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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR014711 | 14,711 | DNA topoisomerase I, catalytic core, alpha-helical subdomain, eukaryotic-type | TopoI_cat_a-hlx-sub_euk | Homologous_superfamily | 18,040 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [
"GO:0003677",
"GO:0003917",
"GO:0006265"
] | [
"DNA binding",
"DNA topoisomerase type I (single strand cut, ATP-independent) activity",
"DNA topological change"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.15.10"
] | [
""
] | [
18040
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.6.2.1",
"R-CEL-4615885",
"R-DDI-4615885",
"R-HSA-4615885",
"R-MMU-4615885",
"R-RNO-4615885",
"R-SCE-4615885",
"R-SPO-4615885"
] | [
"EC:5.6.2.1",
"REACTOME:R-CEL-4615885",
"REACTOME:R-DDI-4615885",
"REACTOME:R-HSA-4615885",
"REACTOME:R-MMU-4615885",
"REACTOME:R-RNO-4615885",
"REACTOME:R-SCE-4615885",
"REACTOME:R-SPO-4615885"
] | 8 | [
"1a31",
"1a35",
"1a36",
"1a41",
"1ej9",
"1k4s",
"1k4t",
"1lpq",
"1nh3",
"1r49",
"1rr8",
"1rrj",
"1sc7",
"1seu",
"1t8i",
"1tl8",
"2b9s",
"2f4q",
"2h7f",
"2h7g",
"3igc",
"3m4a",
"6z01",
"6z03"
] | 24 | [
"PUB00004398",
"PUB00005230",
"PUB00005437",
"PUB00006312",
"PUB00016842",
"PUB00020793",
"PUB00020794",
"PUB00081702",
"PUB00081703",
"PUB00081704",
"PUB00081705"
] | [
"1849260",
"9488644",
"7770916",
"7994576",
"11395412",
"12596227",
"12042765",
"21087076",
"20644584",
"17722649",
"17293019"
] | [
"Molecular cloning of a cDNA of a camptothecin-resistant human DNA topoisomerase I and identification of mutation sites.",
"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.",
"The mechanisms of DNA topoisomerases.",
"Crystal structure of the amino-terminal fragment o... | [
1991,
1998,
1995,
1994,
2001,
2003,
2002,
2010,
2010,
2007,
2007
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
99,
6884,
10769,
203,
85
] | 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... | [
15,
1,
7,
7,
12,
4,
2,
2,
10,
1,
1,
20
] | 12 | true | Homologous_superfamily | DNA topoisomerase I, catalytic core, alpha-helical subdomain, eukaryotic-type | DNA topoisomerase I, catalytic core, alpha-helical subdomain, eukaryotic-type | TopoI_cat_a-hlx-sub_euk | 4 |
IPR014712 | 14,712 | ANTH domain superfamily | ANTH_dom_sf | Homologous_superfamily | 19,391 | false | false | The AP180 N-terminal homology (ANTH) domain is a membrane binding domain found in endocytotic accessory proteins, such as AP180. The ANTH domain is involved in phosphatidylinositol 4,5-bisphosphate (also known as PIP2) binding and is also responsible for membrane localisation of AP180. The ANTH domain containing protei... | [
"GO:0005545",
"GO:0030276",
"GO:0048268",
"GO:0030136"
] | [
"1-phosphatidylinositol binding",
"clathrin binding",
"clathrin coat assembly",
"clathrin-coated vesicle"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.58.150"
] | [
""
] | [
19391
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-432722",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DME-432722",
"R-DME-8856825",
"R-DME-8856828",
"R-HSA-432722",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9696264",
"R-MMU-432722",
"R-MMU-8856825",
"R-MMU-8856828",
"R-MMU-9696264",
"R-RNO-432722",
"R-RNO-8856825",
"R-RNO-8856828",
... | [
"REACTOME:R-CEL-432722",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DME-432722",
"REACTOME:R-DME-8856825",
"REACTOME:R-DME-8856828",
"REACTOME:R-HSA-432722",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-9696264",
"REACTOME:R-MMU-432722",
"REACTOME:R-... | 18 | [
"1hf8",
"1hfa",
"1hg2",
"1hg5",
"1hx8",
"3zyk",
"3zyl",
"3zym",
"7jxv"
] | 9 | [
"PUB00014713",
"PUB00014714",
"PUB00018410"
] | [
"12740367",
"12742163",
"11161218"
] | [
"Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains.",
"ENTH/ANTH domains expand to the Golgi.",
"Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes."
] | [
2003,
2003,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Desulfovibrio gilichinskyi",
"Eukaryota"
] | [
1,
19390
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
60,
1,
134,
10,
12,
14,
1,
40,
24,
2,
1,
114
] | 12 | true | Homologous_superfamily | ANTH domain superfamily | ANTH domain superfamily | ANTH_dom_sf | 3 |
IPR014714 | 14,714 | Glutamate mutase E subunit, C-terminal domain superfamily | Glu_mut_E_C_dom_sf | Homologous_superfamily | 819 | false | false | Glutamate mutase (methylaspartate mutase) catalyses the reversible interconversion of L-glutamate and L-threo-3-methylaspartate, the first step in the pathway of glutamate fermentation [ ]. Catalysis is initiated using the cobalamin cofactor. The E subunit is the catalytic subunit (MutE) [ ]. This superfamily represent... | [
"GO:0016866",
"GO:0031419"
] | [
"intramolecular transferase activity",
"cobalamin binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.970.10"
] | [
""
] | [
819
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.4.99.1",
"PWY-5087",
"PWY-5103",
"PWY-6728"
] | [
"EC:5.4.99.1",
"METACYC:PWY-5087",
"METACYC:PWY-5103",
"METACYC:PWY-6728"
] | 4 | [
"1cb7",
"1ccw",
"1i9c",
"6h9e",
"6h9f"
] | 5 | [
"PUB00034444",
"PUB00034445"
] | [
"16285720",
"14738967"
] | [
"Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase.",
"The role of the conserved histidine-aspartate pair in the 'base-off' binding of cobalamins."
] | [
2005,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales",
"ecological metagenomes"
] | [
663,
139,
17
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Glutamate mutase E subunit, C-terminal domain superfamily | Glutamate mutase E subunit, C-terminal domain superfamily | Glu_mut_E_C_dom_sf | 4 |
IPR014716 | 14,716 | Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 | Fibrinogen_a/b/g_C_1 | Homologous_superfamily | 50,545 | false | false | Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation, the conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin, resulting in the polymerisation of fibrin, which forms a soft clot; this is then converted to a hard clot by factor XIIIA, which cro... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.215.10"
] | [
""
] | [
50545
] | 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-166662",
"R-BTA-166663",
"R-BTA-210993",
"R-BTA-2129379",
"R-BTA-2855086",
"R-BTA-5673001",
"R-BTA-6798695",
"R-BTA-8963889",
"R-BTA-9762292",
"R-CFA-210993",
"R-HSA-114608",
"R-HSA-1236974",
"R-HSA-140875",
"R-HSA-166058",
"R-HSA-166662",
"R-HSA-166663",
"R-HSA-1989781",
"R... | [
"REACTOME:R-BTA-166662",
"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-2855086",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8963889",
"REACTOME:R-BTA-9762292",
"REACTOME:R-CFA-210993",
"REACTOME:R-HSA-114608",
"REACTOME:R-H... | 89 | [
"1deq",
"1ei3",
"1fib",
"1fic",
"1fid",
"1fza",
"1fzb",
"1fzc",
"1fzd",
"1fze",
"1fzf",
"1fzg",
"1jc9",
"1lt9",
"1ltj",
"1lwu",
"1m1j",
"1n73",
"1n86",
"1n8e",
"1re3",
"1re4",
"1rf0",
"1rf1",
"1z3s",
"1z3u",
"2d39",
"2ffd",
"2fib",
"2gy7",
"2h43",
"2hlo"... | 121 | [
"PUB00016231",
"PUB00016232",
"PUB00016233",
"PUB00017188"
] | [
"12799374",
"11460466",
"11593005",
"15837518"
] | [
"Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen.",
"The structure and biological features of fibrinogen and fibrin.",
"Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution... | [
2003,
2001,
2001,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Nanohalococcus occultus",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
547,
1,
8,
49978,
11
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
201,
34,
92,
68,
97
] | 6 | true | Homologous_superfamily | Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 | Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 | Fibrinogen_a/b/g_C_1 | 9 |
IPR014717 | 14,717 | Translation elongation factor EF1B/small ribosomal subunit protein bS6 | Transl_elong_EF1B/ribsomal_bS6 | Homologous_superfamily | 50,702 | false | false | An α+β sandwich domain with a Ferredoxin-like fold can be found in the beta chain of the translation elongation factor EF1B [ ], and in the small ribosomal subunit protein bS6 (ribosomal protein S6) [ ]. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is require... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.70.60"
] | [
""
] | [
50702
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-156842",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-DDI-156842",
"R-DME-156842",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-156842",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-156842",
"R-MMU-5389840",
"R-MMU-5419276",
... | [
"REACTOME:R-BTA-156842",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-DDI-156842",
"REACTOME:R-DME-156842",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-156842",
"REACTOME:R-HSA-5368286",
"REACTOME:R-... | 21 | [
"1b64",
"1cqm",
"1cqn",
"1eg0",
"1f60",
"1fjg",
"1fka",
"1g1x",
"1g7c",
"1gh8",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1ije",
"1ijf",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1lou",
"1ml5",
"1n32",
"1n33",
"1n34"... | 1,333 | [
"PUB00011832",
"PUB00025100",
"PUB00033953"
] | [
"11106763",
"10753109",
"12762045"
] | [
"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.",
"Structure of the S15,S6,S18-rRNA complex: assembly of the 30S ribosome central domain.",
"Structural studies of eukaryotic elongation factors."
] | [
2000,
2000,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
886,
33307,
15751,
1,
757
] | 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",... | [
31,
3,
17,
5,
1,
18,
13,
2,
17,
22,
2,
2,
23
] | 13 | true | Homologous_superfamily | Translation elongation factor EF1B/small ribosomal subunit protein bS6 | Translation elongation factor EF1B/small ribosomal subunit protein bS6 | Transl_elong_EF1B/ribsomal_bS6 | 6 |
IPR014718 | 14,718 | Glycoside hydrolase-type carbohydrate-binding | GH-type_carb-bd | Homologous_superfamily | 142,753 | false | false | This superfamily represents a domain with a distorted supersandwich structure consisting of 18 strands in two sheets, which probably functions to bind carbohydrates in enzymes that act on sugars. Domains with this structure occur in several protein families, including galactose mutarotase ( ); domain 5 of beta-galactos... | [
"GO:0030246"
] | [
"carbohydrate binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.70.98.10"
] | [
""
] | [
142753
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-70370",
"R-HSA-70370",
"R-HSA-9931929",
"R-MMU-70370",
"R-RNO-70370",
"R-SCE-70370",
"R-SPO-70370",
"R-SSC-70370"
] | [
"REACTOME:R-BTA-70370",
"REACTOME:R-HSA-70370",
"REACTOME:R-HSA-9931929",
"REACTOME:R-MMU-70370",
"REACTOME:R-RNO-70370",
"REACTOME:R-SCE-70370",
"REACTOME:R-SPO-70370",
"REACTOME:R-SSC-70370"
] | 8 | [
"1c82",
"1cb8",
"1dp0",
"1egu",
"1f1s",
"1f4a",
"1f4h",
"1f9g",
"1hm2",
"1hm3",
"1hmu",
"1hmw",
"1hn0",
"1hn1",
"1i8q",
"1j0m",
"1j0n",
"1jov",
"1jyn",
"1jyv",
"1jyw",
"1jyx",
"1jz2",
"1jz3",
"1jz4",
"1jz5",
"1jz6",
"1jz7",
"1jz8",
"1k1w",
"1k1x",
"1k1y"... | 275 | [
"PUB00014072",
"PUB00014073"
] | [
"12829379",
"12501412"
] | [
"Purification and characterization of hyaluronic acid from the mollusc bivalve Mytilus galloprovincialis.",
"Glucoamylase from Thermoanaerobacterium thermosaccharolyticum: Sequence studies and analysis of the macromolecular architecture of the enzyme."
] | [
2003,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
694,
107950,
32831,
9,
1269
] | 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",... | [
120,
1,
2,
22,
10,
7,
4,
9,
69,
5,
4,
1,
131
] | 13 | true | Homologous_superfamily | Glycoside hydrolase-type carbohydrate-binding | Glycoside hydrolase-type carbohydrate-binding | GH-type_carb-bd | 7 |
IPR014719 | 14,719 | Ribosomal protein bL12, C-terminal/adaptor protein ClpS-like | Ribosomal_bL12_C/ClpS-like | Homologous_superfamily | 58,538 | false | false | This superfamily represents a domain found at the C terminus of ribosomal proteins bL12, and also in the adaptor protein ClpS, forming an α/β sandwich [ ]. The bL12 ribosomal proteins are part of the large 50S ribosomal subunit, and occur in four copies organised as two dimers. The bL12 dimer probably interacts with EF... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:3.30.1390.10",
"SSF54736"
] | [
"",
""
] | [
58061,
56896
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9837999",
"R-BTA-9937383",
"R-CEL-983168",
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"Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
... | [
1999,
2001,
2001,
2000,
2002,
2002
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
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"Eukaryota",
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4,
43833,
13740,
127,
834
] | 5 | [
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"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
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"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
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35,
2,
12,
4,
2,
8,
9,
1,
20,
12,
1,
1,
33
] | 13 | true | Homologous_superfamily | Ribosomal protein bL12, C-terminal/adaptor protein ClpS-like | Ribosomal protein bL12, C-terminal/adaptor protein ClpS-like | Ribosomal_bL12_C/ClpS-like | 7 |
IPR014720 | 14,720 | Double-stranded RNA-binding domain | dsRBD_dom | Domain | 82,195 | false | false | In contrast to other RNA-binding domains, the about 65 amino acids long dsRBD domain [ , , ] has been found in several proteins that specifically recognise double-stranded RNAs. The dsRBD domain is also known as DSRM (Double-Stranded RNA-binding Motif). dsRBD proteins are mainly involved in posttranscriptional gene reg... | [] | [] | [] | 0 | [
"PFAM",
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"PF00035",
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71350,
76187,
72805
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"2l33"... | 284 | [
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"Interactions between double-stranded RNA regulators and the protein kinase DAI.",
"Preferential selection of adenos... | [
1994,
1994,
1992,
1994,
1994,
1995,
1992
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"IPR033099",
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"IPR044446",
"IPR044449",
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139,
25324,
55333,
713,
686
] | 5 | [
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"Drosophila melanogaster",
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"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
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93,
12,
92,
89,
1,
134,
91,
4,
51,
95,
2,
2,
196
] | 13 | true | Domain | Double-stranded RNA-binding domain | Double-stranded RNA-binding domain | dsRBD_dom | 5 |
IPR014721 | 14,721 | Small ribosomal subunit protein uS5 domain 2-type fold, subgroup | Ribsml_uS5_D2-typ_fold_subgr | Homologous_superfamily | 488,570 | false | false | Domain 2 of the small ribosomal subunit protein uS5, previously known as ribosomal protein S5, has a left-handed β-α-β fold that is found in numerous RNA/DNA-binding proteins, as well as in kinases from the GHMP kinase family. Proteins containing this β-α-β fold domain include: Translational machinery components (ribos... | [] | [] | [] | 0 | [
"CATHGENE3D"
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"1ibk"... | 2,512 | [
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"XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators.",
"Structure and function of the N-terminal 40 kDa fragment of ... | [
2000,
2003,
2001,
1995,
2006,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
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"Eukaryota",
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"unclassified sequences"
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10669,
356068,
113863,
788,
7182
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"Arabidopsis thaliana",
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"Danio rerio",
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"Mus musculus",
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49,
57,
26,
14,
177,
104,
20,
118,
129,
21,
18,
320
] | 13 | true | Homologous_superfamily | Small ribosomal subunit protein uS5 domain 2-type fold, subgroup | Small ribosomal subunit protein uS5 domain 2-type fold, subgroup | Ribsml_uS5_D2-typ_fold_subgr | 1 |
IPR014722 | 14,722 | Large ribosomal subunit protein uL2, domain 2 | Rib_uL2_dom2 | Homologous_superfamily | 194,002 | false | false | This domain superfamily can be found in the large ribosomal subunit protein uL2, previously known as ribosomal protein L2, where it represents domain 2 and it is also found in other ribosomal proteins and in elongation factor P and translation initiation factor 5A, where it constitutes the N-terminal domain [ ]. | [] | [] | [] | 0 | [
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"15210970"
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"Crystal structure of elongation factor P from Thermus thermophilus HB8."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
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4865,
101229,
85691,
54,
2163
] | 5 | [
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"Mus musculus",
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108,
13,
48,
39,
5,
79,
50,
11,
82,
90,
16,
15,
394
] | 13 | true | Homologous_superfamily | Large ribosomal subunit protein uL2, domain 2 | Large ribosomal subunit protein uL2, domain 2 | Rib_uL2_dom2 | 4 |
IPR014724 | 14,724 | RNA polymerase Rpb2, OB-fold | RNA_pol_RPB2_OB-fold | Homologous_superfamily | 70,327 | false | false | RNA polymerases ( ) catalyse the DNA dependent polymerisation of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial and chloroplast polymerases). This entry describes a structural region consisting of an OB-fold β barrel that is found in RNA polymerase II Rpb2 ... | [
"GO:0003899"
] | [
"DNA-directed RNA polymerase activity"
] | [
"molecular_function"
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"CATHGENE3D"
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"G3DSA:2.40.50.150"
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"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-72086",... | 214 | [
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"Functional interaction between TFIIB and the Rpb2 subunit of RNA polymerase II: implications for the mechanism of transcription initiation."
] | [
2001,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
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1212,
29165,
38582,
452,
916
] | 5 | [
"Arabidopsis thaliana",
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"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",
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27,
3,
4,
4,
1,
16,
4,
3,
24,
8,
3,
3,
90
] | 13 | true | Homologous_superfamily | RNA polymerase Rpb2, OB-fold | RNA polymerase Rpb2, OB-fold | RNA_pol_RPB2_OB-fold | 3 |
IPR014726 | 14,726 | Large ribosomal subunit protein uL2, domain 3 | Ribosomal_uL2_dom3 | Homologous_superfamily | 52,013 | false | false | This superfamily represents domain 3 of the ribosomal protein uL2 from the large 50S subunit. The 50S subunit proteins function primarily to stabilise inter-domain interactions that are necessary to maintain the subunit's structural integrity, displaying a wide variety of protein-RNA interactions. This domain has an ir... | [] | [] | [] | 0 | [
"CATHGENE3D"
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] | [
"11297922",
"11290319",
"11114498",
"16285925"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction."
