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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR001326 | 1,326 | Translation elongation factor EF1B, beta/delta chains, conserved site | Transl_elong_EF1B_B/D_CS | Conserved_site | 9,262 | false | false | Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept... | [
"GO:0003746",
"GO:0006414"
] | [
"translation elongation factor activity",
"translational elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00824",
"PS00825"
] | [
"EF1BD_1",
"EF1BD_2"
] | [
7711,
7436
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00648",
"R-BTA-156842",
"R-DDI-156842",
"R-DME-156842",
"R-HSA-156842",
"R-MMU-156842",
"R-RNO-156842",
"R-SCE-156842",
"R-SPO-156842"
] | [
"PROSITEDOC:PDOC00648",
"REACTOME:R-BTA-156842",
"REACTOME:R-DDI-156842",
"REACTOME:R-DME-156842",
"REACTOME:R-HSA-156842",
"REACTOME:R-MMU-156842",
"REACTOME:R-RNO-156842",
"REACTOME:R-SCE-156842",
"REACTOME:R-SPO-156842"
] | 9 | [
"1b64",
"1f60",
"1g7c",
"1ije",
"1ijf",
"2mvm",
"2mvn",
"2n51",
"5o8w"
] | 9 | [
"PUB00033951",
"PUB00033952",
"PUB00033953"
] | [
"12932732",
"15922593",
"12762045"
] | [
"Elongation factors in protein biosynthesis.",
"Elongation factors on the ribosome.",
"Structural studies of eukaryotic elongation factors."
] | [
2003,
2005,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"human gut metagenome"
] | [
6,
9255,
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... | [
20,
2,
16,
3,
17,
12,
1,
7,
20,
1,
1,
16
] | 12 | true | Conserved_site | Translation elongation factor EF1B, beta/delta chains, conserved site | Translation elongation factor EF1B, beta/delta chains, conserved site | Transl_elong_EF1B_B/D_CS | 4 |
IPR001328 | 1,328 | Peptidyl-tRNA hydrolase | Pept_tRNA_hydro | Family | 31,758 | false | false | Peptidyl-tRNA hydrolase ( ) (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis [ , ]. Bacterial PTH has been found to be evo... | [
"GO:0004045"
] | [
"peptidyl-tRNA hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00083",
"PF01195",
"PTHR17224",
"TIGR00447",
"cd00462"
] | [
"Pept_tRNA_hydro_bact",
"Pept_tRNA_hydro",
"",
"pth",
"PTH"
] | [
26590,
31691,
31392,
29772,
27171
] | 5 | [
"EC",
"PROSITEDOC"
] | [
"3.1.1.29",
"PDOC00920"
] | [
"EC:3.1.1.29",
"PROSITEDOC:PDOC00920"
] | 2 | [
"1ryb",
"1rym",
"1ryn",
"2jrc",
"2lgj",
"2mjl",
"2naf",
"2pth",
"2z2i",
"2z2j",
"2z2k",
"3kjz",
"3kk0",
"3nea",
"3ofv",
"3p2j",
"3tck",
"3tcn",
"3td2",
"3td6",
"3v2i",
"3vjr",
"4dhw",
"4djj",
"4erx",
"4fno",
"4fop",
"4fot",
"4fyj",
"4hoy",
"4iko",
"4jc4"... | 81 | [
"PUB00001213",
"PUB00001306",
"PUB00001861",
"PUB00005030",
"PUB00043746",
"PUB00062567",
"PUB00079881",
"PUB00106491"
] | [
"1833189",
"9303320",
"8635758",
"8563640",
"12881426",
"22923517",
"15078105",
"26508479"
] | [
"Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis.",
"Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.",
"Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of Escherichia coli.",
"New protein func... | [
1991,
1997,
1996,
1995,
2003,
2012,
2004,
2015
] | 8 | [] | [
"IPR048076"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_66_E06"
] | [
25861,
5287,
1,
608,
1
] | 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)... | [
20,
2,
1,
5,
2,
1,
10,
4,
1,
1,
25
] | 11 | true | Family | Peptidyl-tRNA hydrolase | Peptidyl-tRNA hydrolase | Pept_tRNA_hydro | 3 |
IPR001329 | 1,329 | Glycoside hydrolase family 56, bee venom hyaluronidase | Venom_Hyaluronidase | Family | 371 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004415",
"GO:0006952"
] | [
"hyalurononglucosaminidase activity",
"defense response"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00847"
] | [
"HYALURONDASE"
] | [
371
] | 1 | [
"CAZY",
"EC",
"METACYC"
] | [
"GH56",
"3.2.1.35",
"PWY-6573"
] | [
"CAZY:GH56",
"EC:3.2.1.35",
"METACYC:PWY-6573"
] | 3 | [
"1fcq",
"1fcu",
"1fcv",
"2atm",
"2j88"
] | 5 | [
"PUB00004814",
"PUB00004870",
"PUB00005266",
"PUB00093389"
] | [
"7682712",
"7624375",
"8535779",
"20608917"
] | [
"Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Purification and characterization of two new allergens from... | [
1993,
1995,
1995,
2011
] | 4 | [
"IPR018155"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
371
] | 1 | [] | [] | 0 | true | Family | Glycoside hydrolase family 56, bee venom hyaluronidase | Glycoside hydrolase family 56, bee venom hyaluronidase | Venom_Hyaluronidase | 7 |
IPR001330 | 1,330 | Prenyltransferase alpha-alpha toroid domain | Prenyltrans | Domain | 16,391 | false | false | The entry includes enzymes involved in the biosynthesis of various terpenes and the prenylation of proteins [ , ]. Terpene cyclases/mutases catalyse the cyclisation of squalene or oxidosqualene into various triterpenes, such as lanosterol, beta-amyrin, and hopene, which are crucial for sterol biosynthesis and other met... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00432"
] | [
"Prenyltrans"
] | [
16391
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.5.1",
"R-BTA-2514859",
"R-BTA-6803205",
"R-BTA-8873719",
"R-BTA-9648002",
"R-CEL-6803205",
"R-CEL-8873719",
"R-DDI-6803205",
"R-DDI-8873719",
"R-DDI-9648002",
"R-HSA-2514859",
"R-HSA-6803205",
"R-HSA-8873719",
"R-HSA-9648002",
"R-HSA-9679191",
"R-MMU-2514859",
"R-MMU-6803205",
"... | [
"EC:2.5.1",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-6803205",
"REACTOME:R-BTA-8873719",
"REACTOME:R-BTA-9648002",
"REACTOME:R-CEL-6803205",
"REACTOME:R-CEL-8873719",
"REACTOME:R-DDI-6803205",
"REACTOME:R-DDI-8873719",
"REACTOME:R-DDI-9648002",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-680320... | 29 | [
"1d8d",
"1d8e",
"1dce",
"1fpp",
"1ft1",
"1ft2",
"1jcq",
"1jcr",
"1jcs",
"1kzo",
"1kzp",
"1ld7",
"1ld8",
"1ltx",
"1mzc",
"1n4p",
"1n4q",
"1n4r",
"1n4s",
"1n94",
"1n95",
"1n9a",
"1ni1",
"1nl4",
"1o1r",
"1o1s",
"1o1t",
"1o5m",
"1qbq",
"1s63",
"1s64",
"1sa4"... | 119 | [
"PUB00005227",
"PUB00005416"
] | [
"9295270",
"8016864"
] | [
"Structure and function of a squalene cyclase.",
"A specific amino acid repeat in squalene and oxidosqualene cyclases."
] | [
1997,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
179,
1355,
14779,
78
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
21,
4,
4,
5,
12,
18,
3,
15,
21,
3,
3,
19
] | 12 | true | Domain | Prenyltransferase alpha-alpha toroid domain | Prenyltransferase alpha-alpha toroid domain | Prenyltrans | 3 |
IPR001332 | 1,332 | Arterivirus GP5 envelope glycoprotein | Arteri_GP5 | Family | 20,220 | false | false | Arterivirus such as porcine reproductive and respiratory syndrome virus (PRRSV) contain four glycoproteins on the virion envelope: the major glycoprotein GP5 and minor glycoproteins GP2a, GP3, and GP4. GP5, previously known as Gl, is encoded in ORF5 and is 30- 45kDa in size [ ]. Gl is heterogeneously glycosylated with ... | [
"GO:0019031"
] | [
"viral envelope"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF00951"
] | [
"Arteri_Gl"
] | [
20220
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005612",
"PUB00019644",
"PUB00076654"
] | [
"8553578",
"10893147",
"19939927"
] | [
"Phylogenetic analysis of open reading frame 5 of field isolates of equine arteritis virus and identification of conserved and nonconserved regions in the GL envelope glycoprotein.",
"Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: comparison of the Nort... | [
1995,
2000,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Arteriviridae"
] | [
20220
] | 1 | [] | [] | 0 | true | Family | Arterivirus GP5 envelope glycoprotein | Arterivirus GP5 envelope glycoprotein | Arteri_GP5 | 6 |
IPR001333 | 1,333 | Peptidase M32, carboxypeptidase Taq | Peptidase_M32_Taq | Family | 10,791 | false | false | This group of metallopeptidases belong to MEROPS peptidase family M32 (carboxypeptidase Taq family, clan MA(E)). The predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH. Over 70 metallopeptidase families have been identified to date. In these... | [
"GO:0004181",
"GO:0006508"
] | [
"metallocarboxypeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROFILE",
"PANTHER"
] | [
"PF02074",
"PIRSF006615",
"PR00998",
"PS52034",
"PTHR34217"
] | [
"Peptidase_M32",
"Zn_crbxpep_Taq",
"CRBOXYPTASET",
"PEPTIDASE_M32",
""
] | [
7745,
7105,
7463,
7722,
10736
] | 5 | [
"EC"
] | [
"3.4.17.19"
] | [
"EC:3.4.17.19"
] | 1 | [
"1k9x",
"1ka2",
"1ka4",
"3dwc",
"3hoa",
"3hq2",
"5e3x",
"5giv",
"5wvu",
"7a03"
] | 10 | [
"PUB00003579",
"PUB00015965",
"PUB00016060",
"PUB00016178",
"PUB00057723",
"PUB00080973",
"PUB00120033",
"PUB00120034",
"PUB00153310",
"PUB00153311"
] | [
"7674922",
"7765282",
"11839307",
"1369078",
"19544567",
"8862545",
"26603937",
"17007610",
"22575602",
"29246805"
] | [
"Evolutionary families of metallopeptidases.",
"Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli.",
"Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus f... | [
1995,
1994,
2002,
1992,
2009,
1996,
2015,
2007,
2012,
2018
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
611,
9629,
423,
128
] | 4 | [] | [] | 0 | true | Family | Peptidase M32, carboxypeptidase Taq | Peptidase M32, carboxypeptidase Taq | Peptidase_M32_Taq | 6 |
IPR001334 | 1,334 | E6 early regulatory protein | E6 | Family | 3,542 | false | false | The papillomavirus E6 oncoproteins are small zinc-binding proteins that share a conserved zinc-binding CXXC motif and do not have identified intrinsic enzymatic activity. E6 proteins are thought to act as adapter proteins, thereby altering the function of E6-associated cellular proteins. This model for E6 function is b... | [] | [] | [] | 0 | [
"HAMAP",
"PFAM"
] | [
"MF_04006",
"PF00518"
] | [
"HPV_E6",
"E6"
] | [
3239,
3542
] | 2 | [] | [] | [] | 0 | [
"2fk4",
"2ljx",
"2ljy",
"2ljz",
"2m3l",
"3py7",
"4giz",
"4xr8",
"6siv",
"6sja",
"6sjv",
"6slm",
"6smv",
"7uaj",
"8gcr",
"8jrn",
"8jro",
"8jrp",
"8jrq",
"8jrr",
"8r1f",
"8r1g",
"9cht"
] | 23 | [
"PUB00009556",
"PUB00009557",
"PUB00087154",
"PUB00087155",
"PUB00087156"
] | [
"10623743",
"9151888",
"26789255",
"15664194",
"17023019"
] | [
"Identification of a second transforming function in bovine papillomavirus type 1 E6 and the role of E6 interactions with paxillin, E6BP, and E6AP.",
"Transformation by bovine papillomavirus type 1 E6 is independent of transcriptional activation by E6.",
"Structure of the E6/E6AP/p53 complex required for HPV-me... | [
2000,
1997,
2016,
2005,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Papillomaviridae"
] | [
4,
3538
] | 2 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | E6 early regulatory protein | E6 early regulatory protein | E6 | 4 |
IPR001337 | 1,337 | Tobacco mosaic virus-like, coat protein | TMV-like_coat | Family | 1,559 | false | false | This family contains virus coat proteins. Examples include those from Tobacco mosaic virus (TMV), Cucumber green mottle mosaic virus and Ribgrass mosaic virus (RMV). In order to establish infections, viruses must be delivered to the cells of potential hosts and must then engage in activities that enable their genomes t... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00721"
] | [
"TMV_coat"
] | [
1559
] | 1 | [] | [] | [] | 0 | [
"1cgm",
"1ei7",
"1rmv",
"1vtm",
"2om3",
"2tmv",
"2xea",
"3j06",
"3kml",
"3pdm",
"4gqh",
"4udv",
"5a79",
"5a7a",
"6i5a",
"6r7m",
"6rlp",
"6sae",
"6sag",
"6x0q",
"6x0r",
"7q22",
"7q23",
"7q2q",
"7q2r",
"7q2s",
"8eaw"
] | 27 | [
"PUB00006501",
"PUB00006502"
] | [
"10212932",
"10212940"
] | [
"The tobacco mosaic virus particle: structure and assembly.",
"Tobacco mosaic virus and the study of early events in virus infections."
] | [
1999,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses"
] | [
297,
1262
] | 2 | [
"Drosophila melanogaster",
"Oryza sativa subsp. japonica"
] | [
2,
6
] | 2 | true | Family | Tobacco mosaic virus-like, coat protein | Tobacco mosaic virus-like, coat protein | TMV-like_coat | 5 |
IPR001338 | 1,338 | Class I Hydrophobin | Class_I_Hydrophobin | Family | 6,168 | false | false | This entry represents class I hydrophobins found in fungi. Hydrophobins are small, moderately hydrophobic extracellular proteins characterised by eight cysteine residues arranged in a strictly conserved motif. They are typically found on the outer surface of conidia and the hyphal wall, where they are thought to mediat... | [
"GO:0005199",
"GO:0009277"
] | [
"structural constituent of cell wall",
"fungal-type cell wall"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF01185",
"SM00075"
] | [
"Hydrophobin",
"HYDRO"
] | [
5983,
5633
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00739"
] | [
"PROSITEDOC:PDOC00739"
] | 1 | [
"2fmc",
"2k6a",
"2lfn",
"2lsh",
"2n4o",
"2nbh",
"5w0y",
"6e98",
"6e9m",
"6gcj",
"7s7s",
"7s86"
] | 12 | [
"PUB00001789",
"PUB00001900",
"PUB00001904",
"PUB00012827",
"PUB00059146",
"PUB00059147",
"PUB00089655",
"PUB00160789"
] | [
"2401401",
"2065971",
"1459459",
"11343402",
"10584000",
"9344630",
"10336622",
"3080312"
] | [
"Two genes specifically expressed in fruiting dikaryons of Schizophyllum commune: homologies with a gene not regulated by mating-type genes.",
"Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation.",
"Developmental and light regulation of eas, the structural gene for the rodl... | [
1990,
1991,
1992,
2001,
1999,
1997,
1999,
1986
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
13,
6155
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Class I Hydrophobin | Class I Hydrophobin | Class_I_Hydrophobin | 3 |
IPR001341 | 1,341 | Aspartate kinase | Asp_kinase | Family | 42,659 | false | false | Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids -lysine, threonine, methionine and isoleucine -in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential compo... | [
"GO:0004072",
"GO:0008652"
] | [
"aspartate kinase activity",
"amino acid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR00657"
] | [
"asp_kinases"
] | [
42659
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"2.7.2.4",
"GenProp0160",
"GenProp1358",
"GenProp1419",
"GenProp1475",
"GenProp1553",
"GenProp1581",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PWY-6160",
"PWY-6559",
"PWY-6562",
"PWY-7153",
"PWY-7977",
"PWY-8088",
"PWY-8179",
"PWY-8296",
"PDOC00289"
] | [
"EC:2.7.2.4",
"GP:GenProp0160",
"GP:GenProp1358",
"GP:GenProp1419",
"GP:GenProp1475",
"GP:GenProp1553",
"GP:GenProp1581",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"METACYC:PWY-6160",
"METACYC:PWY-6559",
"METACYC:PWY-6562",
"METACYC:PWY-7153",
"METACYC:PWY-7977",
"MET... | 19 | [
"2cdq",
"2hmf",
"2j0w",
"2j0x",
"3aaw",
"3ab2",
"3ab4",
"3c1m",
"3c1n",
"3c20",
"3l76",
"3tvi",
"5yei"
] | 13 | [
"PUB00002476",
"PUB00034672"
] | [
"2892836",
"11352712"
] | [
"Structure of the yeast HOM3 gene which encodes aspartokinase.",
"The central enzymes of the aspartate family of amino acid biosynthesis."
] | [
1988,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
779,
36734,
4658,
2,
486
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
23,
3,
1,
24,
1,
1,
38
] | 7 | true | Family | Aspartate kinase | Aspartate kinase | Asp_kinase | 8 |
IPR001342 | 1,342 | Homoserine dehydrogenase, catalytic | HDH_cat | Domain | 36,390 | false | false | This entry represents the catalytic domain of homoserine dehydrogenase. Homoserine dehydrogenase ( ) catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta-semialdehyde into homoserine [ , ]. Homoserine is an intermediate in the biosynthesis of threonine, isoleucine, and met... | [
"GO:0006520"
] | [
"amino acid metabolic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00742"
] | [
"Homoserine_dh"
] | [
36390
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC"
] | [
"1.1.1.3",
"GenProp0159",
"GenProp1358",
"GenProp1419",
"GenProp1475",
"GenProp1553",
"GenProp1581",
"PDOC00800"
] | [
"EC:1.1.1.3",
"GP:GenProp0159",
"GP:GenProp1358",
"GP:GenProp1419",
"GP:GenProp1475",
"GP:GenProp1553",
"GP:GenProp1581",
"PROSITEDOC:PDOC00800"
] | 8 | [
"1ebf",
"1ebu",
"1q7g",
"1tve",
"2ejw",
"3c8m",
"3do5",
"3ing",
"3jsa",
"3mtj",
"4pg4",
"4pg5",
"4pg6",
"4pg7",
"4pg8",
"4xb1",
"4xb2",
"4ydr",
"5avo",
"5x9d",
"5xdf",
"6a0r",
"6a0s",
"6a0t",
"6a0u",
"6dzs",
"7f4b",
"7f4c",
"7m92"
] | 29 | [
"PUB00000699",
"PUB00001656",
"PUB00021481",
"PUB00034672"
] | [
"8395899",
"8500624",
"10700284",
"11352712"
] | [
"Evolutionary comparisons of three enzymes of the threonine biosynthetic pathway among several microbial species.",
"Evolutionary relationships between yeast and bacterial homoserine dehydrogenases.",
"Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.",
"T... | [
1993,
1993,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
902,
30578,
4281,
629
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
21,
2,
1,
17,
1,
1,
27
] | 7 | true | Domain | Homoserine dehydrogenase, catalytic | Homoserine dehydrogenase, catalytic | HDH_cat | 4 |
IPR001343 | 1,343 | RTX calcium-binding nonapeptide repeat | Hemolysn_Ca-bd | Repeat | 45,848 | false | false | Gram-negative bacteria produce a number of proteins that are secreted into the growth medium by a mechanism by the type I secretion system that does not require a cleaved N-terminal signal sequence. These proteins, while having different functions, share two properties: they bind calcium and they contain a multiple tan... | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00353"
] | [
"HemolysinCabind"
] | [
45848
] | 1 | [
"GP",
"PROSITEDOC",
"REACTOME"
] | [
"GenProp0059",
"PDOC00293",
"R-HSA-9760173"
] | [
"GP:GenProp0059",
"PROSITEDOC:PDOC00293",
"REACTOME:R-HSA-9760173"
] | 3 | [
"1af0",
"1akl",
"1g9k",
"1go7",
"1go8",
"1h71",
"1jiw",
"1k7g",
"1k7i",
"1k7q",
"1kap",
"1o0q",
"1o0t",
"1om6",
"1om7",
"1om8",
"1omj",
"1sat",
"1smp",
"1srp",
"2agm",
"2ml1",
"2ml3",
"2qua",
"2qub",
"2z8x",
"2z8z",
"2zj6",
"2zj7",
"2zvd",
"3a6z",
"3a70"... | 57 | [
"PUB00001195",
"PUB00001236",
"PUB00085155"
] | [
"2303029",
"8253063",
"27058787"
] | [
"The Rhizobium nodulation gene nodO encodes a Ca2(+)-binding protein that is exported without N-terminal cleavage and is homologous to haemolysin and related proteins.",
"Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll ... | [
1990,
1993,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
68,
45034,
2,
443,
301
] | 5 | [] | [] | 0 | true | Repeat | RTX calcium-binding nonapeptide repeat | RTX calcium-binding nonapeptide repeat | Hemolysn_Ca-bd | 3 |
IPR001344 | 1,344 | Chlorophyll A-B binding protein, plant and chromista | Chloro_AB-bd_pln | Family | 19,090 | false | false | The light-harvesting complex (LHC) consists of chlorophylls A and B and the chlorophyll A-B binding protein. LHC functions as a light receptor that captures and delivers excitation energy to photosystems I and II with which it is closely associated. Under changing light conditions, the reversible phosphorylation of lig... | [
"GO:0009765",
"GO:0016020"
] | [
"photosynthesis, light harvesting",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR21649"
] | [
""
] | [
19090
] | 1 | [] | [] | [] | 0 | [
"1rwt",
"1vcr",
"2bhw",
"2o01",
"2wsc",
"2wse",
"2wsf",
"3jcu",
"3lw5",
"3pl9",
"4lcz",
"4rku",
"4xk8",
"4y28",
"5l8r",
"5mdx",
"5xnl",
"5xnm",
"5xnn",
"5xno",
"5zgb",
"5zgh",
"5zji",
"6a2w",
"6fos",
"6igz",
"6ijj",
"6ijo",
"6j3y",
"6j3z",
"6j40",
"6jlu"... | 166 | [
"PUB00015383",
"PUB00015384",
"PUB00015385"
] | [
"15225658",
"10682866",
"15033974"
] | [
"NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina.",
"The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis.",
"Regulation of p... | [
2004,
2000,
2004
] | 3 | [
"IPR022796"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
72,
18988,
4,
26
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
73,
51,
116
] | 3 | true | Family | Chlorophyll A-B binding protein, plant and chromista | Chlorophyll A-B binding protein, plant and chromista | Chloro_AB-bd_pln | 2 |
IPR001345 | 1,345 | Phosphoglycerate/bisphosphoglycerate mutase, active site | PG/BPGM_mutase_AS | Active_site | 62,799 | false | false | Phosphoglycerate mutase ( ) (PGAM) and bisphosphoglycerate mutase ( ) (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate [ , , ]. Both enzymes can catalyse three different reactions with different specificities, the... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00175"
] | [
"PG_MUTASE"
] | [
62799
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"5.4.2",
"5.4.2.11",
"PWY-1622",
"PWY-5484",
"PWY-8004",
"PWY-8404",
"PDOC00158",
"R-BTA-5628897",
"R-BTA-6798695",
"R-BTA-70171",
"R-BTA-70263",
"R-BTA-9634600",
"R-CEL-9634600",
"R-DDI-6798695",
"R-DDI-70171",
"R-DDI-70263",
"R-DRE-5628897",
"R-GGA-352875",
"R-GGA-352882",
"R... | [
"EC:5.4.2",
"EC:5.4.2.11",
"METACYC:PWY-1622",
"METACYC:PWY-5484",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"PROSITEDOC:PDOC00158",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70171",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-9634600",
"REACTOME:R-CEL-9634600",
"REACTO... | 44 | [
"1bif",
"1bq3",
"1bq4",
"1c7z",
"1c80",
"1c81",
"1e58",
"1e59",
"1ebb",
"1fbt",
"1fzt",
"1h2e",
"1h2f",
"1k6m",
"1qhf",
"1rii",
"1t8p",
"1tip",
"1v37",
"1v7q",
"1xq9",
"1yfk",
"1yjx",
"2a9j",
"2axn",
"2dwo",
"2dwp",
"2ekb",
"2ekz",
"2enu",
"2enw",
"2eoa"... | 137 | [
"PUB00000183",
"PUB00001554",
"PUB00002873",
"PUB00003558",
"PUB00004695",
"PUB00007922"
] | [
"2847721",
"2831102",
"7929373",
"6294454",
"2557623",
"10958932"
] | [
"Molecular cloning and nucleotide sequence of murine 2,3-bisphosphoglycerate mutase cDNA.",
"Sequence of the gene encoding phosphoglycerate mutase from Saccharomyces cerevisiae.",
"The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin.... | [
1988,
1988,
1994,
1982,
1989,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
264,
34693,
27254,
8,
580
] | 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",... | [
35,
4,
32,
17,
3,
36,
39,
4,
44,
51,
6,
5,
88
] | 13 | true | Active_site | Phosphoglycerate/bisphosphoglycerate mutase, active site | Phosphoglycerate/bisphosphoglycerate mutase, active site | PG/BPGM_mutase_AS | 1 |
IPR001346 | 1,346 | Interferon regulatory factor, DNA-binding domain | Interferon_reg_fact_DNA-bd_dom | Domain | 11,273 | false | false | Viral infections induce the expression of type I interferons (IFN-alpha and IFN-beta) genes. The induction is due to the transcriptional activation of the IFN genes. Interferon regulatory factor I (IRF-1) is one of the transcription factors responsible for that activation. IRF-1 binds to an upstream regulatory cis elem... | [
"GO:0000976"
] | [
"transcription cis-regulatory region binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00605",
"PR00267",
"PS51507",
"SM00348",
"cd00103"
] | [
"IRF",
"INTFRNREGFCT",
"IRF_2",
"IRF",
"IRF"
] | [
11083,
10494,
11237,
10853,
10075
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00522",
"R-BTA-1169408",
"R-BTA-1606341",
"R-BTA-168928",
"R-BTA-3134973",
"R-BTA-3270619",
"R-BTA-9013973",
"R-BTA-918233",
"R-BTA-933541",
"R-BTA-936440",
"R-BTA-936964",
"R-GGA-1227882",
"R-GGA-433819",
"R-GGA-434136",
"R-HSA-1169408",
"R-HSA-1606341",
"R-HSA-168928",
"R-HS... | [
"PROSITEDOC:PDOC00522",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1606341",
"REACTOME:R-BTA-168928",
"REACTOME:R-BTA-3134973",
"REACTOME:R-BTA-3270619",
"REACTOME:R-BTA-9013973",
"REACTOME:R-BTA-918233",
"REACTOME:R-BTA-933541",
"REACTOME:R-BTA-936440",
"REACTOME:R-BTA-936964",
"REACTOME:R-GGA... | 53 | [
"1if1",
"1irf",
"1irg",
"1t2k",
"2dll",
"2irf",
"2o61",
"2o6g",
"2pi0",
"3qu3",
"3qu6",
"4hlx",
"4hly",
"4p55",
"6td4",
"7jm4",
"7o56",
"7ogs",
"7oot",
"7rh2",
"8hcl",
"8hcm",
"8hcs",
"8jkl",
"8jkn",
"8jko",
"8jkq",
"8jks"
] | 28 | [
"PUB00003185",
"PUB00003680",
"PUB00004269",
"PUB00004709",
"PUB00055524"
] | [
