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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000147 | 147 | Angiotensin II receptor type 2 | ATII_AT2_rcpt | Family | 529 | false | false | Angiotensin II is a blood-borne hormone produced in the circulation, it is also formed in many tissues such as the brain, kidney, heart, and blood vessels, where angiotensin II functions as a paracrine and autocrine hormone. The known actions of angiotensin II are mediated through two angiotensin receptor subtypes, Ang... | [
"GO:0004945",
"GO:0006954",
"GO:0007186",
"GO:0042981",
"GO:0097746",
"GO:0016020"
] | [
"angiotensin type II receptor activity",
"inflammatory response",
"G protein-coupled receptor signaling pathway",
"regulation of apoptotic process",
"blood vessel diameter maintenance",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PRINTS"
] | [
"PR00636"
] | [
"ANGIOTENSN2R"
] | [
529
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"35",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594"
] | [
"IUPHAR:35",
"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 | [
"5unf",
"5ung",
"5unh",
"5xjm",
"6jod",
"7c6a",
"7jni"
] | 7 | [
"PUB00063358",
"PUB00063372",
"PUB00063373",
"PUB00063374",
"PUB00063375",
"PUB00063376",
"PUB00063378",
"PUB00063379",
"PUB00063380",
"PUB00063381",
"PUB00063382",
"PUB00063384",
"PUB00063385",
"PUB00063386",
"PUB00063387",
"PUB00063388",
"PUB00063389",
"PUB00063395",
"PUB000633... | [
"17346243",
"8725391",
"9851935",
"10024335",
"10395402",
"8809509",
"10652498",
"10339618",
"8552595",
"9228085",
"11116149",
"11714657",
"11910305",
"10891597",
"7829501",
"11723025",
"7840157",
"10864905",
"14500552",
"11788460",
"12221292"
] | [
"Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology.",
"Angiotensin receptors and their therapeutic implications.",
"Pathophysiological role of angiotensin II type 2 receptor in cardiovascular and renal diseases.",
"Distinct and combined vascular ef... | [
2007,
1996,
1998,
1999,
1999,
1996,
2000,
1999,
1996,
1997,
2001,
2001,
2002,
2000,
1995,
2001,
1995,
2000,
2003,
2002,
2002
] | 21 | [
"IPR000248"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
529
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
2
] | 3 | true | Family | Angiotensin II receptor type 2 | Angiotensin II receptor type 2 | ATII_AT2_rcpt | 5 |
IPR000148 | 148 | Papillomavirus E7 | Papilloma_E7 | Family | 2,307 | false | false | This family includes the E7 oncoprotein from various papillomaviruses [ ]. Along with E5 and E6 their activities seem to be especially important for viral oncogenesis. E5 is located at the cell surface and reduces cell gap-gap junction communication. In cervical cancer E5 is expressed in earlier stages of neoplastic tr... | [
"GO:0003677",
"GO:0003700",
"GO:0006355"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PIRSF"
] | [
"MF_04004",
"PF00527",
"PIRSF003407"
] | [
"PPV_E7",
"E7",
"Papvi_E7"
] | [
1874,
2306,
2152
] | 3 | [] | [] | [] | 0 | [
"2b9d",
"2ewl",
"2f8b",
"6iwd"
] | 4 | [
"PUB00009552",
"PUB00009553"
] | [
"11422538",
"11752153"
] | [
"Biology of human papillomaviruses.",
"Human papillomavirus type 16 E7 maintains elevated levels of the cdc25A tyrosine phosphatase during deregulation of cell cycle arrest."
] | [
2001,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Homo sapiens",
"Papillomaviridae"
] | [
2,
2305
] | 2 | [
"Homo sapiens"
] | [
2
] | 1 | true | Family | Papillomavirus E7 | Papillomavirus E7 | Papilloma_E7 | 9 |
IPR000149 | 149 | Haemagglutinin, influenzavirus A | Hemagglutn_influenz_A | Family | 133,543 | 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 | [
"PRINTS"
] | [
"PR00330"
] | [
"HEMAGGLUTN1"
] | [
133543
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"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"
] | [
"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"
] | 11 | [
"1eo8",
"1ha0",
"1hgd",
"1hge",
"1hgf",
"1hgg",
"1hgh",
"1hgi",
"1hgj",
"1jsd",
"1jsh",
"1jsi",
"1jsm",
"1jsn",
"1jso",
"1ken",
"1mql",
"1mqm",
"1mqn",
"1qfu",
"1rd8",
"1ru7",
"1ruy",
"1ruz",
"1rv0",
"1rvt",
"1rvx",
"1rvz",
"1ti8",
"2fk0",
"2hmg",
"2ibx"... | 771 | [
"PUB00033162",
"PUB00033164",
"PUB00033165",
"PUB00092983",
"PUB00092984"
] | [
"16543414",
"15475582",
"16178512",
"29263889",
"24582528"
] | [
"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.",
"Protective efficacy of influenza group 2 hemagglutinin stem-fragment ... | [
2006,
2005,
2005,
2017,
2014
] | 5 | [
"IPR001364"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Negarnaviricota"
] | [
18,
133525
] | 2 | [] | [] | 0 | true | Family | Haemagglutinin, influenzavirus A | Haemagglutinin, influenzavirus A | Hemagglutn_influenz_A | 1 |
IPR000150 | 150 | Cof family | Cof | Family | 52,433 | false | false | The Haloacid Dehydrogenase (HAD) superfamily includes phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, which are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification [ ]. Proteins in this entry are mostly unchar... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00099"
] | [
"Cof-subfamily"
] | [
52433
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"3.6.1.-",
"GenProp1306",
"GenProp1344",
"GenProp1407",
"GenProp1734",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289",
"PDOC00944"
] | [
"EC:3.6.1.-",
"GP:GenProp1306",
"GP:GenProp1344",
"GP:GenProp1407",
"GP:GenProp1734",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289",
... | 16 | [
"1nf2",
"1nrw",
"1rkq",
"1rlm",
"1rlo",
"1rlt",
"1ymq",
"2b30",
"2hf2",
"2pq0",
"2qyh",
"2rar",
"2rav",
"2rb5",
"2rbk",
"3dao",
"3dnp",
"3fzq",
"3l7y",
"3mpo",
"3niw",
"3pgv",
"3r4c",
"4dw8",
"4dwo",
"4qjb",
"4zev",
"4zew",
"4zex"
] | 29 | [
"PUB00003337",
"PUB00028115",
"PUB00053972"
] | [
"7966317",
"15657928",
"15292217"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"YbiV from Escherichia coli K12 is a HAD phosphatase.",
"A genetic screen for the identification of thiamin metabolic genes."
] | [
1994,
2005,
2004
] | 3 | [
"IPR006379"
] | [
"IPR017223",
"IPR023938"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5,
51128,
1134,
166
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
6,
5,
1,
2
] | 5 | true | Family | Cof family | Cof family | Cof | 7 |
IPR000152 | 152 | EGF-type aspartate/asparagine hydroxylation site | EGF-type_Asp/Asn_hydroxyl_site | PTM | 176,073 | false | false | Post-translational hydroxylation of aspartic acid or asparagine [ ] to form erythro-beta-hydroxyaspartic acid or erythro-beta-hydroxyasparagine has been identified in a number of proteins with domains homologous to epidermal growth factor (EGF). Examples of such proteins are the blood coagulation protein factors VII, I... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00010"
] | [
"ASX_HYDROXYL"
] | [
176073
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00010",
"R-BTA-114608",
"R-BTA-140834",
"R-BTA-140837",
"R-BTA-140875",
"R-BTA-1474228",
"R-BTA-1566948",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-1971475",
"R-BTA-2022870",
"R-BTA-2022923",
"R-BTA-2024101",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA... | [
"PROSITEDOC:PDOC00010",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-140875",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-1971475",
"REACTOME:R-BTA-2... | 361 | [
"1apo",
"1aut",
"1bf9",
"1c5m",
"1ccf",
"1dan",
"1dva",
"1edm",
"1emn",
"1emo",
"1ezq",
"1f0r",
"1f0s",
"1f7e",
"1f7m",
"1fak",
"1fax",
"1ff7",
"1ffm",
"1g2l",
"1g2m",
"1hj7",
"1hz8",
"1i0u",
"1ioe",
"1iqe",
"1iqf",
"1iqg",
"1iqh",
"1iqi",
"1iqj",
"1iqk"... | 267 | [
"PUB00002475"
] | [
"2826439"
] | [
"beta-Hydroxyaspartic acid or beta-hydroxyasparagine in bovine low density lipoprotein receptor and in bovine thrombomodulin."