] | [
2001,
2001,
2000,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
932,
24169,
26493,
419
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
1,
1,
2,
1,
4,
3,
2,
8,
8,
3,
4,
22
] | 13 | true | Homologous_superfamily | Large ribosomal subunit protein uL2, domain 3 | Large ribosomal subunit protein uL2, domain 3 | Ribosomal_uL2_dom3 | 1 |
IPR014727 | 14,727 | DNA topoisomerase I, catalytic core, alpha/beta subdomain | TopoI_cat_a/b-sub_euk | Homologous_superfamily | 9,222 | false | false | DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single-or double-strand breaks, crossing the strands through one another, then resealing the breaks [ ]. These enzymes have several functions: to remove DNA supercoi... | [
"GO:0003677",
"GO:0003917",
"GO:0006265",
"GO:0005694"
] | [
"DNA binding",
"DNA topoisomerase type I (single strand cut, ATP-independent) activity",
"DNA topological change",
"chromosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.132.10"
] | [
""
] | [
9222
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.6.2.1",
"R-CEL-4615885",
"R-DDI-4615885",
"R-HSA-4615885",
"R-MMU-4615885",
"R-RNO-4615885",
"R-SCE-4615885",
"R-SPO-4615885"
] | [
"EC:5.6.2.1",
"REACTOME:R-CEL-4615885",
"REACTOME:R-DDI-4615885",
"REACTOME:R-HSA-4615885",
"REACTOME:R-MMU-4615885",
"REACTOME:R-RNO-4615885",
"REACTOME:R-SCE-4615885",
"REACTOME:R-SPO-4615885"
] | 8 | [
"1a31",
"1a35",
"1a36",
"1ej9",
"1k4s",
"1k4t",
"1lpq",
"1nh3",
"1r49",
"1rr8",
"1rrj",
"1sc7",
"1seu",
"1t8i",
"1tl8",
"2b9s",
"6z01",
"6z03"
] | 18 | [
"PUB00005230",
"PUB00005437",
"PUB00016842",
"PUB00020793",
"PUB00020794",
"PUB00081702",
"PUB00081703",
"PUB00081704",
"PUB00081705"
] | [
"9488644",
"7770916",
"11395412",
"12596227",
"12042765",
"21087076",
"20644584",
"17722649",
"17293019"
] | [
"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.",
"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",... | [
1998,
1995,
2001,
2003,
2002,
2010,
2010,
2007,
2007
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
98,
9072,
33,
19
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
18,
1,
7,
6,
14,
6,
2,
2,
9,
1,
1,
16
] | 12 | true | Homologous_superfamily | DNA topoisomerase I, catalytic core, alpha/beta subdomain | DNA topoisomerase I, catalytic core, alpha/beta subdomain | TopoI_cat_a/b-sub_euk | 6 |
IPR014729 | 14,729 | Rossmann-like alpha/beta/alpha sandwich fold | Rossmann-like_a/b/a_fold | Homologous_superfamily | 1,218,271 | false | false | This superfamily represents domains related by a common ancestor that have a Rossmann-like, 3-layer, α/β/α sandwich fold. Protein families in which the domain is found include: Nucleotidylyl transferases ( ) such as cytidylyltransferases [ ], adenylyltransferases [ ]. Class I aminoacyl-tRNA synthetases (catalytic domai... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.50.620"
] | [
""
] | [
1218271
] | 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-196807",
"R-BTA-5358493",
"R-BTA-70635",
"R-BTA-8963693",
"R-BTA-9856649",
"R-CEL-1483191",
"R-CEL-174362",
"R-CEL-196807",
"R-CEL-196843",
"R-CEL-611105",
"R-CEL-73817",
"R-CEL-9748787",
"R-DDI-1483213",
"R-DDI-196807",
"R-DDI-611105",
"R-DDI-73817",
"R-DDI-8963693",
"R-DDI... | [
"REACTOME:R-BTA-196807",
"REACTOME:R-BTA-5358493",
"REACTOME:R-BTA-70635",
"REACTOME:R-BTA-8963693",
"REACTOME:R-BTA-9856649",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-174362",
"REACTOME:R-CEL-196807",
"REACTOME:R-CEL-196843",
"REACTOME:R-CEL-611105",
"REACTOME:R-CEL-73817",
"REACTOME:R-CEL-9... | 113 | [
"1a8h",
"1b6t",
"1bs2",
"1coz",
"1ct9",
"1d2r",
"1dnp",
"1dto",
"1ee1",
"1efp",
"1efv",
"1ej2",
"1euq",
"1euy",
"1exd",
"1f4l",
"1f7u",
"1f7v",
"1f9a",
"1ffy",
"1fyd",
"1g59",
"1g8f",
"1g8g",
"1g8h",
"1gax",
"1gln",
"1gn8",
"1gpm",
"1gsg",
"1gtr",
"1gts"... | 1,948 | [
"PUB00003933",
"PUB00004879",
"PUB00005294",
"PUB00022325",
"PUB00025297",
"PUB00034486",
"PUB00034487",
"PUB00034488",
"PUB00034489",
"PUB00034490",
"PUB00034491"
] | [
"8548458",
"8962055",
"9261082",
"14684898",
"7701318",
"16344011",
"16460002",
"16387658",
"15894617",
"16952944",
"17101984"
] | [
"The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.",
"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.",
"Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nu... | [
1996,
1996,
1997,
2004,
1995,
2006,
2006,
2006,
2005,
2006,
2006
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
41438,
890662,
263162,
1828,
21181
] | 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",... | [
600,
69,
133,
75,
44,
296,
144,
45,
392,
194,
40,
40,
905
] | 13 | true | Homologous_superfamily | Rossmann-like alpha/beta/alpha sandwich fold | Rossmann-like alpha/beta/alpha sandwich fold | Rossmann-like_a/b/a_fold | 9 |
IPR014730 | 14,730 | Electron transfer flavoprotein, alpha/beta-subunit, N-terminal | ETF_a/b_N | Domain | 68,033 | false | false | This entry represents the N-terminal domain of both the alpha and beta subunits from Group I and Group II ETFs. Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into con... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01012",
"SM00893"
] | [
"ETF",
"ETF"
] | [
68012,
65106
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-611105",
"R-DDI-611105",
"R-HSA-611105",
"R-HSA-8876725",
"R-MMU-611105",
"R-MMU-8876725",
"R-RNO-611105",
"R-RNO-8876725",
"R-SCE-611105",
"R-SPO-611105",
"R-SSC-611105",
"R-SSC-8876725"
] | [
"REACTOME:R-CEL-611105",
"REACTOME:R-DDI-611105",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-8876725",
"REACTOME:R-MMU-611105",
"REACTOME:R-MMU-8876725",
"REACTOME:R-RNO-611105",
"REACTOME:R-RNO-8876725",
"REACTOME:R-SCE-611105",
"REACTOME:R-SPO-611105",
"REACTOME:R-SSC-611105",
"REACTOME:R-SSC-... | 12 | [
"1efp",
"1efv",
"1o94",
"1o95",
"1o96",
"1o97",
"1t9g",
"2a1t",
"2a1u",
"3clr",
"3cls",
"3clt",
"3clu",
"3fet",
"3ih5",
"4kpu",
"4l2i",
"5ol2",
"5ow0",
"6fah",
"7koe",
"7qh2"
] | 22 | [
"PUB00004879",
"PUB00004936",
"PUB00005086",
"PUB00024527",
"PUB00033231",
"PUB00033232"
] | [
"8962055",
"2326318",
"8525056",
"10026281",
"8599534",
"12567183"
] | [
"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.",
"Biosynthesis, molecular cloning and sequencing of electron transfer flavoprotein.",
"Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta.",
"Crystal structure... | [
1996,
1990,
1995,
1999,
1996,
2003
] | 6 | [] | [
"IPR033947",
"IPR033948"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1840,
55662,
9159,
1372
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
2,
2,
4,
6,
18,
8,
2,
2,
7,
2,
2,
25
] | 13 | true | Domain | Electron transfer flavoprotein, alpha/beta-subunit, N-terminal | Electron transfer flavoprotein, alpha/beta-subunit, N-terminal | ETF_a/b_N | 6 |
IPR014731 | 14,731 | Electron transfer flavoprotein, alpha subunit, C-terminal | ETF_asu_C | Domain | 35,492 | false | false | Electron transfer flavoproteins (ETFs) serve as specific electron acceptors for primary dehydrogenases, transferring the electrons to terminal respiratory systems. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00766"
] | [
"ETF_alpha"
] | [
35492
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00583",
"R-CEL-611105",
"R-DDI-611105",
"R-HSA-611105",
"R-MMU-611105",
"R-RNO-611105",
"R-SCE-611105",
"R-SPO-611105"
] | [
"PROSITEDOC:PDOC00583",
"REACTOME:R-CEL-611105",
"REACTOME:R-DDI-611105",
"REACTOME:R-HSA-611105",
"REACTOME:R-MMU-611105",
"REACTOME:R-RNO-611105",
"REACTOME:R-SCE-611105",
"REACTOME:R-SPO-611105"
] | 8 | [
"1efp",
"1efv",
"1o94",
"1o95",
"1o96",
"1o97",
"1t9g",
"2a1t",
"2a1u",
"3clr",
"3cls",
"3clt",
"3clu",
"4kpu",
"4l2i",
"5ol2",
"5ow0",
"6fah",
"7koe",
"7qh2"
] | 20 | [
"PUB00004879",
"PUB00004936",
"PUB00005086",
"PUB00024527",
"PUB00033231",
"PUB00033232"
] | [
"8962055",
"2326318",
"8525056",
"10026281",
"8599534",
"12567183"
] | [
"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.",
"Biosynthesis, molecular cloning and sequencing of electron transfer flavoprotein.",
"Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta.",
"Crystal structure... | [
1996,
1990,
1995,
1999,
1996,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
954,
28760,
5088,
690
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
2,
1,
1,
2,
3,
16,
1,
1,
1,
4,
1,
1,
15
] | 13 | true | Domain | Electron transfer flavoprotein, alpha subunit, C-terminal | Electron transfer flavoprotein, alpha subunit, C-terminal | ETF_asu_C | 6 |
IPR014732 | 14,732 | Orotidine 5'-phosphate decarboxylase | OMPdecase | Family | 20,069 | false | false | Orotidine 5'-phosphate decarboxylase (OMPdecase) ( ) [ , ] catalyses the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are mo... | [
"GO:0004590",
"GO:0044205"
] | [
"orotidine-5'-phosphate decarboxylase activity",
"'de novo' UMP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR32119",
"TIGR01740"
] | [
"",
"pyrF"
] | [
16479,
19171
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.23",
"GenProp0187",
"GenProp1318",
"GenProp1418",
"GenProp1427",
"GenProp1614",
"GenProp1635",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-HSA-500753",
"R-MMU-500753"
] | [
"EC:4.1.1.23",
"GP:GenProp0187",
"GP:GenProp1318",
"GP:GenProp1418",
"GP:GenProp1427",
"GP:GenProp1614",
"GP:GenProp1635",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-HSA-500753",
"REAC... | 15 | [
"1dbt",
"1dqw",
"1dqx",
"1dv7",
"1dvj",
"1eix",
"1jjk",
"1kly",
"1klz",
"1km0",
"1km1",
"1km2",
"1km3",
"1km4",
"1km5",
"1km6",
"1l2u",
"1lol",
"1loq",
"1lor",
"1los",
"1lp6",
"1vqt",
"1x1z",
"2cz5",
"2czd",
"2cze",
"2czf",
"2e6y",
"2eaw",
"2jgy",
"2p1f"... | 221 | [
"PUB00002768",
"PUB00003724",
"PUB00024159",
"PUB00024322"
] | [
"1730672",
"2835631",
"10681442",
"10681441"
] | [
"The orotidine-5'-monophosphate decarboxylase gene of Myxococcus xanthus. Comparison to the OMP decarboxylase gene family.",
"Sequence analysis of the DdPYR5-6 gene coding for UMP synthase in Dictyostelium discoideum and comparison with orotate phosphoribosyl transferases and OMP decarboxylases.",
"The crystal ... | [
1992,
1988,
2000,
2000
] | 4 | [] | [
"IPR047595",
"IPR047596"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
493,
14662,
4488,
3,
423
] | 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",... | [
4,
1,
1,
1,
1,
6,
3,
1,
4,
5,
1,
1,
12
] | 13 | true | Family | Orotidine 5'-phosphate decarboxylase | Orotidine 5'-phosphate decarboxylase | OMPdecase | 4 |
IPR014735 | 14,735 | Transposase, Tn5-like, N-terminal | Transposase_Tn5-like_N | Domain | 1,830 | false | false | This domain is found at the N-terminal of Tn5-type transposase proteins. Prokaryotic Tn5 transposase makes two types of DNA contacts (cis-contacts for DNA recognition and trans-contacts for catalysis) as well as protein-protein contacts [ ]. Tn5 transposase employs two cations at its active site during catalysis, which... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM"
] | [
"NF049926",
"PF14706"
] | [
"IS4_FS_Nterm",
"Tnp_DNA_bind"
] | [
1637,
1826
] | 2 | [] | [] | [] | 0 | [
"1mm8",
"1muh",
"1mus",
"3ecp",
"4dm0"
] | 5 | [
"PUB00027468",
"PUB00034644"
] | [
"11896402",
"15102449"
] | [
"Two-metal active site binding of a Tn5 transposase synaptic complex.",
"Structure/function insights into Tn5 transposition."
] | [
2002,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes",
"plasmids"
] | [
1753,
8,
30,
37,
2
] | 5 | [] | [] | 0 | true | Domain | Transposase, Tn5-like, N-terminal | Transposase, Tn5-like, N-terminal | Transposase_Tn5-like_N | 8 |
IPR014737 | 14,737 | Transposase, Tn5-like, C-terminal | Transposase_Tn5-like_C | Homologous_superfamily | 2,294 | false | false | This superfamily represents a domain found at the C-terminal of Tn5-type transposase proteins. Prokaryotic Tn5 transposase makes two types of DNA contacts (cis-contacts for DNA recognition and trans-contacts for catalysis) as well as protein-protein contacts [ ]. Tn5 transposase employs two cations at its active site d... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.740.10"
] | [
""
] | [
2294
] | 1 | [] | [] | [] | 0 | [
"1b7e",
"1mm8",
"1muh",
"1mus",
"3ecp",
"4dm0"
] | 6 | [
"PUB00027468",
"PUB00034644"
] | [
"11896402",
"15102449"
] | [
"Two-metal active site binding of a Tn5 transposase synaptic complex.",
"Structure/function insights into Tn5 transposition."
] | [
2002,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes",
"plasmids"
] | [
2204,
11,
37,
40,
2
] | 5 | [] | [] | 0 | true | Homologous_superfamily | Transposase, Tn5-like, C-terminal | Transposase, Tn5-like, C-terminal | Transposase_Tn5-like_C | 4 |
IPR014738 | 14,738 | Citrate transporter | Citrate_transporter | Family | 5,742 | false | false | This entry consists of known and predicted citrate transporters. It includes two characterised citrate/proton symporters, CitM and CitH, from Bacillus subtilis [ ]. Both of these proteins couple the uptake of citrate in complex with a divalent cation to the uptake of protons, but differ in their metal ion specificities... | [
"GO:0015137",
"GO:0015746"
] | [
"citrate transmembrane transporter activity",
"citrate transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00784"
] | [
"citMHS"
] | [
5742
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034651",
"PUB00060985",
"PUB00060986"
] | [
"11053381",
"15968054",
"17042778"
] | [
"Complementary metal ion specificity of the metal-citrate transporters CitM and CitH of Bacillus subtilis.",
"Transport and metabolism of citrate by Streptococcus mutans.",
"Functional characterization and Me ion specificity of a Ca-citrate transporter from Enterococcus faecalis."
] | [
2000,
2005,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
5714,
5,
13,
10
] | 4 | [] | [] | 0 | true | Family | Citrate transporter | Citrate transporter | Citrate_transporter | 8 |
IPR014739 | 14,739 | Channel forming colicin, N-terminal domain superfamily | Channel_colicin_N_sf | Homologous_superfamily | 304 | false | false | Colicins are plasmid-encoded polypeptide toxins produced by and active against Escherichia coli and closely related bacteria. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmi... | [
"GO:0140911",
"GO:0031640",
"GO:0050829",
"GO:0016020"
] | [
"pore-forming activity",
"killing of cells of another organism",
"defense response to Gram-negative bacterium",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"SSF"
] | [
"SSF58096"
] | [
""
] | [
304
] | 1 | [] | [] | [] | 0 | [
"1cii",
"2hdi"
] | 2 | [
"PUB00023962",
"PUB00030669",
"PUB00034705"
] | [
"9009197",
"14731273",
"15519318"
] | [
"Crystal structure of colicin Ia.",
"Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution.",
"On the role of lipid in colicin pore formation."
] | [
1997,
2004,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
298,
6
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Channel forming colicin, N-terminal domain superfamily | Channel forming colicin, N-terminal domain superfamily | Channel_colicin_N_sf | 3 |
IPR014740 | 14,740 | Channel forming colicin, central receptor recognition | Channel_colicin_cen | Domain | 230 | false | false | Colicins are plasmid-encoded polypeptide toxins produced by and active against Escherichia coli and closely related bacteria. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmi... | [
"GO:0031640",
"GO:0050829",
"GO:0016020"
] | [
"killing of cells of another organism",
"defense response to Gram-negative bacterium",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF11504"
] | [
"Colicin_Ia"
] | [
230
] | 1 | [] | [] | [] | 0 | [
"1cii",
"2hdi"
] | 2 | [
"PUB00030669",
"PUB00034705",
"PUB00041371"
] | [
"14731273",
"15519318",
"17464289"
] | [
"Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution.",
"On the role of lipid in colicin pore formation.",
"Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import."
] | [
2004,
2004,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
230
] | 1 | [] | [] | 0 | true | Domain | Channel forming colicin, central receptor recognition | Channel forming colicin, central receptor recognition | Channel_colicin_cen | 6 |
IPR014741 | 14,741 | Adaptor protein Cbl, EF hand-like | Adaptor_Cbl_EF_hand-like | Domain | 4,336 | false | false | Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface. The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains:... | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02761"
] | [
"Cbl_N2"
] | [
4336
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.27",
"PWY-7511",
"R-DDI-983168",
"R-HSA-1059683",
"R-HSA-1236382",
"R-HSA-1295596",
"R-HSA-1433559",
"R-HSA-182971",
"R-HSA-2173789",
"R-HSA-5637810",
"R-HSA-5654726",
"R-HSA-5654727",
"R-HSA-5654732",
"R-HSA-5654733",
"R-HSA-6807004",
"R-HSA-8849469",
"R-HSA-8856825",
"R-HS... | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-DDI-983168",
"REACTOME:R-HSA-1059683",
"REACTOME:R-HSA-1236382",
"REACTOME:R-HSA-1295596",
"REACTOME:R-HSA-1433559",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-2173789",
"REACTOME:R-HSA-5637810",
"REACTOME:R-HSA-5654726",
"REACTOME:R-HSA-5654727",
... | 42 | [
"1b47",
"1fbv",
"1yvh",
"2cbl",
"2y1m",
"2y1n",
"3bum",
"3bun",
"3buo",
"3buw",
"3bux",
"3ob1",
"3ob2",
"3op0",
"3pfv",
"3plf",
"3vgo",
"3vrn",
"3vro",
"3vrp",
"3vrq",
"3vrr",
"3zni",
"4a4b",
"4a4c",
"4gpl",
"5axi",
"5hkw",
"5hkx",
"5hky",
"5hkz",
"5hl0"... | 54 | [
"PUB00019259",
"PUB00055526"
] | [
"10078535",
"18840649"
] | [
"Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.",
"A Dictyostelium homologue of the metazoan Cbl proteins regulates STAT signalling."
] | [
1999,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Cas-NS-1 murine leukemia virus",
"Eukaryota",
"viral metagenome"
] | [
1,
4334,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
11,
3,
18,
10,
20
] | 6 | true | Domain | Adaptor protein Cbl, EF hand-like | Adaptor protein Cbl, EF hand-like | Adaptor_Cbl_EF_hand-like | 6 |
IPR014742 | 14,742 | Adaptor protein Cbl, SH2-like domain | Adaptor_Cbl_SH2-like | Domain | 4,334 | false | false | Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface. The N-terminal region of Cbl contains a Cbl-type phosphotyrosine-binding (Cbl-PTB) domain, which is composed of three evolutionarily conserved domains:... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF02762",
"cd09920"
] | [
"Cbl_N3",
"SH2_Cbl-b_TKB"
] | [
4334,
4102
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.27",
"PWY-7511",
"R-HSA-1059683",
"R-HSA-1236382",
"R-HSA-1295596",
"R-HSA-1433559",
"R-HSA-182971",
"R-HSA-2173789",
"R-HSA-5637810",
"R-HSA-5654726",
"R-HSA-5654727",
"R-HSA-5654732",
"R-HSA-5654733",
"R-HSA-6807004",
"R-HSA-8849469",
"R-HSA-8856825",
"R-HSA-8856828",
"R-H... | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-HSA-1059683",
"REACTOME:R-HSA-1236382",
"REACTOME:R-HSA-1295596",
"REACTOME:R-HSA-1433559",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-2173789",
"REACTOME:R-HSA-5637810",
"REACTOME:R-HSA-5654726",
"REACTOME:R-HSA-5654727",
"REACTOME:R-HSA-5654732",
... | 41 | [
"1b47",
"1fbv",
"1yvh",
"2cbl",
"2y1m",
"2y1n",
"3bum",
"3bun",
"3buo",
"3buw",
"3bux",
"3ob1",
"3ob2",
"3op0",
"3pfv",
"3plf",
"3vgo",
"3vrn",
"3vro",
"3vrp",
"3vrq",
"3vrr",
"3zni",
"4a4b",
"4a4c",
"4gpl",
"5axi",
"5hkw",
"5hkx",
"5hky",
"5hkz",
"5hl0"... | 54 | [
"PUB00019259",
"PUB00055526"
] | [
"10078535",
"18840649"
] | [
"Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.",
"A Dictyostelium homologue of the metazoan Cbl proteins regulates STAT signalling."