"2691585",
"1630447",
"9422515",
"2111015",
"10933732"
] | [
"Regulation of interferon-beta gene: structure and function of cis-elements and trans-acting factors.",
"Subunit of an alpha-interferon-responsive transcription factor is related to interferon regulatory factor and Myb families of DNA-binding proteins.",
"Structure of IRF-1 with bound DNA reveals determinants o... | [
1989,
1992,
1998,
1990,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Haloplanus litoreus",
"Rhadinovirus"
] | [
11,
11161,
1,
100
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
32,
115,
58,
37
] | 4 | true | Domain | Interferon regulatory factor, DNA-binding domain | Interferon regulatory factor, DNA-binding domain | Interferon_reg_fact_DNA-bd_dom | 2 |
IPR001347 | 1,347 | SIS domain | SIS_dom | Domain | 160,625 | false | false | The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteins that have a role in phosphosugar isomerization or regulation [ ]. In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugar... | [
"GO:0097367",
"GO:1901135"
] | [
"carbohydrate derivative binding",
"carbohydrate derivative metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF01380",
"PF13580",
"PF22645",
"PS51464"
] | [
"SIS",
"SIS_2",
"GKRP_SIS_N",
"SIS"
] | [
122093,
20262,
13318,
154168
] | 4 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1522",
"GenProp1624",
"R-HSA-170822",
"R-HSA-381038",
"R-HSA-4085023",
"R-HSA-446210",
"R-HSA-5619107",
"R-MMU-170822",
"R-MMU-446210",
"R-RNO-170822",
"R-RNO-446210",
"R-SCE-446210",
"R-SPO-446210"
] | [
"GP:GenProp1522",
"GP:GenProp1624",
"REACTOME:R-HSA-170822",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-4085023",
"REACTOME:R-HSA-446210",
"REACTOME:R-HSA-5619107",
"REACTOME:R-MMU-170822",
"REACTOME:R-MMU-446210",
"REACTOME:R-RNO-170822",
"REACTOME:R-RNO-446210",
"REACTOME:R-SCE-446210",
"REA... | 13 | [
"1j5x",
"1jeo",
"1jxa",
"1m3s",
"1moq",
"1mor",
"1mos",
"1nri",
"1tk9",
"1tzb",
"1tzc",
"1vim",
"1viv",
"1x92",
"1x94",
"1x9h",
"1x9i",
"2a3n",
"2aml",
"2cb0",
"2dec",
"2df8",
"2e5f",
"2i22",
"2i2w",
"2j6h",
"2poc",
"2put",
"2puv",
"2puw",
"2v4m",
"2vf4"... | 132 | [
"PUB00005296",
"PUB00005498",
"PUB00067028",
"PUB00069412",
"PUB00070737",
"PUB00151607",
"PUB00152605",
"PUB00152606"
] | [
"9739095",
"10203754",
"23621087",
"23733961",
"18049859",
"24226772",
"23957911",
"24251551"
] | [
"Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.",
"The SIS domain: a phosphosugar-binding domain.",
"Crystal Structure of Glucokinase Regulatory Protein.",
"Molecular basis for the role o... | [
1998,
1999,
2013,
2013,
2008,
2013,
2013,
2013
] | 8 | [] | [
"IPR035464",
"IPR035466",
"IPR035472",
"IPR035474",
"IPR035484",
"IPR035488",
"IPR035490"
] | 0 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2412,
144555,
11264,
122,
2272
] | 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",... | [
8,
3,
6,
12,
12,
16,
5,
2,
10,
17,
2,
1,
14
] | 13 | true | Domain | SIS domain | SIS domain | SIS_dom | 9 |
IPR001349 | 1,349 | Cytochrome c oxidase, subunit VIa | Cyt_c_oxidase_su6a | Family | 4,872 | false | false | Cytochrome c oxidase ( ) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ ]. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plas... | [
"GO:0005743"
] | [
"mitochondrial inner membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF02046",
"PIRSF000277",
"PTHR11504",
"cd00925"
] | [
"COX6A",
"COX6A1",
"",
"Cyt_c_Oxidase_VIa"
] | [
4432,
2399,
4666,
1708
] | 4 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1426",
"PDOC01032",
"R-BTA-5628897",
"R-BTA-611105",
"R-BTA-9707564",
"R-BTA-9864848",
"R-HSA-5628897",
"R-HSA-611105",
"R-HSA-9707564",
"R-HSA-9864848",
"R-MMU-5628897",
"R-MMU-611105",
"R-MMU-9707564",
"R-MMU-9864848",
"R-RNO-5628897",
"R-RNO-611105",
"R-RNO-9707564"
] | [
"GP:GenProp1426",
"PROSITEDOC:PDOC01032",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9864848",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-9707564",
"REACTOME:R-HSA-9864848",
"REACTOME:R-MMU-5628897",
"REACTOME:R-MMU-6111... | 17 | [
"1occ",
"1oco",
"1ocr",
"1ocz",
"1v54",
"1v55",
"2dyr",
"2dys",
"2eij",
"2eik",
"2eil",
"2eim",
"2ein",
"2occ",
"2y69",
"2ybb",
"2zxw",
"3abk",
"3abl",
"3abm",
"3ag1",
"3ag2",
"3ag3",
"3ag4",
"3asn",
"3aso",
"3wg7",
"3x2q",
"5b1a",
"5b1b",
"5b3s",
"5gpn"... | 125 | [
"PUB00000581",
"PUB00000674",
"PUB00079537"
] | [
"6307356",
"9107314",
"12909344"
] | [
"Structure of cytochrome c oxidase.",
"The cDNA sequences of cytochrome c oxidase subunit VIa from carp and rainbow trout suggest the absence of isoforms in fishes.",
"A third isoform of cytochrome c oxidase subunit VIII is present in mammals."
] | [
1983,
1997,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Ectobacillus ponti",
"Eukaryota"
] | [
1,
4871
] | 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... | [
6,
1,
3,
3,
6,
4,
2,
2,
6,
1,
1,
6
] | 12 | true | Family | Cytochrome c oxidase, subunit VIa | Cytochrome c oxidase, subunit VIa | Cyt_c_oxidase_su6a | 6 |
IPR001351 | 1,351 | Small ribosomal subunit protein uS3, C-terminal | Ribosomal_uS3_C | Domain | 50,155 | false | false | This entry represents the C-terminal domain of the small ribosomal subunit protein uS3. Small ribosomal subunit protein uS3 was previously known as Ribosomal protein S3. In Escherichia coli, S3 is known to be involved in the binding of initiator Met-tRNA. This family of ribosomal proteins includes S3 from bacteria, alg... | [
"GO:0003735",
"GO:0006412"
] | [
"structural constituent of ribosome",
"translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00189"
] | [
"Ribosomal_S3_C"
] | [
50155
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00474",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R... | [
"PROSITEDOC:PDOC00474",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827"... | 111 | [
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo",
"1xmq",
"1xnq",
"1xnr",
"2e5l",
"2f4v"... | 1,730 | [
"PUB00005188",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"8036511",
"11297922",
"11290319",
"11114498"
] | [
"Conserved structures and diversity of functions of RNA-binding proteins.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1994,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
951,
24176,
24308,
720
] | 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",... | [
16,
1,
1,
3,
1,
8,
8,
1,
12,
13,
1,
1,
17
] | 13 | true | Domain | Small ribosomal subunit protein uS3, C-terminal | Small ribosomal subunit protein uS3, C-terminal | Ribosomal_uS3_C | 4 |
IPR001352 | 1,352 | Ribonuclease HII/HIII | RNase_HII/HIII | Family | 34,852 | false | false | This family includes ribonuclease HII and HIII. Ribonuclease H (RNase H) ( ) is a member of the ribonuclease family, which recognises and cleaves the RNA strand of RNA-DNA heteroduplexes. The enzyme is widely present in all three kingdoms of living organisms, including bacteria, archaea, and eukaryotes, and their count... | [
"GO:0003723",
"GO:0004523"
] | [
"RNA binding",
"RNA-DNA hybrid ribonuclease activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PANTHER"
] | [
"PTHR10954"
] | [
""
] | [
34852
] | 1 | [
"EC"
] | [
"3.1.26.4"
] | [
"EC:3.1.26.4"
] | 1 | [
"1eke",
"1i39",
"1i3a",
"1io2",
"1uax",
"1x1p",
"2d0a",
"2d0b",
"2d0c",
"2dfe",
"2dff",
"2dfh",
"2etj",
"3asm",
"3kio",
"3o3f",
"3o3g",
"3o3h",
"3p56",
"3p5j",
"3p83",
"3puf",
"3vn5",
"4hht",
"4py5",
"5y9p",
"7uwe",
"7uwh",
"8yjz"
] | 29 | [
"PUB00006422",
"PUB00006461",
"PUB00015351",
"PUB00015352",
"PUB00015353",
"PUB00025090",
"PUB00040141",
"PUB00042692",
"PUB00079405",
"PUB00081183",
"PUB00096386",
"PUB00100891"
] | [
"9741851",
"10603172",
"2169648",
"8108376",
"1707186",
"11083878",
"16343535",
"17964265",
"19228198",
"17663799",
"16093691",
"31371183"
] | [
"Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension.",
"Sequence and comparative structural analysis of the murine leukaemia virus amphotropic strain 4070A RNase H domain.",
"Structure of ribonuclease H phased at 2 A re... | [
1998,
1999,
1990,
1993,
1991,
2001,
2006,
2007,
2009,
2007,
2005,
2019
] | 12 | [] | [
"IPR004641",
"IPR004649",
"IPR022898"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
989,
28372,
4627,
18,
846
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
6,
1,
2,
11,
1,
5,
4,
1,
2,
5,
1,
1,
8
] | 13 | true | Family | Ribonuclease HII/HIII | Ribonuclease HII/HIII | RNase_HII/HIII | 7 |
IPR001353 | 1,353 | Proteasome, subunit alpha/beta | Proteasome_sua/b | Family | 104,515 | false | false | ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, clpXP) complex in other eubacteria. Gen... | [
"GO:0030163",
"GO:0005839"
] | [
"protein catabolic process",
"proteasome core complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00227"
] | [
"Proteasome"
] | [
104515
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.25",
"R-BTA-1169091",
"R-BTA-1234176",
"R-BTA-1236974",
"R-BTA-1236978",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-187577",
"R-BTA-195253",
"R-BTA-202424",
"R-BTA-2467813",
"R-BTA-2871837",
"R-BTA-349425",
"R-BTA-350562",
"R-BTA-382556",
"R-BTA-450... | [
"EC:3.4.25",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1236974",
"REACTOME:R-BTA-1236978",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACTOME:R-BTA-174178",
"REACTOME:R-BTA-174184",
"REACTOME:R-BTA-187577",
"REACTOME:R-BTA-195253",
"REACTOME:R-BTA-202424",
... | 461 | [
"1e94",
"1fnt",
"1g0u",
"1g3i",
"1g3k",
"1g4a",
"1g4b",
"1g65",
"1hqy",
"1ht1",
"1ht2",
"1iru",
"1j2p",
"1j2q",
"1jd2",
"1jjw",
"1kyi",
"1m4y",
"1ned",
"1ofh",
"1ofi",
"1pma",
"1q5q",
"1q5r",
"1ryp",
"1ya7",
"1yar",
"1yau",
"1yyf",
"1z7q",
"2f16",
"2fak"... | 658 | [
"PUB00000148",
"PUB00000524",
"PUB00001329",
"PUB00004123",
"PUB00005460",
"PUB00011906",
"PUB00014349",
"PUB00014350",
"PUB00030848",
"PUB00080992"
] | [
"2643381",
"7682410",
"7697118",
"1317508",
"8882582",
"12446803",
"12646382",
"12823960",
"9087403",
"2535672"
] | [
"The multicatalytic proteinase of mammalian cells.",
"Proteasomes: multicatalytic proteinase complexes.",
"Proteasomes. Multicatalytic proteinase complexes.",
"Proteolysis, proteasomes and antigen presentation.",
"Proteasomes: destruction as a programme.",
"Eubacterial HslV and HslU subunits homologs in p... | [
1989,
1993,
1993,
1992,
1996,
2002,
2003,
2003,
1997,
1989
] | 10 | [] | [
"IPR022281",
"IPR023332",
"IPR023333"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2713,
22784,
78405,
64,
549
] | 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",... | [
81,
15,
43,
45,
1,
104,
68,
15,
54,
97,
14,
14,
207
] | 13 | true | Family | Proteasome, subunit alpha/beta | Proteasome, subunit alpha/beta | Proteasome_sua/b | 4 |
IPR001355 | 1,355 | CXC chemokine receptor 1 | Chemokine_CXCR1 | Family | 74 | false | false | Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang... | [
"GO:0016494",
"GO:0019959",
"GO:0006935",
"GO:0007186",
"GO:0016020"
] | [
"C-X-C chemokine receptor activity",
"interleukin-8 binding",
"chemotaxis",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00572"
] | [
"INTRLEUKN8AR"
] | [
74
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"68",
"R-HSA-380108",
"R-HSA-418594",
"R-HSA-6798695"
] | [
"IUPHAR:68",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6798695"
] | 4 | [
"2lnl",
"8ic0"
] | 2 | [
"PUB00009401",
"PUB00064589",
"PUB00064621",
"PUB00064622",
"PUB00064810",
"PUB00064812",
"PUB00064819",
"PUB00064820",
"PUB00064821",
"PUB00064822",
"PUB00064834",
"PUB00067945",
"PUB00067946",
"PUB00067948"
] | [
"11544102",
"10714678",
"10601351",
"9500790",
"8384312",
"1379593",
"10878382",
"8955112",
"12239185",
"15967374",
"7527448",
"9689100",
"7592998",
"16720046"
] | [
"Chemokine receptors.",
"Chemokines: a new classification system and their role in immunity.",
"Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.",
"Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte... | [
2001,
2000,
1999,
1998,
1993,
1992,
2000,
1996,
2002,
2005,
1994,
1998,
1995,
2006
] | 14 | [
"IPR000174"
] | [] | 1 | 0 | 1 | [
"Eutheria"
] | [
74
] | 1 | [
"Homo sapiens"
] | [
2
] | 1 | true | Family | CXC chemokine receptor 1 | CXC chemokine receptor 1 | Chemokine_CXCR1 | 5 |
IPR001356 | 1,356 | Homeodomain | HD | Domain | 354,328 | false | false | This entry represents the homeodomain (HD), a protein domain of approximately 60 residues that usually binds DNA. It is encoded by the homeobox sequence [ , , ], which was first identified in a number of Drosophila homeotic and segmentation proteins, but is now known to be well-conserved in many other animals, includin... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00046",
"PS50071",
"SM00389",
"cd00086"
] | [
"Homeodomain",
"HOMEOBOX_2",
"HOX",
"homeodomain"
] | [
283836,
341943,
334742,
345013
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00027",
"R-BTA-1660661",
"R-CEL-2173795",
"R-CEL-373752",
"R-CEL-418885",
"R-CEL-418886",
"R-CEL-4551638",
"R-CEL-9764725",
"R-DDI-8951664",
"R-DDI-983168",
"R-DME-3214847",
"R-DME-373752",
"R-DME-390193",
"R-DME-418885",
"R-DME-418886",
"R-DME-6804759",
"R-DME-6807505",
"R-DM... | [
"PROSITEDOC:PDOC00027",
"REACTOME:R-BTA-1660661",
"REACTOME:R-CEL-2173795",
"REACTOME:R-CEL-373752",
"REACTOME:R-CEL-418885",
"REACTOME:R-CEL-418886",
"REACTOME:R-CEL-4551638",
"REACTOME:R-CEL-9764725",
"REACTOME:R-DDI-8951664",
"REACTOME:R-DDI-983168",
"REACTOME:R-DME-3214847",
"REACTOME:R-DM... | 106 | [
"1ahd",
"1akh",
"1apl",
"1au7",
"1b72",
"1b8i",
"1bw5",
"1cqt",
"1du0",
"1du6",
"1e3o",
"1enh",
"1f43",
"1fjl",
"1ftt",
"1ftz",
"1gt0",
"1hdd",
"1hdp",
"1hf0",
"1hom",
"1ic8",
"1ig7",
"1jgg",
"1k61",
"1kz0",
"1kz2",
"1le8",
"1lfb",
"1lfu",
"1mh3",
"1mh4"... | 261 | [
"PUB00000591",
"PUB00005390",
"PUB00010002",
"PUB00071003",
"PUB00075496",
"PUB00126359",
"PUB00153777",
"PUB00153787"
] | [
"2568852",
"1357790",
"12445403",
"19714215",
"19734295",
"26464018",
"17963489",
"17900520"
] | [
"The structure and function of the homeodomain.",
"The homeobox in perspective.",
"Hox proteins: sculpting body parts by activating localized cell death.",
"The fission yeast homeodomain protein Yox1p binds to MBF and confines MBF-dependent cell-cycle transcription to G1-S via negative feedback.",
"A compre... | [
1989,
1992,
2002,
2009,
2009,
2016,
2007,
2007
] | 8 | [] | [
"IPR008422",
"IPR020479",
"IPR056560",
"IPR058631"
] | 0 | 4 | 0 | [
"Bacteria",
"Eukaryota",
"Megaviricetes",
"Methanobacteriati",
"organismal metagenomes"
] | [
84,
354193,
37,
12,
2
] | 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... | [
472,
143,
971,
293,
866,
639,
7,
243,
711,
9,
2,
720
] | 12 | true | Domain | Homeodomain | Homeodomain | HD | 9 |
IPR001357 | 1,357 | BRCT domain | BRCT_dom | Domain | 118,456 | false | false | The breast cancer susceptibility gene contains at its C terminus two copies of a conserved domain that was named BRCT for BRCA1 C terminus. This domain of about 95 amino acids is found in a large variety of proteins involved in DNA repair, recombination and cell cycle control [ , , ]. The BRCT domain is not limited to ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00533",
"PF12738",
"PF16589",
"PF16770",
"PS50172",
"SM00292"
] | [
"BRCT",
"PTCB-BRCT",
"BRCT_2",
"RTT107_BRCT_5",
"BRCT",
"BRCT"
] | [
75033,
16698,
19365,
8017,
111582,
90617
] | 6 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"6.5.1.2",
"PDOC50172",
"R-BTA-110330",
"R-BTA-110331",
"R-BTA-171306",
"R-BTA-171319",
"R-BTA-174411",
"R-BTA-174414",
"R-BTA-174417",
"R-BTA-174430",
"R-BTA-174437",
"R-BTA-2559586",
"R-BTA-5693571",
"R-BTA-9670095",
"R-BTA-9772755",
"R-BTA-9818564",
"R-CEL-112382",
"R-CEL-113418... | [
"EC:6.5.1.2",
"PROSITEDOC:PDOC50172",
"REACTOME:R-BTA-110330",
"REACTOME:R-BTA-110331",
"REACTOME:R-BTA-171306",
"REACTOME:R-BTA-171319",
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174414",
"REACTOME:R-BTA-174417",
"REACTOME:R-BTA-174430",
"REACTOME:R-BTA-174437",
"REACTOME:R-BTA-2559586",
"RE... | 303 | [
"1cdz",
"1dgs",
"1gzh",
"1imo",
"1in1",
"1jnx",
"1kzy",
"1l0b",
"1l7b",
"1n5o",
"1oqa",
"1t15",
"1t29",
"1t2u",
"1t2v",
"1wf6",
"1y98",
"1z56",
"2ado",
"2azm",
"2coe",
"2cok",
"2cou",
"2d8m",
"2dun",
"2e2w",
"2ebu",
"2ebw",
"2ep8",
"2etx",
"2htf",
"2ing"... | 287 | [
"PUB00001320",
"PUB00001533",
"PUB00001703",
"PUB00003902",
"PUB00026458",
"PUB00031299",
"PUB00094292"
] | [
"9799248",
"9034168",
"9000507",
"8673121",
"11573086",
"15133503",
"15501676"
] | [
"Structure of an XRCC1 BRCT domain: a new protein-protein interaction module.",
"A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.",
"From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair.",
"BRCA1 protein products ... Functional motifs...",
... | [
1998,
1997,
1997,
1996,
2001,
2004,
2004
] | 7 | [] | [
"IPR031916",
"IPR044737",
"IPR045080",
"IPR047249",
"IPR047250",
"IPR049935",
"IPR049936",
"IPR059215"
] | 0 | 8 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
361,
32156,
84673,
462,
804
] | 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",... | [
118,
29,
116,
38,
1,
195,
73,
17,
71,
93,
10,
14,
174
] | 13 | true | Domain | BRCT domain | BRCT domain | BRCT_dom | 5 |
IPR001358 | 1,358 | Neuropeptide Y2 receptor | NPY2_rcpt | Family | 1,539 | false | false | Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01014"
] | [
"NRPEPTIDEY2R"
] | [
1539
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"306",
"R-GGA-375276",
"R-GGA-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594"
] | [
"IUPHAR:306",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594"
] | 7 | [
"7x9b",
"7yon",
"7yoo",
"8k6n"
] | 4 | [
"PUB00063739",
"PUB00063740",
"PUB00063741",
"PUB00063742",
"PUB00063743",
"PUB00063744",
"PUB00063745",
"PUB00063746",
"PUB00063747",
"PUB00063748",
"PUB00063749",
"PUB00063750",
"PUB00063751",
"PUB00063752",
"PUB00063753",
"PUB00063754",
"PUB00063755",
"PUB00063756",
"PUB000637... | [
"6549409",
"16874931",
"6547387",
"6549039",
"2821236",
"8395947",
"16190896",
"7529442",
"7644568",
"15337373",
"8685245",
"8369959",
"11287113",
"7629398",
"6133408",
"3855566",
"12678499",
"17222466",
"8013354",
"9833945",
"9389418",
"9446690",
"2453065",
"1661086",
... | [
"Neuropeptide Y: a potent inducer of consummatory behavior in rats.",
"Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.",
"Neuropeptide Y and human pancreatic polypeptide stimulate feeding behavior in rats.",
"Neuropeptide Y: stimulation of feeding and drinking by injection into the... | [
1984,
2006,
1984,
1984,
1987,
1993,
2005,
1994,
1995,
2004,
1996,
1993,
2001,
1995,
1982,
1985,
2003,
2007,
1994,
1998,
1997,
1998,
1988,
1991,
1995,
2003,
2007,
1998,
2004,
2007,
2007,
2007,
2006,
2007,
2006,
2007,
2008,
1996,
1996,
1998... | 47 | [
"IPR000611"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1539
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
1,
2,
3
] | 4 | true | Family | Neuropeptide Y2 receptor | Neuropeptide Y2 receptor | NPY2_rcpt | 6 |
IPR001360 | 1,360 | Glycoside hydrolase family 1 | Glyco_hydro_1 | Family | 80,083 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00232",
"PR00131",
"PTHR10353"
] | [
"Glyco_hydro_1",
"GLHYDRLASE1",
""
] | [
80032,
68831,
77376
] | 3 | [
"CAZY",
"EC",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GH1",
"3.2.1",
"GenProp1302",
"GenProp1547",
"GenProp1600",
"GenProp1652",
"PDOC00495",
"R-HSA-109704",
"R-HSA-1257604",
"R-HSA-1307965",
"R-HSA-189085",
"R-HSA-190374",
"R-HSA-2219530",
"R-HSA-5654219",
"R-HSA-5654228",
"R-HSA-5654687",
"R-HSA-5654688",
"R-HSA-5654689",
"R-HSA-... | [
"CAZY:GH1",
"EC:3.2.1",
"GP:GenProp1302",
"GP:GenProp1547",
"GP:GenProp1600",
"GP:GenProp1652",
"PROSITEDOC:PDOC00495",
"REACTOME:R-HSA-109704",
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-1307965",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-190374",
"REACTOME:R-HSA-2219530",
"REACTOME:R-HSA-5... | 57 | [
"1bga",
"1bgg",
"1cbg",
"1dwa",
"1dwf",
"1dwg",
"1dwh",
"1dwi",
"1dwj",
"1e1e",
"1e1f",
"1e4i",
"1e4l",
"1e4m",
"1e4n",
"1e55",
"1e56",
"1e6q",
"1e6s",
"1e6x",
"1e70",
"1e71",
"1e72",
"1e73",
"1gnx",
"1gon",
"1gow",
"1h49",
"1hxj",
"1myr",
"1np2",
"1od0"... | 342 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [
"IPR005928",
"IPR017736"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
234,
41901,
37571,
11,
366
] | 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",... | [
314,
2,
31,
1,
3,
17,
10,
1,
94,
17,
230
] | 11 | true | Family | Glycoside hydrolase family 1 | Glycoside hydrolase family 1 | Glyco_hydro_1 | 3 |
IPR001361 | 1,361 | Gp90 envelope polyprotein of equine infectious anemia virus (EIAV) | Gp90_EIAV | Family | 1,975 | false | false | Equine infectious anemia virus(EIAV) belongs to the family retroviridae. EIAV gp90 is hypervariable in the carboxyl-end region and more stable in the amino-end region. This variability is a pathogenicity factor that allows the evasion of the host's immune response [ ]. | [
"GO:0005198",
"GO:0019031"
] | [
"structural molecule activity",
"viral envelope"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00971"
] | [
"EIAV_GP90"
] | [
1975
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003494"
] | [
"1649329"
] | [
"Characterization of variable regions in the envelope and S3 open reading frame of equine infectious anemia virus."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses"
] | [
2,
1973
] | 2 | [] | [] | 0 | true | Family | Gp90 envelope polyprotein of equine infectious anemia virus (EIAV) | Gp90 envelope polyprotein of equine infectious anemia virus (EIAV) | Gp90_EIAV | 1 |
IPR001362 | 1,362 | Glycoside hydrolase, family 32 | Glyco_hydro_32 | Family | 28,334 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SMART"
] | [
"SM00640"
] | [
"Glyco_32"
] | [
28334
] | 1 | [
"CAZY",
"EC",
"EC",
"METACYC",
"PROSITEDOC"
] | [
"GH32",
"3.2.1",
"3.2.1.26",
"PWY-8314",
"PDOC00532"
] | [
"CAZY:GH32",
"EC:3.2.1",
"EC:3.2.1.26",
"METACYC:PWY-8314",
"PROSITEDOC:PDOC00532"
] | 5 | [
"1st8",
"1uyp",
"1w2t",
"1y4w",
"1y9g",
"1y9m",
"2ac1",
"2add",
"2ade",
"2aey",
"2aez",
"2oxb",
"2qqu",
"2qqv",
"2qqw",
"2xqr",
"3kf3",
"3kf5",
"3ldk",
"3ldr",
"3lem",
"3lf7",
"3lfi",
"3lig",
"3lih",
"3pig",
"3pij",
"3rwk",
"3sc7",
"3u14",
"3u75",
"3ugf"... | 84 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [
"IPR006232"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"metagenomes"
] | [
16145,
11937,
149,
5,
98
] | 5 | [
"Arabidopsis thaliana",
"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)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
52,
1,
53,
1,
2,
66
] | 6 | true | Family | Glycoside hydrolase, family 32 | Glycoside hydrolase, family 32 | Glyco_hydro_32 | 7 |
IPR001364 | 1,364 | Haemagglutinin, influenzavirus A/B | Hemagglutn_influenz_A/B | Family | 155,569 | 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 | [
"HAMAP",
"PFAM",
"PRINTS"
] | [
"MF_04072",
"PF00509",
"PR00329"
] | [
"INFV_HEMA",
"Hemagglutinin",
"HEMAGGLUTN12"
] | [
115747,
155369,
137661
] | 3 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1012",
"R-HSA-168255",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168336",
"R-HSA-168874",
"R-HSA-192823",
"R-HSA-198933"
] | [
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-168874",
"REACTOME:R-HSA-192823",
"REACTOME:R-HSA-198933"
] | 12 | [
"1eo8",
"1ha0",
"1hgd",
"1hge",
"1hgf",
"1hgg",
"1hgh",
"1hgi",
"1hgj",
"1htm",
"1jsd",
"1jsh",
"1jsi",
"1jsm",
"1jsn",
"1jso",
"1ken",
"1mql",
"1mqm",
"1mqn",
"1qfu",
"1qu1",
"1rd8",
"1ru7",
"1ruy",
"1ruz",
"1rv0",
"1rvt",
"1rvx",
"1rvz",
"1ti8",
"2fk0"... | 808 | [
"PUB00033162",
"PUB00033164",
"PUB00033165"
] | [
"16543414",
"15475582",
"16178512"
] | [
"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 influenza a virus."