] | [
1988
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
139,
175930,
4
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
24,
81,
468,
89,
496,
295,
126,
446,
84
] | 9 | true | PTM | EGF-type aspartate/asparagine hydroxylation site | EGF-type aspartate/asparagine hydroxylation site | EGF-type_Asp/Asn_hydroxyl_site | 2 |
IPR000153 | 153 | Reovirus, outer capsid sigma 3 | Reo_capsid_sigma3 | Family | 393 | false | false | Reoviruses are double-stranded RNA viruses that lack a membrane envelope. Their capsid is organised in two concentric icosahedral layers: an inner core and an outer capsid layer. The outer capsid is made up of the major proteins mu1 and sigma3, and the minor protein sigma1. The inner core structure is composed of the m... | [
"GO:0005198",
"GO:0019058"
] | [
"structural molecule activity",
"viral life cycle"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00979"
] | [
"Reovirus_cap"
] | [
393
] | 1 | [] | [] | [] | 0 | [
"1fn9",
"1jmu",
"2cse",
"6xf8",
"6zty",
"6ztz",
"7lup",
"9cyt",
"9cyy"
] | 9 | [
"PUB00007495"
] | [
"9971813"
] | [
"The reovirus mutant tsA279 L2 gene is associated with generation of a spikeless core particle: implications for capsid assembly."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Reovirales"
] | [
393
] | 1 | [] | [] | 0 | true | Family | Reovirus, outer capsid sigma 3 | Reovirus, outer capsid sigma 3 | Reo_capsid_sigma3 | 8 |
IPR000154 | 154 | Prostanoid EP3 receptor type 3 | EP3_rcpt_3 | Family | 31 | false | false | EP3 receptors mediate contraction in a wide range of smooth muscles, including gastrointestinal and uterine. They also inhibit neurotransmitter release in central and autonomic nerves through a presynaptic action, and inhibit secretion in glandular tissues (e.g., acid secretion from gastric mucosa, and sodium and water... | [
"GO:0004957",
"GO:0007186",
"GO:0016020"
] | [
"prostaglandin E receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00585"
] | [
"PRSTNOIDE33R"
] | [
31
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-MMU-391908",
"R-MMU-418594",
"R-RNO-391908",
"R-RNO-418594"
] | [
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-391908",
"REACTOME:R-RNO-418594"
] | 4 | [] | 0 | [
"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 | [
"IPR000265"
] | [] | 1 | 0 | 1 | [
"Muroidea"
] | [
31
] | 1 | [
"Mus musculus",
"Rattus norvegicus"
] | [
3,
12
] | 2 | true | Family | Prostanoid EP3 receptor type 3 | Prostanoid EP3 receptor type 3 | EP3_rcpt_3 | 3 |
IPR000155 | 155 | Melanocortin 4 receptor | Mcort_rcpt_4 | Family | 840 | 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:0004977",
"GO:0007186",
"GO:0016020"
] | [
"melanocortin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01062"
] | [
"MELNOCORTN4R"
] | [
840
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"285",
"R-BTA-375276",
"R-BTA-418555",
"R-DRE-375276",
"R-HSA-375276",
"R-HSA-418555",
"R-HSA-9856649",
"R-MMU-375276",
"R-MMU-418555",
"R-RNO-375276",
"R-SSC-375276",
"R-SSC-418555"
] | [
"IUPHAR:285",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418555",
"REACTOME:R-DRE-375276",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-375276",
"REACTOME:R-SSC-375276",
"REACTOME:R-SSC-418555"
] | 12 | [
"6w25",
"7aue",
"7f53",
"7f54",
"7f55",
"7f58",
"7piu",
"7piv",
"8qj2",
"8wky",
"8wkz",
"9k3k"
] | 12 | [
"PUB00000131",
"PUB00000530",
"PUB00002477",
"PUB00002830",
"PUB00003714",
"PUB00003887",
"PUB00004827",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"8172596",
"2830256",
"8463333",
"7854347",
"8794897",
"8415620",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"Molecular cloning, functional expression and pharmacological characterization of a mouse melanocortin receptor gene.",
"G protein involvement in receptor-effector coupling.",
"Molecular cloning of a novel melanocortin receptor.",
"Localization of the melanocortin-4 rec... | [
1990,
1994,
1988,
1993,
1994,
1996,
1993,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 15 | [
"IPR001908"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
840
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
10,
2,
2
] | 4 | true | Family | Melanocortin 4 receptor | Melanocortin 4 receptor | Mcort_rcpt_4 | 6 |
IPR000156 | 156 | Ran binding domain | Ran_bind_dom | Domain | 18,974 | false | false | Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran Binding Protein 1 (RanBP1) has guanine nucleotide dissociation inhibitory activity, specific for the GTP form of Ran and also functions to stimulate Ran GTPase activat... | [
"GO:0046907"
] | [
"intracellular transport"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00638",
"PS50196",
"SM00160"
] | [
"Ran_BP1",
"RANBD1",
"RanBD"
] | [
18306,
18186,
18082
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50196",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-DME-170822",
"R-DME-3108214",
"R-DME-3301854",
"R-DME-4085377",
"R-DME-4551638",
"R-DME-4615885",
"R-DME-5578749",
"R-HSA-1169408",
"R-HSA-141444",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA... | [
"PROSITEDOC:PDOC50196",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3301854",
"REACTOME:R-DME-4085377",
"REACTOME:R-DME-4551638",
"REACTOME:R-DME-4615885",
"REACTOME:R-DME... | 98 | [
"1k5d",
"1k5g",
"1rrp",
"1xke",
"2crf",
"2ec1",
"2y8f",
"2y8g",
"3m1i",
"3n7c",
"3oan",
"3wyf",
"4gmx",
"4gpt",
"4hat",
"4hau",
"4hav",
"4haw",
"4hax",
"4hay",
"4haz",
"4hb0",
"4hb2",
"4hb3",
"4hb4",
"4l6e",
"4wvf",
"5cll",
"5clq",
"5dh9",
"5dha",
"5dhf"... | 100 | [
"PUB00006171",
"PUB00007086",
"PUB00007092"
] | [
"10078529",
"12019565",
"10404224"
] | [
"Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.",
"Regulation of nuclear import and export by the GTPase Ran.",
"Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function."
] | [
1999,
2002,
1999
] | 3 | [] | [
"IPR045207",
"IPR045256"
] | 0 | 2 | 0 | [
"Bacillota",
"Eukaryota",
"Sylvanvirus sp."