] | [
1999,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Cas-NS-1 murine leukemia virus",
"Opisthokonta"
] | [
1,
4333
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
11,
3,
19,
10,
20
] | 6 | true | Domain | Adaptor protein Cbl, SH2-like domain | Adaptor protein Cbl, SH2-like domain | Adaptor_Cbl_SH2-like | 5 |
IPR014743 | 14,743 | Chloride channel, core | Cl-channel_core | Homologous_superfamily | 64,432 | false | false | Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF81340"
] | [
""
] | [
64432
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2672351",
"R-CEL-2672351",
"R-CFA-2672351",
"R-DDI-2672351",
"R-DME-2672351",
"R-HSA-2672351",
"R-HSA-6802952",
"R-MMU-2672351",
"R-RNO-2672351",
"R-SCE-2672351",
"R-SPO-2672351",
"R-SSC-2672351"
] | [
"REACTOME:R-BTA-2672351",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CFA-2672351",
"REACTOME:R-DDI-2672351",
"REACTOME:R-DME-2672351",
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-6802952",
"REACTOME:R-MMU-2672351",
"REACTOME:R-RNO-2672351",
"REACTOME:R-SCE-2672351",
"REACTOME:R-SPO-2672351",
"REACTOM... | 12 | [
"1kpk",
"1kpl",
"1ots",
"1ott",
"1otu",
"2exw",
"2exy",
"2ez0",
"2fec",
"2fed",
"2fee",
"2h2p",
"2h2s",
"2hlf",
"2ht2",
"2ht3",
"2ht4",
"2htk",
"2htl",
"2r9h",
"3det",
"3ejy",
"3ejz",
"3nd0",
"3nmo",
"3org",
"3q17",
"4ene",
"4fg6",
"4kjp",
"4kjq",
"4kjw"... | 119 | [
"PUB00000734",
"PUB00001999",
"PUB00004085",
"PUB00004230",
"PUB00004913",
"PUB00155406"
] | [
"9046241",
"7581380",
"2174129",
"8559248",
"9207144",
"29845874"
] | [
"Chloride channels: an emerging molecular picture.",
"Myotonia levior is a chloride channel disorder.",
"Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.",
"A common molecular basis for three inherited kidney stone diseases.",
"Transmembrane topology... | [
1997,
1995,
1990,
1996,
1997,
2018
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sylvanvirus sp.",
"unclassified sequences"
] | [
440,
31229,
32315,
1,
447
] | 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",... | [
36,
27,
71,
7,
3,
62,
55,
4,
38,
54,
1,
2,
104
] | 13 | true | Homologous_superfamily | Chloride channel, core | Chloride channel, core | Cl-channel_core | 6 |
IPR014745 | 14,745 | MHC class II, alpha/beta chain, N-terminal | MHC_II_a/b_N | Homologous_superfamily | 62,117 | false | false | Major Histocompatibility Complex (MHC) glycoproteins are heterodimeric cell surface receptors that function to present antigen peptide fragments to T cells responsible for cell-mediated immune responses. MHC molecules can be subdivided into two groups on the basis of structure and function: class I molecules present in... | [
"GO:0006955",
"GO:0019882",
"GO:0016020",
"GO:0042613"
] | [
"immune response",
"antigen processing and presentation",
"membrane",
"MHC class II protein complex"
] | [
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:3.10.320.10"
] | [
""
] | [
62117
] | 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-HSA-202424",
"R-HSA-202427",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-2132295",
"R-HSA-389948",
"R-HSA-877300",
"R-MMU-202424",
"R-MMU-202427",
"R-MMU-202430",
"R-MMU-202433",
"R-MMU-2132295",
"R-MMU-389948",
"R-RNO-202424",
"R-RNO-202427",
"R-RNO-202430",
"R-RNO-202433",
"R-RNO-2... | [
"REACTOME:R-HSA-202424",
"REACTOME:R-HSA-202427",
"REACTOME:R-HSA-202430",
"REACTOME:R-HSA-202433",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-389948",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-202424",
"REACTOME:R-MMU-202427",
"REACTOME:R-MMU-202430",
"REACTOME:R-MMU-202433",
"REACTOME:R-MMU-21... | 25 | [
"1a6a",
"1aqd",
"1bx2",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1d9k",
"1dlh",
"1es0",
"1f3j",
"1fne",
"1fng",
"1fv1",
"1fyt",
"1h15",
"1hdm",
"1hqr",
"1hxy",
"1i3r",
"1iak",
"1iao",
"1iea",
"1ieb",
"1j8h",
"1jk8",
"1jl4",
"1jwm",
"1jws",
"1jwu",
"1k2d",
"1k8i"... | 277 | [
"PUB00015254",
"PUB00016273"
] | [
"7612235",
"15120183"
] | [
"The three-dimensional structure of peptide-MHC complexes.",
"Function and regulation of MHC class II molecules in T-lymphocytes: of mice and men."
] | [
1995,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria",
"bird metagenome"
] | [
4,
62112,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
27,
15521,
366,
123
] | 4 | true | Homologous_superfamily | MHC class II, alpha/beta chain, N-terminal | MHC class II, alpha/beta chain, N-terminal | MHC_II_a/b_N | 6 |
IPR014746 | 14,746 | Glutamine synthetase/guanido kinase, catalytic domain | Gln_synth/guanido_kin_cat_dom | Homologous_superfamily | 179,587 | false | false | The C-terminal catalytic domains of glutamine synthetase and the guanido kinase family (which includes creatine kinase and arginine kinase) share a common structural fold, namely a common core consisting of two β-α-β2-α repeats [ ]. Glutamine synthetase ( ) (GS) [ ] plays an essential role in the metabolism of nitrogen... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF55931"
] | [
""
] | [
179587
] | 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-210455",
"R-BTA-71288",
"R-BTA-8964539",
"R-BTA-9696264",
"R-CEL-174403",
"R-CEL-210455",
"R-CEL-8964539",
"R-CFA-71288",
"R-CFA-9696264",
"R-DME-174403",
"R-DME-210455",
"R-DME-8964539",
"R-GGA-71288",
"R-GGA-9696264",
"R-HSA-174403",
"R-HSA-210455",
"R-HSA-5578999",
"R-HSA... | [
"REACTOME:R-BTA-210455",
"REACTOME:R-BTA-71288",
"REACTOME:R-BTA-8964539",
"REACTOME:R-BTA-9696264",
"REACTOME:R-CEL-174403",
"REACTOME:R-CEL-210455",
"REACTOME:R-CEL-8964539",
"REACTOME:R-CFA-71288",
"REACTOME:R-CFA-9696264",
"REACTOME:R-DME-174403",
"REACTOME:R-DME-210455",
"REACTOME:R-DME-8... | 37 | [
"1bg0",
"1crk",
"1f1h",
"1f52",
"1fpy",
"1g0w",
"1hto",
"1htq",
"1i0e",
"1lgr",
"1m15",
"1p50",
"1p52",
"1qh4",
"1qk1",
"1r8g",
"1rl9",
"1sd0",
"1tt4",
"1u6r",
"1v4g",
"1va6",
"1vrp",
"1zq1",
"2bvc",
"2crk",
"2d32",
"2d33",
"2d3a",
"2d3b",
"2d3c",
"2d6f"... | 202 | [
"PUB00000040",
"PUB00000670",
"PUB00002616",
"PUB00002619",
"PUB00003408",
"PUB00003430",
"PUB00004813",
"PUB00006495",
"PUB00034749"
] | [
"3896131",
"7819288",
"2324092",
"2324105",
"2575672",
"7916055",
"8096645",
"9559050",
"9434900"
] | [
"The creatine-creatine phosphate energy shuttle.",
"Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues.",
"A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated str... | [
1985,
1995,
1990,
1990,
1989,
1994,
1993,
1998,
1997
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4248,
122849,
49865,
39,
2586
] | 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",... | [
44,
15,
48,
20,
5,
52,
22,
7,
16,
37,
3,
3,
117
] | 13 | true | Homologous_superfamily | Glutamine synthetase/guanido kinase, catalytic domain | Glutamine synthetase/guanido kinase, catalytic domain | Gln_synth/guanido_kin_cat_dom | 2 |
IPR014747 | 14,747 | Bacterial photosynthetic reaction centre, H-chain, C-terminal | Bac_photo_RC_H_C | Homologous_superfamily | 8,365 | false | false | This superfamily represents the barrel domain of the H subunit from the photosynthetic reaction centre (PRC). The H subunit has a single transmembrane helix and a large cytoplasmic domain [ , ]. The core of the cytoplasmic domain contains the PRC-barrel. The photosynthetic apparatus in non-oxygenic bacteria consists of... | [
"GO:0019684",
"GO:0030077"
] | [
"photosynthesis, light reaction",
"plasma membrane light-harvesting complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.90.50.10"
] | [
""
] | [
8365
] | 1 | [] | [] | [] | 0 | [
"1aig",
"1aij",
"1ds8",
"1dv3",
"1dv6",
"1dxr",
"1e14",
"1e6d",
"1eys",
"1f6n",
"1fnp",
"1fnq",
"1jgw",
"1jgx",
"1jgy",
"1jgz",
"1jh0",
"1k6l",
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"1kby",
"1l9b",
"1l9j",
"1m3x",
"1mps",
"1ogv",
"1pcr",
"1prc",
"1pss",
"1pst",
"1qov",
"1r2c",
"1rg5"... | 219 | [
"PUB00014111",
"PUB00014116",
"PUB00014117",
"PUB00015279",
"PUB00015395",
"PUB00034760",
"PUB00034761",
"PUB00034762",
"PUB00035523"
] | [
"11095707",
"11005826",
"10611277",
"2676514",
"12872158",
"15329728",
"16931113",
"8027023",
"17105193"
] | [
"Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.",
"Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described... | [
2000,
2000,
1999,
1989,
2003,
2004,
2006,
1994,
2006
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
6,
8330,
5,
24
] | 4 | [] | [] | 0 | true | Homologous_superfamily | Bacterial photosynthetic reaction centre, H-chain, C-terminal | Bacterial photosynthetic reaction centre, H-chain, C-terminal | Bac_photo_RC_H_C | 2 |
IPR014748 | 14,748 | Enoyl-CoA hydratase, C-terminal | Enoyl-CoA_hydra_C | Homologous_superfamily | 131,348 | false | false | This entry represents the C-terminal domain found in enoyl-CoA hydratase and related proteins. This domain has an α-helical structure, and may be involved in trimerisation. | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.12.10"
] | [
""
] | [
131348
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"R-DDI-9837999",
"R-HSA-390247",
"R-HSA-70895",
"R... | [
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"REACTOME:R-DDI-70895",
"REACTOME:R-DDI-77310",
"REACTOME:R-DDI-77346",
"REACTOME:R-DDI-77348",
"... | 45 | [
"1dci",
"1dub",
"1ef8",
"1ef9",
"1ey3",
"1hzd",
"1jxz",
"1mj3",
"1nzy",
"1q51",
"1q52",
"1rjm",
"1rjn",
"1uiy",
"1wz8",
"2dub",
"2ej5",
"2f6q",
"2fbm",
"2fw2",
"2gtr",
"2hw5",
"2iex",
"2pbp",
"2ppy",
"2qq3",
"2uzf",
"2vre",
"2vx2",
"2zqq",
"2zqr",
"3fdu"... | 145 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
2311,
103954,
22978,
1,
2104
] | 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",... | [
12,
9,
16,
6,
5,
25,
20,
3,
11,
41,
35
] | 11 | true | Homologous_superfamily | Enoyl-CoA hydratase, C-terminal | Enoyl-CoA hydratase, C-terminal | Enoyl-CoA_hydra_C | 7 |
IPR014751 | 14,751 | DNA repair protein XRCC4-like, C-terminal | XRCC4-like_C | Homologous_superfamily | 26,913 | false | false | XRCC4 is essential for non-homologous DNA end joining (NHDJ) in eukaryotes, which is required for double-strand break repair, and V(D)J recombination in immunoglobulin and T-cell receptor genes. XRCC4 forms a complex with DNA ligase IV, and acts as a regulatory element required for the stability and activity of the lig... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.20.5.370"
] | [
""
] | [
26913
] | 1 | [
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"REACTOM... | [
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"R-MMU-390522",
"R-MMU-445355",
"R-MMU-5693571",
"R-MMU-9013424",
... | [
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"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-390522",
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"REACTOME:R-HSA-5693571",
"REACTOME:R-HSA-9013424",
"REACTOME:R-HSA-9664422",
"REACTOME:R-HSA-9725370",
"REACTOME:R... | 23 | [
"1fu1",
"1ik9",
"1z56",
"3ii6",
"3jbh",
"3mud",
"3q4f",
"3rwr",
"3sr2",
"3w03",
"4xa4",
"5chx",
"5cj0",
"5cj4",
"5tby",
"5wj7",
"5wlz",
"6abo",
"6fsa",
"6so3",
"6xe9",
"6ysy",
"6z47",
"7jh7",
"7kog",
"7lsy",
"7lt3",
"7m3p",
"7mf3",
"7nfc",
"7nfe",
"8bh3"... | 51 | [
"PUB00002350",
"PUB00013254",
"PUB00013321",
"PUB00094302"
] | [
"1939027",
"11702069",
"11080143",
"11919279"
] | [
"The primary structure of skeletal muscle myosin heavy chain: I. Sequence of the amino-terminal 23 kDa fragment.",
"Crystal structure of an Xrcc4-DNA ligase IV complex.",
"Crystal structure of the Xrcc4 DNA repair protein and implications for end joining.",
"Evolutionary implications of three novel members of... | [
1991,
2001,
2000,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
2,
18,
26892,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
6,
71,
16,
46,
43,
1,
5,
67,
1,
4
] | 11 | true | Homologous_superfamily | DNA repair protein XRCC4-like, C-terminal | DNA repair protein XRCC4-like, C-terminal | XRCC4-like_C | 7 |
IPR014752 | 14,752 | Arrestin-like, C-terminal domain superfamily | Arrestin-like_C_sf | Homologous_superfamily | 54,508 | false | false | This superfamily represents the C-terminal domain of arrestin, and Vacuolar protein sorting protein 26 (VPS26), consisting of an immunoglobulin-like β-sandwich structure. Arrestins comprise a family of closely-related proteins. In addition to the inactivation of G protein-coupled receptors, arrestins have been implicat... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.640"
] | [
""
] | [
54508
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"REACTOME",
"REACTOM... | [
"R-BTA-2514859",
"R-BTA-3238698",
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"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-456926",
"REACTOME:R-BTA-5635838",
"REACTOME:R-BTA-5674135",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-... | 92 | [
"1ayr",
"1cf1",
"1g4m",
"1g4r",
"1jsy",
"1suj",
"1zsh",
"2fau",
"2r51",
"2wtr",
"3gc3",
"3gd1",
"3lh8",
"3lh9",
"3lha",
"3p2d",
"3ugu",
"3ugx",
"4gei",
"4gej",
"4gfx",
"4j2q",
"4jqi",
"4ll1",
"4ll4",
"4p2a",
"4r7v",
"4r7x",
"4zrg",
"4zwj",
"5cl2",
"5dgy"... | 121 | [
"PUB00000986",
"PUB00001029",
"PUB00001684",
"PUB00002739",
"PUB00004275",
"PUB00005126",
"PUB00007754"
] | [
"8452755",
"15335861",
"7720881",
"1517224",
"9495348",
"2158671",
"11102511"
] | [
"Arrestin-subtypes in insect antennae.",
"Arresting G-protein coupled receptor activity.",
"The arrestin superfamily: cone arrestins are a fourth family.",
"Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.",
"X-ray crystal structure of arrestin from bovine rod outer segments.",
"A... | [
1993,
1993,
1995,
1992,
1998,
1990,
2000
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Avipoxvirus",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
16,
4,
259,
54221,
8
] | 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... | [
19,
37,
41,
45,
48,
42,
9,
10,
64,
11,
11,
10
] | 12 | true | Homologous_superfamily | Arrestin-like, C-terminal domain superfamily | Arrestin-like, C-terminal domain superfamily | Arrestin-like_C_sf | 7 |
IPR014753 | 14,753 | Arrestin, N-terminal | Arrestin_N | Homologous_superfamily | 8,575 | false | false | G protein-coupled receptors are a large family of signalling molecules that respond to a wide variety of extracellular stimuli. The receptors relay the information encoded by the ligand through the activation of heterotrimeric G proteins and intracellular effector molecules. To ensure the appropriate regulation of the ... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.840"
] | [
""
] | [
8575
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"REACTOM... | [
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"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9839389",
"REACTOME:R-... | 72 | [
"1ayr",
"1cf1",
"1g4m",
"1g4r",
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"6pwc",
"6tko",
"6u1n",
"6up7",
"7f1w",
"7f1x",
"7jsm",
"7jtb"... | 92 | [
"PUB00000986",
"PUB00001029",
"PUB00001684",
"PUB00002739",
"PUB00004275",
"PUB00005126"
] | [
"8452755",
"15335861",
"7720881",
"1517224",
"9495348",
"2158671"
] | [
"Arrestin-subtypes in insect antennae.",
"Arresting G-protein coupled receptor activity.",
"The arrestin superfamily: cone arrestins are a fourth family.",
"Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.",
"X-ray crystal structure of arrestin from bovine rod outer segments.",
"A... | [
1993,
1993,
1995,
1992,
1998,
1990
] | 6 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
8575
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
17,
10,
16,
20,
23
] | 6 | true | Homologous_superfamily | Arrestin, N-terminal | Arrestin, N-terminal | Arrestin_N | 5 |
IPR014755 | 14,755 | Copper resistance protein CopC/internalin, immunoglobulin-like | Cu-Rt/internalin_Ig-like | Homologous_superfamily | 27,435 | false | false | This superfamily represents an immunoglobulin E-set-like β-barrel domain found in the following proteins: Copper-resistance proteins CopC and PcoC. CopC is a bacterial copper protein involved in copper homeostasis that binds 1 equivalent of copper (II). Its immunoglobulin-like fold is similar to that of the unrelated b... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.1220"
] | [
""
] | [
27435
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-8875360",
"R-HSA-8876493"
] | [
"REACTOME:R-HSA-8875360",
"REACTOME:R-HSA-8876493"
] | 2 | [
"1h6t",
"1h6u",
"1ix2",
"1lyq",
"1m42",
"1m9s",
"1nm4",
"1o6s",
"1o6t",
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"1ot4",
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"2c9p",
"2c9q",
"2c9r",
"2omt",
"2omu",
"2omv",
"2omw",
"2omx",
"2omy",
"2omz",
"2ra1",
"2uzx",
"2uzy",
"2wqu",
"2wqv",
"2wqw",
"2wqx",
"2y5q",
"2ya1",
"3bc9"... | 67 | [
"PUB00016543",
"PUB00022139",
"PUB00026166",
"PUB00091273"
] | [
"11575932",
"12377120",
"12459914",
"21565699"
] | [
"Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain.",
"Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis.",
"Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance pro... | [
2001,
2002,
2003,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
250,
26505,
89,
4,
587
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Copper resistance protein CopC/internalin, immunoglobulin-like | Copper resistance protein CopC/internalin, immunoglobulin-like | Cu-Rt/internalin_Ig-like | 8 |
IPR014756 | 14,756 | Immunoglobulin E-set | Ig_E-set | Homologous_superfamily | 462,802 | false | false | The immunoglobulin (Ig) like fold, which consists of a β-sandwich of seven or more strands in two sheets with a greek-key topology, is one of the most common protein modules found in animals. Many different unrelated proteins share an Ig-like fold, which is often involved in interactions, commonly with other Ig-like do... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF81296"
] | [
""
] | [
462802
] | 1 | [
"REACTOME",
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"REACTOME",
"REACTOM... | [
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"R-BTA-1632852",
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"R-BTA-350054",
"R-BTA-380972",
"R-BTA-418555",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-456926",
"R-BTA-5576886",
"R-BTA-5624958",
"R-BTA-5628897",
"R-BTA-5635838",
"R-BTA-5674135",
"R-BTA-5689880",
"R-BTA-6798695",
... | [
"REACTOME:R-BTA-1296041",
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"REACTOME:R-BTA-350054",
"REACTOME:R-BTA-380972",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-456926",
"REACTOME:R-BTA-5576886",
"REACTOME:R-BT... | 608 | [
"1a02",
"1a3q",
"1a47",
"1a9v",
"1ahk",
"1ahm",
"1ajw",
"1ayr",
"1bf2",
"1bfs",
"1bft",
"1bvz",
"1c7s",
"1c7t",
"1cc0",
"1cdg",
"1cf1",
"1cgt",
"1cgu",
"1cgv",
"1cgw",
"1cgx",
"1cgy",
"1ciu",
"1clc",
"1ctn",
"1cvr",
"1cxe",
"1cxf",
"1cxh",
"1cxi",
"1cxk"... | 1,698 | [
"PUB00003330",
"PUB00029122",
"PUB00035293",
"PUB00035294",
"PUB00035295",
"PUB00035296",
"PUB00035297",
"PUB00035298",
"PUB00035299"
] | [
"7932691",
"12651950",
"15380510",
"14671122",
"15513926",
"15290350",
"15516996",
"15102497",
"14756796"
] | [
"The immunoglobulin fold. Structural classification, sequence patterns and common core.",
"A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.",
"Nuclear factor-kappaB: the enemy within.",
"Structural and functional analysis of human cytomeg... | [
1994,
2003,
2004,
2004,
2005,
2004,
2004,
2004,
2004
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
946,
158607,
262805,
38573,
1871
] | 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",... | [
244,
131,
659,
208,
8,
442,
361,
19,
141,
460,
17,
14,
421
] | 13 | true | Homologous_superfamily | Immunoglobulin E-set | Immunoglobulin E-set | Ig_E-set | 7 |
IPR014757 | 14,757 | Transcription regulator IclR, C-terminal | Tscrpt_reg_IclR_C | Domain | 107,333 | false | false | Many bacterial transcription regulation proteins which bind DNA through a 'helix-turn-helix' motif can be classified into subfamilies on the basis of sequence similarities. One of these subfamilies, called 'iclR', groups several proteins including: gylR, a possible activator protein for the gylABX glycerol operon in St... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF01614",
"PS51078"
] | [
"IclR_C",
"ICLR_ED"
] | [
104678,
106931
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00807"
] | [
"PROSITEDOC:PDOC00807"
] | 1 | [
"1mkm",
"1td5",
"1tf1",
"1ysp",
"1ysq",
"2g7u",
"2ia2",
"2o0y",
"2o99",
"2o9a",
"2xrn",
"2xro",
"3bjn",
"3d3o",
"3mq0",
"3obf",
"3r4k",
"5h1a",
"5hpf",
"5hpi",
"5tjj",
"5w1e",
"5whm",
"5y6i",
"7cuo",
"7dqb",
"8eju",
"8ejv",
"9e6a"
] | 29 | [
"PUB00003813",
"PUB00099685"
] | [
"1840643",
"34424339"
] | [
"Characterization of kdgR, a gene of Erwinia chrysanthemi that regulates pectin degradation.",
"A catalogue of signal molecules that interact with sensor kinases, chemoreceptors and transcriptional regulators."