] | [
2006,
2005,
2005
] | 3 | [] | [
"IPR000149",
"IPR000386"
] | 0 | 2 | 0 | [
"Bacteria",
"Negarnaviricota"
] | [
25,
155544
] | 2 | [] | [] | 0 | true | Family | Haemagglutinin, influenzavirus A/B | Haemagglutinin, influenzavirus A/B | Hemagglutn_influenz_A/B | 7 |
IPR001365 | 1,365 | Adenosine deaminase domain | A_deaminase_dom | Domain | 37,263 | false | false | This entry represents the main structural domain of adenosine deaminase proteins. Adenosine deaminases ( ) are monomeric zinc dependent enzymes involved in purine metabolism. They are required for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Adenosine deaminases convert adenosi... | [
"GO:0019239"
] | [
"deaminase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00962"
] | [
"A_deaminase"
] | [
37263
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME... | [
"3.5.4",
"3.5.4.4",
"PWY-6609",
"PWY-6611",
"PWY-7179",
"R-CEL-2161541",
"R-CEL-74217",
"R-DDI-5683826",
"R-DDI-6798695",
"R-DDI-74217",
"R-DDI-9755088",
"R-DME-2161541",
"R-DME-74217",
"R-DRE-2161541",
"R-DRE-5683826",
"R-DRE-6798695",
"R-DRE-74217",
"R-DRE-9755088",
"R-HSA-2161... | [
"EC:3.5.4",
"EC:3.5.4.4",
"METACYC:PWY-6609",
"METACYC:PWY-6611",
"METACYC:PWY-7179",
"REACTOME:R-CEL-2161541",
"REACTOME:R-CEL-74217",
"REACTOME:R-DDI-5683826",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-74217",
"REACTOME:R-DDI-9755088",
"REACTOME:R-DME-2161541",
"REACTOME:R-DME-74217",
"R... | 33 | [
"1a4l",
"1a4m",
"1add",
"1fkw",
"1fkx",
"1krm",
"1ndv",
"1ndw",
"1ndy",
"1ndz",
"1o5r",
"1qxl",
"1uio",
"1uip",
"1uml",
"1v79",
"1v7a",
"1vfl",
"1w1i",
"1wxy",
"1wxz",
"2ada",
"2amx",
"2bgn",
"2e1w",
"2pgf",
"2pgr",
"2qvn",
"2z7g",
"3ewc",
"3ewd",
"3iar"... | 77 | [
"PUB00000343",
"PUB00059155"
] | [
"1998686",
"14643670"
] | [
"Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function.",
"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family."
] | [
1991,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
33,
23481,
13350,
399
] | 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",... | [
7,
3,
6,
13,
1,
50,
5,
3,
3,
10,
1,
2,
8
] | 13 | true | Domain | Adenosine deaminase domain | Adenosine deaminase domain | A_deaminase_dom | 9 |
IPR001367 | 1,367 | Iron dependent repressor, metal binding and dimerisation domain | Fe_dep_repressor | Domain | 20,812 | false | false | The diphtheria toxin repressor protein (DTXR) is a member of this group [ ]. In Corynebacterium diphtheriae where it has been studied in some detail this protein acts as an iron-binding repressor of diphtheria toxin gene expression and may serve as a global regulator of gene expression. DTXR comprises an N-terminal DNA... | [
"GO:0046914",
"GO:0046983"
] | [
"transition metal ion binding",
"protein dimerization activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF02742"
] | [
"Fe_dep_repr_C"
] | [
20812
] | 1 | [
"PROSITEDOC"
] | [
"PDOC50944"
] | [
"PROSITEDOC:PDOC50944"
] | 1 | [
"1b1b",
"1bi0",
"1bi1",
"1bi2",
"1bi3",
"1c0w",
"1ddn",
"1dpr",
"1f5t",
"1fwz",
"1fx7",
"1g3s",
"1g3t",
"1g3w",
"1g3y",
"1on1",
"1on2",
"1p92",
"1u8r",
"1xcv",
"2dtr",
"2ev0",
"2ev5",
"2ev6",
"2f5c",
"2f5d",
"2f5e",
"2f5f",
"2h09",
"2hyf",
"2hyg",
"2isy"... | 69 | [
"PUB00004874",
"PUB00005267"
] | [
"7568230",
"7743135"
] | [
"Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.",
"Three-dimensional structure of the diphtheria toxin repressor in complex with divalent cation co-repressors."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctevH2",
"unclassified sequences"
] | [
1753,
18667,
21,
1,
370
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Iron dependent repressor, metal binding and dimerisation domain | Iron dependent repressor, metal binding and dimerisation domain | Fe_dep_repressor | 7 |
IPR001368 | 1,368 | TNFR/NGFR cysteine-rich region | TNFR/NGFR_Cys_rich_reg | Domain | 27,223 | false | false | A number of proteins, some of which are known to be receptors for growth factors, have been found to contain a cysteine-rich domain of about 110 to 160 amino acids in their N-terminal part, that can be subdivided into four (or in some cases, three) modules of about 40 residues containing 6 conserved cysteines. Some of ... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00020",
"PS00652",
"PS50050",
"SM00208"
] | [
"TNFR_c6",
"TNFR_NGFR_1",
"TNFR_NGFR_2",
"TNFR"
] | [
19768,
15404,
23600,
23297
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00561",
"R-BTA-198933",
"R-BTA-5668541",
"R-BTA-5669034",
"R-BTA-5676594",
"R-GGA-193692",
"R-GGA-205017",
"R-GGA-205043",
"R-GGA-209543",
"R-GGA-209560",
"R-GGA-209563",
"R-HSA-140534",
"R-HSA-1474228",
"R-HSA-193634",
"R-HSA-193648",
"R-HSA-193670",
"R-HSA-193681",
"R-HSA-19... | [
"PROSITEDOC:PDOC00561",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-5668541",
"REACTOME:R-BTA-5669034",
"REACTOME:R-BTA-5676594",
"REACTOME:R-GGA-193692",
"REACTOME:R-GGA-205017",
"REACTOME:R-GGA-205043",
"REACTOME:R-GGA-209543",
"REACTOME:R-GGA-209560",
"REACTOME:R-GGA-209563",
"REACTOME:R-HSA-1... | 107 | [
"1d0g",
"1d4v",
"1du3",
"1ext",
"1ft4",
"1jma",
"1ncf",
"1sg1",
"1tnr",
"1za3",
"2aw2",
"2h9g",
"2hev",
"2hey",
"2uwi",
"3alq",
"3buk",
"3ij2",
"3k51",
"3me2",
"3me4",
"3mhd",
"3mi8",
"3qbq",
"3qd6",
"3qo4",
"3thm",
"3tje",
"3u3p",
"3u3q",
"3u3s",
"3u3t"... | 110 | [
"PUB00000892",
"PUB00001018",
"PUB00005358",
"PUB00015257"
] | [
"8387891",
"15335933",
"2174582",
"15335677"
] | [
"Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation.",
"When apoptosis fails.",
"The divergent receptors for TNF.",
"Emerging families of cytokines and receptors."
] | [
1993,
1992,
1990,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
101,
26495,
623,
4
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
7,
2,
112,
4,
98,
77,
2,
88,
3
] | 9 | true | Domain | TNFR/NGFR cysteine-rich region | TNFR/NGFR cysteine-rich region | TNFR/NGFR_Cys_rich_reg | 2 |
IPR001370 | 1,370 | BIR repeat | BIR_rpt | Repeat | 17,031 | false | false | The BIR domain has a fold that is stabilised by zinc tetrahedrally coordinated by one histidine and three cysteine residues. The structure consists of three short α-helices and turns with the zinc packed in an unusually hydrophobic environment created by residues that are highly conserved among all BIRs. A subclass of ... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00653",
"PS01282",
"PS50143",
"SM00238",
"cd00022"
] | [
"BIR",
"BIR_REPEAT_1",
"BIR_REPEAT_2",
"BIR",
"BIR"
] | [
16712,
5694,
16937,
16463,
15194
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00987",
"R-BTA-141444",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-4615885",
"R-BTA-5663220",
"R-BTA-68877",
"R-BTA-8951664",
"R-BTA-9648025",
"R-CFA-168638",
"R-CFA-5357786",
"R-CFA-5357905",
"R-CFA-5357956",
"R-CFA-5668541",
"R-CFA-5675482",
"R-CFA-5676594",
"R-CFA-5689880",
"... | [
"PROSITEDOC:PDOC00987",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-4615885",
"REACTOME:R-BTA-5663220",
"REACTOME:R-BTA-68877",
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-9648025",
"REACTOME:R-CFA-168638",
"REACTOME:R-CFA-5357786",
"REACTOME:R-CF... | 140 | [
"1c9q",
"1e31",
"1f3h",
"1f9x",
"1g3f",
"1g73",
"1i3o",
"1i4o",
"1i51",
"1jd4",
"1jd5",
"1jd6",
"1kmc",
"1m4m",
"1nw9",
"1oxn",
"1oxq",
"1oy7",
"1q4q",
"1qbh",
"1sdz",
"1se0",
"1tfq",
"1tft",
"1tw6",
"1xb0",
"1xb1",
"1xox",
"2i3h",
"2i3i",
"2jk7",
"2opy"... | 170 | [
"PUB00003506",
"PUB00004228",
"PUB00030194",
"PUB00043773"
] | [
"8139034",
"8552191",
"10404221",
"8445726"
] | [
"An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs.",
"Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes.",
"Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat.",
"An apoptosis-inhibiting ... | [
1994,
1996,
1999,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"invertebrate metagenome"
] | [
51,
16479,
492,
9
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
2,
38,
10,
42,
48,
1,
36,
1,
1
] | 9 | true | Repeat | BIR repeat | BIR repeat | BIR_rpt | 7 |
IPR001371 | 1,371 | Glycoside hydrolase, family 14B, plant | Glyco_hydro_14B_pln | Family | 2,995 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0016161",
"GO:0000272"
] | [
"beta-amylase activity",
"polysaccharide catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00842"
] | [
"GLHYDLASE14B"
] | [
2995
] | 1 | [
"CAZY",
"EC",
"METACYC",
"METACYC"
] | [
"GH14",
"3.2.1.2",
"PWY-6724",
"PWY-842"
] | [
"CAZY:GH14",
"EC:3.2.1.2",
"METACYC:PWY-6724",
"METACYC:PWY-842"
] | 4 | [
"1b1y",
"1bfn",
"1btc",
"1bya",
"1byb",
"1byc",
"1byd",
"1fa2",
"1q6c",
"1q6d",
"1q6e",
"1q6f",
"1q6g",
"1uko",
"1ukp",
"1v3h",
"1v3i",
"1wdp",
"1wdq",
"1wdr",
"1wds",
"2dqx",
"2xff",
"2xfr",
"2xfy",
"2xg9",
"2xgb",
"2xgi",
"5wqs",
"5wqu",
"6f9h",
"6f9j"... | 35 | [
"PUB00002354",
"PUB00004870",
"PUB00005266"
] | [
"1491009",
"7624375",
"8535779"
] | [
"Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrol... | [
1992,
1995,
1995
] | 3 | [
"IPR001554"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2995
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
25,
11,
31
] | 3 | true | Family | Glycoside hydrolase, family 14B, plant | Glycoside hydrolase, family 14B, plant | Glyco_hydro_14B_pln | 1 |
IPR001373 | 1,373 | Cullin, N-terminal | Cullin_N | Domain | 30,371 | false | false | This entry represents the N-terminal region of cullin proteins, which consists of several domains, including cullin repeat domain, a 4-helical bundle domain, an α+β domain, and a winged helix-like domain. Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found th... | [
"GO:0031625",
"GO:0006511"
] | [
"ubiquitin protein ligase binding",
"ubiquitin-dependent protein catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00888"
] | [
"Cullin"
] | [
30371
] | 1 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"GenProp1311",
"GenProp1754",
"R-CEL-110314",
"R-CEL-1234176",
"R-CEL-187577",
"R-CEL-195253",
"R-CEL-2565942",
"R-CEL-4641258",
"R-CEL-5632684",
"R-CEL-5696394",
"R-CEL-5696395",
"R-CEL-5696400",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-68949",
"R-CEL-69231",
"R-C... | [
"GP:GenProp1311",
"GP:GenProp1754",
"REACTOME:R-CEL-110314",
"REACTOME:R-CEL-1234176",
"REACTOME:R-CEL-187577",
"REACTOME:R-CEL-195253",
"REACTOME:R-CEL-2565942",
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-5632684",
"REACTOME:R-CEL-5696394",
"REACTOME:R-CEL-5696395",
"REACTOME:R-CEL-5696400",
... | 198 | [
"1ldj",
"1ldk",
"1u6g",
"2hye",
"2wzk",
"3dpl",
"3dqv",
"3rtr",
"4a0c",
"4a0k",
"4a0l",
"4a64",
"4ap2",
"4apf",
"4eoz",
"4f52",
"4hxi",
"4jgh",
"4n9f",
"4p5o",
"4wqo",
"5n4w",
"5nlb",
"6i2m",
"6r6h",
"6r7f",
"6r7h",
"6r7i",
"6r7n",
"6ttu",
"6v9i",
"6wcq"... | 122 | [
"PUB00000937",
"PUB00010627",
"PUB00031678",
"PUB00042618",
"PUB00075111",
"PUB00103546"
] | [
"8681378",
"11961546",
"15537541",
"15688063",
"24793696",
"36041947"
] | [
"cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.",
"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.",
"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.",... | [
1996,
2002,
2004,
2005,
2014,
2023
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"metagenomes"
] | [
30361,
6,
4
] | 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... | [
42,
7,
29,
10,
77,
37,
3,
28,
38,
2,
3,
66
] | 12 | true | Domain | Cullin, N-terminal | Cullin, N-terminal | Cullin_N | 6 |
IPR001374 | 1,374 | R3H domain | R3H_dom | Domain | 40,930 | false | false | The R3H domain is a conserved sequence motif found in proteins from a diverse range of organisms including eubacteria, green plants, fungi and various groups of metazoans, but not in archaea and Escherichia coli. The domain is named R3H because it contains an invariant arginine and a highly conserved histidine, that ar... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01424",
"PS51061",
"SM00393"
] | [
"R3H",
"R3H",
"R3H"
] | [
38259,
39727,
33054
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51061",
"R-HSA-380994",
"R-HSA-429947",
"R-HSA-450604",
"R-HSA-9930044",
"R-MMU-429947",
"R-MMU-450604",
"R-MMU-9930044"
] | [
"PROSITEDOC:PDOC51061",
"REACTOME:R-HSA-380994",
"REACTOME:R-HSA-429947",
"REACTOME:R-HSA-450604",
"REACTOME:R-HSA-9930044",
"REACTOME:R-MMU-429947",
"REACTOME:R-MMU-450604",
"REACTOME:R-MMU-9930044"
] | 8 | [
"1msz",
"1ug8",
"1whr",
"2a1r",
"2a1s",
"2cpm",
"2lrr",
"3d45",
"3gku",
"7zw0",
"9lrg",
"9lri"
] | 12 | [
"PUB00005485",
"PUB00018517"
] | [
"9787637",
"12547203"
] | [
"The R3H motif: a domain that binds single-stranded nucleic acids.",
"Solution structure of the R3H domain from human Smubp-2."