] | [
9,
18964,
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... | [
25,
3,
23,
7,
47,
12,
3,
13,
30,
3,
3,
32
] | 12 | true | Domain | Ran binding domain | Ran binding domain | Ran_bind_dom | 8 |
IPR000157 | 157 | Toll/interleukin-1 receptor homology (TIR) domain | TIR_dom | Domain | 96,013 | false | false | This entry represents the Toll/interleukin-1 receptor (TIR) domain, which is the conserved cytoplasmic domain of approximately 200 amino acids, found in Toll-like receptors (TLRs) and their adaptors. Proteins containing this domain can also be found in plants, where they mediate disease resistance [ ], and in bacteria,... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01582",
"PF13676",
"PS50104",
"SM00255"
] | [
"TIR",
"TIR_2",
"TIR",
"TIR"
] | [
57711,
33974,
83218,
67255
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50104",
"R-BTA-140534",
"R-BTA-166016",
"R-BTA-166166",
"R-BTA-168142",
"R-BTA-2562578",
"R-BTA-6798695",
"R-BTA-936964",
"R-BTA-937041",
"R-BTA-937072",
"R-BTA-975163",
"R-BTA-9824878",
"R-CFA-109704",
"R-CFA-1679131",
"R-CFA-168138",
"R-DDI-1169408",
"R-DDI-936440",
"R-DDI-9... | [
"PROSITEDOC:PDOC50104",
"REACTOME:R-BTA-140534",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-166166",
"REACTOME:R-BTA-168142",
"REACTOME:R-BTA-2562578",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-936964",
"REACTOME:R-BTA-937041",
"REACTOME:R-BTA-937072",
"REACTOME:R-BTA-975163",
"REACTOME:R-BTA-98... | 166 | [
"1fyv",
"1fyw",
"1fyx",
"1o77",
"1t3g",
"2j67",
"2js7",
"2m1w",
"2m1x",
"2ndh",
"2y92",
"2z5v",
"3h16",
"3j0a",
"3jrn",
"3ozi",
"3ub2",
"3ub3",
"3ub4",
"4c6r",
"4c6s",
"4c6t",
"4c7m",
"4dom",
"4eo7",
"4fz5",
"4lqc",
"4lqd",
"4lzp",
"4om7",
"4w8g",
"4w8h"... | 175 | [
"PUB00005989",
"PUB00005990",
"PUB00005991",
"PUB00005992",
"PUB00005993",
"PUB00018119",
"PUB00018121",
"PUB00097509",
"PUB00097510",
"PUB00097872",
"PUB00099902"
] | [
"8621445",
"9374458",
"10679407",
"9868361",
"10671496",
"10231569",
"11081518",
"31439793",
"31439792",
"29395922",
"34184985"
] | [
"T1/ST2 signaling establishes it as a member of an expanding interleukin-1 receptor family.",
"IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling.",
"Toll signaling pathways in the innate immune response.",
"Plant disease-resistance proteins and the gene-for-gene concept.",
... | [
1996,
1997,
2000,
1998,
2000,
1999,
2000,
2019,
2019,
2018,
2021
] | 11 | [] | [
"IPR047603"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
261,
17151,
78374,
10,
217
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
1023,
8,
109,
36,
140,
83,
5,
119,
8
] | 9 | true | Domain | Toll/interleukin-1 receptor homology (TIR) domain | Toll/interleukin-1 receptor homology (TIR) domain | TIR_dom | 8 |
IPR000158 | 158 | Cell division protein FtsZ | Cell_div_FtsZ | Family | 31,982 | false | false | In bacteria, FtsZ [ , , , ] is an essential cell division protein involved in the initiation of this event. It assembles into a cytokinetic ring on the inner surface of the cytoplasmic membrane at the place where division will occur. The ring serves as a scaffold that is disassembled when septation is completed. FtsZ r... | [
"GO:0003924",
"GO:0005525"
] | [
"GTPase activity",
"GTP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00909",
"TIGR00065",
"cd02201"
] | [
"FtsZ",
"ftsZ",
"FtsZ_type1"
] | [
30261,
30130,
31978
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00873"
] | [
"PROSITEDOC:PDOC00873"
] | 1 | [
"1fsz",
"1ofu",
"1rlu",
"1rq2",
"1rq7",
"1w58",
"1w59",
"1w5a",
"1w5b",
"1w5e",
"1w5f",
"2q1x",
"2q1y",
"2r6r",
"2r75",
"2rhh",
"2rhj",
"2rhl",
"2rho",
"2vam",
"2vap",
"2vaw",
"2vxy",
"3vo8",
"3vo9",
"3voa",
"3vob",
"3vpa",
"3wgj",
"3wgk",
"3wgl",
"3wgm"... | 98 | [
"PUB00000910",
"PUB00002291",
"PUB00003846",
"PUB00004215",
"PUB00007093",
"PUB00074277"
] | [
"7859278",
"8631708",
"8412689",
"7637778",
"12051832",
"17068335"
] | [
"FtsZ, a prokaryotic homolog of tubulin?",
"Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin.",
"FtsZ ring in bacterial cytokinesis.",
"Conserved cell and organelle division.",
"The tubulin ancestor, FtsZ, draughtsman, designe... | [
1995,
1996,
1993,
1995,
2002,
2006
] | 6 | [
"IPR045061"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
1374,
27519,
2509,
1,
579
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
8,
18
] | 4 | true | Family | Cell division protein FtsZ | Cell division protein FtsZ | Cell_div_FtsZ | 5 |
IPR000159 | 159 | Ras-associating domain | RA_dom | Domain | 72,712 | false | false | Ras proteins are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. Ras is a prolific signalling molecule interacting with a spectrum of effector molecules and acting through more than one signalling pathway. A domain of about 100 residues, termed RA for RalGDS/AF-6 or Ras-Asso... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00788",
"PS50200",
"SM00314"
] | [
"RA",
"RA",
"RA"
] | [
49717,
71614,
53599
] | 3 | [
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1511",
"GenProp1548",
"PDOC50200",
"R-BTA-1306955",
"R-BTA-1433557",
"R-BTA-186763",
"R-BTA-210993",
"R-BTA-5673001",
"R-BTA-8853659",
"R-BTA-9696273",
"R-CEL-1855204",
"R-CEL-354192",
"R-CEL-354194",
"R-CEL-5673001",
"R-CEL-5674135",
"R-CFA-5673001",
"R-DDI-264876",
"R-DME... | [
"GP:GenProp1511",
"GP:GenProp1548",
"PROSITEDOC:PDOC50200",
"REACTOME:R-BTA-1306955",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-8853659",
"REACTOME:R-BTA-9696273",
"REACTOME:R-CEL-1855204",
"REACTOME:R-CEL-354192",
"... | 125 | [
"1ef5",
"1lfd",
"1lxd",
"1rax",
"1rlf",
"1wgr",
"1wxa",
"2b3a",
"2byf",
"2c5l",
"2cs4",
"2m4n",
"2rgf",
"3au4",
"3au5",
"3ddc",
"3ec8",
"3hk0",
"3kh0",
"3pzd",
"3tca",
"4gmv",
"4gn1",
"4gxb",
"4k81",
"4kvg",
"4tkn",
"5kho",
"5khq",
"6amb",
"6e31",
"6o6h"... | 43 | [
"PUB00003949",
"PUB00005457",
"PUB00018200",
"PUB00018201",
"PUB00018202"
] | [
"9253406",
"8987396",
"11723130",
"10334925",
"9628477"
] | [
"Three-dimensional structure of the Ras-interacting domain of RalGDS.",
"A novel family of Ras-binding domains.",
"Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase.",
"Sequence analysis identifies a ras-associating (RA)-l... | [
1997,
1996,
2002,
1999,
1998
] | 5 | [] | [
"IPR015758",
"IPR028398",
"IPR029458",
"IPR030748",
"IPR030750",
"IPR033600",
"IPR033618",
"IPR033622",
"IPR033623",
"IPR033631",
"IPR033633",
"IPR037835",
"IPR046986",
"IPR046989",
"IPR047888",
"IPR048945",
"IPR061274",
"IPR061275"
] | 0 | 18 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Salmonella phage PMBT27"
] | [
32,
72677,
2,
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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizo... | [
1,
39,
503,
47,
182,
122,
4,
207,
2,
2
] | 10 | true | Domain | Ras-associating domain | Ras-associating domain | RA_dom | 7 |
IPR000161 | 161 | Vasopressin V2 receptor | Vprsn_rcpt_V2 | Family | 539 | false | false | The V2 receptor is found in high levels in the osmoregulatory epithelia of the terminal urinary tract, where it stimulates water reabsorption. It is also present in lower levels in the endothelium and blood vessels of some species, where it induces vasodilation. In the CNS, binding sites are found in the subiculum, wit... | [
"GO:0005000",
"GO:0007186",
"GO:0016020"
] | [
"vasopressin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00898"
] | [
"VASOPRSNV2R"
] | [
539
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"368",
"R-BTA-388479",
"R-BTA-418555",