] | [
1991,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Myoviridae sp. ctUX613",
"Sym plasmid",
"unclassified sequences"
] | [
103836,
77,
2681,
1,
1,
737
] | 6 | [
"Escherichia coli (strain K12)"
] | [
8
] | 1 | true | Domain | Transcription regulator IclR, C-terminal | Transcription regulator IclR, C-terminal | Tscrpt_reg_IclR_C | 5 |
IPR014759 | 14,759 | Helicase, superfamily 3, single-stranded RNA virus | Helicase_SF3_ssRNA_vir | Domain | 15,824 | false | false | Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A (phosphate-binding loop or P-loop) and Walker B (Mg2+-binding aspartic acid) motifs. Superfamily 3 consists of helicases encoded mainly by small DNA viruses and some larg... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51218"
] | [
"SF3_HELICASE_2"
] | [
15824
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"2.7.7.48",
"3.4.22",
"3.4.22.28",
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"PDOC51206"
] | [
"EC:2.7.7.48",
"EC:3.4.22",
"EC:3.4.22.28",
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"PROSITEDOC:PDOC51206"
] | 10 | [
"5gq1",
"5grb",
"5z3q",
"6s3a",
"6t3w",
"7e6v",
"7xt3",
"8x3v",
"9r34"
] | 9 | [
"PUB00014778",
"PUB00027539",
"PUB00033628",
"PUB00033629",
"PUB00033630"
] | [
"15037234",
"12774115",
"11689653",
"2156730",
"15718137"
] | [
"Evolutionary history and higher order classification of AAA+ ATPases.",
"Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen.",
"Common origin of four diverse families of large eukaryotic DNA viruses.",
"A new superfamily of putative NTP-binding domains encoded by genomes of sm... | [
2004,
2003,
2001,
1990,
2005
] | 5 | [
"IPR000605"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Luteibacter sahnii",
"Viruses",
"organismal metagenomes"
] | [
66,
1,
15755,
2
] | 4 | [] | [] | 0 | true | Domain | Helicase, superfamily 3, single-stranded RNA virus | Helicase, superfamily 3, single-stranded RNA virus | Helicase_SF3_ssRNA_vir | 9 |
IPR014760 | 14,760 | Serum albumin, N-terminal | Serum_albumin_N | Domain | 2,969 | false | false | A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [ , , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs - its main function ... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00273",
"PS51438",
"SM00103",
"cd00015"
] | [
"Serum_albumin",
"ALBUMIN_2",
"ALBUMIN",
"ALBUMIN"
] | [
2919,
2966,
2888,
2470
] | 4 | [
"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-381426",
"R-BTA-8957275",
"R-HSA-114608",
"R-HSA-159418",
"R-HSA-189451",
"R-HSA-189483",
"R-HSA-196791",
"R-HSA-2168880",
"R-HSA-381426",
"R-HSA-8957275",
"R-HSA-8964058",
"R-HSA-9707564",
"R-HSA-9749641",
"R-HSA-9757110",
"R-HSA-9793528",
"R-MMU-114608",
"R-MMU-159418",
"R... | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-159418",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-2168880",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8964058",
"REACTOME:R-HSA... | 43 | [
"1ao6",
"1bj5",
"1bke",
"1bm0",
"1e78",
"1e7a",
"1e7b",
"1e7c",
"1e7e",
"1e7f",
"1e7g",
"1e7h",
"1e7i",
"1gni",
"1gnj",
"1h9z",
"1ha2",
"1hk1",
"1hk2",
"1hk3",
"1hk4",
"1hk5",
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9",
"1n5u",
"1o9x",
"1tf0",
"1uor"... | 243 | [
"PUB00000582",
"PUB00002857",
"PUB00003407",
"PUB00004128"
] | [
"2423133",
"7517938",
"2481749",
"1630489"
] | [
"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.",
"Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.",
"Amphibian albumins as memb... | [
1986,
1994,
1989,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
8,
2959,
2
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
24,
13,
28
] | 4 | true | Domain | Serum albumin, N-terminal | Serum albumin, N-terminal | Serum_albumin_N | 9 |
IPR014762 | 14,762 | DNA mismatch repair, conserved site | DNA_mismatch_repair_CS | Conserved_site | 34,609 | false | false | Mismatch repair contributes to the overall fidelity of DNA replication [ ]. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The sequence of some proteins involved in mismatch repair in different organisms have been found to be evolutio... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00058"
] | [
"DNA_MISMATCH_REPAIR_1"
] | [
34609
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00057",
"R-DDI-5358565",
"R-GGA-5358565",
"R-HSA-199220",
"R-HSA-5358565",
"R-HSA-5358606",
"R-HSA-5545483",
"R-HSA-5632987",
"R-HSA-6796648",
"R-HSA-912446",
"R-MMU-199220",
"R-MMU-5358565",
"R-RNO-199220",
"R-RNO-5358565",
"R-SCE-5358565",
"R-SPO-5358565"
] | [
"PROSITEDOC:PDOC00057",
"REACTOME:R-DDI-5358565",
"REACTOME:R-GGA-5358565",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-5358565",
"REACTOME:R-HSA-5358606",
"REACTOME:R-HSA-5545483",
"REACTOME:R-HSA-5632987",
"REACTOME:R-HSA-6796648",
"REACTOME:R-HSA-912446",
"REACTOME:R-MMU-199220",
"REACTOME:R-M... | 16 | [
"1b62",
"1b63",
"1bkn",
"1ea6",
"1h7s",
"1h7u",
"1nhh",
"1nhi",
"1nhj",
"3h4l",
"4p7a",
"5akb",
"5akc",
"5akd",
"5x9y",
"6lzi",
"6lzj",
"6lzk",
"6mfq",
"7aib",
"7aic",
"7p8v",
"7rcb",
"7rci",
"7rck"
] | 25 | [
"PUB00000050",
"PUB00002089",
"PUB00002090",
"PUB00003695",
"PUB00004174"
] | [
"3304141",
"2676972",
"2676973",
"8264608",
"8145827"
] | [
"DNA mismatch correction.",
"Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae.",
"Nucleotide sequence of the Streptococcus pneumoniae hexB mismatch repair gene: homolog... | [
1987,
1989,
1989,
1994,
1994
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
631,
19570,
14138,
270
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
22,
2,
12,
6,
1,
57,
16,
2,
5,
25,
3,
2,
11
] | 13 | true | Conserved_site | DNA mismatch repair, conserved site | DNA mismatch repair, conserved site | DNA_mismatch_repair_CS | 3 |
IPR014764 | 14,764 | Defective-in-cullin neddylation protein | DCN-prot | Family | 13,440 | false | false | The eukaryotic defective in cullin neddylation (DCN) protein family, contributes to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. These multi-protein complexes are required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [ , , ]. Proteins in the D... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR12281"
] | [
""
] | [
13440
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8951664",
"R-CEL-8951664",
"R-DDI-8951664",
"R-DME-8951664",
"R-DRE-8951664",
"R-GGA-8951664",
"R-HSA-8951664",
"R-MMU-8951664",
"R-RNO-8951664",
"R-XTR-8951664"
] | [
"REACTOME:R-BTA-8951664",
"REACTOME:R-CEL-8951664",
"REACTOME:R-DDI-8951664",
"REACTOME:R-DME-8951664",
"REACTOME:R-DRE-8951664",
"REACTOME:R-GGA-8951664",
"REACTOME:R-HSA-8951664",
"REACTOME:R-MMU-8951664",
"REACTOME:R-RNO-8951664",
"REACTOME:R-XTR-8951664"
] | 10 | [
"2is9",
"3bq3",
"3kev",
"3o2p",
"3o6b",
"3tdi",
"3tdu",
"3tdz",
"4gao",
"4gba",
"4p5o",
"5ufi",
"5v83",
"5v86",
"5v88",
"5v89",
"6b5q",
"6bg3",
"6bg5",
"6p5v",
"6p5w",
"6xol",
"6xom",
"6xon",
"6xoo",
"6xop",
"6xoq",
"7kwa",
"8or2",
"8or3"
] | 30 | [
"PUB00021043",
"PUB00050725",
"PUB00064019",
"PUB00097937",
"PUB00097939"
] | [
"15988528",
"18206966",
"23201271",
"26906416",
"17905859"
] | [
"The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae.",
"Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.",
"Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzyme... | [
2005,
2008,
2013,
2016,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
13440
] | 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... | [
14,
1,
22,
8,
20,
24,
1,
10,
32,
1,
1,
72
] | 12 | true | Family | Defective-in-cullin neddylation protein | Defective-in-cullin neddylation protein | DCN-prot | 1 |
IPR014767 | 14,767 | Diaphanous autoregulatory domain | DAD_dom | Domain | 16,016 | false | false | Formins participate in the assembly of the actin and microtubule cytoskeletons in processes like cell division, migration, and development. Diaphanous-related formins (DRF) contain an N-terminal GTPase-binding domain (GBD) and a C-terminal diaphanous autoregulatory domain (DAD). DRFs are regulated by an autoinhibitory ... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51231"
] | [
"DAD"
] | [
16016
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51231",
"R-DME-5663220",
"R-DME-6785631",
"R-DME-6798695",
"R-DME-8980692",
"R-DME-9013026",
"R-DME-9013149",
"R-DME-9013404",
"R-DME-9013405",
"R-DME-9013406",
"R-DME-9013408",
"R-DME-9013423",
"R-DME-9035034",
"R-DRE-8980692",
"R-HSA-4086400",
"R-HSA-5663220",
"R-HSA-6785631",... | [
"PROSITEDOC:PDOC51231",
"REACTOME:R-DME-5663220",
"REACTOME:R-DME-6785631",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-8980692",
"REACTOME:R-DME-9013026",
"REACTOME:R-DME-9013149",
"REACTOME:R-DME-9013404",
"REACTOME:R-DME-9013405",
"REACTOME:R-DME-9013406",
"REACTOME:R-DME-9013408",
"REACTOME:... | 56 | [
"2bap",
"2f31",
"2j1d",
"3o4x",
"3obv",
"8fg1",
"8ru2"
] | 7 | [
"PUB00017189",
"PUB00019441",
"PUB00035340",
"PUB00035527",
"PUB00035528",
"PUB00035529"
] | [
"15950879",
"11035012",
"15740615",
"16292343",
"16472745",
"16361707"
] | [
"Formin proteins: a domain-based approach.",
"Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain.",
"A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa.",
"The regulation of mDia... | [
2005,
2001,
2005,
2005,
2006,
2006
] | 6 | [] | [
"IPR010465"
] | 0 | 1 | 0 | [
"Bacteria",
"Cyprinid herpesvirus 1",
"Eukaryota",
"Halobaculum saliterrae",
"ecological metagenomes"
] | [
141,
1,
15869,
1,
4
] | 5 | [
"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)"
] | [
109,
20,
31,
29,
1,
1,
39,
2
] | 8 | true | Domain | Diaphanous autoregulatory domain | Diaphanous autoregulatory domain | DAD_dom | 7 |
IPR014768 | 14,768 | Rho GTPase-binding/formin homology 3 (GBD/FH3) domain | GBD/FH3_dom | Domain | 25,824 | false | false | Formins are multidomain proteins conserved from plants to fungi and vertebrates. Due to their pivotal role in the organisation of the actin cytoskeleton formins are involved in processes as diverse as formation of filopodia, microspikes and lamellipodia, establishment and maintenance of cell polarity, vesicular traffic... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51232"
] | [
"GBD_FH3"
] | [
25824
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51232",
"R-BTA-5663220",
"R-BTA-9013106",
"R-DDI-193648",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DME-5663220",
"R-DME-6785631",
"R-DME-6798695",
"R-DME-8980692",
"R-DME-9013026",
"R-DME-9013149",
"R-DME-9013404",
"R-DME-9013405",
"R-DME-9013406",
"R-DME-9013408",
"R-DME-9013423",
... | [
"PROSITEDOC:PDOC51232",
"REACTOME:R-BTA-5663220",
"REACTOME:R-BTA-9013106",
"REACTOME:R-DDI-193648",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013149",
"REACTOME:R-DME-5663220",
"REACTOME:R-DME-6785631",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-8980692",
"REACTOME:R-DME-9013026",
"REACTOME:R... | 61 | [
"1z2c",
"2bap",
"2bnx",
"2f31",
"3dad",
"3eg5",
"3o4x",
"3obv",
"4dvg",
"4uwx",
"4yc7",
"4ydh",
"6xf1",
"6xf2",
"8fg1",
"9azp"
] | 16 | [
"PUB00014914",
"PUB00035340",
"PUB00035341"
] | [
"9606213",
"15740615",
"15864301"
] | [
"FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation.",
"A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa.",
"Structural and mechanistic insights into the interaction betw... | [
1998,
2005,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
25824
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
15,
133,
28,
57,
34,
1,
57,
2,
3
] | 9 | true | Domain | Rho GTPase-binding/formin homology 3 (GBD/FH3) domain | Rho GTPase-binding/formin homology 3 (GBD/FH3) domain | GBD/FH3_dom | 4 |
IPR014770 | 14,770 | Munc13 homology 1 | Munc13_1 | Domain | 23,333 | false | false | This entry represents the Munc13 homology domain 1. Munc13 proteins constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans Unc-13. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51258"
] | [
"MHD1"
] | [
23333
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51258",
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-210500",
"R-CEL-212676",
"R-CEL-264642",
"R-HSA-181429",
"R-HSA-181430",
"R-HSA-210500",
"R-HSA-212676",
"R-HSA-264642",
"R-HSA-6798695",
"R-MMU-181429",
"R-MMU-181430",
"R-MMU-210500",
"R-MMU-212676",
"R-MMU-264642",
"R-MMU-67986... | [
"PROSITEDOC:PDOC51258",
"REACTOME:R-CEL-181429",
"REACTOME:R-CEL-181430",
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-264642",
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-181430",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-212676",
"REACTOME:R-HSA-264642",
"REACTOME:R-HSA-6798... | 24 | [
"3swh",
"4y21",
"5ue8",
"5uf7",
"6a30",
"6a68",
"7t7c",
"7t7r",
"7t7v",
"7t7x",
"7t81",
"9la9"
] | 12 | [
"PUB00035349",
"PUB00035350"
] | [
"10861235",
"16228007"
] | [
"Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform.",
"A minimal domain responsible for Munc13 activity."
] | [
2000,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
23333
] | 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... | [
38,
25,
140,
14,
45,
27,
1,
22,
53,
1,
2,
50
] | 12 | true | Domain | Munc13 homology 1 | Munc13 homology 1 | Munc13_1 | 7 |
IPR014771 | 14,771 | Apoptosis, Bim N-terminal | Apoptosis_Bim_N | Domain | 864 | false | false | Apoptosis, or programmed cell death (PCD), is a common and evolutionarily conserved property of all metazoans [ ]. In many biological processes, apoptosis is required to eliminate supernumerary or dangerous (such as pre-cancerous) cells and to promote normal development. Dysregulation of apoptosis can, therefore, contr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06773"
] | [
"Bim_N"
] | [
864
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-111446",
"R-HSA-111453",
"R-HSA-193648",
"R-HSA-6802952",
"R-HSA-8862803",
"R-HSA-8952158",
"R-HSA-9607240",
"R-HSA-9614657",
"R-MMU-111446",
"R-MMU-111453",
"R-MMU-193648",
"R-RNO-111446",
"R-RNO-111453",
"R-RNO-193648"
] | [
"REACTOME:R-HSA-111446",
"REACTOME:R-HSA-111453",
"REACTOME:R-HSA-193648",
"REACTOME:R-HSA-6802952",
"REACTOME:R-HSA-8862803",
"REACTOME:R-HSA-8952158",
"REACTOME:R-HSA-9607240",
"REACTOME:R-HSA-9614657",
"REACTOME:R-MMU-111446",
"REACTOME:R-MMU-111453",
"REACTOME:R-MMU-193648",
"REACTOME:R-RN... | 14 | [] | 0 | [
"PUB00017281",
"PUB00017291",
"PUB00017301"
] | [
"11341280",
"9735050",
"12631689"
] | [
"Apoptosis. Death of a monopoly?",
"The Bcl-2 protein family: arbiters of cell survival.",
"Cellular distribution of Bcl-2 family proteins."
] | [
2001,
1998,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Tetrapoda"
] | [
864
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
11
] | 3 | true | Domain | Apoptosis, Bim N-terminal | Apoptosis, Bim N-terminal | Apoptosis_Bim_N | 9 |
IPR014772 | 14,772 | Mammalian uncoordinated homology 13, domain 2 | Munc13_dom-2 | Domain | 16,563 | false | false | This entry represents the Munc13 homology domain 2. Munc13 proteins constitute a family of three highly homologous molecules (Munc13-1, Munc13-2 and Munc13-3) with homology to Caenorhabditis elegans Unc-13. Munc13 proteins contain a phorbol ester-binding C1 domain and two C2 domains, which are Ca2+/phospholipid binding... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51259"
] | [
"MHD2"
] | [
16563
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51258",
"R-CEL-181429",
"R-CEL-181430",
"R-CEL-210500",
"R-CEL-212676",
"R-CEL-264642",
"R-HSA-181429",
"R-HSA-181430",
"R-HSA-210500",
"R-HSA-212676",
"R-HSA-264642",
"R-HSA-6798695",
"R-MMU-181429",
"R-MMU-181430",
"R-MMU-210500",
"R-MMU-212676",
"R-MMU-264642",
"R-MMU-67986... | [
"PROSITEDOC:PDOC51258",
"REACTOME:R-CEL-181429",
"REACTOME:R-CEL-181430",
"REACTOME:R-CEL-210500",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-264642",
"REACTOME:R-HSA-181429",
"REACTOME:R-HSA-181430",
"REACTOME:R-HSA-210500",
"REACTOME:R-HSA-212676",
"REACTOME:R-HSA-264642",
"REACTOME:R-HSA-6798... | 24 | [
"3swh",
"4y21",
"5ue8",
"5uf7",
"6a30",
"7t7c",
"7t7r",
"7t7v",
"7t7x",
"7t81",
"9la9"
] | 11 | [
"PUB00035349",
"PUB00035350"
] | [
"10861235",
"16228007"
] | [
"Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform.",
"A minimal domain responsible for Munc13 activity."