] | [
1998,
2003
] | 2 | [] | [
"IPR034042",
"IPR034068",
"IPR034069",
"IPR034071",
"IPR034072",
"IPR034076",
"IPR034077",
"IPR034079",
"IPR034081",
"IPR034082",
"IPR034083"
] | 0 | 11 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
2,
12131,
28443,
33,
321
] | 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... | [
29,
3,
88,
13,
61,
30,
5,
14,
53,
3,
3,
63
] | 12 | true | Domain | R3H domain | R3H domain | R3H_dom | 4 |
IPR001377 | 1,377 | Small ribosomal subunit protein eS6 | Ribosomal_eS6 | Family | 8,161 | false | false | A number of eukaryotic and archaeal ribosomal proteins have been grouped on the basis of sequence similarities. Small ribosomal subunit protein eS6, previously known as Ribosomal protein S6 is the major substrate of protein kinases in eukaryotic ribosomes [ ] and may play an important role in controlling cell growth an... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER",
"SMART"
] | [
"PF01092",
"PTHR11502",
"SM01405"
] | [
"Ribosomal_S6e",
"",
"Ribosomal_S6e"
] | [
7874,
8025,
7793
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00500",
"R-BTA-156827",
"R-BTA-166208",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-9629569",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-166208",
"R-CEL-1799339",
"R-CEL-6791226",
"R-CEL-72649"... | [
"PROSITEDOC:PDOC00500",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-166208",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-9629569",
"REACTOME:R-BTA-975956... | 116 | [
"3j16",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q"... | 628 | [
"PUB00002823",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"8440735",
"11297922",
"11290319",
"11114498"
] | [
"Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1993,
2001,
2001,
2000
] | 4 | [] | [
"IPR014401",
"IPR020924"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
913,
5,
7203,
40
] | 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,
2,
1,
7,
6,
4,
2,
4,
16,
2,
2,
23
] | 12 | true | Family | Small ribosomal subunit protein eS6 | Small ribosomal subunit protein eS6 | Ribosomal_eS6 | 5 |
IPR001379 | 1,379 | Egg lysin (Sperm-lysin) | Egg_lysin | Family | 88 | false | false | This entry represents Egg-lysin from Haliotis rufescens and similar proteins from molluscs. This protein, also known as Sperm-lysin, binds to the egg vitelline envelope (VE) via the VE receptor for lysin (VERL) following its release from sperm. It then dissolves the VE non-enzymatically to create a hole, thereby allowi... | [
"GO:0007338"
] | [
"single fertilization"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS",
"CDD"
] | [
"PF01303",
"PR01882",
"cd00243"
] | [
"Egg_lysin",
"LYSIN",
"Lysin-Sp18"
] | [
84,
46,
50
] | 3 | [] | [] | [] | 0 | [
"1gak",
"1lis",
"1lyn",
"2lis",
"2lyn",
"3lyn",
"5ii7",
"5ii8",
"5ii9",
"5iia",
"5iib",
"5mr3",
"5utg"
] | 13 | [
"PUB00005176",
"PUB00011856",
"PUB00011857",
"PUB00011858"
] | [
"8266073",
"10666624",
"10698629",
"11331004"
] | [
"The crystal structure of lysin, a fertilization protein.",
"1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding.",
"The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of th... | [
1993,
2000,
2000,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Vetigastropoda"
] | [
88
] | 1 | [] | [] | 0 | true | Family | Egg lysin (Sperm-lysin) | Egg lysin (Sperm-lysin) | Egg_lysin | 3 |
IPR001380 | 1,380 | Large ribosomal subunit protein eL13 | Ribosomal_eL13 | Family | 6,279 | false | false | This entry represents the ribosomal protein eL13 found in vertebrates [ ], fruit fly, plants, yeast, amongst other eukaryotes and archaea. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to t... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_00499",
"PF01294",
"PTHR11722"
] | [
"Ribosomal_eL13",
"Ribosomal_L13e",
""
] | [
5532,
6253,
6098
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00848",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
... | [
"PROSITEDOC:PDOC00848",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956... | 68 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j79",
"3j7o",
"3j7p",
"3j7q",
"3j7r",
"3j92",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jan",
"3jbn",
"3jbo",
"3jbp",
"3jcs",
"3jct",
"4d5y",
"4d67",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r",
"4u4u",
"4u4y",
"4u4z"... | 584 | [
"PUB00000235",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"8198561",
"11297922",
"11290319",
"11114498"
] | [
"The primary structure of rat ribosomal protein L13.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1994,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
106,
4,
6168,
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... | [
16,
1,
1,
2,
9,
2,
1,
6,
11,
2,
1,
11
] | 12 | true | Family | Large ribosomal subunit protein eL13 | Large ribosomal subunit protein eL13 | Ribosomal_eL13 | 6 |
IPR001381 | 1,381 | 3-dehydroquinate dehydratase type I | DHquinase_I | Family | 13,094 | false | false | 3-dehydroquinate dehydratase ( ), or dehydroquinase, catalyzes the conversion of 3-dehydroquinate into 3-dehydroshikimate. It is the third step in the shikimate pathway for the biosynthesis of aromatic amino acids from chorismate. Two classes of dehydroquinases exist, known as types I and II. The best studied type I en... | [
"GO:0003855"
] | [
"3-dehydroquinate dehydratase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"NCBIFAM",
"CDD"
] | [
"MF_00214",
"PF01487",
"TIGR01093",
"cd00502"
] | [
"AroD",
"DHquinase_I",
"aroD",
"DHQase_I"
] | [
6556,
13092,
8581,
12102
] | 4 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"4.2.1.10",
"GenProp0001",
"GenProp1478",
"GenProp1643",
"GenProp1731",
"PWY-6163",
"PWY-6416",
"PWY-6707",
"PDOC00788"
] | [
"EC:4.2.1.10",
"GP:GenProp0001",
"GP:GenProp1478",
"GP:GenProp1643",
"GP:GenProp1731",
"METACYC:PWY-6163",
"METACYC:PWY-6416",
"METACYC:PWY-6707",
"PROSITEDOC:PDOC00788"
] | 9 | [
"1gqn",
"1l9w",
"1qfe",
"1sfj",
"1sfl",
"2egz",
"2gpt",
"2o7q",
"2o7s",
"2ocz",
"2ox1",
"2yr1",
"2ysw",
"3js3",
"3l2i",
"3l9c",
"3lb0",
"3m7w",
"3nnt",
"3o1n",
"3oex",
"3s42",
"4clm",
"4cnn",
"4cno",
"4cnp",
"4gfs",
"4guf",
"4gug",
"4guh",
"4gui",
"4guj"... | 55 | [
"PUB00002745"
] | [
"1429576"
] | [
"Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
882,
5227,
6875,
1,
109
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
4,
12,
1,
1,
26
] | 7 | true | Family | 3-dehydroquinate dehydratase type I | 3-dehydroquinate dehydratase type I | DHquinase_I | 1 |
IPR001382 | 1,382 | Glycoside hydrolase family 47 | Glyco_hydro_47 | Family | 32,785 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004571",
"GO:0005509",
"GO:0016020"
] | [
"mannosyl-oligosaccharide 1,2-alpha-mannosidase activity",
"calcium ion binding",
"membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF01532",
"PR00747"
] | [
"Glyco_hydro_47",
"GLYHDRLASE47"
] | [
32782,
30968
] | 2 | [
"CAZY",
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH47",
"3.2.1.113",
"GenProp1706",
"PWY-7919",
"R-CEL-964827",
"R-DME-964827",
"R-HSA-381038",
"R-HSA-4793950",
"R-HSA-6811438",
"R-HSA-901032",
"R-HSA-964827",
"R-HSA-9694548",
"R-MMU-964827"
] | [
"CAZY:GH47",
"EC:3.2.1.113",
"GP:GenProp1706",
"METACYC:PWY-7919",
"REACTOME:R-CEL-964827",
"REACTOME:R-DME-964827",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-4793950",
"REACTOME:R-HSA-6811438",
"REACTOME:R-HSA-901032",
"REACTOME:R-HSA-964827",
"REACTOME:R-HSA-9694548",
"REACTOME:R-MMU-964827... | 13 | [
"1dl2",
"1fmi",
"1fo2",
"1fo3",
"1g6i",
"1hcu",
"1kkt",
"1kre",
"1krf",
"1nxc",
"1x9d",
"2ri8",
"2ri9",
"4ayo",
"4ayp",
"4ayq",
"4ayr",
"5kij",
"5kk7",
"5kkb",
"5meh",
"5ne5",
"8b5m",
"8pko",
"8zpw"
] | 25 | [
"PUB00002897",
"PUB00004870",
"PUB00005266"
] | [
"8144580",
"7624375",
"8535779"
] | [
"Isolation and expression of murine and rabbit cDNAs encoding an alpha 1,2-mannosidase involved in the processing of asparagine-linked oligosaccharides.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydr... | [
1994,
1995,
1995
] | 3 | [] | [
"IPR044674"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halopelagius longus"
] | [
260,
32524,
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... | [
26,
9,
19,
10,
53,
28,
8,
12,
34,
3,
2,
79
] | 12 | true | Family | Glycoside hydrolase family 47 | Glycoside hydrolase family 47 | Glyco_hydro_47 | 3 |
IPR001383 | 1,383 | Large ribosomal subunit protein bL28, bacteria | Ribosomal_bL28_bact | Family | 25,330 | false | false | The ribosomal bL28 protein family include proteins from bacteria (also known as L28) and chloroplasts (bL28c). Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino ac... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00009"
] | [
"L28"
] | [
25330
] | 1 | [] | [] | [] | 0 | [
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"2jz6",
"2zjp",
"2zjq",
"2zjr",
"3cf5",
"3dll",
"3j5l",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce",
"3jcj",
"3jcn",
"3pio",
"3pip",
"4csu",
"4io9",
"4ioa",
"4ioc",
"4l47",
"4l71"... | 1,048 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [
"IPR026569"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctf8W5",
"Thermoproteota archaeon",
"unclassified sequences"
] | [
23763,
1180,
1,
2,
384
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
2,
7
] | 4 | true | Family | Large ribosomal subunit protein bL28, bacteria | Large ribosomal subunit protein bL28, bacteria | Ribosomal_bL28_bact | 1 |
IPR001384 | 1,384 | Peptidase M35, deuterolysin | Peptidase_M35 | Family | 2,205 | false | false | This group of metallopeptidases belong to MEROPS peptidase family M35 (deuterolysin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. Deuterolysin is a microbial zinc-containing metalloprotease that shows some similarity... | [
"GO:0004222",
"GO:0006508"
] | [
"metalloendopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF02102",
"PR00768"
] | [
"Peptidase_M35",
"DEUTEROLYSIN"
] | [
1970,
1877
] | 2 | [
"EC"
] | [
"3.4.24.39"
] | [
"EC:3.4.24.39"
] | 1 | [
"1eb6"
] | 1 | [
"PUB00000575",
"PUB00003579",
"PUB00003745"
] | [
"8049277",
"7674922",
"1886621"
] | [
"Molecular cloning and nucleotide sequence of the complementary DNA for penicillolysin gene, plnC, and 18 kDa metalloendopeptidase gene from Penicillium citrinum.",
"Evolutionary families of metallopeptidases.",
"Cloning and expression in yeast of a cDNA clone encoding Aspergillus oryzae neutral protease II, a ... | [
1994,
1995,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Fungi"
] | [
2205
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Family | Peptidase M35, deuterolysin | Peptidase M35, deuterolysin | Peptidase_M35 | 1 |
IPR001387 | 1,387 | Cro/C1-type, helix-turn-helix domain | Cro/C1-type_HTH | Domain | 611,228 | false | false | The cro/C1-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 residues present in transcriptional regulators. The domain is named after the transcriptional repressors cro and C1 of temperate bacteriophages 434 and lambda, respectively. Besides in bacteriophages, cro/C1-type regulators are pr... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF01381",
"PF12844",
"PF13443",
"PS50943",
"SM00530",
"cd00093"
] | [
"HTH_3",
"HTH_19",
"HTH_26",
"HTH_CROC1",
"HTH_XRE",
"HTH_XRE"
] | [
322797,
7527,
33002,
542131,
465966,
545137
] | 6 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC"
] | [
"GenProp0321",
"GenProp0457",
"GenProp1120",
"GenProp1658",
"PDOC50943"
] | [
"GP:GenProp0321",
"GP:GenProp0457",
"GP:GenProp1120",
"GP:GenProp1658",
"PROSITEDOC:PDOC50943"
] | 5 | [
"1adr",
"1b0n",
"1lli",
"1lmb",
"1lrp",
"1per",
"1pra",
"1r63",
"1r69",
"1rio",
"1rpe",
"1sq8",
"1utx",
"1x57",
"1y7y",
"1y9q",
"1zug",
"1zz6",
"1zz7",
"1zz8",
"1zz9",
"1zzb",
"1zzc",
"2a6c",
"2aw6",
"2awi",
"2axu",
"2axv",
"2axz",
"2b5a",
"2bnm",
"2bnn"... | 293 | [
"PUB00018412",
"PUB00018413"
] | [
"3187531",
"11972345"
] | [
"Recognition of a DNA operator by the repressor of phage 434: a view at high resolution.",
"CopR binds and bends its target DNA: a footprinting and fluorescence resonance energy transfer study."
] | [
1988,
2002
] | 2 | [] | [
"IPR039554",
"IPR055172",
"IPR057937"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
6726,
581729,
10543,
6297,
15,
5918
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
1,
15,
2,
20,
6,
8,
1,
7,
12,
1,
1,
14
] | 13 | true | Domain | Cro/C1-type, helix-turn-helix domain | Cro/C1-type, helix-turn-helix domain | Cro/C1-type_HTH | 1 |
IPR001388 | 1,388 | Synaptobrevin-like | Synaptobrevin-like | Family | 23,501 | false | false | Synaptobrevin is an intrinsic membrane protein of small synaptic vesicles [ ], specialised secretory organelles of neurons that actively accumulate neurotransmitters and participate in their calcium-dependent release by exocytosis. Vesicle function is mediated by proteins in their membranes, although the precise nature... | [
"GO:0016192",
"GO:0016020"
] | [
"vesicle-mediated transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS",
"PROSITE"
] | [
"PR00219",
"PS00417"
] | [
"SYNAPTOBREVN",
"SYNAPTOBREVIN"
] | [
22803,
15255
] | 2 | [
"PROSITEDOC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"PDOC00368",
"PDOC50892",
"R-BTA-1236974",
"R-BTA-181429",
"R-BTA-181430",
"R-BTA-199992",
"R-BTA-210500",
"R-BTA-212676",
"R-BTA-264642",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-449836",
"R-BTA-6798695",
"R-BTA-6811440",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-888590",
"R-BTA-9609... | [
"PROSITEDOC:PDOC00368",
"PROSITEDOC:PDOC50892",
"REACTOME:R-BTA-1236974",
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-199992",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-264642",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-4498... | 198 | [
"1gl2",
"1kil",
"1l4a",
"1n7s",
"1sfc",
"2kog",
"2n1t",
"2nps",
"2nup",
"2nut",
"3b5n",
"3hd7",
"3ipd",
"3j96",
"3j97",
"3j98",
"3j99",
"3rk2",
"3rk3",
"3rl0",
"4b93",
"4wy4",
"5ccg",
"5cch",
"5cci",
"5kj7",
"5kj8",
"5w5c",
"5w5d",
"6ip1",
"6mdm",
"6mdn"... | 46 | [
"PUB00001832",
"PUB00002580",
"PUB00004302"
] | [
"8406010",
"1976629",
"2560644"
] | [
"Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells.",
"Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2.",
"A synaptic vesicle membrane protein is conserved from mammals ... | [
1993,
1990,
1989
] | 3 | [] | [
"IPR016444",
"IPR042166",
"IPR042887",
"IPR044565"
] | 0 | 4 | 0 | [
"Eukaryota",
"Gammaproteobacteria",
"Methanosphaera stadtmanae",
"Viruses",
"metagenomes"
] | [
23463,
10,
2,
20,
6
] | 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... | [
45,
10,
16,
5,
26,
21,
2,
28,
36,
4,
2,
63
] | 12 | true | Family | Synaptobrevin-like | Synaptobrevin-like | Synaptobrevin-like | 6 |
IPR001389 | 1,389 | Flocculin | Flocculin | Repeat | 371 | false | false | Yeast flocculation protein may be directly involved in the flocculation process [ ]. The extensively O-glycosylated protein is probably attached to the membrane by a GPI-anchor. | [
"GO:0000128"
] | [
"flocculation"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00624"
] | [
"Flocculin"
] | [
371
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005655"
] | [
"7502576"
] | [
"Review: the dominant flocculation genes of Saccharomyces cerevisiae constitute a new subtelomeric gene family."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Lactococcus lactis"
] | [
370,
1
] | 2 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
5
] | 1 | true | Repeat | Flocculin | Flocculin | Flocculin | 9 |
IPR001390 | 1,390 | Gamma-aminobutyric-acid A receptor, alpha subunit | GABAAa_rcpt | Family | 8,571 | false | false | This entry represents the alpha subunit of the Gamma-aminobutyric acid receptor (GABAA), which largely determine benzodiazepine binding properties [ ]. Mutagenesis and agonist/antagonist binding studies have suggested a close functional and structural association of alpha-subunits with the agonist/antagonist binding si... | [
"GO:0004890",
"GO:0005216",
"GO:0006811",
"GO:0016020"
] | [
"GABA-A receptor activity",
"monoatomic ion channel activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01079"
] | [
"GABAARALPHA"
] | [
8571
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-977443",
"R-GGA-977443",
"R-HSA-1236394",
"R-HSA-977443",
"R-MMU-977443",
"R-RNO-977443"
] | [
"REACTOME:R-BTA-977443",
"REACTOME:R-GGA-977443",
"REACTOME:R-HSA-1236394",
"REACTOME:R-HSA-977443",
"REACTOME:R-MMU-977443",
"REACTOME:R-RNO-977443"
] | 6 | [
"6a96",
"6d6t",
"6d6u",
"6dw0",
"6dw1",
"6hug",
"6huj",
"6huk",
"6huo",
"6hup",
"6i53",
"6x3s",
"6x3t",
"6x3u",
"6x3v",
"6x3w",
"6x3x",
"6x3z",
"6x40",
"7pbd",
"7pbz",
"7pc0",
"7qn5",
"7qn7",
"7qn9",
"7qna",
"7qnc",
"7qne",
"7t0w",
"7t0z",
"8bej",
"8bgi"... | 111 | [
"PUB00001220",
"PUB00002675",
"PUB00003454",
"PUB00003455",
"PUB00007821",
"PUB00007822",
"PUB00007823",
"PUB00007824",
"PUB00009393",
"PUB00009394",
"PUB00010340",
"PUB00044612",
"PUB00044613",
"PUB00044614",
"PUB00044615"
] | [
"1376242",
"1721053",
"1849552",
"1846404",
"11712530",
"8537206",
"9647870",
"11282419",
"10449790",
"2538761",
"10026168",
"18446614",
"15383648",
"18760291",
"15165736"
] | [
"Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels.",
"Determination of the tyrosine phosphorylation sites of the nicotinic acetylcholine receptor.",
"Sequence and regional distribution of the mRNA encoding the alpha 2 polypeptide of rat gamma-aminobutyric aci... | [
1992,
1991,
1991,
1991,
2001,
1995,
1998,
2001,
1999,
1989,
1999,
2008,
2004,
2008,
2004
] | 15 | [
"IPR006028"
] | [
"IPR005431",
"IPR005432",
"IPR005433",
"IPR005434",
"IPR005435",
"IPR005436"
] | 1 | 6 | 0 | [
"Eumetazoa"
] | [
8571
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
14,
3,
42,
22,
22
] | 6 | true | Family | Gamma-aminobutyric-acid A receptor, alpha subunit | Gamma-aminobutyric-acid A receptor, alpha subunit | GABAAa_rcpt | 5 |
IPR001392 | 1,392 | Clathrin adaptor, mu subunit | Clathrin_mu | Family | 20,463 | false | false | Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are ... | [
"GO:0006886",
"GO:0016192",
"GO:0030131"
] | [
"intracellular protein transport",
"vesicle-mediated transport",
"clathrin adaptor complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF005992",
"PR00314"
] | [
"Clathrin_mu",
"CLATHRINADPT"
] | [
17757,
19320
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00761",
"R-BTA-177504",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-416993",
"R-BTA-432720",
"R-BTA-432722",
"R-BTA-437239",
"R-BTA-5099900",
"R-BTA-5140745",
"R-BTA-6798695",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8866427",
"R-BTA-8964038",
"R-CEL-190873",
"R-CE... | [
"PROSITEDOC:PDOC00761",
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-416993",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-432722",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-5099900",
"REACTOME:R-BTA-5140745",
"REACTOME:R-BTA-6... | 122 | [
"1bw8",
"1bxx",
"1h6e",
"1hes",
"1i31",
"1w63",
"2bp5",
"2jkr",
"2jkt",
"2pr9",
"2vgl",
"2xa7",
"3h85",
"3l81",
"3ml6",
"4emz",
"4en2",
"4hmy",
"4mdr",
"4p6z",
"4uqi",
"5c7z",
"5fpi",
"5wrk",
"5wrl",
"5wrm",
"6bnt",
"6cm9",
"6cri",
"6d83",
"6d84",
"6dff"... | 83 | [
"PUB00001404",
"PUB00010644",
"PUB00025539",
"PUB00035753",
"PUB00035754",
"PUB00035755",
"PUB00035756",
"PUB00035757",
"PUB00035765",
"PUB00035769"
] | [
"1761056",
"11080148",
"11583591",
"17449236",
"15107467",
"12952931",
"16542748",
"17254016",
"11598180",
"15261670"
] | [
"The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast.",
"Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.",
"Study of the interaction of the medium chain mu 2 subunit of the clathrin-associated adapter protein complex 2... | [
1991,
2000,
2001,
2007,
2004,
2003,
2006,
2007,
2001,
2004
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
20462,
1
] | 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... | [
18,
5,
23,
4,
53,
23,
3,
13,
31,
3,
3,
36
] | 12 | true | Family | Clathrin adaptor, mu subunit | Clathrin adaptor, mu subunit | Clathrin_mu | 8 |
IPR001393 | 1,393 | Calsequestrin | Calsequestrin | Family | 3,245 | false | false | Calsequestrin is the principal calcium-binding protein present in the sarcoplasmic reticulum of cardiac and skeletal muscle [ ]. It is a highly acidic protein that is able to bind over 40 calcium ions and acts as an internal calcium store in muscle. Sequence analysis has suggested that calcium is not bound in distinct ... | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01216"
] | [
"Calsequestrin"
] | [
3245
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00675",
"R-HSA-2672351",
"R-HSA-5578775",
"R-MMU-2672351",
"R-MMU-5578775",
"R-RNO-2672351",
"R-RNO-5578775"
] | [
"PROSITEDOC:PDOC00675",
"REACTOME:R-HSA-2672351",
"REACTOME:R-HSA-5578775",
"REACTOME:R-MMU-2672351",
"REACTOME:R-MMU-5578775",
"REACTOME:R-RNO-2672351",
"REACTOME:R-RNO-5578775"
] | 7 | [
"1a8y",
"1sji",
"2vaf",
"3trp",
"3trq",
"3uom",
"3us3",
"3v1w",
"5crd",
"5cre",
"5crg",
"5crh",
"5kn0",
"5kn1",
"5kn2",
"5kn3",
"6owv",
"6oww",
"7f05",
"8f48"
] | 20 | [
"PUB00000289",
"PUB00002488",
"PUB00002682"
] | [
"3427023",
"3379055",
"1985907"
] | [
"Characterization of cardiac calsequestrin.",
"Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning.",
"Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calseque... | [
1987,
1988,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Enterobacterales",
"Eumetazoa"
] | [
3,
3242
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
6,
14,
9,
11
] | 5 | true | Family | Calsequestrin | Calsequestrin | Calsequestrin | 8 |
IPR001394 | 1,394 | Peptidase C19, ubiquitin carboxyl-terminal hydrolase | Peptidase_C19_UCH | Domain | 153,676 | false | false | Ubiquitin carboxyl-terminal hydrolases (UCH) ( ) [ ] are thiol proteases that recognise and hydrolyse the peptide bond at the C-terminal glycine of ubiquitin. These enzymes are involved in the processing of poly-ubiquitin precursors as well as that of ubiquinated proteins. The deubiquitinsing proteases can be split int... | [
"GO:0004843",
"GO:0016579"
] | [
"cysteine-type deubiquitinase activity",
"protein deubiquitination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00443"
] | [
"UCH"
] | [
153676
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.19.12",
"PDOC00750",
"R-BTA-168638",
"R-BTA-5357786",
"R-BTA-5357905",
"R-BTA-5357956",
"R-BTA-5689880",
"R-BTA-8948751",
"R-BTA-9010553",
"R-BTA-936440",
"R-BTA-9758274",
"R-CEL-1169408",
"R-CEL-5689880",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-8866652",
"R-... | [
"EC:3.4.19.12",
"PROSITEDOC:PDOC00750",
"REACTOME:R-BTA-168638",
"REACTOME:R-BTA-5357786",
"REACTOME:R-BTA-5357905",
"REACTOME:R-BTA-5357956",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8948751",
"REACTOME:R-BTA-9010553",
"REACTOME:R-BTA-936440",
"REACTOME:R-BTA-9758274",
"REACTOME:R-CEL-116940... | 152 | [
"1nb8",
"1nbf",
"1vjv",
"2ayn",
"2ayo",
"2f1z",
"2gfo",
"2hd5",
"2ibi",
"2vhf",
"2y5b",
"2y6e",
"3i3t",
"3ihp",
"3jcr",
"3m99",
"3mhh",
"3mhs",
"3mtn",
"3n3k",
"3nhe",
"3v6c",
"3v6e",
"3wxe",
"3wxf",
"3wxg",
"4fip",
"4fjc",
"4fk5",
"4m5w",
"4m5x",
"4msx"... | 205 | [
"PUB00000623",
"PUB00003577",
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00069571",
"PUB00069572",
"PUB00076953"
] | [
"1647207",
"7845226",
"11517925",
"9891971",
"14725770",
"23845989",
"2050695",
"7044372"
] | [
"Genetic analysis of the ubiquitin system.",
"Families of cysteine peptidases.",
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"The structure of sortase B, a cysteine t... | [
1991,
1994,
2001,
1998,
2004,
2014,
1991,
1982
] | 8 | [
"IPR028889"
] | [
"IPR033815",
"IPR033840",
"IPR033841"
] | 1 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
96,
153165,
125,
290
] | 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... | [
264,
57,
258,
63,
256,
159,
15,
143,
209,
17,
15,
407
] | 12 | true | Domain | Peptidase C19, ubiquitin carboxyl-terminal hydrolase | Peptidase C19, ubiquitin carboxyl-terminal hydrolase | Peptidase_C19_UCH | 2 |
IPR001396 | 1,396 | Metallothionein, family 4, echinoidea | Metalthion_4_echinoidea | Family | 23 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00873"
] | [
"MTECHINOIDEA"
] | [
23
] | 1 | [] | [] | [] | 0 | [
"1qjk"
] | 1 | [
"PUB00001490",
"PUB00003570",
"PUB00003571",
"PUB00005944",
"PUB00078698"
] | [
"2959513",
"1779825",
"1779826",
"2959504",
"21633816"
] | [
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein.",
"Definitions and nomenclature of metallothioneins.",
"Nomenclature of metallothionein.",
"Metallothionein protein evolution: a miniassay."