"R-BTA-432040",
"R-BTA-8856825",
"R-BTA-8856828",
"R-HSA-388479",
"R-HSA-418555",
"R-HSA-432040",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9036092",
"R-MMU-388479",
"R-MMU-418555",
"R-MMU-432040",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-38847... | [
"IUPHAR:368",
"REACTOME:R-BTA-388479",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-432040",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-HSA-388479",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-432040",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-9036092",
... | 21 | [
"2jx4",
"7bb6",
"7bb7",
"7kh0",
"7r0c",
"9hap",
"9hb3"
] | 7 | [
"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 | [
"IPR001817"
] | [] | 1 | 0 | 1 | [
"Actinomycetospora lemnae",
"Opisthokonta"
] | [
1,
538
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
5,
2
] | 3 | true | Family | Vasopressin V2 receptor | Vasopressin V2 receptor | Vprsn_rcpt_V2 | 1 |
IPR000162 | 162 | GPCR, family 3, metabotropic glutamate receptor | GPCR_3_mtglu_rcpt | Family | 13,740 | 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"
] | [
"PR00593"
] | [
"MTABOTROPICR"
] | [
13740
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-418594",
"R-CEL-420499",
"R-DME-418594",
"R-DME-420499",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-420499",
"R-HSA-6794361",
"R-HSA-9717207",
"R-MMU-416476",
"R-MMU-418594",
"R-MMU-420499",
"R-MMU-6794361",
"R-RNO-416476",
"R-RNO-418594",
"R-RNO-420499",
"R-RNO-6794361"
] | [
"REACTOME:R-CEL-418594",
"REACTOME:R-CEL-420499",
"REACTOME:R-DME-418594",
"REACTOME:R-DME-420499",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-HSA-6794361",
"REACTOME:R-HSA-9717207",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-4... | 17 | [
"1ewk",
"1ewt",
"1ewv",
"1isr",
"1iss",
"2e4u",
"2e4v",
"2e4w",
"2e4x",
"2e4y",
"2e4z",
"3ks9",
"3lmk",
"3mq4",
"3sm9",
"4or2",
"4xaq",
"4xar",
"4xas",
"5c5c",
"5cni",
"5cnj",
"5cnk",
"5cnm",
"5kzn",
"5kzq",
"6b7h",
"6bsz",
"6bt5",
"6e5v",
"6n4x",
"6n4y"... | 83 | [
"PUB00002720",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"1320017",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"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
] | 15 | [
"IPR000337"
] | [
"IPR000112",
"IPR000144",
"IPR000202",
"IPR001234",
"IPR001256",
"IPR001458",
"IPR001786",
"IPR001883"
] | 1 | 8 | 0 | [
"Eukaryota"
] | [
13740
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
35,
9,
45,
29,
37
] | 6 | true | Family | GPCR, family 3, metabotropic glutamate receptor | GPCR, family 3, metabotropic glutamate receptor | GPCR_3_mtglu_rcpt | 3 |
IPR000163 | 163 | Prohibitin | Prohibitin | Family | 20,039 | false | false | This entry describes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes [ ]. These microdomains, in addition to being stable scaffolds, ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PRINTS",
"PANTHER",
"CDD"
] | [
"PR00679",
"PTHR23222",
"cd03401"
] | [
"PROHIBITIN",
"",
"SPFH_prohibitin"
] | [
15558,
18939,
17233
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5673000",
"R-BTA-8949664",
"R-BTA-9840373",
"R-CEL-5673000",
"R-CEL-8949664",
"R-DME-5673000",
"R-DME-8949664",
"R-HSA-5673000",
"R-HSA-6802946",
"R-HSA-6802955",
"R-HSA-8949664",
"R-HSA-9649948",
"R-HSA-9840373",
"R-MMU-5673000",
"R-MMU-8949664",
"R-MMU-9840373",
"R-RNO-56730... | [
"REACTOME:R-BTA-5673000",
"REACTOME:R-BTA-8949664",
"REACTOME:R-BTA-9840373",
"REACTOME:R-CEL-5673000",
"REACTOME:R-CEL-8949664",
"REACTOME:R-DME-5673000",
"REACTOME:R-DME-8949664",
"REACTOME:R-HSA-5673000",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802955",
"REACTOME:R-HSA-8949664",
"REACTOM... | 20 | [
"6iqe",
"8j4i",
"8rrh",
"9o6s",
"9o6t",
"9o9z",
"9oa0",
"9unl"
] | 8 | [
"PUB00000784",
"PUB00003666",
"PUB00019208",
"PUB00080174",
"PUB00080176",
"PUB00080921",
"PUB00080922",
"PUB00080923",
"PUB00080924"
] | [
"1540973",
"1996099",
"10542406",
"16091845",
"17766116",
"15489194",
"11498003",
"10207067",
"21296110"
] | [
"The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer.",
"Prohibitin, an evolutionarily conserved intracellular protein that blocks DNA synthesis in normal fibroblasts and HeLa cells.",
"The SPFH domain: implicated in regulating targeted protein turnover in stomatins and ot... | [
1992,
1991,
1999,
2005,
2007,
2004,
2001,
1999,
2011
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
174,
4841,
14774,
140,
110
] | 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... | [
23,
2,
7,
5,
25,
9,
2,
22,
12,
2,
2,
17
] | 12 | true | Family | Prohibitin | Prohibitin | Prohibitin | 5 |
IPR000164 | 164 | Histone H3/CENP-A | Histone_H3/CENP-A | Family | 63,391 | false | false | This entry includes histone H3 and its variant, CENP-A (Cse4 in budding yeast, Cnp1 in fission yeast, and CID/CenH3 in fruit flies). Two primate-specific forms of H3, known as H3.X and H3.Y, are found in the brain [ ]. Histone H3 is one of the five histones, along with H1/H5, H2A, H2B and H4. Two copies of each of the ... | [
"GO:0003677",
"GO:0030527",
"GO:0000786"
] | [
"DNA binding",
"structural constituent of chromatin",
"nucleosome"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PRINTS",
"PROSITE",
"PROSITE",
"PANTHER",
"PANTHER",
"SMART"
] | [
"PR00622",
"PS00322",
"PS00959",
"PTHR11426",
"PTHR45810",
"SM00428"
] | [
"HISTONEH3",
"HISTONE_H3_1",
"HISTONE_H3_2",
"",
"",
"H3"
] | [
60148,
43933,
55235,
58001,
3924,
61523
] | 6 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00287",
"R-BTA-1266695",
"R-BTA-201722",
"R-BTA-212300",
"R-BTA-2299718",
"R-BTA-2559580",
"R-BTA-2559582",
"R-BTA-3214815",
"R-BTA-3214841",
"R-BTA-3214842",
"R-BTA-3214847",
"R-BTA-3214858",
"R-BTA-3247509",
"R-BTA-427359",
"R-BTA-427413",
"R-BTA-5250924",
"R-BTA-5578749",
"... | [
"PROSITEDOC:PDOC00287",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559582",
"REACTOME:R-BTA-3214815",
"REACTOME:R-BTA-3214841",
"REACTOME:R-BTA-3214842",
"REACTOME:R-BTA-3214847",
"REACTOME:R-... | 265 | [
"1aoi",
"1eqz",
"1f66",
"1hio",
"1hq3",
"1id3",
"1kx3",
"1kx4",
"1kx5",
"1m18",
"1m19",
"1m1a",
"1m1d",
"1p34",
"1p3a",
"1p3b",
"1p3f",
"1p3g",
"1p3i",
"1p3k",
"1p3l",
"1p3m",
"1p3o",
"1p3p",
"1pu9",
"1pua",
"1s32",
"1tzy",
"1u35",
"1zbb",
"1zla",
"2aro"... | 1,049 | [
"PUB00004388",
"PUB00004448",
"PUB00066796",
"PUB00070934",
"PUB00070935",
"PUB00070936",
"PUB00070937",
"PUB00070938",
"PUB00090177"
] | [
"2041803",
"8121801",
"16472024",
"22729156",
"21743476",
"22127263",
"24666101",
"21478274",
"20819935"
] | [
"Histone and histone gene compilation and alignment update.",
"Phylogenetic analysis of the core histones H2A, H2B, H3, and H4.",
"Recognition and classification of histones using support vector machine.",
"Putting CENP-A in its place.",
"Crystal structure of the human centromeric nucleosome containing CENP... | [
1991,
1994,
2006,
2013,
2011,
2012,
2014,
2011,
2010
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobiales",
"Viruses",
"metagenomes"
] | [
14,
63337,
2,
18,
20
] | 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... | [
31,
11,
16,
6,
25,
17,
2,
26,
25,
2,
3,
42
] | 12 | true | Family | Histone H3/CENP-A | Histone H3/CENP-A | Histone_H3/CENP-A | 2 |
IPR000165 | 165 | Glucoamylase | Glucoamylase | Family | 3,107 | false | false | This entry represents glucoamylase (GA), also known as glucan 1,4-alpha-glucosidase, which belongs to family 15 ( ) in the classification of glycosyl hydrolases. GA catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or polysaccharides. Studies of fungal GA have indicated 3 closely-... | [
