuramid_paramyxoV",
"HN"
] | [
3122,
3516
] | 2 | [
"EC",
"REACTOME"
] | [
"3.2.1.18",
"R-HSA-198933"
] | [
"EC:3.2.1.18",
"REACTOME:R-HSA-198933"
] | 2 | [
"1e8t",
"1e8u",
"1e8v",
"1usr",
"1usx",
"1v2i",
"1v3b",
"1v3c",
"1v3d",
"1v3e",
"1z4v",
"1z4w",
"1z4x",
"1z4y",
"1z4z",
"1z50",
"3t1e",
"4fzh",
"4jf7",
"4mza",
"4mze",
"4wef",
"4xjq",
"4xjr",
"5b2c",
"5b2d",
"5kv8",
"5kv9",
"6c0m",
"6jjm",
"6jjn",
"6sg8"... | 43 | [
"PUB00031893",
"PUB00031976"
] | [
"15016893",
"14729348"
] | [
"Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion.",
"Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III."
] | [
2004,
2004
] | 2 | [
"IPR000665"
] | [] | 1 | 0 | 1 | [
"Paramyxoviridae"
] | [
3608
] | 1 | [] | [] | 0 | true | Family | Haemagglutinin-neuraminidase | Haemagglutinin-neuraminidase | Hemagglutn-neuramid | 9 |
IPR016286 | 16,286 | Alpha-L-fucosidase, metazoa-type | FUC_metazoa-typ | Family | 17,024 | false | false | O-Glycosyl hydrolases family 29 ( ) encompasses alpha-L-fucosidases ( ) [ ], which is a lysosomal enzyme responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-l... | [
"GO:0004560",
"GO:0006004"
] | [
"alpha-L-fucosidase activity",
"fucose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF001092",
"PR00741"
] | [
"Alpha-L-fucosidase",
"GLHYDRLASE29"
] | [
11546,
14915
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"3.2.1.51",
"PWY-6807",
"R-BTA-6798695",
"R-BTA-975578",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-CEL-975578",
"R-DDI-6798695",
"R-DDI-975578",
"R-DME-381426",
"R-DME-6798695",
"R-DME-8957275",
"R-DME-975578",
"R-HSA-381426",
"R-HSA-6798695",
"R-HSA-8957275",
"R-HSA-975... | [
"EC:3.2.1.51",
"METACYC:PWY-6807",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-975578",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CEL-975578",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-975578",
"REACTOME:R-DME-381426",
"REACTOME:R-DME-6798695",
"R... | 26 | [
"1hl8",
"1hl9",
"1odu",
"2wsp",
"2wvs",
"2wvt",
"2wvu",
"2wvv",
"2xib",
"2xii",
"2zwy",
"2zwz",
"2zx5",
"2zx6",
"2zx7",
"2zx8",
"2zx9",
"2zxa",
"2zxb",
"2zxd",
"4j27",
"4j28",
"4jfs",
"4jft",
"4jfu",
"4jfv",
"4jfw",
"4jl1",
"4jl2",
"4ni3",
"4pcs",
"4pct"... | 68 | [
"PUB00000482",
"PUB00021761",
"PUB00043486",
"PUB00043487"
] | [
"2482732",
"14715651",
"18556148",
"18522672"
] | [
"Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase.",
"Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis.",
"Expression study of an alpha-l-fucosidase gene in the Drosophilidae family.",
"Sta... | [
1989,
2004,
2008,
2008
] | 4 | [
"IPR000933"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
69,
11718,
5019,
5,
213
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
1,
3,
5,
7
] | 6 | true | Family | Alpha-L-fucosidase, metazoa-type | Alpha-L-fucosidase, metazoa-type | FUC_metazoa-typ | 5 |
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