] | [
1987,
1991,
1991,
1987,
2011
] | 5 | [
"IPR017980"
] | [] | 1 | 0 | 1 | [
"Candidatus Ureaplasma intestinipullorum",
"Eukaryota"
] | [
1,
22
] | 2 | [] | [] | 0 | true | Family | Metallothionein, family 4, echinoidea | Metallothionein, family 4, echinoidea | Metalthion_4_echinoidea | 1 |
IPR001397 | 1,397 | 5-Hydroxytryptamine 5A receptor | 5HT5A_rcpt | Family | 749 | false | false | 5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n... | [
"GO:0004993",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled serotonin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00518"
] | [
"5HT5ARECEPTR"
] | [
749
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"10",
"R-HSA-390666",
"R-HSA-418594",
"R-MMU-390666",
"R-MMU-418594",
"R-RNO-390666",
"R-RNO-418594"
] | [
"IUPHAR:10",
"REACTOME:R-HSA-390666",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-390666",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-390666",
"REACTOME:R-RNO-418594"
] | 7 | [
"7um4",
"7um5",
"7um6",
"7um7",
"7x5h"
] | 5 | [
"PUB00064376",
"PUB00064498",
"PUB00064499",
"PUB00064500",
"PUB00064503",
"PUB00064504",
"PUB00064505",
"PUB00064586",
"PUB00066704"
] | [
"18476671",
"9865521",
"16846620",
"12558985",
"7682702",
"7988681",
"10197537",
"15921820",
"11989819"
] | [
"Serotonin receptors.",
"The human 5-ht5A receptor couples to Gi/Go proteins and inhibits adenylate cyclase in HEK 293 cells.",
"SB-699551-A (3-cyclopentyl-N-[2-(dimethylamino)ethyl]-N-[(4'-{[(2-phenylethyl)amino]methyl}-4-biphenylyl)methyl]propanamide dihydrochloride), a novel 5-ht5A receptor-selective antagon... | [
2008,
1998,
2006,
2003,
1993,
1994,
1999,
2005,
2002
] | 9 | [
"IPR002231"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
749
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
3
] | 4 | true | Family | 5-Hydroxytryptamine 5A receptor | 5-Hydroxytryptamine 5A receptor | 5HT5A_rcpt | 4 |
IPR001398 | 1,398 | Macrophage migration inhibitory factor | Macrophage_inhib_fac | Family | 7,600 | false | false | Macrophage migration inhibitory factor (MIF) is a key regulatory cytokine within innate and adaptive immune responses, capable of promoting and modulating the magnitude of the response [ ]. MIF is released from T-cells and macrophages, and acts within the neuroendocrine system. MIF is capable of tautomerase activity, a... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF01187",
"PTHR11954"
] | [
"MIF",
""
] | [
7524,
7026
] | 2 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.3.2.1",
"5.3.3.12",
"PWY-6498",
"PDOC00892",
"R-BTA-202733",
"R-BTA-6798695",
"R-GGA-202733",
"R-GGA-6798695",
"R-HSA-202733",
"R-HSA-6798695",
"R-HSA-8950505",
"R-MMU-202733",
"R-MMU-6798695",
"R-RNO-202733",
"R-RNO-6798695",
"R-SSC-202733",
"R-SSC-6798695",
"R-XTR-6798695"
] | [
"EC:5.3.2.1",
"EC:5.3.3.12",
"METACYC:PWY-6498",
"PROSITEDOC:PDOC00892",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-6798695",
"REACTOME:R-GGA-202733",
"REACTOME:R-GGA-6798695",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8950505",
"REACTOME:R-MMU-202733",
"REACTOME:R-MMU... | 18 | [
"1ca7",
"1cgq",
"1dpt",
"1fim",
"1gcz",
"1gd0",
"1gif",
"1hfo",
"1ljt",
"1mff",
"1mfi",
"1mif",
"1p1g",
"1uiz",
"2gdg",
"2ooh",
"2oow",
"2ooz",
"2os5",
"2wkb",
"2wkf",
"2xcz",
"3b64",
"3b9s",
"3ce4",
"3djh",
"3dji",
"3fwt",
"3fwu",
"3gac",
"3gad",
"3hof"... | 179 | [
"PUB00024290",
"PUB00034437",
"PUB00034438",
"PUB00034439",
"PUB00034440"
] | [
"10079069",
"15225126",
"16331703",
"16628200",
"10644007"
] | [
"Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution.",
"Macrophage migration inhibitory factor: molecular, cellular and genetic aspects of a key neuroendocrine molecule.",
"How glucocorticoids control their own strength and the balanc... | [
1999,
2004,
2005,
2006,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2,
1003,
6580,
15
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
14,
6,
2,
13,
6,
1,
8,
12,
5
] | 9 | true | Family | Macrophage migration inhibitory factor | Macrophage migration inhibitory factor | Macrophage_inhib_fac | 2 |
IPR001399 | 1,399 | VP6 blue-tongue virus inner capsid protein | Orbi_VP6 | Family | 1,021 | false | false | Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyses the unwinding of double-stranded RNA substrates [ ]. VP6 from five United States prototype bluetongue virus (BTV) serotypes contain unusually high concentrations of glycine, few aromatic amino aci... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF01516",
"PR00902"
] | [
"Orbi_VP6",
"VP6CAPSID"
] | [
989,
791
] | 2 | [
"EC",
"GP"
] | [
"3.6.4.13",
"GenProp1006"
] | [
"EC:3.6.4.13",
"GP:GenProp1006"
] | 2 | [
"8w12",
"8w19",
"8w1c"
] | 3 | [
"PUB00003535",
"PUB00005635"
] | [
"9311795",
"1329371"
] | [
"Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates.",
"Comparative sequence analyses of the cognate structural protein VP6 genes of five US bluetongue viruses."
] | [
1997,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Riboviria"
] | [
2,
30,
989
] | 3 | [] | [] | 0 | true | Family | VP6 blue-tongue virus inner capsid protein | VP6 blue-tongue virus inner capsid protein | Orbi_VP6 | 4 |
IPR001400 | 1,400 | Somatotropin/prolactin | Somatotropin/Prolactin | Family | 6,159 | false | false | Somatotropin is a hormone that plays an important role in growth control. It belongs to a family that includes choriomammotropin (lactogen), its placental analogue; prolactin, which promotes lactation in the mammary gland, and placental prolactin-related proteins; proliferin and proliferin related protein; and somatola... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00103",
"PR00836",
"PTHR11417"
] | [
"Hormone_1",
"SOMATOTROPIN",
""
] | [
6119,
5540,
6096
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00239",
"R-CFA-1170546",
"R-CFA-422085",
"R-CFA-982772",
"R-GGA-1170546",
"R-GGA-422085",
"R-GGA-982772",
"R-HSA-1170546",
"R-HSA-422085",
"R-HSA-977225",
"R-HSA-982772",
"R-MMU-1170546",
"R-MMU-422085",
"R-MMU-982772",
"R-RNO-1170546",
"R-RNO-422085",
"R-RNO-982772",
"R-SSC-1... | [
"PROSITEDOC:PDOC00239",
"REACTOME:R-CFA-1170546",
"REACTOME:R-CFA-422085",
"REACTOME:R-CFA-982772",
"REACTOME:R-GGA-1170546",
"REACTOME:R-GGA-422085",
"REACTOME:R-GGA-982772",
"REACTOME:R-HSA-1170546",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-977225",
"REACTOME:R-HSA-982772",
"REACTOME:R-MMU-1... | 20 | [
"1a22",
"1axi",
"1bp3",
"1f6f",
"1hgu",
"1huw",
"1hwg",
"1hwh",
"1kf9",
"1rw5",
"1z7c",
"2q98",
"3d48",
"3ew3",
"3hhr",
"3mzg",
"3n06",
"3n0p",
"3ncb",
"3ncc",
"3nce",
"3ncf",
"3npz"
] | 23 | [
"PUB00000308",
"PUB00000338",
"PUB00000346",
"PUB00000588"
] | [
"2765528",
"1993170",
"2021631",
"2790033"
] | [
"A subfamily of bovine prolactin-related transcripts distinct from placental lactogen in the fetal placenta.",
"Isolation and characterization of somatolactin, a new protein related to growth hormone and prolactin from Atlantic cod (Gadus morhua) pituitary glands.",
"A heuristic approach to predicting the terti... | [
1989,
1991,
1991,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
6159
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
40,
78,
124
] | 4 | true | Family | Somatotropin/prolactin | Somatotropin/prolactin | Somatotropin/Prolactin | 4 |
IPR001401 | 1,401 | Dynamin, GTPase domain | Dynamin_GTPase | Domain | 43,676 | false | false | Membrane transport between compartments in eukaryotic cells requires proteins that allow the budding and scission of nascent cargo vesicles from one compartment and their targeting and fusion with another. Dynamins are large GTPases that belong to a protein superfamily [ ] that, in eukaryotic cells, includes classical ... | [
"GO:0003924",
"GO:0005525"
] | [
"GTPase activity",
"GTP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SMART",
"CDD"
] | [
"SM00053",
"cd08771"
] | [
"DYNc",
"DLP_1"
] | [
43556,
41118
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00362",
"R-BTA-1169408",
"R-BTA-166016",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-437239",
"R-BTA-75153",
"R-BTA-8856828",
"R-CEL-190873",
"R-CEL-196025",
"R-CEL-3928665",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-437239",
"R-CEL-75153",
"R-CEL-8856828",
"R-CFA-116... | [
"PROSITEDOC:PDOC00362",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-75153",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-190873",
"REACTOME:R-CEL-196025",
"REACTOME:R-CEL-39... | 80 | [
"1jwy",
"1jx2",
"2aka",
"2x2e",
"2x2f",
"3l43",
"3snh",
"3szr",
"3t34",
"3t35",
"3w6n",
"3w6o",
"3w6p",
"3zvr",
"3zyc",
"3zys",
"4bej",
"4h1u",
"4h1v",
"4p4s",
"4p4t",
"4p4u",
"4uud",
"4uuk",
"4whj",
"5a3f",
"5d3q",
"5gtm",
"5uot",
"5wp9",
"6def",
"6di7"... | 68 | [
"PUB00000075",
"PUB00000836",
"PUB00001910",
"PUB00003186",
"PUB00014977",
"PUB00057048"
] | [
"2142876",
"2112425",
"1532158",
"2607176",
"15040446",
"21927001"
] | [
"Motor proteins of cytoplasmic microtubules.",
"A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.",
"Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin.",
... | [
1990,
1990,
1992,
1989,
2004,
2011
] | 6 | [
"IPR030381"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Viruses",
"metagenomes"
] | [
43646,
23,
7
] | 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... | [
67,
4,
97,
17,
70,
34,
8,
46,
51,
3,
3,
94
] | 12 | true | Domain | Dynamin, GTPase domain | Dynamin, GTPase domain | Dynamin_GTPase | 8 |
IPR001402 | 1,402 | Prolactin-releasing peptide receptor | Prolrel_pep_rcpt | Family | 1,997 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01018"
] | [
"PRPRECEPTOR"
] | [
1997
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"337",
"R-BTA-375276",
"R-HSA-375276",
"R-MMU-375276",
"R-RNO-375276"
] | [
"IUPHAR:337",
"REACTOME:R-BTA-375276",
"REACTOME:R-HSA-375276",
"REACTOME:R-MMU-375276",
"REACTOME:R-RNO-375276"
] | 5 | [
"8zps",
"8zpt",
"9k26",
"9k27"
] | 4 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00007141",
"PUB00007142",
"PUB00007143",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"9607765",
"11030716",
"10498338",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"A prolactin-releasing peptide in the brain.",
"Characterization of the binding of [(125)I... | [
1990,
1988,
1993,
1994,
1998,
2000,
1999,
2003,
1994,
2005,
2009,
2006,
2013
] | 13 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
1997
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
1,
3
] | 4 | true | Family | Prolactin-releasing peptide receptor | Prolactin-releasing peptide receptor | Prolrel_pep_rcpt | 3 |
IPR001403 | 1,403 | Coat protein VP1/VP2, Parvovirus | Parvovirus_coat | Domain | 10,575 | false | false | This entry represents a domain found in the Parvovirus coat protein VP1 and VP2. Parvoviruses are some of the smallest viruses containing linear, non-segmented single-stranded DNA genomes, with an average genome size of 5000 nucleotides. Parvoviruses have been described that infect a wide range of invertebrates and ver... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00740"
] | [
"VP1_2"
] | [
10575
] | 1 | [] | [] | [] | 0 | [
"1c8d",
"1c8e",
"1c8f",
"1c8g",
"1c8h",
"1fpv",
"1ijs",
"1k3v",
"1lp3",
"1mvm",
"1p5w",
"1p5y",
"1s58",
"1z14",
"1z1c",
"2cas",
"2g8g",
"2qa0",
"2xgk",
"3j1q",
"3j1s",
"3j4p",
"3jcx",
"3kic",
"3kie",
"3ng9",
"3ntt",
"3oah",
"3ra2",
"3ra4",
"3ra8",
"3ra9"... | 215 | [
"PUB00003172",
"PUB00054921",
"PUB00096898"
] | [
"9129667",
"20097398",
"12050365"
] | [
"Tropic determinant for canine parvovirus and feline panleukopenia virus functions through the capsid protein VP2.",
"Determination and analysis of the full-length chicken parvovirus genome.",
"Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA replication sy... | [
1997,
2010,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Parvoviridae",
"Rhinolophus ferrumequinum"
] | [
7,
10566,
2
] | 3 | [] | [] | 0 | true | Domain | Coat protein VP1/VP2, Parvovirus | Coat protein VP1/VP2, Parvovirus | Parvovirus_coat | 5 |
IPR001404 | 1,404 | Heat shock protein Hsp90 family | Hsp90_fam | Family | 44,900 | false | false | Molecular chaperones, or heat shock proteins (Hsps) are ubiquitous proteins that act to maintain proper protein folding within the cell [ ]. They assist in the folding of nascent polypeptide chains, and are also involved in the refolding of denatured proteins following proteotoxic stress. As their name implies, the hea... | [
"GO:0005524",
"GO:0016887",
"GO:0051082",
"GO:0140662",
"GO:0006457"
] | [
"ATP binding",
"ATP hydrolysis activity",
"unfolded protein binding",
"ATP-dependent protein folding chaperone",
"protein folding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 5 | [
"HAMAP",
"NCBIFAM",
"PFAM",
"PIRSF",
"PANTHER"
] | [
"MF_00505",
"NF003555",
"PF00183",
"PIRSF002583",
"PTHR11528"
] | [
"HSP90",
"PRK05218.1",
"HSP90",
"Hsp90",
""
] | [
27894,
33095,
41795,
34842,
44336
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00270",
"R-BTA-1227986",
"R-BTA-1474151",
"R-BTA-1679131",
"R-BTA-168928",
"R-BTA-2029482",
"R-BTA-203615",
"R-BTA-2565942",
"R-BTA-3371497",
"R-BTA-3371511",
"R-BTA-3371568",
"R-BTA-3371571",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-381426",
"R-B... | [
"PROSITEDOC:PDOC00270",
"REACTOME:R-BTA-1227986",
"REACTOME:R-BTA-1474151",
"REACTOME:R-BTA-1679131",
"REACTOME:R-BTA-168928",
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-203615",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-3371511",
"REACTOME:R-BTA-3371568",
"REACTOME:R-... | 277 | [
"1a4h",
"1ah6",
"1ah8",
"1am1",
"1amw",
"1bgq",
"1byq",
"1hk7",
"1osf",
"1qy8",
"1qye",
"1sf8",
"1tbw",
"1tc0",
"1tc6",
"1u0z",
"1u2o",
"1us7",
"1usu",
"1usv",
"1uy6",
"1uy7",
"1uy8",
"1uy9",
"1uyc",
"1uyd",
"1uye",
"1uyf",
"1uyg",
"1uyh",
"1uyi",
"1uyk"... | 659 | [
"PUB00035214",
"PUB00035215",
"PUB00112352",
"PUB00112353",
"PUB00141629",
"PUB00141630",
"PUB00141631",
"PUB00141642"
] | [
"11407116",
"9521088",
"19697319",
"24462206",
"26616658",
"26884463",
"26929380",
"22008467"
] | [
"Microbial molecular chaperones.",
"The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors.",
"Hsp90 and co-chaperones twist the functions of diverse client proteins.",
"Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) ... | [
2001,
1998,
2010,
2014,
2015,
2016,
2016,
2012
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
24,
19160,
25381,
10,
325
] | 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",... | [
38,
5,
8,
8,
1,
62,
37,
1,
40,
24,
2,
1,
107
] | 13 | true | Family | Heat shock protein Hsp90 family | Heat shock protein Hsp90 family | Hsp90_fam | 1 |
IPR001406 | 1,406 | Pseudouridine synthase I, TruA | PsdUridine_synth_TruA | Family | 44,287 | false | false | This entry represents pseudouridine synthase I (TruA) from prokaryotes and tRNA pseudouridine synthase 1 (Pus1) from eukaryotes, which belongs to the TruA family. TruA from Escherichia coli modifies positions uracil-38, U-39 and/or U-40 in tRNA [ , ]. TruA contains one atom of zinc essential for its native conformation... | [
"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",
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00171",
"PIRSF001430",
"PTHR11142",
"TIGR00071",
"cd02570"
] | [
"TruA",
"tRNA_psdUrid_synth",
"",
"hisT_truA",
"PseudoU_synth_EcTruA"
] | [
34098,
28267,
44158,
33149,
28948
] | 5 | [
"EC",
"EC",
"REACTOME",
"REACTOME"
] | [
"5.4.99",
"5.4.99.12",
"R-HSA-6782315",
"R-HSA-6787450"
] | [
"EC:5.4.99",
"EC:5.4.99.12",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6787450"
] | 4 | [
"1dj0",
"1vs3",
"2nqp",
"2nr0",
"2nre",
"4iqm",
"4its",
"4j37",
"4nz6",
"4nz7",
"6sga",
"6sgb",
"7r9f",
"7r9g",
"8okd",
"8q70",
"9enb",
"9enc",
"9ene",
"9enf",
"9f9q",
"9hny"
] | 22 | [
"PUB00000455",
"PUB00015686",
"PUB00042017",
"PUB00045922",
"PUB00091708",
"PUB00092579",
"PUB00100729",
"PUB00100730",
"PUB00100731"
] | [
"9585540",
"10625422",
"17466622",
"10529181",
"9671058",
"19664587",
"10356324",
"31477916",
"25219674"
] | [
"Transfer RNA-pseudouridine synthetase Pus1 of Saccharomyces cerevisiae contains one atom of zinc essential for its native conformation and tRNA recognition.",
"The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.",
"How U38, 39, and 40 of many tRNAs become the targ... | [
1998,
2000,
2007,
1999,
1998,
2009,
1999,
2019,
2014
] | 9 | [] | [
"IPR041707",
"IPR041708"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
706,
27498,
15507,
2,
574
] | 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",... | [
40,
4,
7,
6,
1,
16,
8,
3,
21,
13,
3,
4,
47
] | 13 | true | Family | Pseudouridine synthase I, TruA | Pseudouridine synthase I, TruA | PsdUridine_synth_TruA | 2 |
IPR001407 | 1,407 | Influenza RNA-dependent RNA polymerase subunit PB1 | RNA_pol_PB1_influenza | Family | 66,122 | false | false | Influenza RNA-dependent RNA polymerase is composed of three subunits; P1 (or PB1), P2 (or PA), and P3 (or PB2). There are two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits [ , ]. PB1 is the core of the complex and accounts for the polymerase activity [ ]. | [
"GO:0003723",
"GO:0003968",
"GO:0039694"
] | [
"RNA binding",
"RNA-directed RNA polymerase activity",
"viral RNA genome replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PIRSF"
] | [
"MF_04065",
"PF00602",
"PIRSF000827"
] | [
"INFV_RDRP",
"Flu_PB1",
"RdRPol_OMV"
] | [
61904,
66122,
62809
] | 3 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.48",
"GenProp1012",
"R-HSA-168255",
"R-HSA-168271",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168325",
"R-HSA-168330",
"R-HSA-168333",
"R-HSA-168336",
"R-HSA-192814",
"R-HSA-192823",
"R-HSA-192869",
"R-HSA-192905"
] | [
"EC:2.7.7.48",
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168271",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168325",
"REACTOME:R-HSA-168330",
"REACTOME:R-HSA-168333",
"REACTOME... | 17 | [
"2znl",
"2ztt",
"3a1g",
"3cm8",
"4wrt",
"4wsa",
"4wsb",
"5d98",
"5d9a",
"5epi",
"5fmz",
"5m3h",
"5m3j",
"5msg",
"6evj",
"6evk",
"6f5o",
"6f5p",
"6fhh",
"6fhi",
"6kuj",
"6kuk",
"6kup",
"6kur",
"6kut",
"6kuu",
"6kuv",
"6kv5",
"6qcs",
"6qct",
"6qcv",
"6qcw"... | 141 | [
"PUB00002362",
"PUB00004471",
"PUB00087126"
] | [
"9348094",
"8948635",
"10393191"
] | [
"Identification of two nucleotide-binding domains on the PB1 subunit of influenza virus RNA polymerase.",
"Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure.",
"Distinct regions of in... | [
1997,
1996,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Neoptera",
"Viruses"
] | [
4,
35,
66083
] | 3 | [] | [] | 0 | true | Family | Influenza RNA-dependent RNA polymerase subunit PB1 | Influenza RNA-dependent RNA polymerase subunit PB1 | RNA_pol_PB1_influenza | 6 |
IPR001408 | 1,408 | G-protein alpha subunit, group I | Gprotein_alpha_I | Family | 10,139 | false | false | Guanine nucleotide binding proteins (G-proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian cells, regulating systems as diverse as sensory perce... | [
"GO:0003924",
"GO:0005525",
"GO:0031683",
"GO:0007186",
"GO:0007188"
] | [
"GTPase activity",
"GTP binding",
"G-protein beta/gamma-subunit complex binding",
"G protein-coupled receptor signaling pathway",
"adenylate cyclase-modulating G protein-coupled receptor signaling pathway"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"PRINTS"
] | [
"PR00441"
] | [
"GPROTEINAI"
] | [
10139
] | 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-170670",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-381771",
"R-BTA-392170",
"R-BTA-400042",
"R-BTA-4086398",
"R-BTA-418594",
"R-BTA-9009391",
"R-BTA-9717207",
"R-CEL-170670",
"R-CEL-392170",
"R-CEL-400042",
"R-CEL-4086398",
"R-CEL-418594",
"R-CFA-170670",
"R-CFA-2485179",
"R-... | [
"REACTOME:R-BTA-170670",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-381771",
"REACTOME:R-BTA-392170",
"REACTOME:R-BTA-400042",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-9009391",
"REACTOME:R-BTA-9717207",
"REACTOME:R-CEL-170670",
"REACTOME:R-CE... | 66 | [
"1agr",
"1as0",
"1as2",
"1as3",
"1bh2",
"1bof",
"1cip",
"1fqj",
"1fqk",
"1gdd",
"1gfi",
"1gg2",
"1gia",
"1gil",
"1git",
"1got",
"1gp2",
"1kjy",
"1shz",
"1svk",
"1svs",
"1tad",
"1tag",
"1tnd",
"1y3a",
"2g83",
"2gtp",
"2ihb",
"2ik8",
"2ode",
"2om2",
"2v4z"... | 609 | [
"PUB00005142",
"PUB00014096",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172",
"PUB00015181",
"PUB00015183"
] | [
"1902986",
"12966076",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385",
"10669512",
"12854997"
] | [
"Diversity of G proteins in signal transduction.",
"Two-step mechanism of interaction of rhodopsin intermediates with the C-terminal region of the transducin alpha-subunit.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane... | [
1991,
2003,
2004,
2004,
2004,
2001,
1997,
2002,
2000,
2003
] | 10 | [
"IPR001019"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
10139
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
18,
3,
23,
21,
27
] | 6 | true | Family | G-protein alpha subunit, group I | G-protein alpha subunit, group I | Gprotein_alpha_I | 6 |
IPR001409 | 1,409 | Glucocorticoid receptor | Glcrtcd_rcpt | Family | 1,460 | false | false | null | [
"GO:0003677",
"GO:0004883",
"GO:0005496",
"GO:0006355",
"GO:0042921",
"GO:0005634"
] | [
"DNA binding",
"nuclear glucocorticoid receptor activity",
"steroid binding",
"regulation of DNA-templated transcription",
"nuclear receptor-mediated glucocorticoid signaling pathway",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PFAM",
"PRINTS"
] | [
"PF02155",
"PR00528"
] | [
"GCR",
"GLCORTICOIDR"
] | [
1460,
1044
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-3371497",
"R-HSA-383280",
"R-HSA-4090294",
"R-HSA-8849473",
"R-HSA-8939902",
"R-HSA-9615017",
"R-HSA-9679191",
"R-HSA-9768777",
"R-MMU-3371497",
"R-MMU-383280",
"R-MMU-4090294",
"R-RNO-3371497",
"R-RNO-383280",
"R-RNO-4090294"
] | [
"REACTOME:R-HSA-3371497",
"REACTOME:R-HSA-383280",
"REACTOME:R-HSA-4090294",
"REACTOME:R-HSA-8849473",
"REACTOME:R-HSA-8939902",
"REACTOME:R-HSA-9615017",
"REACTOME:R-HSA-9679191",
"REACTOME:R-HSA-9768777",
"REACTOME:R-MMU-3371497",
"REACTOME:R-MMU-383280",
"REACTOME:R-MMU-4090294",
"REACTOME:... | 14 | [
"7kw7"
] | 1 | [
"PUB00004464",
"PUB00006168"
] | [
"7899080",
"8165128"
] | [
"Vitamin D receptor contains multiple dimerization interfaces that are functionally different.",
"Human androgen receptor expressed in HeLa cells activates transcription in vitro."