"GO:0004339",
"GO:0005976"
] | [
"glucan 1,4-alpha-glucosidase activity",
"polysaccharide metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00736"
] | [
"GLHYDRLASE15"
] | [
3107
] | 1 | [
"CAZY",
"EC",
"METACYC",
"PROSITEDOC"
] | [
"GH15",
"3.2.1.3",
"PWY-5941",
"PDOC00646"
] | [
"CAZY:GH15",
"EC:3.2.1.3",
"METACYC:PWY-5941",
"PROSITEDOC:PDOC00646"
] | 4 | [
"1agm",
"1ayx",
"1dog",
"1gah",
"1gai",
"1glm",
"2f6d",
"2fba",
"2vn4",
"2vn7",
"3eqa",
"3gly",
"6fhv",
"6fhw",
"6frv"
] | 15 | [
"PUB00001422",
"PUB00002848",
"PUB00004952"
] | [
"1633799",
"8195212",
"1970434"
] | [
"Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.",
"Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.",
"Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp17... | [
1992,
1994,
1990
] | 3 | [] | [
"IPR006425",
"IPR006465",
"IPR008291"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Mimiviridae",
"viral metagenome"
] | [
239,
2863,
2,
3
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | Glucoamylase | Glucoamylase | Glucoamylase | 8 |
IPR000167 | 167 | Dehydrin | Dehydrin | Family | 3,697 | false | false | LEA (late embryogenesis abundant) proteins were first identified in land plants. Plant LEA proteins have been found to accumulate to high levels during the last stage of seed formation (when a natural desiccation of the seed tissues takes place) and during periods of water deficit in vegetative organs. Later, LEA homol... | [
"GO:0009415"
] | [
"response to water"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF00257",
"PTHR33346"
] | [
"Dehydrin",
""
] | [
3527,
3460
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00285"
] | [
"PROSITEDOC:PDOC00285"
] | 1 | [] | 0 | [
"PUB00009713",
"PUB00015239",
"PUB00088595",
"PUB00088596"
] | [
"10681550",
"15356392",
"18318901",
"21034219"
] | [
"Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit.",
"Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis.",
"LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana.",
"LEA pr... | [
2000,
2004,
2008,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
3,
3694
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
32,
16,
30
] | 3 | true | Family | Dehydrin | Dehydrin | Dehydrin | 9 |
IPR000170 | 170 | High potential iron-sulphur protein | High_potential_FeS_prot | Domain | 2,175 | false | false | High potential iron-sulphur proteins (HiPIP) [ , ] are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs commonly in purple photosynthetic bacteria and in other bacteria, such as Paracoccus denitrificans and Thiobacillus ferrooxidans [ ]. HiPIPs ... | [
"GO:0009055",
"GO:0019646"
] | [
"electron transfer activity",
"aerobic electron transport chain"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF01355",
"PS51373"
] | [
"HIPIP",
"HIPIP"
] | [
2036,
2145
] | 2 | [] | [] | [] | 0 | [
"1b0y",
"1cku",
"1eyt",
"1hip",
"1hlq",
"1hpi",
"1hrq",
"1hrr",
"1isu",
"1iua",
"1js2",
"1neh",
"1noe",
"1pih",
"1pij",
"2ams",
"2fla",
"2hip",
"3a38",
"3a39",
"3h31",
"3hip",
"5d8v",
"5wqq",
"5wqr",
"6aiq",
"6air",
"6xyv",
"7a4l",
"7a58",
"7c52",
"7vos"... | 33 | [
"PUB00002658",
"PUB00043697",
"PUB00043698"
] | [
"1917989",
"1317860",
"14562962"
] | [
"The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution.",
"Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. High homology of the gene product with HiPIP.",
"Amino acid sequences and distribution... | [
1991,
1992,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
2033,
2,
7,
108,
25
] | 5 | [] | [] | 0 | true | Domain | High potential iron-sulphur protein | High potential iron-sulphur protein | High_potential_FeS_prot | 5 |
IPR000172 | 172 | Glucose-methanol-choline oxidoreductase, N-terminal | GMC_OxRdtase_N | Domain | 109,609 | false | false | The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases [ , ]. These enzymes include a variety of proteins, including choline dehydrogenase (CHD), methanol oxidase (MOX) and cellobiose dehydrogenase ( ) [ ] which share a number of regions of sequence similarities. One of these regions, ... | [
"GO:0016614",
"GO:0050660"
] | [
"oxidoreductase activity, acting on CH-OH group of donors",
"flavin adenine dinucleotide binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROSITE",
"PROSITE"
] | [
"PF00732",
"PS00623",
"PS00624"
] | [
"GMC_oxred_N",
"GMC_OXRED_1",
"GMC_OXRED_2"
] | [
109300,
38978,
64168
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.99",
"PDOC00543",
"R-HSA-6798163",
"R-MMU-6798163",
"R-RNO-6798163"
] | [
"EC:1.1.99",
"PROSITEDOC:PDOC00543",
"REACTOME:R-HSA-6798163",
"REACTOME:R-MMU-6798163",
"REACTOME:R-RNO-6798163"
] | 5 | [
"1b4v",
"1b8s",
"1cbo",
"1cc2",
"1cf3",
"1coy",
"1gal",
"1gpe",
"1ijh",
"1ju2",
"1kdg",
"1mxt",
"1n1p",
"1n4u",
"1n4v",
"1n4w",
"1naa",
"2gew",
"2jbv",
"3b3r",
"3b6d",
"3cnj",
"3cox",
"3fim",
"3gdn",
"3gdp",
"3gyi",
"3gyj",
"3ljp",
"3nne",
"3q9t",
"3qvp"... | 147 | [
"PUB00000376",
"PUB00003282",
"PUB00006692"
] | [
"8218217",
"1542121",
"10725534"
] | [
"Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases.",
"GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.",
"A critical review of cellobiose dehydrogenases."
] | [
1993,
1992,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
595,
52453,
55667,
1,
102,
791
] | 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",... | [
71,
1,
1,
42,
1,
2,
2,
9,
36,
3,
49
] | 11 | true | Domain | Glucose-methanol-choline oxidoreductase, N-terminal | Glucose-methanol-choline oxidoreductase, N-terminal | GMC_OxRdtase_N | 5 |
IPR000175 | 175 | Sodium:neurotransmitter symporter | Na/ntran_symport | Family | 71,660 | false | false | Neurotransmitter transport systems are integral to the release, re-uptake and recycling of neurotransmitters at synapses. High affinity transport proteins found in the plasma membrane of presynaptic nerve terminals and glial cells are responsible for the removal from the extracellular space of released-transmitters, th... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROSITE",
"PROFILE",
"PANTHER",
"PANTHER"
] | [
"PF00209",
"PR00176",
"PS00610",
"PS00754",
"PS50267",
"PTHR11616",
"PTHR42948"
] | [
"SNF",
"NANEUSMPORT",
"NA_NEUROTRAN_SYMP_1",
"NA_NEUROTRAN_SYMP_2",
"NA_NEUROTRAN_SYMP_3",
"",
""
] | [
70381,
64942,
45324,
27208,
71139,
51936,
18236
] | 7 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00533",
"R-BTA-352230",
"R-BTA-380615",
"R-BTA-442660",
"R-BTA-71288",
"R-BTA-888593",
"R-CEL-352230",
"R-CEL-379401",
"R-CEL-442660",
"R-CFA-352230",
"R-CFA-442660",
"R-CFA-71288",
"R-CFA-888593",
"R-DME-352230",
"R-DME-379401",
"R-DME-380615",
"R-DME-442660",
"R-HSA-352230",... | [
"PROSITEDOC:PDOC00533",
"REACTOME:R-BTA-352230",
"REACTOME:R-BTA-380615",
"REACTOME:R-BTA-442660",
"REACTOME:R-BTA-71288",
"REACTOME:R-BTA-888593",
"REACTOME:R-CEL-352230",
"REACTOME:R-CEL-379401",
"REACTOME:R-CEL-442660",
"REACTOME:R-CFA-352230",
"REACTOME:R-CFA-442660",
"REACTOME:R-CFA-71288... | 46 | [
"2a65",
"2q6h",
"2q72",
"2qb4",
"2qei",
"2qju",
"3f3a",
"3f3c",
"3f3d",
"3f3e",
"3f48",
"3f4i",
"3f4j",
"3gjc",
"3gjd",
"3gwu",
"3gwv",
"3gww",
"3mpn",
"3mpq",
"3qs4",
"3qs5",
"3qs6",
"3tt1",
"3tt3",
"3tu0",
"3usg",
"3usi",
"3usj",
"3usk",
"3usl",
"3usm"... | 244 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008"
] | [
"15336049",
"8811182",
"8103691",
"7823024"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function."