] | [
2000,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Geoglobus ahangari"
] | [
16,
16546,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
39,
12,
83,
13,
25,
16,
1,
24,
33,
1,
2,
44
] | 12 | true | Domain | Mammalian uncoordinated homology 13, domain 2 | Mammalian uncoordinated homology 13, domain 2 | Munc13_dom-2 | 1 |
IPR014773 | 14,773 | Virulence factor YopE, GAP domain | YopE_GAP_dom | Domain | 800 | false | false | Secretion of virulence factors in Gram-negative bacteria involves transportation of the protein across two membranes to reach the cell exterior. There have been four secretion systems described in animal enteropathogens, such as Salmonella and Yersinia, with further sequence similarities in plant pathogens like Ralston... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF03545",
"cd00219"
] | [
"YopE",
"ToxGAP"
] | [
800,
714
] | 2 | [] | [] | [] | 0 | [
"1g4u",
"1g4w",
"1he1",
"1he9",
"1hy5",
"1r4t",
"6x6n"
] | 7 | [
"PUB00003585",
"PUB00006631",
"PUB00006632",
"PUB00006679",
"PUB00080406"
] | [
"9618447",
"2307658",
"2191183",
"10419539",
"10931345"
] | [
"Type III protein secretion systems in bacterial pathogens of animals and plants.",
"Genetic analysis of the yopE region of Yersinia spp.: identification of a novel conserved locus, yerA, regulating yopE expression.",
"The cytotoxic protein YopE of Yersinia obstructs the primary host defence.",
"Yersinia ente... | [
1998,
1990,
1990,
1999,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
800
] | 1 | [] | [] | 0 | true | Domain | Virulence factor YopE, GAP domain | Virulence factor YopE, GAP domain | YopE_GAP_dom | 5 |
IPR014774 | 14,774 | KaiC-like domain | KaiC-like_dom | Domain | 10,932 | false | false | This entry represents a domain found in KaiC, which is a core component of the KaiBC clock oscillator complex that constitutes the main circadian regulator in cyanobacteria [ ]. The Circadian clock oscillator protein KaiC, is encoded in the kaiABC operon that controls circadian rhythms and may be universal in Cyanobact... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF06745"
] | [
"ATPase"
] | [
10932
] | 1 | [] | [] | [] | 0 | [
"1tf7",
"1u9i",
"2dr3",
"2gbl",
"2w0m",
"2zts",
"3dvl",
"3jzm",
"3k09",
"3k0a",
"3k0c",
"3k0e",
"3k0f",
"3s1a",
"4dug",
"4ijm",
"4o0m",
"4tl6",
"4tl7",
"4tl8",
"4tl9",
"4tla",
"4tlb",
"4tlc",
"4tld",
"4tle",
"4wia",
"4yds",
"5jwo",
"5jwq",
"5jwr",
"5n8y"... | 61 | [
"PUB00012817",
"PUB00103716",
"PUB00103717",
"PUB00153718"
] | [
"10064581",
"26113637",
"16816190",
"26508112"
] | [
"Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria.",
"Circadian rhythms. Atomic-scale origins of slowness in the cyanobacterial circadian clock.",
"RecA and RadA proteins of Brucella abortus do not perform overlapping protective DNA repair functions following oxidative b... | [
1999,
2015,
2006,
2016
] | 4 | [] | [
"IPR010624"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3548,
6907,
315,
17,
145
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1
] | 2 | true | Domain | KaiC-like domain | KaiC-like domain | KaiC-like_dom | 5 |
IPR014775 | 14,775 | L27 domain, C-terminal | L27_C | Domain | 17,399 | false | false | The L27 domain is found, among others, in receptor targeting proteins Lin-2 and Lin-7 [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02828"
] | [
"L27"
] | [
17399
] | 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-212676",
"R-BTA-5666185",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013406",
"R-BTA-9013408",
"R-BTA-9013423",
"R-CEL-212676",
"R-CEL-6794361",
"R-DME-212676",
"R-DME-264876",
"R-DME-5620916",
"R-DME-6794361",
"R-DRE-9013404",
"R-DRE-9013406",
"R-DRE-9013408",
"R-GGA-212676",
... | [
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-5666185",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013404",
"REACTOME:R-BTA-9013406",
"REACTOME:R-BTA-9013408",
"REACTOME:R-BTA-9013423",
"REACTOME:R-CEL-212676",
"REACTOME:R-CEL-6794361",
"REACTOME:R-DME-212676",
"REACTOME:R-DME-264876",
"REACTOME:R-... | 54 | [
"1rso",
"1y74",
"1zl8",
"3lra",
"3uit"
] | 5 | [
"PUB00018473"
] | [
"10871881"
] | [
"L27, a novel heterodimerization domain in receptor targeting proteins Lin-2 and Lin-7."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
17399
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
122,
37,
62,
36,
48
] | 6 | true | Domain | L27 domain, C-terminal | L27 domain, C-terminal | L27_C | 8 |
IPR014776 | 14,776 | Tetrapyrrole methylase, subdomain 2 | 4pyrrole_Mease_sub2 | Homologous_superfamily | 113,650 | false | false | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including cobalamin (vitamin B12), haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [ ]. This entry represents the C-... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.950.10"
] | [
""
] | [
113650
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"R-BTA-5358493",
"R-DDI-5358493",
"R-HSA-5358493",
"R-MMU-5358493",
"R-SCE-5358493",
"R-SPO-5358493"
] | [
"EC:2.1.1",
"REACTOME:R-BTA-5358493",
"REACTOME:R-DDI-5358493",
"REACTOME:R-HSA-5358493",
"REACTOME:R-MMU-5358493",
"REACTOME:R-SCE-5358493",
"REACTOME:R-SPO-5358493"
] | 7 | [
"1cbf",
"1pjq",
"1pjs",
"1pjt",
"1s4d",
"1v9a",
"1va0",
"1vce",
"1ve2",
"1vhv",
"1wde",
"1wng",
"1wyz",
"2bb3",
"2cbf",
"2dek",
"2dsg",
"2dsh",
"2dsi",
"2dv3",
"2dv4",
"2dv5",
"2dv7",
"2dxv",
"2dxw",
"2dxx",
"2e07",
"2e08",
"2e0k",
"2e0n",
"2e15",
"2e16"... | 127 | [
"PUB00009744",
"PUB00029889",
"PUB00030902",
"PUB00035315",
"PUB00035496",
"PUB00035497"
] | [
"11215515",
"14595395",
"15522295",
"16866557",
"17227226",
"17229157"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.",
"Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of... | [
2000,
2003,
2004,
2006,
2007,
2007
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
3788,
100210,
8182,
1467,
3
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
1,
2,
1,
2,
4,
2,
2,
9,
3,
2,
2,
24
] | 13 | true | Homologous_superfamily | Tetrapyrrole methylase, subdomain 2 | Tetrapyrrole methylase, subdomain 2 | 4pyrrole_Mease_sub2 | 9 |
IPR014777 | 14,777 | Tetrapyrrole methylase, subdomain 1 | 4pyrrole_Mease_sub1 | Homologous_superfamily | 122,728 | false | false | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including cobalamin (vitamin B12), haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [ ]. This entry represents the N-... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.1010.10"
] | [
""
] | [
122728
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"R-BTA-5358493",
"R-DDI-5358493",
"R-HSA-5358493",
"R-MMU-5358493",
"R-SCE-5358493",
"R-SPO-5358493"
] | [
"EC:2.1.1",
"REACTOME:R-BTA-5358493",
"REACTOME:R-DDI-5358493",
"REACTOME:R-HSA-5358493",
"REACTOME:R-MMU-5358493",
"REACTOME:R-SCE-5358493",
"REACTOME:R-SPO-5358493"
] | 7 | [
"1cbf",
"1pjq",
"1pjs",
"1pjt",
"1s4d",
"1v9a",
"1va0",
"1vce",
"1ve2",
"1vhv",
"1wde",
"1wng",
"1wyz",
"2bb3",
"2cbf",
"2cwo",
"2dek",
"2dsg",
"2dsh",
"2dsi",
"2dv3",
"2dv4",
"2dv5",
"2dv7",
"2dxv",
"2dxw",
"2dxx",
"2e07",
"2e08",
"2e0k",
"2e0n",
"2e15"... | 172 | [
"PUB00009744",
"PUB00029889",
"PUB00030902",
"PUB00035315",
"PUB00035496",
"PUB00035497"
] | [
"11215515",
"14595395",
"15522295",
"16866557",
"17227226",
"17229157"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.",
"Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of... | [
2000,
2003,
2004,
2006,
2007,
2007
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
4304,
108634,
8264,
1523,
3
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
1,
2,
1,
2,
1,
4,
2,
8,
3,
2,
2,
22
] | 13 | true | Homologous_superfamily | Tetrapyrrole methylase, subdomain 1 | Tetrapyrrole methylase, subdomain 1 | 4pyrrole_Mease_sub1 | 8 |
IPR014780 | 14,780 | tRNA pseudouridine synthase II, TruB | tRNA_psdUridine_synth_TruB | Family | 30,019 | false | false | This family represents TruB proteins found in the three domains of life which includes bacterial TruB, TruB1 from mammals and PUS4 from yeast. TruB is responsible for the pseudouridine residue present in the T loops of virtually all tRNAs. TruB recognises the preformed 3D structure of the T loop primarily through shape... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01080",
"PTHR13767",
"TIGR00431",
"cd02573"
] | [
"TruB_bact",
"",
"TruB",
"PseudoU_synth_EcTruB"
] | [
28520,
29967,
27231,
25292
] | 4 | [
"EC"
] | [
"5.4.99.25"
] | [
"EC:5.4.99.25"
] | 1 | [
"1k8w",
"1r3e",
"1r3f",
"1sgv",
"1ze1",
"1ze2",
"1zl3",
"2ab4",
"8jfx"
] | 9 | [
"PUB00026665",
"PUB00045922",
"PUB00092579",
"PUB00100731",
"PUB00114190"
] | [
"11779468",
"10529181",
"19664587",
"25219674",
"9358157"
] | [
"Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.",
"Role of cysteine residues in pseudouridine synthases of different families.",
"Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases.",
"Transcriptom... | [
2001,
1999,
2009,
2014,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
25452,
3947,
2,
10,
608
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)... | [
5,
1,
1,
3,
4,
1,
3,
5,
1,
1,
5
] | 11 | true | Family | tRNA pseudouridine synthase II, TruB | tRNA pseudouridine synthase II, TruB | tRNA_psdUridine_synth_TruB | 6 |
IPR014781 | 14,781 | Anthrax toxin, lethal/endema factor, N-/C-terminal | Anthrax_toxin_lethal/edema_N/C | Domain | 728 | false | false | Anthrax toxin is a plasmid-encoded toxin complex produced by the Gram-positive, spore-forming bacteria, Bacillus anthracis. The toxin consists of three non-toxic proteins: the protective antigen (PA), the lethal factor (LF) and the edema factor (EF) [ ]. These component proteins self-assemble at the surface of host cel... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07737"
] | [
"ATLF"
] | [
728
] | 1 | [
"REACTOME"
] | [
"R-HSA-5210891"
] | [
"REACTOME:R-HSA-5210891"
] | 1 | [
"1j7n",
"1jky",
"1pwp",
"1pwq",
"1pwu",
"1pwv",
"1pww",
"1xfu",
"1xfv",
"1xfw",
"1xfx",
"1xfy",
"1xfz",
"1y0v",
"1yqy",
"1zxv",
"2l0r",
"2n6j",
"3kwv",
"4dv8",
"4fxq",
"4gf1",
"4pkq",
"4pkr",
"4pks",
"4pkt",
"4pku",
"4pkv",
"4pkw",
"4wf6",
"4xm6",
"4xm7"... | 73 | [
"PUB00026280",
"PUB00031089",
"PUB00035784",
"PUB00035785",
"PUB00035786",
"PUB00035787"
] | [
"11700563",
"15131111",
"14570563",
"17335404",
"17381430",
"14616089"
] | [
"Crystal structure of the anthrax lethal factor.",
"Structural and kinetic analyses of the interaction of anthrax adenylyl cyclase toxin with reaction products cAMP and pyrophosphate.",
"Anthrax toxin.",
"Anthrax toxin: receptor binding, internalization, pore formation, and translocation.",
"Characterizatio... | [
2001,
2004,
2003,
2007,
2007,
2004
] | 6 | [
"IPR047568"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Mollusca",
"metagenomes"
] | [
718,
6,
4
] | 3 | [] | [] | 0 | true | Domain | Anthrax toxin, lethal/endema factor, N-/C-terminal | Anthrax toxin, lethal/endema factor, N-/C-terminal | Anthrax_toxin_lethal/edema_N/C | 4 |
IPR014782 | 14,782 | Peptidase M1, membrane alanine aminopeptidase | Peptidase_M1_dom | Domain | 91,750 | false | false | This group of metallopeptidases belong to the MEROPS peptidase family M1 (clan MA(E)), the type example being aminopeptidase N from Homo sapiens (Human). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. Membrane alanine aminopeptidase ( ) i... | [
"GO:0008237",
"GO:0008270"
] | [
"metallopeptidase activity",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF01433"
] | [
"Peptidase_M1"
] | [
91750
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.4.11",
"GenProp1664",
"R-BTA-2142691",
"R-BTA-6798695",
"R-BTA-9018676",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9020265",
"R-BTA-9023661",
"R-BTA-983170",
"R-CEL-2022377",
"R-CEL-2142691",
"R-CEL-674695",
"R-CEL-6798695",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-760... | [
"EC:3.4.11",
"GP:GenProp1664",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9018676",
"REACTOME:R-BTA-9018681",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9020265",
"REACTOME:R-BTA-9023661",
"REACTOME:R-BTA-983170",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CEL-2142691",
"R... | 90 | [
"1gw6",
"1h19",
"1hs6",
"1sqm",
"1z1w",
"1z5h",
"2dq6",
"2dqm",
"2gtq",
"2hpo",
"2hpt",
"2r59",
"2vj8",
"2xpy",
"2xpz",
"2xq0",
"2yd0",
"2zxg",
"3b2p",
"3b2x",
"3b34",
"3b37",
"3b3b",
"3b7r",
"3b7s",
"3b7t",
"3b7u",
"3cho",
"3chp",
"3chq",
"3chr",
"3chs"... | 297 | [
"PUB00000193",
"PUB00003579",
"PUB00008035",
"PUB00008036"
] | [
"2244921",
"7674922",
"8691132",
"8627182"
] | [
"Leukotriene A4 hydrolase: a zinc metalloenzyme.",
"Evolutionary families of metallopeptidases.",
"T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides.",
"Deletion of the NH2-terminal residue converts monocyte chemotactic protein 1... | [
1990,
1995,
1996,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
414,
49304,
41370,
11,
651
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
29,
16,
44,
66,
1,
81,
35,
3,
14,
58,
4,
2,
57
] | 13 | true | Domain | Peptidase M1, membrane alanine aminopeptidase | Peptidase M1, membrane alanine aminopeptidase | Peptidase_M1_dom | 3 |
IPR014783 | 14,783 | Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site | Cu2_ascorb_mOase_CS-2 | Conserved_site | 2,537 | false | false | Copper type II, ascorbate-dependent monooxygenases [ ] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase ( ) and peptidyl-glycine alpha-amidating monooxygenase ( ). There are a few regions of seq... | [
"GO:0016715"
] | [
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00085"
] | [
"CU2_MONOOXYGENASE_2"
] | [
2537
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"1.14.17.3",
"PDOC00080",
"R-HSA-209905",
"R-MMU-209905"
] | [
"EC:1.14.17.3",
"PROSITEDOC:PDOC00080",
"REACTOME:R-HSA-209905",
"REACTOME:R-MMU-209905"
] | 4 | [
"1opm",
"1phm",
"1sdw",
"1yi9",
"1yip",
"1yjk",
"1yjl",
"3mib",
"3mic",
"3mid",
"3mie",
"3mif",
"3mig",
"3mih",
"3mlj",
"3mlk",
"3mll",
"3phm",
"4e4z",
"4zel",
"5wja",
"5wkw",
"5wm0",
"6ala",
"6alv",
"6amp",
"6an3",
"6ao6",
"6ay0",
"6nck",
"8dsj",
"8dsl"... | 33 | [
"PUB00001578"
] | [
"2792366"
] | [
"Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
15,
2522
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
2,
9,
5,
10
] | 6 | true | Conserved_site | Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site | Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site | Cu2_ascorb_mOase_CS-2 | 2 |
IPR014784 | 14,784 | Copper type II, ascorbate-dependent monooxygenase-like, C-terminal | Cu2_ascorb_mOase-like_C | Homologous_superfamily | 12,541 | false | false | Copper type II, ascorbate-dependent monooxygenases [ ] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase ( ) and peptidyl-glycine alpha-amidating monooxygenase ( ). There are a few regions of seq... | [
"GO:0016715"
] | [
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.120.230"
] | [
""
] | [
12541
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.17",
"R-DME-209905",
"R-HSA-209905",
"R-MMU-209905",
"R-RNO-209905"
] | [
"EC:1.14.17",
"REACTOME:R-DME-209905",
"REACTOME:R-HSA-209905",
"REACTOME:R-MMU-209905",
"REACTOME:R-RNO-209905"
] | 5 | [
"1opm",
"1pgs",
"1phm",
"1pnf",
"1png",
"1sdw",
"1yi9",
"1yip",
"1yjk",
"1yjl",
"3ks7",
"3mib",
"3mic",
"3mid",
"3mie",
"3mif",
"3mig",
"3mih",
"3mlj",
"3mlk",
"3mll",
"3phm",
"3pms",
"4e4z",
"4qhb",
"4r4x",
"4r4z",
"4zel",
"5wja",
"5wkw",
"5wm0",
"6ala"... | 42 | [
"PUB00001578"
] | [
"2792366"
] | [
"Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
2774,
9585,
7,
175
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
19,
8,
11,
9,
19
] | 6 | true | Homologous_superfamily | Copper type II, ascorbate-dependent monooxygenase-like, C-terminal | Copper type II, ascorbate-dependent monooxygenase-like, C-terminal | Cu2_ascorb_mOase-like_C | 8 |
IPR014786 | 14,786 | Anaphase-promoting complex subunit 2, C-terminal | ANAPC2_C | Domain | 3,899 | false | false | This entry represents a domain found in the C-terminal of APC subunit 2 (ANAPC2). ANAPC2 is part of the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle [ , ]. The anaphase-pro... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08672",
"SM01013"
] | [
"ANAPC2",
"APC2"
] | [
3826,
3740
] | 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-983168",
"R-DDI-141430",
"R-DDI-174048",
"R-DDI-174084",
"R-DDI-174154",
"R-DDI-174178",
"R-DDI-174184",
"R-DDI-176407",
"R-DDI-176408",
"R-DDI-176409",
"R-DDI-176412",
"R-DDI-179409",
"R-DDI-2467813",
"R-DDI-2559582",
"R-DDI-69017",
"R-DDI-983168",
"R-HSA-141430",
"R-HSA-17... | [
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-141430",
"REACTOME:R-DDI-174048",
"REACTOME:R-DDI-174084",
"REACTOME:R-DDI-174154",
"REACTOME:R-DDI-174178",
"REACTOME:R-DDI-174184",
"REACTOME:R-DDI-176407",
"REACTOME:R-DDI-176408",
"REACTOME:R-DDI-176409",
"REACTOME:R-DDI-176412",
"REACTOME:R-DDI-179... | 52 | [
"1ldd",
"4ui9",
"4yii",
"5a31",
"5g04",
"5g05",
"5khr",
"5khu",
"5l9t",
"5l9u",
"5lcw",
"6nxk",
"6ob1",
"6q6g",
"6q6h",
"6tlj",
"6tm5",
"6tnt",
"8a3t",
"8a5y",
"8a61",
"8pkp",
"8tar",
"8tau",
"9gaw",
"9n9r"
] | 26 | [
"PUB00059221",
"PUB00137338"
] | [
"18485873",
"11739784"
] | [
"Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex.",
"APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex."