] | [
1995,
1994
] | 2 | [
"IPR001723"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1460
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
16,
4,
8
] | 4 | true | Family | Glucocorticoid receptor | Glucocorticoid receptor | Glcrtcd_rcpt | 1 |
IPR001412 | 1,412 | Aminoacyl-tRNA synthetase, class I, conserved site | aa-tRNA-synth_I_CS | Conserved_site | 271,532 | false | false | This entry represents a conserved sequence in their N-terminal section of class I aminoacyl-tRNA synthetases. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes ... | [
"GO:0000166",
"GO:0004812",
"GO:0005524",
"GO:0006418"
] | [
"nucleotide binding",
"aminoacyl-tRNA ligase activity",
"ATP binding",
"tRNA aminoacylation for protein translation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PROSITE"
] | [
"PS00178"
] | [
"AA_TRNA_LIGASE_I"
] | [
271532
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"PDOC00161",
"R-BTA-9856649",
"R-DDI-9837999",
"R-DDI-9856649",
"R-DME-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-6782315",
"R-HSA-9837999",
"R-HSA-9856649",
"R-MMU-9837999",
"R-MMU-9856649",
"R-RNO-9856649",
"R-SCE-9837999",
"R-SPO-9837999"
] | [
"EC:6.1.1",
"PROSITEDOC:PDOC00161",
"REACTOME:R-BTA-9856649",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DDI-9856649",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9856649",
... | 17 | [
"1bs2",
"1d2r",
"1euq",
"1euy",
"1exd",
"1f4l",
"1f7u",
"1f7v",
"1ffy",
"1g59",
"1gax",
"1gln",
"1gsg",
"1gtr",
"1gts",
"1h3n",
"1i6k",
"1i6l",
"1i6m",
"1ile",
"1iq0",
"1irx",
"1ivs",
"1iyw",
"1j09",
"1j1u",
"1jii",
"1jij",
"1jik",
"1jil",
"1jzq",
"1jzs"... | 382 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4817,
201366,
61642,
147,
3560
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
85,
16,
25,
27,
9,
107,
53,
11,
66,
59,
13,
11,
157
] | 13 | true | Conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | Aminoacyl-tRNA synthetase, class I, conserved site | aa-tRNA-synth_I_CS | 6 |
IPR001413 | 1,413 | Dopamine D1 receptor | Dopamine_D1_rcpt | Family | 897 | false | false | Dopamine receptors are members of the rhodopsin-like G-protein coupled receptor family and are prominent in the vertebrate central nervous system (CNS). Dysfunction of dopaminergic neurotransmission in the CNS has been implicated in a variety of neuropsychiatric disorders [ ], including social phobia [ ], Tourette's sy... | [
"GO:0004952",
"GO:0007189",
"GO:0042311",
"GO:0005886"
] | [
"dopamine neurotransmitter receptor activity",
"adenylate cyclase-activating G protein-coupled receptor signaling pathway",
"vasodilation",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00565"
] | [
"DOPAMINED1AR"
] | [
897
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"214",
"R-BTA-390651",
"R-BTA-418555",
"R-HSA-390651",
"R-HSA-418555",
"R-MMU-390651",
"R-MMU-418555"
] | [
"IUPHAR:214",
"REACTOME:R-BTA-390651",
"REACTOME:R-BTA-418555",
"REACTOME:R-HSA-390651",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-390651",
"REACTOME:R-MMU-418555"
] | 7 | [
"7ckw",
"7ckx",
"7cky",
"7ckz",
"7crh",
"7f0t",
"7f1o",
"7f1z",
"7f23",
"7f24",
"7jv5",
"7jvp",
"7jvq",
"7ljc",
"7ljd",
"7x2c",
"7x2d",
"7x2f",
"8irr",
"8jxr",
"8jxs",
"9i52",
"9i54"
] | 23 | [
"PUB00064281",
"PUB00064282",
"PUB00064283",
"PUB00064284",
"PUB00064285",
"PUB00064286",
"PUB00064287",
"PUB00064288",
"PUB00064289",
"PUB00064290",
"PUB00064291",
"PUB00064292",
"PUB00064293",
"PUB00064296",
"PUB00064301",
"PUB00067001",
"PUB00067004",
"PUB00067005"
] | [
"15148138",
"10698826",
"16613557",
"17017512",
"12555236",
"16961425",
"11920678",
"9633679",
"16433053",
"14060771",
"1060115",
"12836695",
"9457173",
"12563019",
"16968475",
"16458973",
"9726645",
"15704231"
] | [
"The neurobiology of dopamine signaling.",
"Low dopamine D(2) receptor binding potential in social phobia.",
"Dopamine and the diseased brain.",
"The nigrostriatal DA pathway and Parkinson's disease.",
"Relationship between functional dopamine D2 and D3 receptors gene polymorphisms and neuroleptic malignant... | [
2004,
2000,
2006,
2006,
2003,
2006,
2002,
1998,
2005,
1963,
1975,
2003,
1998,
2003,
2006,
2006,
1998,
2005
] | 18 | [
"IPR000929"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
897
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
3,
3
] | 4 | true | Family | Dopamine D1 receptor | Dopamine D1 receptor | Dopamine_D1_rcpt | 3 |
IPR001414 | 1,414 | G-protein coupled receptor 143 | GPR143 | Family | 1,390 | false | false | G-protein coupled receptor 143 (also known as ocular albinism type 1, OA1) is a receptor for tyrosine, L-DOPA and dopamine. After binding to L-DOPA, it stimulates Ca2+ influx into the cytoplasm, increases secretion of the neurotrophic factor SERPINF1 and relocalises beta arrestin at the plasma membrane; this ligand-dep... | [
"GO:0004930",
"GO:0035240",
"GO:0072544",
"GO:0072545",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"dopamine binding",
"L-DOPA binding",
"L-tyrosine binding",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 6 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02101",
"PR00965",
"PTHR15177"
] | [
"Ocular_alb",
"OCULARALBNSM",
""
] | [
1384,
1288,
1382
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-375280",
"R-HSA-416476",
"R-HSA-9824585",
"R-MMU-375280",
"R-MMU-416476"
] | [
"REACTOME:R-HSA-375280",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-9824585",
"REACTOME:R-MMU-375280",
"REACTOME:R-MMU-416476"
] | 5 | [] | 0 | [
"PUB00003897",
"PUB00077410"
] | [
"7647783",
"1869779"
] | [
"Cloning of the gene for ocular albinism type 1 from the distal short arm of the X chromosome.",
"[Autoimmune thrombocytopenic purpura and pregnancy: significance of fetal blood punction]"
] | [
1995,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1390
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
3,
2
] | 4 | true | Family | G-protein coupled receptor 143 | G-protein coupled receptor 143 | GPR143 | 5 |
IPR001415 | 1,415 | Parathyroid hormone/parathyroid hormone-related protein | PTH/PTH-rel | Family | 2,451 | false | false | Parathyroid hormone (PTH) is a polypeptidic hormone that elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Parathyroid hormone-related protein (PTH-rP) is structurally related to PTH [ ] and seems to play a physiological role in lactation, possibly as a hormone for the mobilis... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROSITE",
"SMART"
] | [
"PF01279",
"PS00335",
"SM00087"
] | [
"Parathyroid",
"PARATHYROID",
"PTH"
] | [
2308,
1354,
2417
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00296",
"R-BTA-373080",
"R-BTA-418555",
"R-CFA-373080",
"R-GGA-373080",
"R-GGA-418555",
"R-HSA-373080",
"R-HSA-418555",
"R-MMU-373080",
"R-MMU-418555",
"R-RNO-373080",
"R-SSC-373080",
"R-SSC-418555"
] | [
"PROSITEDOC:PDOC00296",
"REACTOME:R-BTA-373080",
"REACTOME:R-BTA-418555",
"REACTOME:R-CFA-373080",
"REACTOME:R-GGA-373080",
"REACTOME:R-GGA-418555",
"REACTOME:R-HSA-373080",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-373080",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-373080",
"REACTOME:R-SSC-3730... | 13 | [
"1bwx",
"1bzg",
"1et1",
"1fvy",
"1hph",
"1hpy",
"1hth",
"1m5n",
"1zwa",
"1zwb",
"1zwc",
"1zwd",
"1zwe",
"1zwf",
"1zwg",
"2l1x",
"3ffd",
"3h3g",
"6fj3",
"6nbf",
"6nbh",
"6nbi",
"7uzo",
"7vvj",
"7vvk",
"7vvl",
"7vvm",
"7vvn",
"7vvo",
"7y35",
"7y36",
"8d51"... | 47 | [
"PUB00005076",
"PUB00056855"
] | [
"2682846",
"11760831"
] | [
"Parathyroid hormone-related protein: isolation, molecular cloning, and mechanism of action.",
"Parathyroid hormone-related protein is required for normal intramembranous bone development."
] | [
1989,
2001
] | 2 | [] | [
"IPR003625",
"IPR003626"
] | 0 | 2 | 0 | [
"Bacillati",
"Eukaryota"
] | [
2,
2449
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
5,
5,
6
] | 4 | true | Family | Parathyroid hormone/parathyroid hormone-related protein | Parathyroid hormone/parathyroid hormone-related protein | PTH/PTH-rel | 1 |
IPR001416 | 1,416 | Atypical chemokine receptor 3 | ACKR3 | Family | 952 | false | false | Just like classical chemokine receptors, atypical chemokine receptors (ACKRs) are seven-transmembrane-helix (7TM) receptors that bind chemokines [ ]. However, they lack the canonical DRYLAIV motif necessary for GPCR coupling to G proteins and induction of classical signalling pathways. Instead, ACKRs internalise their ... | [
"GO:0015026",
"GO:0019956",
"GO:0001525",
"GO:0001570",
"GO:0006935",
"GO:0016020"
] | [
"coreceptor activity",
"chemokine binding",
"angiogenesis",
"vasculogenesis",
"chemotaxis",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PRINTS"
] | [
"PR00646"
] | [
"RDC1ORPHANR"
] | [
952
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-380108",
"R-HSA-418594",
"R-MMU-380108",
"R-MMU-418594",
"R-RNO-380108",
"R-RNO-418594"
] | [
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-380108",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-380108",
"REACTOME:R-RNO-418594"
] | 6 | [
"7sk3",
"7sk4",
"7sk5",
"7sk6",
"7sk7",
"7sk8",
"7sk9",
"8tii",
"8til",
"8tin",
"8tio",
"8vj9",
"9e82"
] | 13 | [
"PUB00064797",
"PUB00064935",
"PUB00064936",
"PUB00064937",
"PUB00064938",
"PUB00064949",
"PUB00064950",
"PUB00064951",
"PUB00064959",
"PUB00077489",
"PUB00077491"
] | [
"20161793",
"10623723",
"18442043",
"17804806",
"20018651",
"20388803",
"16940167",
"17898181",
"19641136",
"24319779",
"24549061"
] | [
"CXCR7 functions as a scavenger for CXCL12 and CXCL11.",
"A putative G protein-coupled receptor, RDC1, is a novel coreceptor for human and simian immunodeficiency viruses.",
"Early postnatal lethality and cardiovascular defects in CXCR7-deficient mice.",
"Disrupted cardiac development but normal hematopoiesis... | [
2010,
2000,
2008,
2007,
2010,
2010,
2006,
2007,
2009,
2013,
2014
] | 11 | [
"IPR047143"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
952
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
2,
1,
1
] | 4 | true | Family | Atypical chemokine receptor 3 | Atypical chemokine receptor 3 | ACKR3 | 1 |
IPR001418 | 1,418 | Opioid receptor | Opioid_rcpt | Family | 4,867 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004985",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled opioid receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00384"
] | [
"OPIOIDR"
] | [
4867
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-375276",
"R-BTA-418594",
"R-HSA-111885",
"R-HSA-202040",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-6785807",
"R-HSA-9022699",
"R-MMU-111885",
"R-MMU-202040",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-111885",
"R-RNO-202040",
"R-RNO-375276",
"R-RNO-418594"
] | [
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418594",
"REACTOME:R-HSA-111885",
"REACTOME:R-HSA-202040",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-9022699",
"REACTOME:R-MMU-111885",
"REACTOME:R-MMU-202040",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-4... | 16 | [
"4ea3",
"4n6h",
"4rwa",
"4rwd",
"5c1m",
"5dhg",
"5dhh",
"6b73",
"6dde",
"6ddf",
"6pt2",
"6pt3",
"6vi4",
"7sbf",
"7scg",
"7t2g",
"7t2h",
"7u2k",
"7u2l",
"7ul4",
"7y1f",
"7yit",
"8dzp",
"8dzq",
"8dzr",
"8dzs",
"8e0g",
"8ef5",
"8ef6",
"8efb",
"8efl",
"8efo"... | 66 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR000276"
] | [
"IPR000105",
"IPR000321",
"IPR000452",
"IPR001420"
] | 1 | 4 | 0 | [
"Bilateria"
] | [
4867
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
20,
24,
26,
28
] | 4 | true | Family | Opioid receptor | Opioid receptor | Opioid_rcpt | 2 |
IPR001419 | 1,419 | HMW glutenin | Glutenin | Family | 754 | false | false | Gluten is the protein component of wheat flour. It consists of numerous proteins, which are of two different types responsible for different physical properties of dough: the glutenins, which are primarily responsible for the elasticity, and the gliadins, which contribute to the extensibility. The glutenins are of two ... | [
"GO:0045735"
] | [
"nutrient reservoir activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF03157",
"PR00210"
] | [
"Glutenin_hmw",
"GLUTENIN"
] | [
747,
735
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00004336",
"PUB00007144"
] | [
"3840588",
"11084370"
] | [
"Nucleotide sequence of a gene from chromosome 1D of wheat encoding a HMW-glutenin subunit.",
"Elastomeric proteins: biological roles, structures and mechanisms."
] | [
1985,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
749
] | 2 | [
"Oryza sativa subsp. japonica"
] | [
1
] | 1 | true | Family | HMW glutenin | HMW glutenin | Glutenin | 3 |
IPR001420 | 1,420 | X opioid receptor | X_opioid_rcpt | Family | 867 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0001626",
"GO:0007186",
"GO:0016020"
] | [
"nociceptin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00547"
] | [
"XOPIOIDR"
] | [
867
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"320",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594"
] | [
"IUPHAR:320",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594"
] | 7 | [
"4ea3",
"5dhg",
"5dhh",
"8f7x"
] | 4 | [
"PUB00000131",
"PUB00001674",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"8137918",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"ORL1, a novel member of the opioid receptor family. Cloning, functional expression and localization.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled r... | [
1990,
1994,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 11 | [
"IPR001418"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
867
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
8,
7,
12
] | 4 | true | Family | X opioid receptor | X opioid receptor | X_opioid_rcpt | 9 |
IPR001421 | 1,421 | ATP synthase protein 8, metazoa | ATP8_metazoa | Family | 22,691 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [
"GO:0015078",
"GO:0015986"
] | [
"proton transmembrane transporter activity",
"proton motive force-driven ATP synthesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00895"
] | [
"ATP-synt_8"
] | [
22691
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-163210",
"R-BTA-5419276",
"R-BTA-8949613",
"R-HSA-163210",
"R-HSA-5419276",
"R-HSA-8949613",
"R-MMU-163210",
"R-MMU-5419276",
"R-MMU-8949613",
"R-RNO-163210",
"R-RNO-5419276",
"R-RNO-8949613",
"R-SSC-163210",
"R-SSC-5419276",
"R-SSC-8949613"
] | [
"REACTOME:R-BTA-163210",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-8949613",
"REACTOME:R-HSA-163210",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-8949613",
"REACTOME:R-MMU-163210",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-8949613",
"REACTOME:R-RNO-163210",
"REACTOME:R-RNO-5419276",
"REACTOME:R-... | 15 | [
"6j54",
"6j5a",
"6j5i",
"6j5j",
"6j5k",
"6tt7",
"6za9",
"6zbb",
"6ziq",
"6zit",
"6ziu",
"6zmr",
"6zna",
"6zpo",
"6zqm",
"6zqn",
"7ajb",
"7ajc",
"7ajd",
"7aje",
"7ajf",
"7ajg",
"7ajh",
"7aji",
"7ajj",
"8h9f",
"8h9j",
"8h9m",
"8h9q",
"8h9s",
"8h9t",
"8h9u"... | 37 | [
"PUB00009752",
"PUB00020603",
"PUB00020604",
"PUB00020648",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"11309608",
"15473999",
"15078220",
"12626501",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"The molecular neighborhood ... | [
2001,
2004,
2004,
2003,
2010,
2008,
1992,
1998
] | 8 | [] | [
"IPR039017"
] | 0 | 1 | 0 | [
"Bilateria"
] | [
22691
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
288,
6,
4
] | 5 | true | Family | ATP synthase protein 8, metazoa | ATP synthase protein 8, metazoa | ATP8_metazoa | 5 |
IPR001423 | 1,423 | Lysophospholipase patatin, conserved site | LysoPLipase_patatin_CS | Conserved_site | 5,463 | false | false | Lysophospholipase NTE1 was identified in yeast as an endoplasmic reticulum integral membrane protein that acts as a phospholipase B, catalysing the double deacylation of phosphatidylcholine to glycerophosphocholine [ ]. Phosphatidylcholine is the major phospholipid component of eukaryotic membranes. NTE1 plays an impor... | [
"GO:0004622",
"GO:0046470"
] | [
"phosphatidylcholine lysophospholipase A1 activity",
"phosphatidylcholine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01237"
] | [
"UPF0028"
] | [
5463
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1.5",
"PWY-7409",
"PDOC00951",
"R-CEL-6814848",
"R-DME-6814848",
"R-HSA-6814848",
"R-MMU-6814848",
"R-SCE-6814848"
] | [
"EC:3.1.1.5",
"METACYC:PWY-7409",
"PROSITEDOC:PDOC00951",
"REACTOME:R-CEL-6814848",
"REACTOME:R-DME-6814848",
"REACTOME:R-HSA-6814848",
"REACTOME:R-MMU-6814848",
"REACTOME:R-SCE-6814848"
] | 8 | [] | 0 | [
"PUB00042556",
"PUB00042557"
] | [
"16731034",
"16781190"
] | [
"Phosphatidylcholine synthesis and its catabolism by yeast neuropathy target esterase 1.",
"Transport and metabolism of glycerophosphodiesters produced through phospholipid deacylation."
] | [
2007,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1848,
3609,
6
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
2,
11,
2,
1,
3,
4,
1,
5,
1
] | 9 | true | Conserved_site | Lysophospholipase patatin, conserved site | Lysophospholipase patatin, conserved site | LysoPLipase_patatin_CS | 3 |
IPR001425 | 1,425 | Archaeal/bacterial/fungal rhodopsins | Arc/bac/fun_rhodopsins | Family | 10,329 | false | false | Bacterial rhodopsins are a family of bacterial opsins. They are retinal-binding proteins that provide light-dependent ion transport and sensory functions to a family of halophilic bacteria [ , ]. They are integral membrane proteins believed to contain seven transmembrane (TM) domains, the last of which contains the att... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER",
"SMART"
] | [
"PF01036",
"PR00251",
"PTHR28286",
"SM01021"
] | [
"Bac_rhodopsin",
"BACTRLOPSIN",
"",
"Bac_rhodopsin"
] | [
9942,
5529,
6156,
6737
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00291"
] | [
"PROSITEDOC:PDOC00291"
] | 1 | [
"1ap9",
"1at9",
"1bct",
"1bha",
"1bhb",
"1bm1",
"1brd",
"1brr",
"1brx",
"1c3w",
"1c8r",
"1c8s",
"1cwq",
"1dze",
"1e0p",
"1e12",
"1f4z",
"1f50",
"1fbb",
"1fbk",
"1gu8",
"1gue",
"1h2s",
"1h68",
"1iw6",
"1iw9",
"1ixf",
"1jgj",
"1jv6",
"1jv7",
"1kg8",
"1kg9"... | 477 | [
"PUB00001180",
"PUB00005349",
"PUB00160333",
"PUB00160334"
] | [
"2591367",
"2468194",
"25589426",
"37871207"
] | [
"Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.",
"Two pumps, one principle: light-driven ion transport in halobacteria.",
"The CarO rhodopsin of the fungus Fusarium fujikuroi is a light-driven proton pump that retards spore germination.",
"Diversity of rhodopsin cyclases in zoospore-f... | [
1989,
1989,
2015,
2023
] | 4 | [] | [
"IPR017402"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1124,
1532,
4277,
7,
3389
] | 5 | [
"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)"
] | [
2,
3,
1
] | 3 | true | Family | Archaeal/bacterial/fungal rhodopsins | Archaeal/bacterial/fungal rhodopsins | Arc/bac/fun_rhodopsins | 7 |
IPR001426 | 1,426 | Tyrosine-protein kinase, receptor class V, conserved site | Tyr_kinase_rcpt_V_CS | Conserved_site | 19,424 | false | false | null | [
"GO:0005003",
"GO:0005524",
"GO:0006468",
"GO:0007169",
"GO:0016020"
] | [
"ephrin receptor activity",
"ATP binding",
"protein phosphorylation",
"cell surface receptor protein tyrosine kinase signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PROSITE",
"PROSITE"
] | [
"PS00790",
"PS00791"
] | [
"RECEPTOR_TYR_KIN_V_1",
"RECEPTOR_TYR_KIN_V_2"
] | [
16799,
17741
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"PDOC00629",
"R-DRE-2682334",
"R-DRE-3928662",
"R-DRE-3928663",
"R-DRE-3928664",
"R-DRE-3928665",
"R-GGA-2682334",
"R-GGA-3928663",
"R-GGA-3928665",
"R-HSA-2682334",
"R-HSA-2892247",
"R-HSA-373760",
"R-HSA-3928662",
"R-HSA-3928663",
"R-HSA-3928664",
"R-HSA-3928665",
"R-... | [
"EC:2.7.10.1",
"PROSITEDOC:PDOC00629",
"REACTOME:R-DRE-2682334",
"REACTOME:R-DRE-3928662",
"REACTOME:R-DRE-3928663",
"REACTOME:R-DRE-3928664",
"REACTOME:R-DRE-3928665",
"REACTOME:R-GGA-2682334",
"REACTOME:R-GGA-3928663",
"REACTOME:R-GGA-3928665",
"REACTOME:R-HSA-2682334",
"REACTOME:R-HSA-28922... | 46 | [
"1kgy",
"1nuk",
"1shw",
"2x10",
"2x11",
"3c8x",
"3czu",
"3etp",
"3fl7",
"3mbw",
"3mx0",
"3skj",
"4bk4",
"4bk5",
"4bka",
"4bkf",
"4m4p",
"4m4r",
"7b7n",
"7czf",
"7k7j",
"7s7k",
"8trs",
"8trt",
"8trv",
"8tv1",
"8tv5"
] | 27 | [
"PUB00000055",
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
] | [
"3052279",
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350"
] | [
"Growth factor receptor tyrosine kinases.",
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery... | [
1988,
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 9 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
19424
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
86,
10,
54,
48,
57
] | 5 | true | Conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | Tyrosine-protein kinase, receptor class V, conserved site | Tyr_kinase_rcpt_V_CS | 7 |
IPR001427 | 1,427 | Pancreatic ribonuclease | RNaseA | Family | 4,075 | false | false | Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [ ]. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cycli... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR00794",
"PTHR11437"
] | [
"RIBONUCLEASE",
""
] | [
2811,
4052
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00118",
"R-BTA-6803157",
"R-DRE-418990",
"R-DRE-6798695",
"R-DRE-6803157",
"R-GGA-418990",
"R-GGA-6798695",
"R-GGA-6803157",
"R-HSA-418990",
"R-HSA-6798695",
"R-HSA-6803157",
"R-HSA-9613829",
"R-HSA-9615710",
"R-HSA-9708296",
"R-HSA-9925561",
"R-MMU-418990",
"R-MMU-6798695",
"... | [
"PROSITEDOC:PDOC00118",
"REACTOME:R-BTA-6803157",
"REACTOME:R-DRE-418990",
"REACTOME:R-DRE-6798695",
"REACTOME:R-DRE-6803157",
"REACTOME:R-GGA-418990",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-6803157",
"REACTOME:R-HSA-418990",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6803157",
"REACTOME:R-H... | 20 | [
"11ba",
"11bg",
"1a2w",
"1a4y",
"1a5p",
"1a5q",
"1afk",
"1afl",
"1afu",
"1agi",
"1ang",
"1aqp",
"1awz",
"1b1e",
"1b1i",
"1b1j",
"1b6v",
"1bc4",
"1bel",
"1bsr",
"1bzq",
"1c0b",
"1c0c",
"1c8w",
"1c9v",
"1c9x",
"1cjq",
"1cjr",
"1d5d",
"1d5e",
"1d5h",
"1dfj"... | 521 | [
"PUB00000315",
"PUB00001546",
"PUB00003106",
"PUB00004682"
] | [
"2611266",
"3940901",
"2473157",
"2734298"
] | [
"Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily.",
"Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases.",
"Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclea... | [
1989,
1986,
1989,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
4075
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
1,
41,
58,
47
] | 5 | true | Family | Pancreatic ribonuclease | Pancreatic ribonuclease | RNaseA | 9 |
IPR001429 | 1,429 | P2X purinoreceptor | P2X_purnocptor | Family | 7,923 | false | false | This entry represents all P2X purinoreceptor subtypes. P2X purinoceptors are cell membrane ion channels, gated by adenosine 5'-triphosphate (ATP) and other nucleotides; they have been found to be widely expressed on mammalian cells, and, by means of their functional properties, can be differentiated into three sub-grou... | [
"GO:0001614",
"GO:0004931",
"GO:0033198",
"GO:0098655",
"GO:0005886"
] | [
"purinergic nucleotide receptor activity",
"extracellularly ATP-gated monoatomic cation channel activity",
"response to ATP",
"monoatomic cation transmembrane transport",
"plasma membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PIRSF",
"PRINTS",
"NCBIFAM"
] | [
"PIRSF005713",
"PR01307",
"TIGR00863"
] | [
"P2X_purinoceptor",
"P2XRECEPTOR",
"P2X"
] | [
5057,
7805,
7172
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00932",
"R-BTA-139853",
"R-BTA-418346",
"R-DRE-139853",
"R-DRE-418346",
"R-HSA-139853",
"R-HSA-418346",
"R-HSA-6798695",
"R-HSA-844456",
"R-HSA-9660826",
"R-HSA-9856532",
"R-MMU-139853",
"R-MMU-418346",
"R-MMU-6798695",
"R-MMU-844456",
"R-RNO-139853",
"R-RNO-418346",
"R-RNO-67... | [
"PROSITEDOC:PDOC00932",
"REACTOME:R-BTA-139853",
"REACTOME:R-BTA-418346",
"REACTOME:R-DRE-139853",
"REACTOME:R-DRE-418346",
"REACTOME:R-HSA-139853",
"REACTOME:R-HSA-418346",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-844456",
"REACTOME:R-HSA-9660826",
"REACTOME:R-HSA-9856532",
"REACTOME:R-MMU-1... | 19 | [
"3h9v",
"3i5d",
"4dw0",
"4dw1",
"5f1c",
"5svj",
"5svk",
"5svl",
"5svm",
"5svp",
"5svq",
"5svr",
"5svs",
"5svt",
"5u1l",
"5u1u",
"5u1v",
"5u1w",
"5u1x",
"5u1y",
"5u2h",
"5wzy",
"5xw6",
"5yve",
"6ah4",
"6ah5",
"6u9v",
"6u9w",
"8jv5",
"8jv6",
"8jv7",
"8jv8"... | 71 | [
"PUB00006451",
"PUB00007054",
"PUB00100494"
] | [
"10414359",
"12270951",
"29631184"
] | [
"Functional and molecular diversity of purinergic ion channel receptors.",
"Molecular physiology of P2X receptors.",
"Modulation of innate and adaptive immunity by P2X ion channels."