] | [
1992,
1996,
1993,
1994
] | 4 | [] | [
"IPR002434",
"IPR002435",
"IPR002436",
"IPR002438",
"IPR002944",
"IPR002980",
"IPR002981",
"IPR002982",
"IPR002983",
"IPR002984",
"IPR003028",
"IPR047218"
] | 0 | 12 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
970,
17516,
52808,
1,
365
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
84,
63,
127,
88,
82
] | 6 | true | Family | Sodium:neurotransmitter symporter | Sodium:neurotransmitter symporter | Na/ntran_symport | 5 |
IPR000176 | 176 | mRNA methyltransferase-like | mRNA_MeTrfase-like | Family | 442 | false | false | This family contains viral proteins that are bifunctional, acting as both an mRNA (nucleoside-2'-O-)-methyltransferase and a poly(A) polymerase processivity factor [ , ]. The family also includes a number of uncharacterised eukaryotic sequences. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01358"
] | [
"PARP_regulatory"
] | [
442
] | 1 | [
"EC",
"METACYC"
] | [
"2.1.1.57",
"PWY-7379"
] | [
"EC:2.1.1.57",
"METACYC:PWY-7379"
] | 2 | [
"1av6",
"1b42",
"1bky",
"1eam",
"1eqa",
"1jsz",
"1jte",
"1jtf",
"1p39",
"1v39",
"1vp3",
"1vp9",
"1vpt",
"2ga9",
"2gaf",
"2vp3",
"3er8",
"3er9",
"3erc",
"3mag",
"3mct",
"4dcg",
"8b07",
"8ceq",
"8cer",
"8ces",
"8cet",
"8cev",
"8cgb",
"8oiv"
] | 30 | [
"PUB00058105",
"PUB00058106"
] | [
"1313572",
"12359447"
] | [
"Cap-specific mRNA (nucleoside-O2'-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein.",
"The positive transcription elongation factor activity of the vaccinia virus J3 protein is independent from its (nucleoside-2'-O-) methyltransferase and poly(A... | [
1992,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"metagenomes"
] | [
240,
190,
12
] | 3 | [] | [] | 0 | true | Family | mRNA methyltransferase-like | mRNA methyltransferase-like | mRNA_MeTrfase-like | 9 |
IPR000177 | 177 | Apple domain | Apple | Domain | 6,594 | false | false | Plasma kallikrein ( ) and coagulation factor XI ( ) are two related plasma serine proteases activated by factor XIIA and which share the same domain topology: an N-terminal region that contains four tandem repeats of about 90 amino acids and a C-terminal catalytic domain. The 90 amino-acid repeated domain contains 6 co... | [
"GO:0005515",
"GO:0006508",
"GO:0005576"
] | [
"protein binding",
"proteolysis",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PROSITE",
"SMART",
"CDD"
] | [
"PR00005",
"PS00495",
"SM00223",
"cd01100"
] | [
"APPLEDOMAIN",
"APPLE",
"APPLE",
"APPLE_Factor_XI_like"
] | [
1032,
616,
5740,
4795
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.21",
"PDOC00376",
"R-BTA-140837",
"R-BTA-1592389",
"R-HSA-140837",
"R-HSA-1592389",
"R-HSA-9657688",
"R-HSA-9657689",
"R-HSA-9673221",
"R-MMU-140837",
"R-MMU-1592389",
"R-RNO-140837",
"R-RNO-1592389"
] | [
"EC:3.4.21",
"PROSITEDOC:PDOC00376",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-1592389",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA-1592389",
"REACTOME:R-HSA-9657688",
"REACTOME:R-HSA-9657689",
"REACTOME:R-HSA-9673221",
"REACTOME:R-MMU-140837",
"REACTOME:R-MMU-1592389",
"REACTOME:R-RNO-140837",
... | 13 | [
"1hky",
"2j8j",
"2j8l",
"2ll3",
"2ll4",
"2yil",
"2yio",
"2yip",
"4a5v",
"5eod",
"5eok",
"5i25",
"6i44",
"6i58",
"6o1g",
"7qot",
"7qox",
"8fgx"
] | 18 | [
"PUB00000342",
"PUB00017941",
"PUB00017942"
] | [
"1998666",
"8662705",
"9632702"
] | [
"Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.",
"Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4.",
"A binding site for... | [
1991,
1996,
1998
] | 3 | [
"IPR003609"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
1376,
5167,
35,
16
] | 4 | [
"Caenorhabditis elegans",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
12,
2,
9
] | 4 | true | Domain | Apple domain | Apple domain | Apple | 6 |
IPR000178 | 178 | Translation initiation factor IF-2, bacterial-like | TF_IF2_bacterial-like | Family | 31,433 | false | false | Initiation factor 2 (IF-2) (gene infB) [ ] is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-2 promotes the GTP-dependent binding of the initiator tRNA to the small subunit of the ribosome. IF-2 is a protein of about 70 to 95 Kd which contains a central GTP-binding domain f... | [
"GO:0003743",
"GO:0003924",
"GO:0005525",
"GO:0006413"
] | [
"translation initiation factor activity",
"GTPase activity",
"GTP binding",
"translational initiation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"HAMAP",
"PROSITE",
"NCBIFAM"
] | [
"MF_00100_B",
"PS01176",
"TIGR00487"
] | [
"IF_2_B",
"IF2",
"IF-2"
] | [
29098,
24235,
29320
] | 3 | [
"GP",
"PROSITEDOC",
"REACTOME"
] | [
"GenProp0740",
"PDOC00905",
"R-HSA-5368286"
] | [
"GP:GenProp0740",
"PROSITEDOC:PDOC00905",
"REACTOME:R-HSA-5368286"
] | 3 | [
"1d1n",
"1zo1",
"2crv",
"3izy",
"3j4j",
"3jcj",
"3jcn",
"4b3x",
"4b44",
"4b47",
"4b48",
"4kjz",
"5lmv",
"5me0",
"5me1",
"6gaw",
"6gaz",
"6gb2",
"6o7k",
"6o9k",
"6rw5",
"7po2",
"7pua",
"7pub",
"7uiu",
"7unq",
"7unr",
"7unt",
"7unu",
"7unv",
"7unw",
"8qrn"... | 37 | [
"PUB00000691",
"PUB00002916",
"PUB00004567"
] | [
"1805969",
"7829522",
"8219057"
] | [
"Structural and functional domains of E coli initiation factor IF2.",
"Cloning and sequence analysis of the human mitochondrial translational initiation factor 2 cDNA.",
"Organization of plastid-encoded ATPase genes and flanking regions including homologues of infB and tsf in the thermophilic red alga Galdieria... | [
1991,
1995,
1993
] | 3 | [
"IPR015760"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4,
26030,
4801,
598
] | 4 | [
"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)... | [
12,
1,
1,
1,
1,
1,
5,
2,
1,
1,
11
] | 11 | true | Family | Translation initiation factor IF-2, bacterial-like | Translation initiation factor IF-2, bacterial-like | TF_IF2_bacterial-like | 3 |
IPR000180 | 180 | Membrane dipeptidase, active site | Dipep_AS | Active_site | 3,865 | false | false | This signature defines the active site of peptidases belong to the MEROPS peptidase family M19 (membrane dipeptidase family, clan MJ). The protein fold of the peptidase domain for members of this family resembles that of Klebsiella urease, the type example for clan MJ [ ]. Renal dipeptidase (rDP) ( ), also known as mic... | [
"GO:0070573",
"GO:0006508"
] | [
"metallodipeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00869"
] | [
"RENAL_DIPEPTIDASE_1"
] | [
3865
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.13.19",
"PWY-7533",
"PWY-8355",
"PWY-8397",
"PDOC00678",
"R-BTA-2142691",
"R-BTA-5423646",
"R-HSA-2142691",
"R-HSA-5423646",
"R-HSA-9664535",
"R-MMU-2142691",
"R-MMU-5423646",
"R-RNO-2142691",
"R-RNO-5423646",
"R-SSC-2142691",
"R-SSC-5423646"
] | [
"EC:3.4.13.19",
"METACYC:PWY-7533",
"METACYC:PWY-8355",
"METACYC:PWY-8397",
"PROSITEDOC:PDOC00678",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-5423646",
"REACTOME:R-HSA-2142691",
"REACTOME:R-HSA-5423646",
"REACTOME:R-HSA-9664535",
"REACTOME:R-MMU-2142691",
"REACTOME:R-MMU-5423646",
"REACTOME:... | 16 | [
"1itq",
"1itu",
"6vgo",
"6vgr",
"9h0b"
] | 5 | [
"PUB00000644",
"PUB00021853"
] | [
"8097406",
"12144777"
] | [
"Importance of Glu-125 in the catalytic activity of human renal dipeptidase.",
"Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."