] | [
2008,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Thermus"
] | [
5,
3891,
3
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
3,
1,
1,
2,
1,
4,
1,
4,
3,
1,
1,
7
] | 12 | true | Domain | Anaphase-promoting complex subunit 2, C-terminal | Anaphase-promoting complex subunit 2, C-terminal | ANAPC2_C | 5 |
IPR014787 | 14,787 | Phosphoserine phosphatase RsbU, N-terminal | PSer_Pase_RsbU_N | Domain | 1,465 | false | false | The phosphoserine phosphatase RsbU acts as a positive regulator of the general stress-response factor of Gram-positive organisms, sigma-B. RsbU dephosphorylates rsbV in response to environmental stress conveyed from the rsbXST module. The phosphatase activity of RsbU is stimulated during the stress response by associat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08673"
] | [
"RsbU_N"
] | [
1465
] | 1 | [] | [] | [] | 0 | [
"1w53",
"2j6y",
"2j6z",
"2j70"
] | 4 | [
"PUB00032184"
] | [
"15263010"
] | [
"Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanosarcinales",
"Rhizophagus irregularis"
] | [
1446,
18,
1
] | 3 | [] | [] | 0 | true | Domain | Phosphoserine phosphatase RsbU, N-terminal | Phosphoserine phosphatase RsbU, N-terminal | PSer_Pase_RsbU_N | 4 |
IPR014788 | 14,788 | Acetylcholinesterase, tetramerisation domain | AChE_tetra | Domain | 1,259 | false | false | Cholinesterase enzymes are members of the broader alpha/beta hydrolase family and can be dividied into two distinct groups: those that catalyse the hydrolysis of acetylcholine to choline and acetate (acetylcholinesterases ) acetylcholine + H 2 O ->choline + acetate and those that catalyse the conversion of other acylch... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08674"
] | [
"AChE_tetra"
] | [
1259
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1",
"R-BTA-422085",
"R-BTA-9749641",
"R-HSA-112311",
"R-HSA-1483191",
"R-HSA-422085",
"R-HSA-9749641",
"R-MMU-422085",
"R-MMU-9749641"
] | [
"EC:3.1.1",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9749641",
"REACTOME:R-HSA-112311",
"REACTOME:R-HSA-1483191",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-9749641",
"REACTOME:R-MMU-422085",
"REACTOME:R-MMU-9749641"
] | 9 | [
"1f8u",
"1vzj",
"2pm8",
"2x8b",
"3o9m",
"4bdt",
"4tpk",
"5lkr",
"6euc",
"6i2t",
"6rua",
"6tt0",
"7aiy"
] | 13 | [
"PUB00010129",
"PUB00029676",
"PUB00036069",
"PUB00036070",
"PUB00036071",
"PUB00036072",
"PUB00036073"
] | [
"1678899",
"12869558",
"15907917",
"8161450",
"8890157",
"8608006",
"11169626"
] | [
"Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.",
"Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.",
"Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology.",
"Acetylch... | [
1991,
2003,
2005,
1994,
1996,
1996,
2001
] | 7 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1259
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
6,
5
] | 4 | true | Domain | Acetylcholinesterase, tetramerisation domain | Acetylcholinesterase, tetramerisation domain | AChE_tetra | 3 |
IPR014789 | 14,789 | Poly(A)-specific ribonuclease, RNA-binding | PolyA-riboNase_RNA-binding | Domain | 2,012 | false | false | This domain corresponds to the RNA binding domain of Poly(A)-specific ribonuclease (PARN). PARN is a 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails [ ]. | [
"GO:0003723",
"GO:0004535",
"GO:0046872",
"GO:0006402",
"GO:0005634",
"GO:0005737"
] | [
"RNA binding",
"poly(A)-specific ribonuclease activity",
"metal ion binding",
"mRNA catabolic process",
"nucleus",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 6 | [
"PFAM"
] | [
"PF08675"
] | [
"RNA_bind"
] | [
2012
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.13.4",
"R-HSA-380994",
"R-HSA-429947",
"R-HSA-450604",
"R-MMU-429947",
"R-MMU-450604"
] | [
"EC:3.1.13.4",
"REACTOME:R-HSA-380994",
"REACTOME:R-HSA-429947",
"REACTOME:R-HSA-450604",
"REACTOME:R-MMU-429947",
"REACTOME:R-MMU-450604"
] | 6 | [
"1whv",
"2rok",
"3ctr",
"3d45"
] | 4 | [
"PUB00019240"
] | [
"9736620"
] | [
"The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2012
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
13,
3,
7
] | 4 | true | Domain | Poly(A)-specific ribonuclease, RNA-binding | Poly(A)-specific ribonuclease, RNA-binding | PolyA-riboNase_RNA-binding | 8 |
IPR014790 | 14,790 | MutL, C-terminal, dimerisation | MutL_C | Domain | 30,302 | false | false | MutL and MutS are key components of the DNA repair machinery that corrects replication errors [ ]. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signalling complex for repair. The N-terminal region of MutL contains the ATPase domain and the C-termina... | [
"GO:0005524",
"GO:0006298"
] | [
"ATP binding",
"mismatch repair"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF08676",
"SM00853"
] | [
"MutL_C",
"MutL_C"
] | [
29030,
29433
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-5358565",
"R-GGA-5358565",
"R-HSA-5358565",
"R-HSA-5358606",
"R-HSA-5545483",
"R-HSA-5632987",
"R-HSA-6796648",
"R-HSA-912446",
"R-MMU-5358565",
"R-SCE-5358565",
"R-SPO-5358565"
] | [
"REACTOME:R-DDI-5358565",
"REACTOME:R-GGA-5358565",
"REACTOME:R-HSA-5358565",
"REACTOME:R-HSA-5358606",
"REACTOME:R-HSA-5545483",
"REACTOME:R-HSA-5632987",
"REACTOME:R-HSA-6796648",
"REACTOME:R-HSA-912446",
"REACTOME:R-MMU-5358565",
"REACTOME:R-SCE-5358565",
"REACTOME:R-SPO-5358565"
] | 11 | [
"1x9z",
"3gab",
"3kdg",
"3kdk",
"3ncv",
"4e4w",
"4fmn",
"4fmo",
"5b42",
"5z41",
"5z42",
"6e8d",
"6e8e",
"6rmn",
"6shx",
"6sns",
"6snv",
"7p8v",
"8h1e",
"8h1f",
"8h1g",
"8xla"
] | 22 | [
"PUB00032360",
"PUB00035423"
] | [
"15470502",
"8811176"
] | [
"Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair.",
"Mismatch repair in replication fidelity, genetic recombination, and cancer biology."
] | [
2004,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
639,
20221,
9147,
295
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
20,
1,
11,
3,
1,
23,
9,
2,
4,
10,
2,
1,
14
] | 13 | true | Domain | MutL, C-terminal, dimerisation | MutL, C-terminal, dimerisation | MutL_C | 3 |
IPR014791 | 14,791 | Baseplate structural protein Gp11 | Baseplate_struct_Gp11 | Family | 327 | false | false | The bacteriophage baseplate controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. The baseplate is a multi-subunit assembly at the distal end of the tail, which is composed of long and short tail fibres [ ]. The tail region is responsible for attachment to the host bacteria during ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08677"
] | [
"GP11"
] | [
327
] | 1 | [] | [] | [] | 0 | [
"1el6",
"1pdf",
"1tja",
"5iv5",
"5iv7",
"9f4b"
] | 6 | [
"PUB00029807",
"PUB00036076"
] | [
"12923574",
"10966799"
] | [
"Three-dimensional structure of bacteriophage T4 baseplate.",
"Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
6,
321
] | 2 | [] | [] | 0 | true | Family | Baseplate structural protein Gp11 | Baseplate structural protein Gp11 | Baseplate_struct_Gp11 | 9 |
IPR014792 | 14,792 | RsbS co-antagonist protein RsbRA N-terminal domain | RsbRA_N | Domain | 716 | false | false | The general stress response in Bacillus subtilis is governed by sigma(B), whose activity is controlled by a partner switching mechanism in which key protein interactions are governed by serine phosphorylation. In the environmental stress pathway, the RsbS antagonist binds and inactivates the RsbT switch protein/kinase.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08678"
] | [
"Rsbr_N"
] | [
716
] | 1 | [] | [] | [] | 0 | [
"2bnl",
"7b0u"
] | 2 | [
"PUB00035456",
"PUB00057943",
"PUB00077074"
] | [
"16301540",
"15312768",
"11157946"
] | [
"Structure of a nonheme globin in environmental stress signaling.",
"A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis.",
"New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subt... | [
2005,
2004,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacilli"
] | [
716
] | 1 | [] | [] | 0 | true | Domain | RsbS co-antagonist protein RsbRA N-terminal domain | RsbS co-antagonist protein RsbRA N-terminal domain | RsbRA_N | 5 |
IPR014793 | 14,793 | Dissimilatory sulphite reductase D | DsrD | Domain | 248 | false | false | The structure of the dissimilatory sulphite reductase D (DsrD) protein has shown it to contain a winged-helix motif similar to those found in DNA binding proteins [ ]. The structure suggests a possible role for DsrD in transcription or translation of genes, which catalyse dissimilatory sulphite reduction. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08679"
] | [
"DsrD"
] | [
248
] | 1 | [] | [] | [] | 0 | [
"1ucr",
"1wq2"
] | 2 | [
"PUB00031735"
] | [
"12962631"
] | [
"Crystal structure of dissimilatory sulfite reductase D (DsrD) protein--possible interaction with B- and Z-DNA by its winged-helix motif."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaeoglobaceae",
"Bacteria",
"ecological metagenomes"
] | [
11,
230,
7
] | 3 | [] | [] | 0 | true | Domain | Dissimilatory sulphite reductase D | Dissimilatory sulphite reductase D | DsrD | 2 |
IPR014794 | 14,794 | Sporulation protein SpoIIT | SpoIIT | Family | 1,622 | false | false | This entry represents sporulation protein SpoIIT and related proteins. SpoIIT participates in cell-cell signalling pathways during sporulation, functioning specifically in the SpoIIGA-dependent proteolytic activation of sigma E in the mother cell. SpoIIT may act as a coactivator alongside SpoIIR to trigger SpoIIGA-depe... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08680"
] | [
"DUF1779"
] | [
1622
] | 1 | [] | [] | [] | 0 | [
"2fpn"
] | 1 | [
"PUB00162567"
] | [
"26735940"
] | [
"High-Throughput Genetic Screens Identify a Large and Diverse Collection of New Sporulation Genes in Bacillus subtilis."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillota",
"metagenomes"
] | [
1617,
5
] | 2 | [] | [] | 0 | true | Family | Sporulation protein SpoIIT | Sporulation protein SpoIIT | SpoIIT | 1 |
IPR014795 | 14,795 | Antitoxin TacA 1-like | TacA_1-like | Family | 6,692 | false | false | This protein family includes Antitoxin TacA 1 from Salmonella typhimurium and similar short sequences mainly found in bacteria. TacA1, the antitoxin component of a type II toxin-antitoxin (TA) system, counteracts the toxic effect of cognate toxin TacT1. TacT1 is active in complex with its antitoxin, acetylation of this... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08681",
"PTHR35401"
] | [
"TacA1",
""
] | [
6692,
5764
] | 2 | [] | [] | [] | 0 | [
"1y9b",
"5zgn",
"6ajm",
"6ajn",
"6gto",
"6gtq",
"6gtr",
"6gts",
"7ak7",
"7ak8",
"7ak9",
"7f37",
"7zg5",
"7zg6"
] | 14 | [
"PUB00158918",
"PUB00158919"
] | [
"28559487",
"34556858"
] | [
"A Toxin Involved in <i>Salmonella</i> Persistence Regulates Its Activity by Acetylating Its Cognate Antitoxin, a Modification Reversed by CobB Sirtuin Deacetylase.",
"Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing."
] | [
2017,
2021
] | 2 | [] | [
"IPR016547"
] | 0 | 1 | 0 | [
"Bacteria",
"Caudoviricetes",
"Eumetazoa",
"unclassified sequences"
] | [
6582,
13,
4,
93
] | 4 | [] | [] | 0 | true | Family | Antitoxin TacA 1-like | Antitoxin TacA 1-like | TacA_1-like | 5 |
IPR014796 | 14,796 | Protein of unknown function DUF1780, putative endonuclease | DUF1780 | Family | 671 | false | false | This is a family of uncharacterised proteins. The structure of a hypothetical protein from Pseudomonas aeruginosa has shown it to adopt an α/β fold, placing it in the Endonuclease superfamily/clan of restriction endonucleases. | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF08682",
"cd22342"
] | [
"DUF1780",
"Pa4535-like"
] | [
671,
628
] | 2 | [] | [] | [] | 0 | [
"1y0k"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"Steinernema glaseri",
"mine drainage metagenome"
] | [
668,
1,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF1780, putative endonuclease | Protein of unknown function DUF1780, putative endonuclease | DUF1780 | 8 |
IPR014797 | 14,797 | CAMSAP, CKK domain | CKK_CAMSAP | Domain | 7,396 | false | false | The CKK domain occurs at the C-terminal in CAMSAP proteins. The structure of the CKK domain is a β-barrel with an associated α-helical hairpin. Characteristically, the CKK domain has a single invariant tryptophan residue within the core of the predicted β-barrel. Residues that interact with this Trp to form part of thi... | [
"GO:0008017"
] | [
"microtubule binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF08683",
"PS51508",
"SM01051"
] | [
"CAMSAP_CKK",
"CKK",
"CAMSAP_CKK"
] | [
7318,
7372,
7181
] | 3 | [] | [] | [] | 0 | [
"1ugj",
"5lzn",
"5m50",
"5m54",
"5m5c",
"6qus",
"6quy",
"6qve",
"6qvj"
] | 9 | [
"PUB00055957",
"PUB00075742",
"PUB00077209",
"PUB00077210"
] | [
"19508979",
"24117850",
"24706919",
"20946984"
] | [
"The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins.",
"A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth.",
"Regulation of microtubule minus-end dynamics by CAMSAPs an... | [
2009,
2014,
2014,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
2,
7393,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
44,
14,
9,
8,
15
] | 6 | true | Domain | CAMSAP, CKK domain | CAMSAP, CKK domain | CKK_CAMSAP | 1 |
IPR014798 | 14,798 | Protein Ocr | Ocr | Family | 219 | false | false | Protein Ocr protects Bacteriophage T7 DNA from degradation and modification by the host restriction-modification complex [ , ]. The structure of Ocr from T7 has shown that this protein mimics the size and shape of a bent DNA molecule, that binds to and completely occupies the DNA-binding sites of all known families of ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08684"
] | [
"ocr"
] | [
219
] | 1 | [] | [] | [] | 0 | [
"1s7z",
"2y7c",
"6r9b",
"6r9g",
"7bst",
"7btp",
"7eew",
"8q56",
"8v45",
"8zek",
"9ex7"
] | 11 | [
"PUB00030951",
"PUB00096662",
"PUB00096663",
"PUB00096664",
"PUB00096665"
] | [
"11804597",
"32039758",
"32483229",
"32338761",
"1095770"
] | [
"Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA.",
"Structural basis of transcription inhibition by the DNA mimic protein Ocr of bacteriophage T7.",
"Structural insights into assembly, operation and inhibition of a type I restriction-modification system.",
"Phage T7 DNA mimic protein... | [
2002,
2020,
2020,
2020,
1975
] | 5 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"Viruses",
"marine sediment metagenome"
] | [
2,
210,
7
] | 3 | [] | [] | 0 | true | Family | Protein Ocr | Protein Ocr | Ocr | 3 |
IPR014800 | 14,800 | Apx/Shrm Domain 1 | ASD1_dom | Domain | 3,259 | false | false | null | [
"GO:0051015"
] | [
"actin filament binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF08688",
"PS51306"
] | [
"ASD1",
"ASD1"
] | [
3235,
3250
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00043542",
"PUB00043668",
"PUB00043669",
"PUB00071560"
] | [
"16684770",
"17009331",
"10589677",
"19137261"
] | [
"Differential actin-dependent localization modulates the evolutionarily conserved activity of Shroom family proteins.",
"Shroom4 (Kiaa1202) is an actin-associated protein implicated in cytoskeletal organization.",
"Shroom, a PDZ domain-containing actin-binding protein, is required for neural tube morphogenesis ... | [
2006,
2007,
1999,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
3254
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
36,
9,
8,
14
] | 4 | true | Domain | Apx/Shrm Domain 1 | Apx/Shrm Domain 1 | ASD1_dom | 8 |
IPR014801 | 14,801 | Mediator complex, subunit Med5, fungi | Mediator_Med5_fun | Family | 1,648 | false | false | The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact confor... | [
"GO:0003712",
"GO:0006357",
"GO:0016592"
] | [
"transcription coregulator activity",
"regulation of transcription by RNA polymerase II",
"mediator complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF08689",
"PTHR35784"
] | [
"Med5",
""
] | [
1532,
1639
] | 2 | [] | [] | [] | 0 | [
"7jmn",
"7uic",
"7uik",
"7uil",
"7uio"
] | 5 | [
"PUB00035419"
] | [
"16230344"
] | [
"The structural and functional role of Med5 in the yeast Mediator tail module."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1648
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1
] | 2 | true | Family | Mediator complex, subunit Med5, fungi | Mediator complex, subunit Med5, fungi | Mediator_Med5_fun | 9 |
IPR014802 | 14,802 | Golgi to ER traffic protein 2 | GET2 | Family | 109 | false | false | The Golgi to ER traffic (GET) complex is composed of Get1, Get2 and Get3. The complex is involved in the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum [ ]. Get1 and Get2 form a transmembrane complex and interact with Get3, an ATPase which recognises and selectively binds the tr... | [
"GO:0045048",
"GO:0043529"
] | [
"protein insertion into ER membrane",
"GET complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP"
] | [
"MF_03114"
] | [
"Get2"
] | [
109
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00059039",
"PUB00064829"
] | [
"21719644",
"21835666"
] | [
"Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex.",
"The mechanism of tail-anchored protein insertion into the ER membrane."
] | [
2011,
2011
] | 2 | [
"IPR028143"
] | [] | 1 | 0 | 1 | [
"Dikarya"
] | [
109
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Golgi to ER traffic protein 2 | Golgi to ER traffic protein 2 | GET2 | 5 |
IPR014803 | 14,803 | DNA repair protein Nse5/Nse6 | DNA_repair_Nse5/Nse6 | Family | 122 | false | false | Nse5 and Nse6 are non-structural nuclear proteins that are critical for chromosome segregation in fission yeast [ ]. Nse5 forms a dimer with Nse6 and facilitates DNA repair as part of the Smc5-Smc6 holocomplex. Nse6 is also known as KRE29. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08691"
] | [
"Nse5"
] | [
122
] | 1 | [] | [] | [] | 0 | [
"7lto",
"7ogg",
"7sde",
"7yqh",
"8hqs",
"8i4w",
"8i4x",
"8t8e",
"8t8f",
"8wjo"
] | 10 | [
"PUB00035434"
] | [
"16478984"
] | [
"The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
122
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2
] | 2 | true | Family | DNA repair protein Nse5/Nse6 | DNA repair protein Nse5/Nse6 | DNA_repair_Nse5/Nse6 | 4 |
IPR014804 | 14,804 | Mitochondrial protein Pet20-like | Pet20-like | Family | 245 | false | false | This entry includes a group of fungi mitochondrial proteins, including Pet20, Sue1 and Mrx6 (YNL295W) from budding yeasts. This entry also includes Cox24 from fission yeasts. Pet20 is a mitochondrial protein which is thought to play a role in the correct assembly/maintenance of mitochondrial components [ ]. Sue1 is req... | [
"GO:0005739"
] | [
"mitochondrion"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF08692"
] | [
"Pet20"
] | [
245
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035446",
"PUB00074990",
"PUB00076420"
] | [
"16491469",
"15123691",
"16339141"
] | [
"Phenotypes of yeast mutants lacking the mitochondrial protein Pet20p.",
"Sue1p is required for degradation of labile forms of altered cytochromes C in yeast mitochondria.",
"COX24 codes for a mitochondrial protein required for processing of the COX1 transcript."
] | [
2006,
2004,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Ascomycota"
] | [
245
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
3,
1
] | 2 | true | Family | Mitochondrial protein Pet20-like | Mitochondrial protein Pet20-like | Pet20-like | 7 |
IPR014805 | 14,805 | SKG6/TOS2-like | SKG6/TOS2-like | Family | 207 | false | false | This fungal protein family includes SKG6 and TOS2 from Saccharomyces cerevisiae, which are membrane proteins that show polarised intracellular localisation [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08693"
] | [
"SKG6"
] | [
207
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035464",
"PUB00044754",
"PUB00044755",
"PUB00101172"
] | [
"16314687",
"17460121",
"16816427",
"14872283"
] | [
"SKG6, a suppressor gene of synthetic lethality of kex2Delta gas1Delta mutations, encodes a novel membrane protein showing polarized intracellular localization.",
"Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle.",
"Four novel suppressors of... | [
2005,
2007,
2006,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
207
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2
] | 1 | true | Family | SKG6/TOS2-like | SKG6/TOS2-like | SKG6/TOS2-like | 5 |
IPR014806 | 14,806 | Ubiquitin-fold modifier-conjugating enzyme 1 | Ufc1 | Family | 2,167 | false | false | Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a... | [
"GO:0061657",
"GO:0071569"
] | [
"UFM1 conjugating enzyme activity",
"protein ufmylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF08694",
"PIRSF008716",
"PTHR12921",
"cd11686"
] | [
"UFC1",
"DUF1782",
"",
"UBCc_UFC1"
] | [
2167,
1554,
2130,
1881
] | 4 | [] | [] | [] | 0 | [
"2k07",
"2z6o",
"2z6p",
"3evx",
"3kpa",
"7nvj",
"7nvk",
"7nw1",
"7ovc",
"8bzr",
"8c0d",
"9glh",
"9gli",
"9glj",
"9glk",
"9gll",
"9glm",
"9gln",
"9glo",
"9glp",
"9gmm",
"9gmn",
"9gn8",
"9i9m",
"9i9n",
"9i9o",
"9i9p",
"9ia8"
] | 28 | [
"PUB00034740",
"PUB00042603",
"PUB00051812",
"PUB00054168",
"PUB00095668",
"PUB00095672",
"PUB00113746",
"PUB00156109",
"PUB00156111",
"PUB00156112",
"PUB00156113",
"PUB00156941",
"PUB00156942"
] | [
"15071506",
"17825256",
"19101823",
"20018847",
"29868776",
"30886146",
"11265246",
"28625848",
"21158740",
"19940261",
"32326224",
"31052337",
"16132835"
] | [
"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier.",
"Crystal structure of Ufc1, the Ufm1-conjugating enzyme.",
"NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiqui... | [
2004,
2007,
2009,
2010,
2018,
2019,
2001,
2017,
2011,
2010,
2020,
2019,
2005
] | 13 | [] | [] | 0 | 0 | null | [
"Candidatus Heimdallarchaeum aukensis",
"Eukaryota",
"metagenomes"
] | [
1,
2164,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
3,
1,
1,
1,
1,
2,
2,
4,
4
] | 9 | true | Family | Ubiquitin-fold modifier-conjugating enzyme 1 | Ubiquitin-fold modifier-conjugating enzyme 1 | Ufc1 | 2 |
IPR014807 | 14,807 | Cytochrome c oxidase assembly factor 1 | Coa1 | Family | 4,061 | false | false | Coa1 is an inner mitochondrial membrane protein that associates with Shy1 and is required for cytochrome oxidase complex IV assembly. It contains a conserved hydrophobic segment (amino acids 74-92) with the potential to form a membrane-spanning helix. The N terminus of Coa1 is rich in positively charged amino acids and... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08695"
] | [
"Coa1"
] | [
4061
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9864848"
] | [
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-6799198",
"REACTOME:R-HSA-9864848"
] | 3 | [] | 0 | [
"PUB00053932",
"PUB00053933"
] | [
"17882260",
"17882259"
] | [
"Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly.",
"Shy1 couples Cox1 translational regulation to cytochrome c oxidase assembly."