] | [
1999,
2002,
2018
] | 3 | [
"IPR059116"
] | [
"IPR003044",
"IPR003045",
"IPR003046",
"IPR003047",
"IPR003048",
"IPR003049",
"IPR003050"
] | 1 | 7 | 0 | [
"Eukaryota"
] | [
7923
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
22,
25,
33,
54
] | 4 | true | Family | P2X purinoreceptor | P2X purinoreceptor | P2X_purnocptor | 4 |
IPR001431 | 1,431 | Peptidase M16, zinc-binding site | Pept_M16_Zn_BS | Binding_site | 45,429 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [
"GO:0004222",
"GO:0006508"
] | [
"metalloendopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00143"
] | [
"INSULINASE"
] | [
45429
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.24",
"PDOC00130",
"R-BTA-5689880",
"R-BTA-611105",
"R-BTA-77387",
"R-BTA-8949664",
"R-BTA-9033241",
"R-BTA-9837999",
"R-BTA-9865881",
"R-CEL-611105",
"R-CEL-8949664",
"R-CEL-9865881",
"R-DDI-611105",
"R-DDI-9033241",
"R-DME-5689880",
"R-DME-9033241",
"R-HSA-1268020",
"R-HSA-56... | [
"EC:3.4.24",
"PROSITEDOC:PDOC00130",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-8949664",
"REACTOME:R-BTA-9033241",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9865881",
"REACTOME:R-CEL-611105",
"REACTOME:R-CEL-8949664",
"REACTOME:R-CEL-9865881",
... | 46 | [
"1bcc",
"1be3",
"1bgy",
"1ezv",
"1hr6",
"1hr7",
"1hr8",
"1hr9",
"1kb9",
"1kyo",
"1l0l",
"1l0n",
"1ntk",
"1ntm",
"1ntz",
"1nu1",
"1p84",
"1pp9",
"1ppj",
"1q2l",
"1qcr",
"1sqb",
"1sqp",
"1sqq",
"1sqv",
"1sqx",
"2a06",
"2bcc",
"2fyu",
"2ibz",
"2jg4",
"2ybb"... | 192 | [
"PUB00000495",
"PUB00003579",
"PUB00004194",
"PUB00004779",
"PUB00005438",
"PUB00015338"
] | [
"2025223",
"7674922",
"7990931",
"1570301",
"7610476",
"7674956"
] | [
"Homologues of insulinase, a new superfamily of metalloendopeptidases.",
"Evolutionary families of metallopeptidases.",
"A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes.",
"An unusual active site identified in a family of zinc metalloendopeptidases.",
"Ar... | [
1991,
1995,
1994,
1992,
1995,
1995
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5,
25910,
18985,
35,
494
] | 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",... | [
26,
10,
10,
7,
2,
51,
14,
2,
31,
34,
5,
3,
54
] | 13 | true | Binding_site | Peptidase M16, zinc-binding site | Peptidase M16, zinc-binding site | Pept_M16_Zn_BS | 9 |
IPR001432 | 1,432 | Muscarinic acetylcholine receptor M4 | Musac_Ach_M4_rcpt | Family | 1,805 | false | false | Muscarinic acetylcholine receptors are members of rhodopsin-like G-protein coupled receptor family. They play several important roles; they mediate many of the effects of acetylcholine in the central and peripheral nervous system and modulate a variety of physiological functions, such as airway, eye and intestinal smoo... | [
"GO:0016907",
"GO:0007186",
"GO:0040012",
"GO:0005886"
] | [
"G protein-coupled acetylcholine receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of locomotion",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"CDD"
] | [
"PR00541",
"cd15298"
] | [
"MUSCRINICM4R",
"7tmA_mAChR_M4"
] | [
1785,
692
] | 2 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"16",
"R-HSA-390648",
"R-HSA-418594",
"R-MMU-390648",
"R-MMU-418594",
"R-RNO-390648",
"R-RNO-418594"
] | [
"IUPHAR:16",
"REACTOME:R-HSA-390648",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-390648",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-390648",
"REACTOME:R-RNO-418594"
] | 7 | [
"5dsg",
"7trk",
"7trp",
"7trq",
"7trs",
"7v68",
"7v69",
"7v6a",
"8e9x",
"8fx5",
"9iqs"
] | 11 | [
"PUB00064316",
"PUB00064317",
"PUB00064318",
"PUB00064319",
"PUB00064320",
"PUB00064321",
"PUB00064322",
"PUB00064323",
"PUB00064324",
"PUB00064325",
"PUB00064326",
"PUB00064331",
"PUB00064336",
"PUB00064337",
"PUB00064343",
"PUB00064356",
"PUB00064357",
"PUB00064358",
"PUB000643... | [
"3443095",
"3272174",
"3037705",
"9647869",
"2470172",
"8853955",
"10841527",
"14641022",
"12725869",
"17762886",
"15850824",
"7751967",
"14744253",
"15474550",
"11714883",
"2402490",
"8429821",
"9353395",
"10711347",
"12144929",
"10468635",
"20147565",
"21373792",
"180... | [
"Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.",
"Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.",
"Identification of a family of muscarinic acetylcholine receptor genes.",
"Inter... | [
1987,
1988,
1987,
1998,
1989,
1996,
2000,
2003,
2003,
2007,
2005,
1995,
2004,
2004,
2001,
1990,
1993,
1997,
2000,
2002,
1999,
2010,
2011,
2008,
2010,
2010
] | 26 | [
"IPR000995"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1805
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
3
] | 4 | true | Family | Muscarinic acetylcholine receptor M4 | Muscarinic acetylcholine receptor M4 | Musac_Ach_M4_rcpt | 8 |
IPR001433 | 1,433 | Oxidoreductase FAD/NAD(P)-binding | OxRdtase_FAD/NAD-bd | Domain | 154,947 | false | false | Bacterial ferredoxin-NADP + reductase may be bound to the thylakoid membrane or anchored to the thylakoid-bound phycobilisomes. Chloroplast ferredoxin-NADP + reductase ( ) may play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing ... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00175"
] | [
"NAD_binding_1"
] | [
154947
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1320",
"GenProp1418",
"GenProp1481",
"GenProp1554",
"R-BTA-114608",
"R-BTA-1237044",
"R-BTA-196836",
"R-BTA-211945",
"R-BTA-6798695",
"R-CEL-156581",
"R-CEL-1614635",
"R-CEL-9759218",
"R-CFA-196836",
"R-CFA-211945",
"R-CFA-6798695",
"R-DDI-114608",
"R-DDI-1222556",
"R-DDI-1... | [
"GP:GenProp1320",
"GP:GenProp1418",
"GP:GenProp1481",
"GP:GenProp1554",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1237044",
"REACTOME:R-BTA-196836",
"REACTOME:R-BTA-211945",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-156581",
"REACTOME:R-CEL-1614635",
"REACTOME:R-CEL-9759218",
"REACTOME:R-CFA-... | 131 | [
"1a8p",
"1amo",
"1b2r",
"1bjk",
"1bqe",
"1bx0",
"1bx1",
"1cne",
"1cnf",
"1cqx",
"1ddg",
"1ddi",
"1e62",
"1e63",
"1e64",
"1ep1",
"1ep2",
"1ep3",
"1ewy",
"1f20",
"1fdr",
"1fnb",
"1fnc",
"1fnd",
"1frn",
"1frq",
"1gaq",
"1gaw",
"1gjr",
"1go2",
"1gr1",
"1gvh"... | 260 | [] | [] | [] | [] | 0 | [] | [
"IPR001709"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Vibrio phage VP-HS15",
"plasmids",
"unclassified sequences"
] | [
859,
100165,
52932,
1,
3,
987
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
56,
9,
45,
22,
6,
51,
26,
12,
39,
66,
7,
7,
138
] | 13 | true | Domain | Oxidoreductase FAD/NAD(P)-binding | Oxidoreductase FAD/NAD(P)-binding | OxRdtase_FAD/NAD-bd | 4 |
IPR001434 | 1,434 | Large cysteine-rich periplasmic protein OmcB-like, DUF11 domain | OmcB-like_DUF11 | Domain | 16,203 | false | false | This entry represents DUF11 domain found in large cysteine-rich periplasmic protein OmcB proteins from bacteria and archaea. It adopts an Ig-like fold. Some members contain conserved N-terminal lysine and C-terminal asparagine with central aspartate/glutamate suggesting that these domains may contain an isopeptide bond... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01345"
] | [
"DUF11"
] | [
16203
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009430",
"PUB00097782"
] | [
"2287277",
"31189768"
] | [
"Cysteine-rich outer membrane proteins of Chlamydia trachomatis display compensatory sequence changes between biovariants.",
"An Aggregation-defective Mutant of Methanothermobacter sp. CaT2 Reveals Unique Protein-dependent Aggregation."
] | [
1990,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1038,
14866,
58,
6,
235
] | 5 | [] | [] | 0 | true | Domain | Large cysteine-rich periplasmic protein OmcB-like, DUF11 domain | Large cysteine-rich periplasmic protein OmcB-like, DUF11 domain | OmcB-like_DUF11 | 2 |
IPR001435 | 1,435 | Adenosine A2B receptor | Adeno_A2B_rcpt | Family | 577 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00554"
] | [
"ADENOSINA2BR"
] | [
577
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"20",
"R-BTA-417973",
"R-BTA-418555",
"R-BTA-5683826",
"R-GGA-417973",
"R-GGA-418555",
"R-GGA-5683826",
"R-HSA-417973",
"R-HSA-418555",
"R-HSA-5683826",
"R-HSA-9660821",
"R-MMU-417973",
"R-MMU-418555",
"R-MMU-5683826",
"R-RNO-417973",
"R-RNO-5683826"
] | [
"IUPHAR:20",
"REACTOME:R-BTA-417973",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-5683826",
"REACTOME:R-GGA-417973",
"REACTOME:R-GGA-418555",
"REACTOME:R-GGA-5683826",
"REACTOME:R-HSA-417973",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-5683826",
"REACTOME:R-HSA-9660821",
"REACTOME:R-MMU-417973",
... | 16 | [
"7xy6",
"7xy7",
"8hdo",
"8hdp"
] | 4 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR001634"
] | [] | 1 | 0 | 1 | [
"Tetrapoda"
] | [
577
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
5
] | 3 | true | Family | Adenosine A2B receptor | Adenosine A2B receptor | Adeno_A2B_rcpt | 1 |
IPR001436 | 1,436 | Alpha crystallin/Small heat shock protein, animal type | Alpha-crystallin/sHSP_animal | Family | 17,491 | false | false | This entry represents a group of alpha-crystallin domain containing proteins from animals, including the A and B subunits (or chains) of alpha-crystallin and related small heat shock proteins. HSPs can be divided into HSP100, HSP90, HSP70, HSP60, HSP40 and small heat shock proteins (sHSPs) according to their molecular ... | [] | [] | [] | 0 | [
"PRINTS",
"PANTHER"
] | [
"PR00299",
"PTHR45640"
] | [
"ACRYSTALLIN",
""
] | [
13331,
15197
] | 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-3371571",
"R-BTA-4420097",
"R-BTA-450408",
"R-BTA-5687128",
"R-BTA-9009391",
"R-CEL-3371571",
"R-CEL-4420097",
"R-DME-3371571",
"R-DME-4420097",
"R-DME-9009391",
"R-GGA-3371571",
"R-HSA-3371571",
"R-HSA-4420097",
"R-HSA-450408",
"R-HSA-5687128",
"R-HSA-9009391",
"R-MMU-3371571... | [
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-450408",
"REACTOME:R-BTA-5687128",
"REACTOME:R-BTA-9009391",
"REACTOME:R-CEL-3371571",
"REACTOME:R-CEL-4420097",
"REACTOME:R-DME-3371571",
"REACTOME:R-DME-4420097",
"REACTOME:R-DME-9009391",
"REACTOME:R-GGA-3371571",
"REACTOME... | 27 | [
"2bol",
"2klr",
"2n0k",
"2n3j",
"2wj5",
"2wj7",
"2y1y",
"2y1z",
"2y22",
"2ygd",
"3j07",
"3l1e",
"3l1f",
"3l1g",
"3n3e",
"3q9p",
"3q9q",
"4jus",
"4jut",
"4m5s",
"4m5t",
"4mjh",
"4ydz",
"4ye0",
"5ltw",
"5lum",
"6bp9",
"6dv5",
"6f2r",
"6gjh",
"6t1r",
"7pe3"... | 37 | [
"PUB00003917",
"PUB00005345",
"PUB00034659",
"PUB00087792",
"PUB00087815"
] | [
"7634077",
"2688200",
"15575808",
"11875128",
"10950306"
] | [
"The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes.",
"Evolution of eye lens crystallins: the stress connection.",
"alpha-crystallin: a review of its structure and function.",
"Alpha-crystallin-type heat shock proteins: socializing minichaperones in th... | [
1994,
1989,
2004,
2002,
2000
] | 5 | [] | [
"IPR043254",
"IPR055269"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
43,
17433,
13,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
19,
18,
43,
18,
25
] | 6 | true | Family | Alpha crystallin/Small heat shock protein, animal type | Alpha crystallin/Small heat shock protein, animal type | Alpha-crystallin/sHSP_animal | 1 |
IPR001437 | 1,437 | Transcription elongation factor, GreA/GreB, C-terminal | Tscrpt_elong_fac_GreA/B_C | Domain | 44,514 | false | false | Bacterial proteins GreA and GreB are necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. Arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked DNA/RNA/ polymerase ternary complexes. ... | [
"GO:0003677",
"GO:0032784"
] | [
"DNA binding",
"regulation of DNA-templated transcription elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01272"
] | [
"GreA_GreB"
] | [
44514
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00651"
] | [
"PROSITEDOC:PDOC00651"
] | 1 | [
"1grj",
"2etn",
"2eul",
"2f23",
"2p4v",
"2pn0",
"3aoh",
"3aoi",
"3bmb",
"4wqt",
"6ri7",
"6rin"
] | 12 | [
"PUB00000884",
"PUB00004205",
"PUB00011909"
] | [
"8431948",
"7854424",
"12914698"
] | [
"Transcript cleavage factors from E. coli.",
"Crystal structure of the GreA transcript cleavage factor from Escherichia coli.",
"Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase."
] | [
1993,
1995,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
12,
43707,
92,
2,
701
] | 5 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Transcription elongation factor, GreA/GreB, C-terminal | Transcription elongation factor, GreA/GreB, C-terminal | Tscrpt_elong_fac_GreA/B_C | 8 |
IPR001439 | 1,439 | Hyaluronidase PH20/Hyaluronidase-5 | Hyaluronidase_PH20/Hyal5 | Family | 690 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004415",
"GO:0007342"
] | [
"hyalurononglucosaminidase activity",
"fusion of sperm to egg plasma membrane involved in single fertilization"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF500773"
] | [
"Hyaluronidase_PH20_Hyal5"
] | [
690
] | 1 | [
"CAZY",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH56",
"3.2.1.35",
"PWY-6573",
"R-HSA-2160916",
"R-HSA-2534343",
"R-MMU-2160916",
"R-MMU-2534343"
] | [
"CAZY:GH56",
"EC:3.2.1.35",
"METACYC:PWY-6573",
"REACTOME:R-HSA-2160916",
"REACTOME:R-HSA-2534343",
"REACTOME:R-MMU-2160916",
"REACTOME:R-MMU-2534343"
] | 7 | [
"9jub"
] | 1 | [
"PUB00001670",
"PUB00003064",
"PUB00004870",
"PUB00005266",
"PUB00086642",
"PUB00086643"
] | [
"8282124",
"2269661",
"7624375",
"8535779",
"19605784",
"16330764"
] | [
"The human sperm protein PH-20 has hyaluronidase activity.",
"cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals.",
"Conserved catalytic machinery and the prediction of a common fold for several famil... | [
1993,
1990,
1995,
1995,
2009,
2005
] | 6 | [
"IPR018155"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
690
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
4
] | 3 | true | Family | Hyaluronidase PH20/Hyaluronidase-5 | Hyaluronidase PH20/Hyaluronidase-5 | Hyaluronidase_PH20/Hyal5 | 5 |
IPR001441 | 1,441 | Decaprenyl diphosphate synthase-like | UPP_synth-like | Family | 42,126 | false | false | In prokaryotes, undecaprenyl diphosphate synthase (UPP synthase, di-trans-poly-cis-decaprenylcistransferase or ditrans,polycis-undecaprenyl-diphosphate synthase ( )), catalyzes the formation of the carrier lipid undecaprenyl pyrophosphate (UPP) in bacterial cell wall peptidoglycan biosynthesis from isopentenyl pyrophos... | [
"GO:0016765"
] | [
"transferase activity, transferring alkyl or aryl (other than methyl) groups"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_01139",
"PF01255",
"PTHR10291",
"TIGR00055",
"cd00475"
] | [
"ISPT",
"Prenyltransf",
"",
"uppS",
"Cis_IPPS"
] | [
36807,
42110,
41029,
39029,
39516
] | 5 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"GenProp0971",
"GenProp1479",
"GenProp1670",
"GenProp1709",
"PDOC00817",
"R-DRE-446199",
"R-HSA-446199",
"R-HSA-4755609",
"R-MMU-446199",
"R-SCE-446199",
"R-SPO-446199"
] | [
"EC:2.5.1",
"GP:GenProp0971",
"GP:GenProp1479",
"GP:GenProp1670",
"GP:GenProp1709",
"PROSITEDOC:PDOC00817",
"REACTOME:R-DRE-446199",
"REACTOME:R-HSA-446199",
"REACTOME:R-HSA-4755609",
"REACTOME:R-MMU-446199",
"REACTOME:R-SCE-446199",
"REACTOME:R-SPO-446199"
] | 12 | [
"1f75",
"1jp3",
"1ueh",
"1v7u",
"1x06",
"1x07",
"1x08",
"1x09",
"2d2r",
"2dtn",
"2e98",
"2e99",
"2e9a",
"2e9c",
"2e9d",
"2vfw",
"2vg0",
"2vg1",
"2vg2",
"2vg3",
"2vg4",
"3qas",
"3sgt",
"3sgv",
"3sgx",
"3sh0",
"3th8",
"3ugs",
"3wyi",
"3wyj",
"4h2j",
"4h2m"... | 103 | [
"PUB00002321",
"PUB00003021",
"PUB00010618",
"PUB00079916",
"PUB00079917",
"PUB00079918",
"PUB00079919",
"PUB00079920",
"PUB00079921",
"PUB00079922",
"PUB00079923",
"PUB00079926",
"PUB00079927",
"PUB00079928"
] | [
"9882662",
"9677368",
"12135472",
"16900467",
"23134568",
"12636086",
"22471620",
"11076526",
"11346651",
"10908715",
"10586494",
"1181565",
"11442630",
"10816587"
] | [
"Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene.",
"Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases.",
"St... | [
1999,
1998,
2002,
2006,
2013,
2003,
2012,
2000,
2001,
2000,
1999,
1975,
2001,
2000
] | 14 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1461,
30886,
8805,
5,
969
] | 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",... | [
41,
1,
2,
1,
1,
23,
6,
1,
7,
6,
2,
1,
24
] | 13 | true | Family | Decaprenyl diphosphate synthase-like | Decaprenyl diphosphate synthase-like | UPP_synth-like | 6 |
IPR001442 | 1,442 | Collagen IV, non-collagenous | Collagen_IV_NC | Domain | 8,172 | false | false | Collagens are major components of the extracellular matrices of all metazoan life and play crucial roles in developmental processes and tissue homeostasis. Collagens are composed of three polypeptide chains (alpha chains) that fold together to form the characteristic triple helical collagenous domain. Some types of tri... | [
"GO:0005201",
"GO:0005581"
] | [
"extracellular matrix structural constituent",
"collagen trimer"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01413",
"PS51403",
"SM00111"
] | [
"C4",
"NC1_IV",
"C4"
] | [
8151,
8153,
8122
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1442490",
"R-BTA-1566977",
"R-BTA-1650814",
"R-BTA-186797",
"R-BTA-2022090",
"R-BTA-216083",
"R-BTA-2243919",
"R-BTA-3000157",
"R-BTA-3000171",
"R-CEL-1442490",
"R-CEL-1650814",
"R-CEL-216083",
"R-CEL-8948216",
"R-DME-1442490",
"R-DME-1650814",
"R-DME-216083",
"R-DME-8948216",... | [
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1566977",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-186797",
"REACTOME:R-BTA-2022090",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2243919",
"REACTOME:R-BTA-3000157",
"REACTOME:R-BTA-3000171",
"REACTOME:R-CEL-1442490",
"REACTOME:R-CEL-1650814",
"REACTOME:... | 44 | [
"1li1",
"1m3d",
"1t60",
"1t61",
"5nax",
"5nay",
"5naz",
"5nb0",
"5nb1",
"5nb2",
"6mpx",
"6wku",
"8txn",
"8tys"
] | 14 | [
"PUB00001643",
"PUB00027036",
"PUB00027213",
"PUB00037677",
"PUB00052628"
] | [
"1639194",
"12011424",
"11970952",
"15299013",
"12539240"
] | [
"The modular architecture of vertebrate collagens.",
"The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link.",
"Crystal structure of NC1 domains. Structural basis for type IV collagen assembly in basement ... | [
1992,
2002,
2002,
2004,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Gammaproteobacteria"
] | [
8169,
3
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
13,
4,
34,
16,
25
] | 6 | true | Domain | Collagen IV, non-collagenous | Collagen IV, non-collagenous | Collagen_IV_NC | 4 |
IPR001443 | 1,443 | Staphylocoagulase repeat | Staphylcoagulase_rpt | Repeat | 204 | false | false | Staphylocoagulase is an extracellular protein produced by several strains of Staphylococcus aureus and which specifically forms a complex with prothrombin [ , ]. This complex named staphylothrombin can clot fibrinogen without any proteolytic cleavage of prothrombin. The C terminus of staphylocoagulase contains the tand... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF04022",
"PS00429"
] | [
"Staphylcoagulse",
"STAPHYLOCOAGULASE"
] | [
204,
199
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00353"
] | [
"PROSITEDOC:PDOC00353"
] | 1 | [] | 0 | [
"PUB00002330",
"PUB00004367"
] | [
"3481366",
"2587230"
] | [
"Nucleotide sequence of the staphylocoagulase gene: its unique COOH-terminal 8 tandem repeats.",
"Nucleotide and deduced amino acid sequences of staphylocoagulase gene from Staphylococcus aureus strain 213."