] | [
1993,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes"
] | [
1198,
2602,
25,
40
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
8,
7,
8
] | 5 | true | Active_site | Membrane dipeptidase, active site | Membrane dipeptidase, active site | Dipep_AS | 9 |
IPR000182 | 182 | GNAT domain | GNAT_dom | Domain | 913,056 | false | false | This entry represents the entire GNAT domain. The N-acetyltransferases (NAT) ([ec:2.3.1.-]) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodelling. Th... | [
"GO:0016747"
] | [
"acyltransferase activity, transferring groups other than amino-acyl groups"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00583",
"PF13302",
"PF13508",
"PF13673",
"PF13718",
"PS51186"
] | [
"Acetyltransf_1",
"Acetyltransf_3",
"Acetyltransf_7",
"Acetyltransf_10",
"GNAT_acetyltr_2",
"GNAT"
] | [
540396,
171293,
62377,
55212,
9294,
864222
] | 6 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"2.3.1",
"GenProp0232",
"GenProp0796",
"GenProp1222",
"GenProp1610",
"GenProp1630",
"GenProp1695",
"PDOC51186",
"R-BTA-351200",
"R-CEL-351200",
"R-DDI-3214847",
"R-DDI-446210",
"R-DME-2468052",
"R-DME-446210",
"R-DRE-2032785",
"R-DRE-5689880",
"R-DRE-5689901",
"R-DRE-8963693",
"R... | [
"EC:2.3.1",
"GP:GenProp0232",
"GP:GenProp0796",
"GP:GenProp1222",
"GP:GenProp1610",
"GP:GenProp1630",
"GP:GenProp1695",
"PROSITEDOC:PDOC51186",
"REACTOME:R-BTA-351200",
"REACTOME:R-CEL-351200",
"REACTOME:R-DDI-3214847",
"REACTOME:R-DDI-446210",
"REACTOME:R-DME-2468052",
"REACTOME:R-DME-446... | 86 | [
"1b6b",
"1b87",
"1bo4",
"1bob",
"1cjw",
"1cm0",
"1ghe",
"1i12",
"1i1d",
"1i21",
"1ib1",
"1j4j",
"1kuv",
"1kux",
"1kuy",
"1l0c",
"1m1d",
"1m44",
"1m4d",
"1m4g",
"1m4i",
"1mk4",
"1n71",
"1nsl",
"1on0",
"1ozp",
"1p0h",
"1pu9",
"1pua",
"1q2c",
"1q2d",
"1q2y"... | 699 | [
"PUB00005463",
"PUB00025257",
"PUB00027579",
"PUB00033792",
"PUB00033793"
] | [
"9175471",
"12527305",
"12592013",
"10940244",
"15581578"
] | [
"GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein.",
"Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.",
"X-ray structure of the AAC(6')-Ii antibiotic resistance enz... | [
1997,
2003,
2003,
2000,
2005
] | 5 | [] | [
"IPR040448"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
13602,
751441,
139853,
757,
6,
7397
] | 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",... | [
171,
37,
51,
49,
24,
78,
81,
30,
123,
100,
15,
20,
256
] | 13 | true | Domain | GNAT domain | GNAT domain | GNAT_dom | 1 |
IPR000183 | 183 | Ornithine/DAP/Arg decarboxylase | Orn/DAP/Arg_de-COase | Family | 58,428 | false | false | Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [ , ]. Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. PLP-depende... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR01179"
] | [
"ODADCRBXLASE"
] | [
58428
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.1.1",
"PDOC00685",
"R-BTA-350562",
"R-BTA-351202",
"R-CEL-350562",
"R-CEL-351143",
"R-CEL-351202",
"R-DDI-351143",
"R-DDI-351202",
"R-DME-350562",
"R-DME-351143",
"R-DME-351202",
"R-HSA-350562",
"R-HSA-351143",
"R-HSA-351202",
"R-MMU-350562",
"R-MMU-351143",
"R-MMU-351202",
"R... | [
"EC:4.1.1",
"PROSITEDOC:PDOC00685",
"REACTOME:R-BTA-350562",
"REACTOME:R-BTA-351202",
"REACTOME:R-CEL-350562",
"REACTOME:R-CEL-351143",
"REACTOME:R-CEL-351202",
"REACTOME:R-DDI-351143",
"REACTOME:R-DDI-351202",
"REACTOME:R-DME-350562",
"REACTOME:R-DME-351143",
"REACTOME:R-DME-351202",
"REACT... | 26 | [
"1d7k",
"1f3t",
"1hkv",
"1hkw",
"1knw",
"1ko0",
"1njj",
"1qu4",
"1szr",
"1tuf",
"1twi",
"2j66",
"2nv9",
"2nva",
"2o0t",
"2on3",
"2oo0",
"2p3e",
"2plj",
"2plk",
"2qgh",
"2tod",
"2yxx",
"3btn",
"3c5q",
"3n2b",
"3n2o",
"3nzp",
"3nzq",
"3vab",
"4aib",
"4xg1"... | 66 | [
"PUB00001452",
"PUB00002116",
"PUB00002726",
"PUB00003632",
"PUB00095574"
] | [
"8181483",
"2198270",
"1730582",
"3143046",
"30699288"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli.",
"Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluorometh... | [
1994,
1990,
1992,
1988,
2019
] | 5 | [] | [
"IPR002433",
"IPR002985",
"IPR002986",
"IPR017530",
"IPR042152"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
772,
45391,
11414,
22,
829
] | 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",... | [
15,
2,
8,
2,
2,
13,
13,
1,
17,
15,
1,
1,
22
] | 13 | true | Family | Ornithine/DAP/Arg decarboxylase | Ornithine/DAP/Arg decarboxylase | Orn/DAP/Arg_de-COase | 4 |
IPR000184 | 184 | Bacterial surface antigen (D15) | Bac_surfAg_D15 | Domain | 46,889 | false | false | The protein sequences of d15 from various strains of Haemophilus influenzae are highly conserved, with only a small variable region identified near the carboxyl terminus of the protein [ ]. D15 is a highly conserved antigen that is protective in animal models and it may be a useful component of a universal subunit vacc... | [
"GO:0019867"
] | [
"outer membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF01103"
] | [
"Omp85"
] | [
46889
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9013404",
"R-CEL-9013404",
"R-DME-9013404",
"R-DRE-9013404",
"R-HSA-1268020",
"R-HSA-8949613",
"R-HSA-9013404",
"R-HSA-9760173",
"R-MMU-9013404",
"R-RNO-9013404",
"R-XTR-9013404"
] | [
"REACTOME:R-BTA-9013404",
"REACTOME:R-CEL-9013404",
"REACTOME:R-DME-9013404",
"REACTOME:R-DRE-9013404",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-8949613",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9760173",
"REACTOME:R-MMU-9013404",
"REACTOME:R-RNO-9013404",
"REACTOME:R-XTR-9013404"
] | 11 | [
"4c00",
"4c4v",
"4k3b",
"4k3c",
"4n74",
"4n75",
"5ayw",
"5d0o",
"5d0q",
"5ekq",
"5ljo",
"5or1",
"6fsu",
"6lyq",
"6lyr",
"6lys",
"6lyu",
"6qgw",
"6qgx",
"6qgy",
"6smx",
"6sn0",
"6sn2",
"6sn3",
"6sn4",
"6sn5",
"6sn7",
"6sn8",
"6sn9",
"6so7",
"6so8",
"6soa"... | 136 | [
"PUB00001856",
"PUB00002032",
"PUB00006381"
] | [
"7737523",
"8757848",
"9284140"
] | [