] | [
2007,
2007
] | 2 | [] | [
"IPR042432"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
698,
3361,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosacchar... | [
9,
2,
3,
4,
3,
1,
1,
1,
1,
4
] | 10 | true | Family | Cytochrome c oxidase assembly factor 1 | Cytochrome c oxidase assembly factor 1 | Coa1 | 9 |
IPR014808 | 14,808 | DNA replication factor Dna2, N-terminal | DNA_replication_fac_Dna2_N | Domain | 4,755 | false | false | This entry represents N-terminal domain of the DNA replication factor Dna2. Dna2 and its plant homologue JHS1 are DNA replication factors with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, (5'-flap endonuclease) and helicase activities. It is required for Okazaki fragment processing and is involved in D... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08696"
] | [
"Dna2"
] | [
4755
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.12",
"R-BTA-174437",
"R-BTA-5685938",
"R-BTA-5685942",
"R-BTA-5693568",
"R-BTA-5693579",
"R-BTA-5693607",
"R-BTA-5693616",
"R-BTA-6804756",
"R-BTA-69166",
"R-BTA-69473",
"R-GGA-5685938",
"R-GGA-5685942",
"R-GGA-5693568",
"R-GGA-5693579",
"R-GGA-5693607",
"R-GGA-5693616",
"R-... | [
"EC:3.6.4.12",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5685942",
"REACTOME:R-BTA-5693568",
"REACTOME:R-BTA-5693579",
"REACTOME:R-BTA-5693607",
"REACTOME:R-BTA-5693616",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-69166",
"REACTOME:R-BTA-69473",
"REACTOME:R-GGA-5685938"... | 56 | [
"5ean",
"5eaw",
"5eax"
] | 3 | [
"PUB00035381",
"PUB00062303",
"PUB00062304",
"PUB00062306",
"PUB00062307",
"PUB00062308"
] | [
"10880469",
"10636853",
"16595799",
"22570407",
"16595800",
"20019387"
] | [
"Genetic analyses of Schizosaccharomyces pombe dna2(+) reveal that dna2 plays an essential role in Okazaki fragment metabolism.",
"Identification of the Xenopus laevis homolog of Saccharomyces cerevisiae DNA2 and its role in DNA replication.",
"Isolation of human Dna2 endonuclease and characterization of its en... | [
2000,
2000,
2006,
2012,
2006,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
328,
27,
4398,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
2,
4,
2,
2,
2,
3,
3,
1,
1,
10
] | 12 | true | Domain | DNA replication factor Dna2, N-terminal | DNA replication factor Dna2, N-terminal | DNA_replication_fac_Dna2_N | 2 |
IPR014811 | 14,811 | Argonaute, linker 1 domain | ArgoL1 | Domain | 24,544 | false | false | ArgoL1 is a region found in argonaute [ ] proteins. It normally co-occurs with BAG domain ( ) and Piwi domain ( ). It is a linker region between the N-terminal and the PAZ domains. It contains an α-helix packed against a three-stranded antiparallel β-sheet with two long β-strands (β8 and β9) of the sheet spanning one f... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08699",
"SM01163"
] | [
"ArgoL1",
"DUF1785"
] | [
24433,
22725
] | 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-203927",
"R-CEL-426486",
"R-CEL-5578749",
"R-DME-203927",
"R-DME-426486",
"R-DME-426496",
"R-DME-5578749",
"R-GGA-203927",
"R-GGA-426486",
"R-GGA-426496",
"R-HSA-1912408",
"R-HSA-203927",
"R-HSA-2559580",
"R-HSA-2559585",
"R-HSA-4086398",
"R-HSA-426486",
"R-HSA-426496",
"R-H... | [
"REACTOME:R-CEL-203927",
"REACTOME:R-CEL-426486",
"REACTOME:R-CEL-5578749",
"REACTOME:R-DME-203927",
"REACTOME:R-DME-426486",
"REACTOME:R-DME-426496",
"REACTOME:R-DME-5578749",
"REACTOME:R-GGA-203927",
"REACTOME:R-GGA-426486",
"REACTOME:R-GGA-426496",
"REACTOME:R-HSA-1912408",
"REACTOME:R-HSA-... | 52 | [
"4f3t",
"4kre",
"4krf",
"4kxt",
"4ola",
"4olb",
"4w5n",
"4w5o",
"4w5q",
"4w5r",
"4w5t",
"4z4c",
"4z4d",
"4z4e",
"4z4f",
"4z4g",
"4z4h",
"4z4i",
"5js1",
"5js2",
"5ki6",
"5t7b",
"5vm9",
"5w6v",
"5wea",
"6cbd",
"6mdz",
"6mfn",
"6mfr",
"6n4o",
"6nit",
"6oon"... | 56 | [
"PUB00035384",
"PUB00038652"
] | [
"16216572",
"16061186"
] | [
"Structure and function of argonaute proteins.",
"Crystal structure of A. aeolicus argonaute, a site-specific DNA-guided endoribonuclease, provides insights into RISC-mediated mRNA cleavage."
] | [
2005,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
24544
] | 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",
"Schizosaccharomyces pombe (stra... | [
49,
9,
17,
6,
20,
15,
3,
39,
22,
1,
203
] | 11 | true | Domain | Argonaute, linker 1 domain | Argonaute, linker 1 domain | ArgoL1 | 3 |
IPR014812 | 14,812 | Vacuolar protein sorting-associated protein 51 | Vps51 | Family | 4,776 | false | false | The VFT tethering complex (also known as GARP complex, Golgi associated retrograde protein complex, Vps53 tethering complex) is a conserved eukaryotic docking complex which is involved in recycling of proteins from endosomes to the late Golgi. Vps51 (also known as Ang2 or Vps67) is a subunit of VFT and interacts with t... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR15954"
] | [
""
] | [
4776
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-6811440",
"R-GGA-6811440",
"R-HSA-6811440",
"R-MMU-6811440"
] | [
"REACTOME:R-DME-6811440",
"REACTOME:R-GGA-6811440",
"REACTOME:R-HSA-6811440",
"REACTOME:R-MMU-6811440"
] | 4 | [] | 0 | [
"PUB00035483",
"PUB00077150"
] | [
"12377769",
"25799061"
] | [
"Vps51p links the VFT complex to the SNARE Tlg1p.",
"EARP is a multisubunit tethering complex involved in endocytic recycling."
] | [
2002,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4776
] | 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",
"Schizosaccharomyces pombe (stra... | [
5,
2,
2,
1,
9,
2,
1,
6,
3,
1,
16
] | 11 | true | Family | Vacuolar protein sorting-associated protein 51 | Vacuolar protein sorting-associated protein 51 | Vps51 | 8 |
IPR014815 | 14,815 | Phospholipase C-beta, C-terminal domain | PLC-beta_C | Domain | 5,838 | false | false | This domain corresponds to the α helical C-terminal domain of phospholipase C beta (also known a 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta) [ ]. | [
"GO:0004435",
"GO:0005509",
"GO:0016042"
] | [
"phosphatidylinositol-4,5-bisphosphate phospholipase C activity",
"calcium ion binding",
"lipid catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08703"
] | [
"PLC-beta_C"
] | [
5838
] | 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",
"GenProp1511",
"GenProp1548",
"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-HSA-112043",
"R-HSA-1855204",
"R-HSA-399997",
"R-HSA-4086... | [
"EC:3.1.4.11",
"GP:GenProp1511",
"GP:GenProp1548",
"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... | 37 | [
"1jad",
"4gnk",
"8emv",
"8emw",
"8emx",
"8uqn",
"8uqo"
] | 7 | [
"PUB00028729"
] | [
"11753430"
] | [
"A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
5838
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
22,
32,
14,
25
] | 5 | true | Domain | Phospholipase C-beta, C-terminal domain | Phospholipase C-beta, C-terminal domain | PLC-beta_C | 7 |
IPR014816 | 14,816 | tRNA (1-methyladenosine) methyltransferase catalytic subunit Gcd14 | tRNA_MeTrfase_Gcd14 | Family | 12,819 | false | false | Gcd14, also known as Trm61, is the catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase [ , ], which is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA [ ]. | [
"GO:0160107",
"GO:0030488",
"GO:0031515"
] | [
"tRNA (adenine(58)-N1)-methyltransferase activity",
"tRNA methylation",
"tRNA (m1A) methyltransferase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PROFILE",
"PANTHER"
] | [
"PIRSF017269",
"PS51620",
"PTHR12133"
] | [
"GCD14",
"SAM_TRM61",
""
] | [
6758,
12749,
12714
] | 3 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.220",
"PWY-6829",
"R-HSA-6782315",
"R-HSA-6787450",
"R-HSA-9937008"
] | [
"EC:2.1.1.220",
"METACYC:PWY-6829",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6787450",
"REACTOME:R-HSA-9937008"
] | 5 | [
"1i9g",
"1o54",
"1yb2",
"2b25",
"2pwy",
"2yvl",
"3lga",
"3lhd",
"3mb5",
"5c0o",
"5c1i",
"5ccb",
"5ccx",
"5cd1",
"5eqj",
"5erg"
] | 16 | [
"PUB00009896",
"PUB00016770",
"PUB00057403"
] | [
"9851972",
"10779558",
"14739239"
] | [
"The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.",
"The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae.",
"A primordial RNA modification enzyme: the ca... | [
1998,
2000,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
859,
4930,
6743,
287
] | 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... | [
4,
1,
5,
1,
6,
3,
1,
6,
2,
1,
1,
2
] | 12 | true | Family | tRNA (1-methyladenosine) methyltransferase catalytic subunit Gcd14 | tRNA (1-methyladenosine) methyltransferase catalytic subunit Gcd14 | tRNA_MeTrfase_Gcd14 | 7 |
IPR014817 | 14,817 | Gag protein p6 | Gag_p6 | Domain | 63,218 | false | false | HIV protein p6 contains two late-budding domains (L domains) which are short sequence motifs essential for viral particle release. p6 interacts with the endosomal sorting complex and represents a docking site for several cellular and binding factors [ ]. The PTAP motif interacts with the cellular budding factor TSG101 ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08705"
] | [
"Gag_p6"
] | [
63218
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1169408",
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-174490",
"R-HSA-174495",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910"
] | [
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-174495",
"REACTOME:R-HSA-17... | 16 | [
"2c55",
"5kp9",
"5o2u",
"7p3o"
] | 4 | [
"PUB00035401"
] | [
"16234236"
] | [
"Solution structure of the human immunodeficiency virus type 1 p6 protein."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Lentivirus",
"Thalassovita mangrovi"
] | [
63217,
1
] | 2 | [] | [] | 0 | true | Domain | Gag protein p6 | Gag protein p6 | Gag_p6 | 8 |
IPR014818 | 14,818 | Bacteriophage/plasmid primase, P4, C-terminal | Phage/plasmid_primase_P4_C | Domain | 8,245 | false | false | This domain is found in D5 proteins of DNA viruses, also known as Uncoating factor OPG117, and bacteriophage P4 DNA primase. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08706",
"SM00885"
] | [
"D5_N",
"D5_N"
] | [
8111,
6265
] | 2 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"7ola",
"7om0",
"8apl",
"8apm",
"8hwa",
"8hwb",
"8hwc",
"8hwd",
"8hwe",
"8hwf",
"8hwg",
"8hwh",
"8iqh",
"8iqi",
"8wgy",
"8wgz",
"8wh0",
"8wh2",
"8wh3",
"8wh4",
"8wh6",
"8wvz",
"8ww6",
"8ww7",
"8ww8",
"8ww9",
"8wwa",
"8xj6",
"8xj7",
"8xj8",
"9ily",
"9ilz"... | 36 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
163,
6364,
367,
939,
412
] | 5 | [] | [] | 0 | true | Domain | Bacteriophage/plasmid primase, P4, C-terminal | Bacteriophage/plasmid primase, P4, C-terminal | Phage/plasmid_primase_P4_C | 1 |
IPR014819 | 14,819 | Primase, C-terminal 2 | PriCT_2 | Domain | 3,334 | false | false | This α helical domain is found at the C-terminal of primases. | [
"GO:0016817"
] | [
"hydrolase activity, acting on acid anhydrides"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08707"
] | [
"PriCT_2"
] | [
3334
] | 1 | [
"EC",
"METACYC"
] | [
"3.6.4.-",
"PWY-7250"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250"
] | 2 | [
"8iqh",
"8iqi",
"8wvz",
"8ww6",
"8ww7",
"8ww8",
"8ww9",
"8wwa"
] | 8 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
2338,
226,
19,
507,
244
] | 5 | [] | [] | 0 | true | Domain | Primase, C-terminal 2 | Primase, C-terminal 2 | PriCT_2 | 6 |
IPR014820 | 14,820 | Primase, C-terminal 1 | PriCT_1 | Domain | 5,357 | false | false | This α helical domain is found at the C-terminal of primases. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08708",
"SM00942"
] | [
"PriCT_1",
"PriCT_1"
] | [
3795,
3896
] | 2 | [] | [] | [] | 0 | [
"3vw4"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
17,
4910,
11,
340,
79
] | 5 | [] | [] | 0 | true | Domain | Primase, C-terminal 1 | Primase, C-terminal 1 | PriCT_1 | 7 |
IPR014822 | 14,822 | Non-structural protein NSP9, coronavirus | NSP9_CoV | Domain | 7,851 | false | false | NSP9 is a single-stranded RNA-binding viral protein involved in RNA synthesis, essential for the coronavirus replication [ , , ]. The dimerisation of NSP9 is essential for binding and orienting RNA for subsequent use by the replicase machinery. NSP9 is composed of seven antiparallel β-strands and a single α-helix hat a... | [
"GO:0003723",
"GO:0019079"
] | [
"RNA binding",
"viral genome replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF08710",
"PS51951"
] | [
"CoV_NSP9",
"COV_NSP9_SSRNA_BD"
] | [
7851,
7634
] | 2 | [
"EC",
"EC",
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.50",
"3.4.19.12",
"3.4.22.-",
"GenProp1009",
"PWY-7375",
"R-HSA-191859",
"R-HSA-918233",
"R-HSA-9679504",
"R-HSA-9682706",
"R-HSA-9682708",
"R-HSA-9683439",
"R-HSA-9684325",
"R-HSA-9692916",
"R-HSA-9694271",
"R-HSA-9694301",
"R-HSA-9694676",
"R-HSA-9694686",
"R-HSA-9694786",... | [
"EC:2.7.7.50",
"EC:3.4.19.12",
"EC:3.4.22.-",
"GP:GenProp1009",
"METACYC:PWY-7375",
"REACTOME:R-HSA-191859",
"REACTOME:R-HSA-918233",
"REACTOME:R-HSA-9679504",
"REACTOME:R-HSA-9682706",
"REACTOME:R-HSA-9682708",
"REACTOME:R-HSA-9683439",
"REACTOME:R-HSA-9684325",
"REACTOME:R-HSA-9692916",
... | 21 | [
"1qz8",
"1uw7",
"2j97",
"2j98",
"3ee7",
"5c94",
"5hiy",
"5hiz",
"5ym6",
"5ym8",
"6w4b",
"6w9q",
"6wc1",
"6wxd",
"7bwq",
"7cyq",
"7egq",
"7eiz",
"7kri",
"7n3k",
"7thm",
"8dqu",
"8eir",
"8gw1",
"8gwb",
"8gwe",
"8gwf",
"8gwg",
"8gwi",
"8gwk",
"8gwm",
"8gwn"... | 42 | [
"PUB00030460",
"PUB00051675",
"PUB00094094",
"PUB00097960",
"PUB00100897"
] | [
"15007178",
"19153232",
"29925659",
"33080218",
"32592996"
] | [
"The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world.",
"Severe acute respiratory syndrome coronavirus nsp9 dimerization is essential for efficient viral growth.",
"Dimerization of Coronavirus nsp9 with Diverse Modes E... | [
2004,
2009,
2018,
2020,
2020
] | 5 | [] | [] | 0 | 0 | null | [
"Coronaviridae"
] | [
7851
] | 1 | [] | [] | 0 | true | Domain | Non-structural protein NSP9, coronavirus | Non-structural protein NSP9, coronavirus | NSP9_CoV | 6 |
IPR014824 | 14,824 | Scaffold protein Nfu/NifU, N-terminal | Nfu/NifU_N | Domain | 12,216 | false | false | Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S] [ ]. FeS clus... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08712",
"SM00932"
] | [
"Nfu_N",
"Nfu_N"
] | [
12200,
12159
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-9857492",
"R-HSA-9857492",
"R-MMU-9857492"
] | [
"REACTOME:R-DME-9857492",
"REACTOME:R-HSA-9857492",
"REACTOME:R-MMU-9857492"
] | 3 | [
"1pqx",
"2ffm",
"2k1h",
"2ltl",
"2ltm",
"2m6q",
"2m8w"
] | 7 | [
"PUB00003442",
"PUB00028014",
"PUB00035424",
"PUB00035425",
"PUB00035635"
] | [
"8875867",
"11498000",
"12886008",
"14993221",
"16221578"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Incorporation of iron-sulphur clusters in membrane-bound proteins.",
"Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster.",
"... | [
1996,
2001,
2003,
2004,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8,
7147,
4966,
95
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
8,
1,
5,
1,
1,
3,
1,
2,
2,
1,
1,
8
] | 12 | true | Domain | Scaffold protein Nfu/NifU, N-terminal | Scaffold protein Nfu/NifU, N-terminal | Nfu/NifU_N | 1 |
IPR014825 | 14,825 | DNA alkylation repair enzyme | DNA_alkylation | Family | 17,595 | false | false | These proteins are predicted to be DNA alkylation repair enzymes. The structure of a hypothetical protein shows it to adopt a super coiled α helical structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08713"
] | [
"DNA_alkylation"
] | [
17595
] | 1 | [] | [] | [] | 0 | [
"1t06",
"2b6c",
"3bvs",
"3jx7",
"3jxy",
"3jxz",
"3jy1",
"3l9t",
"3zbo",
"4x8q",
"5cl3",
"5cl4",
"5cl5",
"5cl6",
"5cl7",
"5cl8",
"5cl9",
"5cla",
"5clb",
"5clc",
"5cld",
"5cle",
"5kub",
"5uuf",
"5uug",
"5uuh",
"5vhv",
"5vi0",
"6m9m",
"7lxh",
"7lxj"
] | 31 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctQLz13",
"metagenomes"
] | [
192,
16758,
337,
1,
307
] | 5 | [] | [] | 0 | true | Family | DNA alkylation repair enzyme | DNA alkylation repair enzyme | DNA_alkylation | 1 |
IPR014826 | 14,826 | Formaldehyde-activating enzyme | HCHO-activating_enzyme | Domain | 2,219 | false | false | This family consists of formaldehyde-activating enzyme, or the corresponding domain of longer, bifunctional proteins. It links formaldehyde to the C1 carrier tetrahydromethanopterin (H4MPT), an analog of tetrahydrofolate, and is common among species with H4MPT [ ]. The ribulose monophosphate (RuMP) pathway, which remov... | [
"GO:0016840",
"GO:0016051"
] | [
"carbon-nitrogen lyase activity",
"carbohydrate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"NCBIFAM"
] | [
"PF08714",
"TIGR03126"
] | [
"Fae",
"one_C_fae"
] | [
2219,
1988
] | 2 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.43",
"4.2.1.147",
"GenProp0671",
"PWY-1723",
"PWY-1861",
"PWY-7796"
] | [
"EC:4.1.2.43",
"EC:4.2.1.147",
"GP:GenProp0671",
"METACYC:PWY-1723",
"METACYC:PWY-1861",
"METACYC:PWY-7796"
] | 6 | [
"1y5y",
"1y60",
"8ub7",
"8ub8",
"8ub9",
"8uba",
"8ubb",
"8ubc",
"8ubd",
"8ube",
"8ubf"
] | 11 | [
"PUB00035396"
] | [
"11073907"
] | [
"Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1 required for growth on methanol."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
317,
1824,
3,
75
] | 4 | [] | [] | 0 | true | Domain | Formaldehyde-activating enzyme | Formaldehyde-activating enzyme | HCHO-activating_enzyme | 9 |