] | [
1987,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
204
] | 1 | [] | [] | 0 | true | Repeat | Staphylocoagulase repeat | Staphylocoagulase repeat | Staphylcoagulase_rpt | 2 |
IPR001444 | 1,444 | Flagellar basal body rod protein, N-terminal | Flag_bb_rod_N | Domain | 72,069 | false | false | Many bacterial species swim actively by means of flagella. The flagella organelle is made of three parts: the basal body, the hook and the filament. The basal body consists of four rings (L,P,S, and M) mounted on a central rod [ ]. In Salmonella typhimurium and related organisms the rod has been shown to consist of fou... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00460"
] | [
"Flg_bb_rod"
] | [
72069
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00508"
] | [
"PROSITEDOC:PDOC00508"
] | 1 | [
"3a69",
"5jxl",
"5wrh",
"6jzr",
"6jzt",
"6k3i",
"6k9q",
"6kfk",
"7bin",
"7cbm",
"7cg0",
"7cgb",
"7cgo",
"7e80",
"7e82",
"7nvg",
"8wk3",
"8wk4",
"8wki",
"8wkk",
"8wkq",
"8wl2",
"8wlh",
"8wln",
"8wlp",
"8wlq",
"8wlt",
"8wo5",
"8woe",
"8z5s",
"8z5u",
"8z5w"... | 38 | [
"PUB00003254"
] | [
"2129540"
] | [
"FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
71219,
3,
93,
754
] | 4 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Domain | Flagellar basal body rod protein, N-terminal | Flagellar basal body rod protein, N-terminal | Flag_bb_rod_N | 9 |
IPR001445 | 1,445 | Acetylcholinesterase, insect | Acylcholinesterase_insect | Family | 421 | 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... | [
"GO:0003990",
"GO:0001507"
] | [
"acetylcholinesterase activity",
"acetylcholine catabolic process in synaptic cleft"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00880"
] | [
"ACHEINSECT"
] | [
421
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1.7",
"R-DME-112311",
"R-DME-1483191",
"R-DME-9749641"
] | [
"EC:3.1.1.7",
"REACTOME:R-DME-112311",
"REACTOME:R-DME-1483191",
"REACTOME:R-DME-9749641"
] | 4 | [
"6xys",
"6xyu",
"6xyy"
] | 3 | [
"PUB00002039",
"PUB00010129",
"PUB00029676",
"PUB00036069",
"PUB00036070",
"PUB00036071",
"PUB00036072",
"PUB00036073"
] | [
"9459425",
"1678899",
"12869558",
"15907917",
"8161450",
"8890157",
"8608006",
"11169626"
] | [
"Analysis of a mosquito acetylcholinesterase gene promoter.",
"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: 'classica... | [
1998,
1991,
2003,
2005,
1994,
1996,
1996,
2001
] | 8 | [
"IPR000997"
] | [] | 1 | 0 | 1 | [
"Neoptera"
] | [
421
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Family | Acetylcholinesterase, insect | Acetylcholinesterase, insect | Acylcholinesterase_insect | 3 |
IPR001446 | 1,446 | 5-lipoxygenase-activating protein | 5_LipOase_AP | Family | 2,320 | false | false | 5-lipoxygenase-activating protein (FLAP) is an integral membrane protein found in cells that produce leukotrienes, the biologically active metabolites of arachidonic acid that have been implicated in a variety of inflammatory responses, including asthma, arthritis and psoriasis [ ]. FLAP appears to activatate 5-lipoxyg... | [
"GO:0008047",
"GO:0006691",
"GO:0016020"
] | [
"enzyme activator activity",
"leukotriene metabolic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00488"
] | [
"5LPOXGNASEAP"
] | [
2320
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00999",
"R-BTA-156590",
"R-BTA-2142688",
"R-BTA-2142691",
"R-BTA-2142700",
"R-BTA-5423646",
"R-BTA-9026762",
"R-BTA-9026766",
"R-HSA-156590",
"R-HSA-2142688",
"R-HSA-2142691",
"R-HSA-2142700",
"R-HSA-5423646",
"R-HSA-9026762",
"R-HSA-9026766",
"R-MMU-156590",
"R-MMU-2142688",
... | [
"PROSITEDOC:PDOC00999",
"REACTOME:R-BTA-156590",
"REACTOME:R-BTA-2142688",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142700",
"REACTOME:R-BTA-5423646",
"REACTOME:R-BTA-9026762",
"REACTOME:R-BTA-9026766",
"REACTOME:R-HSA-156590",
"REACTOME:R-HSA-2142688",
"REACTOME:R-HSA-2142691",
"REACTOME:R-... | 27 | [
"2pno",
"2q7m",
"2q7r",
"2uuh",
"2uui",
"3b29",
"3hkk",
"3leo",
"3pcv",
"4j7t",
"4j7y",
"4jc7",
"4jcz",
"4jrz",
"4nta",
"4ntb",
"4ntf",
"5hv9",
"6r7d",
"6ssr",
"6sss",
"6ssu",
"6ssw",
"6vgc",
"6vgi",
"9g0u",
"9g0v",
"9g14",
"9g1t"
] | 29 | [
"PUB00002588",
"PUB00003108",
"PUB00004052"
] | [
"2174053",
"8245774",
"2300173"
] | [
"Correlation between expression of 5-lipoxygenase-activating protein, 5-lipoxygenase, and cellular leukotriene synthesis.",
"5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes.",
"Requirement of a 5-lipoxygenase-activating protein for leukotr... | [
1990,
1993,
1990
] | 3 | [
"IPR001129"
] | [] | 1 | 0 | 1 | [
"Eumetazoa",
"Pseudomonadati",
"marine metagenome"
] | [
2312,
7,
1
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
7,
13
] | 4 | true | Family | 5-lipoxygenase-activating protein | 5-lipoxygenase-activating protein | 5_LipOase_AP | 4 |
IPR001447 | 1,447 | Arylamine N-acetyltransferase | Arylamine_N-AcTrfase | Family | 14,892 | false | false | Arylamine N-acetyltransferase (NAT) facilitates the transfer of an acetyl group from acetyl coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (Mycobacterium tuberculosis, Mycoba... | [
"GO:0016407"
] | [
"acetyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00797",
"PR01543",
"PTHR11786"
] | [
"Acetyltransf_2",
"ANATRNSFRASE",
""
] | [
14843,
10568,
14556
] | 3 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1",
"2.3.1.5",
"R-BTA-156582",
"R-BTA-9753281",
"R-GGA-156582",
"R-GGA-9753281",
"R-HSA-156582",
"R-HSA-9753281",
"R-MMU-156582",
"R-MMU-9753281",
"R-RNO-156582",
"R-RNO-9753281"
] | [
"EC:2.3.1",
"EC:2.3.1.5",
"REACTOME:R-BTA-156582",
"REACTOME:R-BTA-9753281",
"REACTOME:R-GGA-156582",
"REACTOME:R-GGA-9753281",
"REACTOME:R-HSA-156582",
"REACTOME:R-HSA-9753281",
"REACTOME:R-MMU-156582",
"REACTOME:R-MMU-9753281",
"REACTOME:R-RNO-156582",
"REACTOME:R-RNO-9753281"
] | 12 | [
"1e2t",
"1gx3",
"1w4t",
"1w5r",
"1w6f",
"2bsz",
"2ija",
"2pfr",
"2pqt",
"2vfb",
"2vfc",
"3d9w",
"3lnb",
"3ltw",
"4b55",
"4bgf",
"4c5p",
"4dmo",
"4guz",
"4nv7",
"4nv8",
"7qi3",
"8btm",
"8k51",
"8k56",
"8oom",
"8osv",
"8osz",
"8ot2"
] | 29 | [
"PUB00048759",
"PUB00100366",
"PUB00100367",
"PUB00100368",
"PUB00100369",
"PUB00100370",
"PUB00100371",
"PUB00100372",
"PUB00100373",
"PUB00100374"
] | [
"17656365",
"19302487",
"25727347",
"33094670",
"28574024",
"18680471",
"1381364",
"26808652",
"18852012",
"18642144"
] | [
"Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.",
"FDB2 encodes a member of the arylamine N-acetyltransferase family and is necessary for biotransformation of benzoxazolinones by Fusarium verticillioides.",
"Degradation of the benzoxazolinone class of phytoalexins is ... | [
2007,
2009,
2015,
2021,
2017,
2008,
1992,
2016,
2008,
2008
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
40,
9391,
5378,
49,
34
] | 5 | [
"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)",
"Rattus norvegicus"
] | [
12,
1,
47,
9,
1,
11
] | 6 | true | Family | Arylamine N-acetyltransferase | Arylamine N-acetyltransferase | Arylamine_N-AcTrfase | 7 |
IPR001448 | 1,448 | Small acid-soluble spore protein, alpha/beta-type | SASP_alpha/beta-type | Family | 10,596 | false | false | Small, acid-soluble spore proteins (SASP or ASSP) are proteins bound to the spore DNA of bacteria of the genera Bacillus, Thermoactynomycetes, and Clostridium [ , ]. They are double-stranded DNA-binding proteins that cause DNA to change to an A-like conformation. They protect the DNA backbone from chemical and enzymati... | [
"GO:0003690",
"GO:0006265"
] | [
"double-stranded DNA binding",
"DNA topological change"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00269"
] | [
"SASP"
] | [
10596
] | 1 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0610",
"PDOC00276"
] | [
"GP:GenProp0610",
"PROSITEDOC:PDOC00276"
] | 2 | [
"2z3x"
] | 1 | [
"PUB00000113",
"PUB00002172"
] | [
"3059997",
"1569005"
] | [
"Small, acid-soluble spore proteins of Bacillus species: structure, synthesis, genetics, function, and degradation.",
"I will survive: protecting and repairing spore DNA."
] | [
1988,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"metagenomes"
] | [
10511,
10,
75
] | 3 | [] | [] | 0 | true | Family | Small acid-soluble spore protein, alpha/beta-type | Small acid-soluble spore protein, alpha/beta-type | SASP_alpha/beta-type | 7 |
IPR001451 | 1,451 | Hexapeptide repeat | Hexapep | Repeat | 189,664 | false | false | A variety of bacterial transferases contain a repeat structure composed of tandem repeats of a [LIV]-G-X(4) hexapeptide, which, in the tertiary structure of LpxA (Acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase) [ ], has been shown to form a left-handed parallel β-helix. A number of different tran... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF00132",
"PF14602"
] | [
"Hexapep",
"Hexapep_2"
] | [
160980,
46282
] | 2 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1",
"GenProp1468",
"PDOC00094",
"R-BTA-2132295",
"R-BTA-3371497",
"R-BTA-6807878",
"R-BTA-6811436",
"R-MTU-936721"
] | [
"EC:2.3.1",
"GP:GenProp1468",
"PROSITEDOC:PDOC00094",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811436",
"REACTOME:R-MTU-936721"
] | 8 | [
"1g95",
"1g97",
"1hm0",
"1hm8",
"1hm9",
"1hv9",
"1j2z",
"1kgq",
"1kgt",
"1khr",
"1kk4",
"1kk5",
"1kk6",
"1kqa",
"1krr",
"1kru",
"1krv",
"1lxa",
"1mr7",
"1mr9",
"1mrl",
"1ocx",
"1s80",
"1ssm",
"1ssq",
"1sst",
"1t3d",
"1tdt",
"1xat",
"1xhd",
"2aq9",
"2ggo"... | 291 | [
"PUB00005215",
"PUB00013969",
"PUB00013970",
"PUB00013971",
"PUB00094377"
] | [
"7481807",
"11937062",
"10924115",
"11910040",
"17519228"
] | [
"A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.",
"Structure of the lac operon galactoside acetyltransferase.",
"A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosar... | [
1995,
2002,
2000,
2002,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
3213,
173181,
10360,
1,
47,
2862
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"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)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"... | [
37,
14,
1,
4,
20,
1,
2,
32
] | 8 | true | Repeat | Hexapeptide repeat | Hexapeptide repeat | Hexapep | 8 |
IPR001452 | 1,452 | SH3 domain | SH3_domain | Domain | 420,633 | false | false | SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues [ , ]. They are found in a great variety of intracellular or membrane-associated proteins [ , , ] for example, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin bind... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00018",
"PF07653",
"PF14604",
"PR00452",
"PS50002",
"SM00326"
] | [
"SH3_1",
"SH3_2",
"SH3_9",
"SH3DOMAIN",
"SH3",
"SH3"
] | [
215025,
94581,
109835,
152117,
414877,
374156
] | 6 | [
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"GenProp1511",
"GenProp1524",
"GenProp1548",
"PDOC50002",
"R-BTA-109704",
"R-BTA-112308",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1227986",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-1433559",
"R-BTA-1660499",
"R-BTA-180292",
"R-BTA-182971",
"R-BTA-18... | [
"GP:GenProp1511",
"GP:GenProp1524",
"GP:GenProp1548",
"PROSITEDOC:PDOC50002",
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112308",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1227986",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1266695",
"REACTOME:... | 1,450 | [
"1a0n",
"1abo",
"1abq",
"1ad5",
"1aey",
"1aoj",
"1ark",
"1avz",
"1awj",
"1awo",
"1aww",
"1awx",
"1aze",
"1azg",
"1b07",
"1bb9",
"1bbz",
"1bk2",
"1bu1",
"1cka",
"1ckb",
"1csk",
"1e6g",
"1e6h",
"1e7o",
"1efn",
"1fmk",
"1fyn",
"1g2b",
"1g83",
"1gbq",
"1gbr"... | 846 | [
"PUB00000887",
"PUB00000895",
"PUB00001025",
"PUB00001031",
"PUB00001644",
"PUB00004135",
"PUB00004203",
"PUB00005506",
"PUB00007145"
] | [
"7681365",
"7684655",
"15335710",
"7953536",
"1639195",
"1279434",
"7531822",
"14731533",
"11256992"
] | [
"Solution structure of the SH3 domain of phospholipase C-gamma.",
"Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.",
"SH2 and SH3 domains.",
"SH3 domains. Molecular 'Velcro'.",
"SH3--an abundant protein domain in search of a function.",... | [
1993,
1993,
1993,
1994,
1992,
1992,
1995,
1993,
2001
] | 9 | [] | [
"IPR028455",
"IPR028503",
"IPR028570",
"IPR029294",
"IPR030642",
"IPR030777",
"IPR034889",
"IPR035449",
"IPR035450",
"IPR035452",
"IPR035453",
"IPR035454",
"IPR035456",
"IPR035457",
"IPR035458",
"IPR035460",
"IPR035462",
"IPR035465",
"IPR035468",
"IPR035470",
"IPR035471",
"... | 0 | 188 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"unclassified sequences"
] | [
1443,
419123,
2,
33,
32
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
19,
148,
2602,
351,
1189,
816,
24,
18,
1129,
24,
21,
51
] | 12 | true | Domain | SH3 domain | SH3 domain | SH3_domain | 9 |
IPR001453 | 1,453 | MoaB/Mog domain | MoaB/Mog_dom | Domain | 88,192 | false | false | MoaB/Mog domain, also known as Cnx1G domain, is found in the bacterial molybdenum cofactor (Moco) biosynthesis protein MoaB/Mog and N-terminal of the eukaryotic MoCF biosynthesis proteins, such as the Drosophila protein cinnamon, the Arabidopsis protein cnx1 and the mammal protein gephyrin [ ]. These proteins are invol... | [] | [] | [] | 0 | [
"PFAM",
"SMART",
"NCBIFAM",
"CDD",
"CDD"
] | [
"PF00994",
"SM00852",
"TIGR00177",
"cd00885",
"cd00886"
] | [
"MoCF_biosynth",
"MoCF_biosynth",
"molyb_syn",
"cinA",
"MogA_MoaB"
] | [
87664,
86941,
59839,
19675,
28189
] | 5 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1711",
"GenProp1764",
"R-CEL-196843",
"R-DDI-947581",
"R-DME-947581",
"R-DRE-196843",
"R-HSA-196843",
"R-HSA-947581",
"R-MMU-196843",
"R-MMU-947581",
"R-RNO-947581"
] | [
"GP:GenProp1711",
"GP:GenProp1764",
"REACTOME:R-CEL-196843",
"REACTOME:R-DDI-947581",
"REACTOME:R-DME-947581",
"REACTOME:R-DRE-196843",
"REACTOME:R-HSA-196843",
"REACTOME:R-HSA-947581",
"REACTOME:R-MMU-196843",
"REACTOME:R-MMU-947581",
"REACTOME:R-RNO-947581"
] | 11 | [
"1di6",
"1di7",
"1eav",
"1fc5",
"1g8l",
"1g8r",
"1ihc",
"1jlj",
"1mkz",
"1o8n",
"1o8o",
"1o8q",
"1r2k",
"1t3e",
"1uux",
"1uuy",
"1uz5",
"1wu2",
"1xi8",
"1y5e",
"2f7w",
"2f7y",
"2fts",
"2fu3",
"2g2c",
"2g4r",
"2is8",
"2nqk",
"2nqm",
"2nqn",
"2nqq",
"2nqr"... | 100 | [
"PUB00016078",
"PUB00029346",
"PUB00069588",
"PUB00073238",
"PUB00073239",
"PUB00073253"
] | [
"10636880",
"12590921",
"15073332",
"23776507",
"19675644",
"25313401"
] | [
"Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.",
"The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G.",
"Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in h... | [
2000,
2003,
2004,
2013,
2009,
2014
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3747,
71103,
11837,
1505
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
9,
3,
65,
5,
4,
12,
5,
4,
4,
12,
1,
20
] | 12 | true | Domain | MoaB/Mog domain | MoaB/Mog domain | MoaB/Mog_dom | 7 |
IPR001455 | 1,455 | TusA-like domain | TusA-like | Domain | 26,025 | false | false | The structure of TusA (also known YhhP and SirA) consists of an α/β sandwich with a β-α-β-α-β(2) fold, comprising a mixed four-stranded β-sheet stacked against two α-helices, both of which are nearly parallel to the strands of the β-sheet [ ]. Several uncharacterised bacterial proteins (73 to 81 amino-acid residues in ... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF01206",
"PS01148"
] | [
"TusA",
"UPF0033"
] | [
26000,
18521
] | 2 | [
"GP",
"PROSITEDOC"
] | [
"GenProp1555",
"PDOC00884"
] | [
"GP:GenProp1555",
"PROSITEDOC:PDOC00884"
] | 2 | [
"1dcj",
"1jdq",
"1je3",
"1pav",
"3hz7",
"3lvj",
"3lvk",
"8j4c",
"8k1r"
] | 9 | [
"PUB00013981"
] | [
"11080457"
] | [
"High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Dickeya phage phiDP23.1",
"Eukaryota",
"unclassified sequences"
] | [
1586,
23892,
1,
25,
521
] | 5 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | TusA-like domain | TusA-like domain | TusA-like | 9 |
IPR001456 | 1,456 | Helper component proteinase | HC-pro | Family | 5,205 | false | false | This entry represents the potyvirus helper component protease found in genome polyproteins of potyviruses. It is is a cysteine peptidase belonging to the MEROPS peptidase family C6 (clan CA). The helper component-proteinase is required for aphid transmission. A cysteine peptidase is a proteolytic enzyme that hydrolyses... | [
"GO:0004197",
"GO:0006508"
] | [
"cysteine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00851"
] | [
"Peptidase_C6"
] | [
5205
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"3.4.21.-",
"3.4.22.45",
"PWY-7884"
] | [
"EC:3.4.21.-",
"EC:3.4.22.45",
"METACYC:PWY-7884"
] | 3 | [
"3rnv"
] | 1 | [
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00076953"
] | [
"11517925",
"9891971",
"14725770",
"7044372"
] | [
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.",
... | [
2001,
1998,
2004,
1982
] | 4 | [] | [] | 0 | 0 | null | [
"Orthornavirae"
] | [
5205
] | 1 | [] | [] | 0 | true | Family | Helper component proteinase | Helper component proteinase | HC-pro | 1 |
IPR001458 | 1,458 | GPCR, family 3, metabotropic glutamate receptor 2 | GPCR_3_mGluR2 | Family | 1,008 | false | false | The mRNA for GRM2 is widespread in the brain, with a unique distribution; it is found in high levels in neurons in olfactory bulb, cerebral cortex, cerebellum Golgi cells, and dentate gyrus granule cells. GRM2 inhibits adenylyl cyclase through a pertussis-toxin-sensitive G-protein, probably of the Gi/Go class; the rece... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01052"
] | [
"MTABOTROPC2R"
] | [
1008
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"290",
"R-HSA-418594",
"R-HSA-420499",
"R-MMU-418594",
"R-MMU-420499",
"R-RNO-418594",
"R-RNO-420499"
] | [
"IUPHAR:290",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-420499",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-420499"
] | 7 | [
"4xaq",
"4xas",
"5cni",
"5cnj",
"5kzn",
"5kzq",
"8jcu",
"8jcv",
"8jcw",
"8jcx",
"8jcy",
"8jcz",
"8jd0",
"8jd1",
"8jd2",
"8jd3",
"8jd4",
"8jd5",
"8wg9",
"8wgb",
"8wgc",
"8wgd"
] | 22 | [
"PUB00002720",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816",
"PUB00100445",
"PUB00100446",
"PUB00100447"
] | [
"1320017",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293",
"22300836",
"23129762",
"18297054"
] | [
"Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.",
"Sequence and expression of a metabotropic glutamate receptor.",
"Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.",
"A famil... | [
1992,
1991,
1993,
1992,
1994,
1991,
1997,
2007,
2000,
2003,
1994,
2005,
2009,
2006,
2013,
2012,
2012,
2008
] | 18 | [
"IPR000162"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1008
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
8,
3,
4
] | 4 | true | Family | GPCR, family 3, metabotropic glutamate receptor 2 | GPCR, family 3, metabotropic glutamate receptor 2 | GPCR_3_mGluR2 | 9 |
IPR001461 | 1,461 | Aspartic peptidase A1 | Aspartic_peptidase_A1 | Family | 89,045 | false | false | Peptidase family A1, also known as the pepsin family, contains peptidases with bilobed structures [ , ]. The two domains most probably evolved from the duplication of an ancestral gene encoding a primordial domain [ ]. The active site is formed from an aspartic acid residue from each domain. Each aspartic acid occurs w... | [
"GO:0004190",
"GO:0006508"
] | [
"aspartic-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER",
"PANTHER",
"PANTHER"
] | [
"PR00792",
"PTHR13683",
"PTHR47965",
"PTHR47966"
] | [
"PEPSIN",
"",
"",
""
] | [
64545,
20302,
10343,
52146
] | 4 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.23",
"R-CEL-2022377",
"R-CEL-5683826",
"R-CFA-1442490",
"R-CFA-2022377",
"R-CFA-2132295",
"R-CFA-5683826",
"R-CFA-6798695",
"R-CFA-77387",
"R-DDI-2132295",
"R-DDI-5683826",
"R-DDI-6798695",
"R-GGA-2022377",
"R-GGA-2132295",
"R-GGA-6798695",
"R-GGA-77387",
"R-HSA-1442490",
"R-H... | [
"EC:3.4.23",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CEL-5683826",
"REACTOME:R-CFA-1442490",
"REACTOME:R-CFA-2022377",
"REACTOME:R-CFA-2132295",
"REACTOME:R-CFA-5683826",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-77387",
"REACTOME:R-DDI-2132295",
"REACTOME:R-DDI-5683826",
"REACTOME:R-DDI-6798695... | 38 | [
"1am5",
"1apt",
"1apu",
"1apv",
"1apw",
"1avf",
"1b5f",
"1bbs",
"1bil",
"1bim",
"1bxo",
"1bxq",
"1cms",
"1czi",
"1dp5",
"1dpj",
"1e5o",
"1e80",
"1e81",
"1e82",
"1eag",
"1eed",
"1ent",
"1epl",
"1epm",
"1epn",
"1epo",
"1epp",
"1epq",
"1epr",
"1er8",
"1f34"... | 1,717 | [
"PUB00003678",
"PUB00023201",
"PUB00031354",
"PUB00042527",
"PUB00076777",
"PUB00076778",
"PUB00076780",
"PUB00076781",
"PUB00094521"
] | [
"1549128",
"2115088",
"15166216",
"2115087",
"19758436",
"21749650",
"11782538",
"24179",
"27872247"
] | [
"Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.",
"X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution.",
"Structural basis for inhibition of Aspergillus niger xylanase b... | [
1992,
1990,
2004,
1990,
2009,
2011,
2002,
1978,
2017
] | 9 | [] | [
"IPR009119",
"IPR033144"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"marine metagenome"
] | [
180,
88863,
1,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
301,
19,
14,
19,
59,
48,
18,
268,
31,
7,
2,
389
] | 12 | true | Family | Aspartic peptidase A1 | Aspartic peptidase A1 | Aspartic_peptidase_A1 | 9 |
IPR001462 | 1,462 | Hepadnaviral P protein, C-terminal | DNApol_viral_C | Domain | 20,007 | false | false | This domain is at the C terminus of hepatitis B-type viruses P proteins and represents a functional domain that controls the RNase H activities of the protein. The domain is always associated with and . | [
"GO:0004523"
] | [
"RNA-DNA hybrid ribonuclease activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00336"
] | [
"DNA_pol_viral_C"
] | [
20007
] | 1 | [
"EC",
"EC",
"EC"
] | [
"2.7.7.49",
"2.7.7.7",
"3.1.26.4"
] | [
"EC:2.7.7.49",
"EC:2.7.7.7",
"EC:3.1.26.4"
] | 3 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Qipengyuania pelagi",
"Revtraviricetes"
] | [
16,
1,
19990
] | 3 | [] | [] | 0 | true | Domain | Hepadnaviral P protein, C-terminal | Hepadnaviral P protein, C-terminal | DNApol_viral_C | 4 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.