IPR014828 | 14,828 | Non-structural protein NSP7, coronavirus | NSP7_CoV | Domain | 7,760 | false | false | Non-structural protein NSP7 has been implicated in viral RNA replication and is predominantly α-helical in structure. Its central core is an N-terminal helical bundle (HB), with helices HB1, HB2 and HB3, forming a triple-stranded antiparallel coiled coil with a right-handed superhelical pitch. It is part of the RNA-dep... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08716",
"PS51949"
] | [
"CoV_NSP7",
"COV_NSP7"
] | [
7759,
7538
] | 2 | [
"EC",
"EC",
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.50",
"3.4.19.12",
"3.4.22.-",
"GenProp1009",
"PWY-7375",
"R-HSA-191859",
"R-HSA-918233",
"R-HSA-9679504",
"R-HSA-9682706",
"R-HSA-9682708",
"R-HSA-9683439",
"R-HSA-9684325",
"R-HSA-9692916",
"R-HSA-9694271",
"R-HSA-9694301",
"R-HSA-9694676",
"R-HSA-9694686",
"R-HSA-9694786",... | [
"EC:2.7.7.50",
"EC:3.4.19.12",
"EC:3.4.22.-",
"GP:GenProp1009",
"METACYC:PWY-7375",
"REACTOME:R-HSA-191859",
"REACTOME:R-HSA-918233",
"REACTOME:R-HSA-9679504",
"REACTOME:R-HSA-9682706",
"REACTOME:R-HSA-9682708",
"REACTOME:R-HSA-9683439",
"REACTOME:R-HSA-9684325",
"REACTOME:R-HSA-9692916",
... | 21 | [
"1ysy",
"2ahm",
"2kys",
"3ub0",
"5f22",
"6m5i",
"6m71",
"6nur",
"6wiq",
"6wqd",
"6wtc",
"6xez",
"6xip",
"6xqb",
"6yhu",
"6yyt",
"7aap",
"7b3b",
"7b3c",
"7b3d",
"7btf",
"7bv1",
"7bv2",
"7bw4",
"7bzf",
"7c2k",
"7ctt",
"7cxm",
"7cxn",
"7cyq",
"7d4f",
"7dcd"... | 97 | [
"PUB00035435",
"PUB00035436",
"PUB00094093",
"PUB00095923",
"PUB00097961",
"PUB00098221",
"PUB00099876",
"PUB00100892",
"PUB00100893",
"PUB00100894"
] | [
"16188992",
"16228002",
"31138817",
"32277040",
"32526208",
"32438371",
"34580920",
"33190493",
"32531208",
"33116300"
] | [
"Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.",
"Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer.",
"Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-fa... | [
2005,
2005,
2019,
2020,
2020,
2020,
2021,
2020,
2020,
2021
] | 10 | [] | [] | 0 | 0 | null | [
"Coronaviridae"
] | [
7760
] | 1 | [] | [] | 0 | true | Domain | Non-structural protein NSP7, coronavirus | Non-structural protein NSP7, coronavirus | NSP7_CoV | 3 |
IPR014829 | 14,829 | Non-structural protein NSP8, coronavirus | NSP8_CoV | Domain | 7,756 | false | false | Viral non-structural protein NSP8 is part of the RNA-dependent RNA polymerase (RdRp) complex and forms a heterotetramer consisting of one molecule of NSP7, two copies of NSP8 and one of NSP12 [ ]. NSP8 and NSP7 adopts a hollow cylinder-like structure [ , ] in which the dimensions of the central channel and positive ele... | [
"GO:0004197",
"GO:0008242",
"GO:0016740"
] | [
"cysteine-type endopeptidase activity",
"omega peptidase activity",
"transferase activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF08717",
"PS51950"
] | [
"CoV_NSP8",
"COV_NSP8"
] | [
7754,
7538
] | 2 | [
"EC",
"EC",
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.50",
"3.4.19.12",
"3.4.22.-",
"GenProp1009",
"PWY-7375",
"R-HSA-191859",
"R-HSA-918233",
"R-HSA-9679504",
"R-HSA-9682706",
"R-HSA-9682708",
"R-HSA-9683439",
"R-HSA-9684325",
"R-HSA-9692916",
"R-HSA-9694271",
"R-HSA-9694301",
"R-HSA-9694676",
"R-HSA-9694686",
"R-HSA-9694786",... | [
"EC:2.7.7.50",
"EC:3.4.19.12",
"EC:3.4.22.-",
"GP:GenProp1009",
"METACYC:PWY-7375",
"REACTOME:R-HSA-191859",
"REACTOME:R-HSA-918233",
"REACTOME:R-HSA-9679504",
"REACTOME:R-HSA-9682706",
"REACTOME:R-HSA-9682708",
"REACTOME:R-HSA-9683439",
"REACTOME:R-HSA-9684325",
"REACTOME:R-HSA-9692916",
... | 21 | [
"2ahm",
"3ub0",
"5f22",
"6m5i",
"6m71",
"6nur",
"6nus",
"6wiq",
"6wqd",
"6wtc",
"6xez",
"6xip",
"6xqb",
"6yhu",
"6yyt",
"7aap",
"7b3b",
"7b3c",
"7b3d",
"7btf",
"7bv1",
"7bv2",
"7bw4",
"7bzf",
"7c2k",
"7ctt",
"7cxm",
"7cxn",
"7cyq",
"7d4f",
"7dcd",
"7dfg"... | 96 | [
"PUB00035436",
"PUB00094088",
"PUB00094093",
"PUB00094104",
"PUB00097960",
"PUB00097961",
"PUB00099876",
"PUB00100895",
"PUB00100896"
] | [
"16228002",
"22039154",
"31138817",
"30918070",
"33080218",
"32526208",
"34580920",
"17024178",
"20709084"
] | [
"Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer.",
"The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension.",
"Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-... | [
2005,
2012,
2019,
2019,
2020,
2020,
2021,
2006,
2010
] | 9 | [] | [] | 0 | 0 | null | [
"Nidovirales"
] | [
7756
] | 1 | [] | [] | 0 | true | Domain | Non-structural protein NSP8, coronavirus | Non-structural protein NSP8, coronavirus | NSP8_CoV | 3 |
IPR014830 | 14,830 | Glycolipid transfer protein domain | Glycolipid_transfer_prot_dom | Domain | 11,664 | false | false | Glycolipid transfer protein (GLTP) is a cytosolic protein that catalyses the intermembrane transfer of glycolipids such as glycosphingolipids, glyceroglycolipids, and possibly glucosylceramides, but not of phospholipids. The GLTP protein consists of a single domain with a multi-helical structure consisting of two layer... | [
"GO:0120013",
"GO:0120009",
"GO:0005737"
] | [
"lipid transfer activity",
"intermembrane lipid transfer",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF08718",
"PTHR10219"
] | [
"GLTP",
""
] | [
11656,
11125
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1660499",
"R-BTA-9845576",
"R-CFA-1660499",
"R-CFA-9845576",
"R-DRE-1660499",
"R-DRE-9845576",
"R-HSA-1660499",
"R-HSA-9845576",
"R-MMU-1660499",
"R-MMU-9845576",
"R-RNO-1660499",
"R-RNO-9845576",
"R-XTR-9845576"
] | [
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-9845576",
"REACTOME:R-CFA-1660499",
"REACTOME:R-CFA-9845576",
"REACTOME:R-DRE-1660499",
"REACTOME:R-DRE-9845576",
"REACTOME:R-HSA-1660499",
"REACTOME:R-HSA-9845576",
"REACTOME:R-MMU-1660499",
"REACTOME:R-MMU-9845576",
"REACTOME:R-RNO-1660499",
"REACTOM... | 13 | [
"1swx",
"1sx6",
"1tfj",
"1wbe",
"2bv7",
"2euk",
"2eum",
"2evd",
"2evl",
"2evs",
"2evt",
"2i3f",
"2q52",
"3kv0",
"3ric",
"3rwv",
"3rzn",
"3s0i",
"3s0k",
"4gh0",
"4ghp",
"4ghs",
"4gix",
"4gjq",
"4gvt",
"4gxd",
"4gxg",
"4h2z",
"4k80",
"4k84",
"4k85",
"4k8n"... | 41 | [
"PUB00035403",
"PUB00035404",
"PUB00054004",
"PUB00106849"
] | [
"15504043",
"16309699",
"15107860",
"17687330"
] | [
"Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses.",
"Structural evidence for adaptive ligand binding of glycolipid transfer protein.",
"FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and... | [
2004,
2006,
2004,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
11664
] | 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",
"Zea mays"
] | [
20,
5,
7,
4,
13,
10,
1,
22,
8,
40
] | 10 | true | Domain | Glycolipid transfer protein domain | Glycolipid transfer protein domain | Glycolipid_transfer_prot_dom | 3 |
IPR014831 | 14,831 | Haemagglutinin stalk, influenza C | Hemagglutn_stalk_influenz-C | Domain | 416 | false | false | Haemagglutinin (HA) is one of two main surface fusion glycoproteins embedded in the envelope of influenza viruses, the other being neuraminidase (NA). There are sixteen known HA subtypes (H1-H16) and nine NA subtypes (N1-N9), which together are used to classify influenza viruses (e.g. H5N1). The antigenic variations in... | [
"GO:0046789",
"GO:0019064",
"GO:0019031"
] | [
"host cell surface receptor binding",
"fusion of virus membrane with host plasma membrane",
"viral envelope"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF08720"
] | [
"Hema_stalk"
] | [
416
] | 1 | [
"EC"
] | [
"3.1.1.53"
] | [
"EC:3.1.1.53"
] | 1 | [
"1flc",
"5e5w",
"5e62",
"5e64",
"5e65",
"5e66",
"6wko",
"6yi5"
] | 8 | [
"PUB00010667",
"PUB00033162",
"PUB00033164",
"PUB00033165"
] | [
"9817207",
"16543414",
"15475582",
"16178512"
] | [
"Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus.",
"Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus.",
"Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers.",
"The factors of virulence of influ... | [
1998,
2006,
2005,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Orthomyxoviridae"
] | [
416
] | 1 | [] | [] | 0 | true | Domain | Haemagglutinin stalk, influenza C | Haemagglutinin stalk, influenza C | Hemagglutn_stalk_influenz-C | 6 |
IPR014832 | 14,832 | TnsA endonuclease C-terminal | TnsA_C | Domain | 1,290 | false | false | The Tn7 transposase is composed of proteins TnsA and TnsB. DNA breakage at the 5'-end of the transposon is carried out by TnsA, and breakage and joining at the 3'-end is carried out by TnsB. The C-terminal domain of TnsA binds DNA. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08721"
] | [
"Tn7_Tnp_TnsA_C"
] | [
1290
] | 1 | [] | [] | [] | 0 | [
"1f1z",
"1t0f",
"9bw1"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Fungi",
"ecological metagenomes"
] | [
1279,
2,
9
] | 3 | [] | [] | 0 | true | Domain | TnsA endonuclease C-terminal | TnsA endonuclease C-terminal | TnsA_C | 9 |
IPR014834 | 14,834 | Gag protein p15 | Gag_p15 | Domain | 366 | false | false | Gag p15 is a viral membrane-binding matrix protein which is α helical in structure. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08723"
] | [
"Gag_p15"
] | [
366
] | 1 | [] | [] | [] | 0 | [
"1hek",
"6t61",
"6t63",
"6t64"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Lentivirus"
] | [
366
] | 1 | [] | [] | 0 | true | Domain | Gag protein p15 | Gag protein p15 | Gag_p15 | 1 |
IPR014835 | 14,835 | NS1 nuclease, NS1-Nuc domain, parvovirinae | NS1-Nuc | Domain | 869 | false | false | This entry represents the NS1-Nuc domain found mainly in the Parvovirinae subfamily of viruses in the family Parvoviridae. Adeno-associated virus (AAV) Replication (Rep) protein is essential for viral replication and integration. The catalytic domain has DNA binding and endonuclease activity. The family Parvoviridae is... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08724"
] | [
"Rep_N"
] | [
869
] | 1 | [] | [] | [] | 0 | [
"1m55",
"1rz9",
"1uut",
"4zo0",
"4zq9",
"5byg",
"5dcx",
"6usm",
"6xb8",
"7jse",
"7jsf",
"7jsg",
"7jsh",
"7jsi",
"7szx",
"7szy",
"7y56",
"7y57",
"9bc5",
"9bu7",
"9kbg",
"9kbh",
"9kbi"
] | 23 | [
"PUB00028927",
"PUB00153284",
"PUB00153285",
"PUB00153286",
"PUB00153287",
"PUB00153288",
"PUB00153289",
"PUB00153290",
"PUB00153291"
] | [
"12191478",
"36253516",
"26791818",
"23966383",
"25528417",
"36090819",
"35435730",
"10704358",
"33291793"
] | [
"Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep.",
"Structure and function of the parvoviral NS1 protein: a review.",
"Characterization and Distribution Analysis of a Densovirus Infecting Myzus persicae nicotianae (Hemiptera: Aphidida... | [
2002,
2023,
2016,
2013,
2015,
2022,
2022,
2000,
2020
] | 9 | [
"IPR049901"
] | [] | 1 | 0 | 1 | [
"Bacillati",
"Eutheria",
"Viruses"
] | [
5,
4,
860
] | 3 | [
"Homo sapiens"
] | [
1
] | 1 | true | Domain | NS1 nuclease, NS1-Nuc domain, parvovirinae | NS1 nuclease, NS1-Nuc domain, parvovirinae | NS1-Nuc | 9 |
IPR014836 | 14,836 | Integrin beta subunit, cytoplasmic domain | Integrin_bsu_cyt_dom | Domain | 9,924 | false | false | This entry represents the cytoplasmic domain of integrin beta subunits [ ]. Integrin beta subunits consist of an extracellular domain with a head region, a stalk/leg section, a transmembrane domain, and a cytoplasmic tail. The head region contains a β-I-like domain inserted into a hybrid domain, connected to a plexin-s... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08725",
"SM01241"
] | [
"Integrin_b_cyt",
"Integrin_b_cyt"
] | [
9871,
9685
] | 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-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-114608",
"R-CEL-1236973",
"R-CEL-2129379",
"R-CEL-216083",
"R-CEL-2173789",
"R-CEL-3000157",
"R-CEL-3000170",
"R-CEL-3000178",
... | [
"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-114608",
"REACTOME:R-CEL-1236973",
"REACTOME:R-C... | 154 | [
"1kup",
"1kuz",
"1m8o",
"1s4x",
"2brq",
"2h7d",
"2h7e",
"2jf1",
"2knc",
"2kv9",
"2l1c",
"2ljd",
"2lje",
"2ljf",
"2mtp",
"3g9w",
"4um8",
"6vgu",
"7la4",
"7nwl",
"7nxd",
"7s47",
"8gcd",
"8gce",
"8oxz",
"8t2u",
"8t2v",
"8xei",
"8xek",
"8xel",
"8xen",
"8xer"... | 46 | [
"PUB00006148",
"PUB00009789",
"PUB00015915",
"PUB00015985",
"PUB00027259",
"PUB00035000",
"PUB00035002",
"PUB00057248",
"PUB00160425"
] | [
"9009218",
"12297042",
"14689578",
"2467745",
"12230976",
"12361595",
"12234368",
"12388743",
"28510180"
] | [
"A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.",
"Integrins: bidirectional, allosteric signaling machines.",
"Integrin clipping: a novel adhesion switch?",
"A novel vitronectin receptor integrin (alpha v beta x... | [
1997,
2002,
2004,
1989,
2002,
2002,
2002,
2002,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9924
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
19,
6,
31,
14,
25
] | 6 | true | Domain | Integrin beta subunit, cytoplasmic domain | Integrin beta subunit, cytoplasmic domain | Integrin_bsu_cyt_dom | 2 |
IPR014837 | 14,837 | EF-hand, Ca insensitive | EF-hand_Ca_insen | Domain | 12,900 | false | false | EF hands are helix-loop-helix binding motifs involved in the regulation of many cellular processes. EF hands usually bind to Ca2+ ions, which cause a major conformational change that allows the protein to interact with its designated targets. This protein corresponds to an EF hand which has partially or entirely lost i... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08726"
] | [
"EFhand_Ca_insen"
] | [
12900
] | 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-114608",
"R-BTA-390522",
"R-BTA-438066",
"R-BTA-446388",
"R-BTA-5673001",
"R-BTA-9013405",
"R-BTA-9013418",
"R-BTA-9035034",
"R-DDI-114608",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9013418",
"R-DDI-9013420",
"R-DDI-9013424",
"R-DME-114608",
"R-DME-264870",
"R-DME-375165",
"... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-390522",
"REACTOME:R-BTA-438066",
"REACTOME:R-BTA-446388",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-9013405",
"REACTOME:R-BTA-9013418",
"REACTOME:R-BTA-9035034",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6807878",
"REACTOME:R-D... | 92 | [
"1h8b",
"1sjj",
"2n8y",
"2n8z",
"4d1e",
"6c0a",
"6ts3",
"7ank",
"7b55",
"7b56",
"7b57",
"8iah"
] | 12 | [
"PUB00025570"
] | [
"11573089"
] | [
"Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
12900
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
6,
68,
8,
53,
30,
1,
42,
1
] | 8 | true | Domain | EF-hand, Ca insensitive | EF-hand, Ca insensitive | EF-hand_Ca_insen | 2 |
IPR014838 | 14,838 | Poliovirus 3A protein-like | P3A | Domain | 6,790 | false | false | The 3A protein is found in positive-strand RNA viruses. It is a critical component of the poliovirus replication complex, and is also an inhibitor of host cell ER to Golgi transport. | [
"GO:0003968",
"GO:0004197",
"GO:0017111"
] | [
"RNA-directed RNA polymerase activity",
"cysteine-type endopeptidase activity",
"ribonucleoside triphosphate phosphatase activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM"
] | [
"PF08727"
] | [
"P3A"
] | [
6790
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.22.28",
"3.4.22.29",
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:2.7.7.48",
"EC:3.4.22.28",
"EC:3.4.22.29",
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 9 | [
"1ng7",
"6hln",
"6hlt",
"6hlv",
"6hlw",
"6hm8",
"6hmv",
"6q68",
"6q69"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Adhaeribacter rhizoryzae",
"Picornavirales",
"Trichinella"
] | [
1,
6786,
3
] | 3 | [] | [] | 0 | true | Domain | Poliovirus 3A protein-like | Poliovirus 3A protein-like | P3A | 7 |
IPR014839 | 14,839 | Ribonucleotide reductase, transcriptional regulator Crt10 | Crt10 | Family | 1,121 | false | false | Crt10 is a transcriptional regulator of ribonucleotide reductase (RNR) genes [ ]. RNR catalyses the rate limiting step in dNTP synthesis. Mutations in CRT10 have been shown to enhance hydroxyurea resistance [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08728"
] | [
"CRT10"
] | [
1121
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035376"
] | [
"16600900"
] | [
"Identification and characterization of CRT10 as a novel regulator of Saccharomyces cerevisiae ribonucleotide reductase genes."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1121
] | 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 | Ribonucleotide reductase, transcriptional regulator Crt10 | Ribonucleotide reductase, transcriptional regulator Crt10 | Crt10 | 4 |
IPR014840 | 14,840 | Hpc2-related domain | HRD | Domain | 6,372 | false | false | HPC2 (Histone promoter control 2) is required for cell-cycle regulation of histone transcription [ ]. It regulates transcription of the histone genes during the S-phase of the cell cycle by repressing transcription at other cell cycle stages. HPC2 mutants display synthetic interactions with FACT complex which allows RN... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08729"
] | [
"HUN"
] | [
6372
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2559584",
"R-MMU-2559584",
"R-SCE-2559584"
] | [
"REACTOME:R-HSA-2559584",
"REACTOME:R-MMU-2559584",
"REACTOME:R-SCE-2559584"
] | 3 | [
"4zbj",
"8gha",
"8ghm",
"8ghn"
] | 4 | [
"PUB00033373",
"PUB00035410",
"PUB00057241"
] | [
"12524332",
"1406694",
"20976105"
] | [
"Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure.",
"Identification of a new set of cell cycle-regulatory genes that regulate S-phase transcription of histone genes in Saccharomyces cerevisiae.",
"Silencing ... | [
2002,
1992,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6372
] | 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... | [
16,
6,
6,
3,
5,
3,
2,
3,
9,
1,
1,
11
] | 12 | true | Domain | Hpc2-related domain | Hpc2-related domain | HRD | 9 |
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