"The sequencing of the 80-kDa D15 protective surface antigen of Haemophilus influenzae.",
"Cloning, sequencing, expression, and protective capacity of the oma87 gene encoding the Pasteurella multocida 87-kilodalton outer membrane antigen.",
"Outer membrane protein D15 is conserved among Haemophilus influenzae s... | [
1995,
1996,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Microviridae sp. ctdfd8",
"unclassified sequences"
] | [
38304,
7983,
1,
601
] | 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",... | [
39,
1,
3,
2,
2,
3,
1,
3,
24,
4,
1,
1,
50
] | 13 | true | Domain | Bacterial surface antigen (D15) | Bacterial surface antigen (D15) | Bac_surfAg_D15 | 6 |
IPR000185 | 185 | Protein translocase subunit SecA | SecA | Family | 37,668 | false | false | Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component [ ]. From there, the mature proteins are either targeted to the outer membra... | [
"GO:0005524",
"GO:0006605",
"GO:0006886"
] | [
"ATP binding",
"protein targeting",
"intracellular protein transport"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_01382",
"PR00906",
"PTHR30612",
"TIGR00963"
] | [
"SecA",
"SECA",
"",
"secA"
] | [
31836,
34197,
37636,
27001
] | 4 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.4.2.8",
"GenProp0209",
"PDOC01016",
"R-HSA-1222387",
"R-HSA-9636383",
"R-HSA-9760173"
] | [
"EC:7.4.2.8",
"GP:GenProp0209",
"PROSITEDOC:PDOC01016",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-9636383",
"REACTOME:R-HSA-9760173"
] | 6 | [
"1m6n",
"1m74",
"1nkt",
"1nl3",
"1tf2",
"1tf5",
"2fsf",
"2fsg",
"2fsh",
"2fsi",
"2ibm",
"2ipc",
"2vda",
"3bxz",
"3din",
"3dl8",
"3iqm",
"3iqy",
"3jux",
"3jv2",
"4uaq",
"4ys0",
"5eul",
"5k9t",
"6gox",
"6itc",
"6s0k",
"6sxh",
"6t4h",
"7xha",
"7xhb",
"8y9y"... | 36 | [
"PUB00001687",
"PUB00003757",
"PUB00007064",
"PUB00007065",
"PUB00007066"
] | [
"7758587",
"8437571",
"2202721",
"11336818",
"10418149"
] | [
"Isolation and characterization of the cDNA for pea chloroplast SecA. Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts.",
"SecA is plastid-encoded in a red alga: implications for the evolution of plastid genomes and the thylakoid protein import apparatus.",
"T... | [
1995,
1993,
1990,
2001,
1999
] | 5 | [] | [
"IPR022490",
"IPR026389",
"IPR030908"
] | 0 | 3 | 0 | [
"Bacteria",
"Candidatus Methanogaster sp.",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
31976,
1,
4786,
1,
904
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
3,
1,
9,
13
] | 5 | true | Family | Protein translocase subunit SecA | Protein translocase subunit SecA | SecA | 4 |
IPR000186 | 186 | Interleukin-5 | IL-5 | Family | 376 | false | false | This entry represents interleukin-5 (IL5), also known as eosinophil differentiation factor (EDF), is a lineage-specific cytokine for eosinophilpoiesis [ , ]. It regulates eosinophil growth and activation [ ], and thus plays an important role in diseases associated with increased levels of eosinophils, including asthma ... | [
"GO:0005137",
"GO:0008083",
"GO:0006955",
"GO:0005576"
] | [
"interleukin-5 receptor binding",
"growth factor activity",
"immune response",
"extracellular region"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02025",
"PR00432",
"PTHR48491"
] | [
"IL5",
"INTERLEUKIN5",
""
] | [
352,
216,
374
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-512988",
"R-BTA-5673001",
"R-BTA-912526",
"R-CFA-512988",
"R-CFA-5673001",
"R-CFA-912526",
"R-HSA-512988",
"R-HSA-5673001",
"R-HSA-912526",
"R-MMU-512988",
"R-MMU-5673001",
"R-MMU-912526",
"R-RNO-512988",
"R-RNO-5673001",
"R-RNO-912526",
"R-SSC-512988",
"R-SSC-5673001",
"R-S... | [
"REACTOME:R-BTA-512988",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-912526",
"REACTOME:R-CFA-512988",
"REACTOME:R-CFA-5673001",
"REACTOME:R-CFA-912526",
"REACTOME:R-HSA-512988",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-912526",
"REACTOME:R-MMU-512988",
"REACTOME:R-MMU-5673001",
"REACTOME:R-MMU... | 18 | [
"1hul",
"3b5k",
"3qt2",
"3va2",
"8tld"
] | 5 | [
"PUB00001613",
"PUB00004146",
"PUB00004643"
] | [
"2037074",
"8483502",
"3498940"
] | [
"Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein.",
"A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5.",
"Molecular cloning, nucleotide sequence, and expression of the gene encod... | [
1991,
1993,
1987
] | 3 | [] | [] | 0 | 0 | null | [
"Tetrapoda"
] | [
376
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
3
] | 3 | true | Family | Interleukin-5 | Interleukin-5 | IL-5 | 8 |
IPR000187 | 187 | Corticotropin-releasing factor | CRF | Domain | 2,815 | false | false | This entry represents a domain found in the corticotropin-releasing factor family members. Corticotropin-releasing factor (CRF), urotensin-I, urocortin and sauvagine form a family of related neuropeptides in vertebrates. The family can be grouped into 2 separate paralogous lineages, with urotensin-I, urocortin and sauv... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF00473",
"SM00039"
] | [
"CRF",
"CRF"
] | [
2802,
1985
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00442",
"R-BTA-373080",
"R-BTA-418555",
"R-HSA-373080",
"R-HSA-418555",
"R-HSA-422085",
"R-HSA-9022702",
"R-MMU-373080",
"R-MMU-418555",
"R-RNO-373080",
"R-SSC-373080",
"R-SSC-418555"
] | [
"PROSITEDOC:PDOC00442",
"REACTOME:R-BTA-373080",
"REACTOME:R-BTA-418555",
"REACTOME:R-HSA-373080",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-422085",
"REACTOME:R-HSA-9022702",
"REACTOME:R-MMU-373080",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-373080",
"REACTOME:R-SSC-373080",
"REACTOME:R-SSC-418... | 12 | [
"1go9",
"1goe",
"2jnd",
"2l27",
"2rm9",
"2rmd",
"2rme",
"2rmf",
"2rmg",
"2rmh",
"2rmi",
"6p9x",
"6pb0",
"6pb1",
"7try",
"7ts0"
] | 16 | [
"PUB00004937",
"PUB00007067"
] | [
"2200028",
"10375459"
] | [
"Evolutionary aspects of corticotropin releasing hormones.",
"Evolution and physiology of the corticotropin-releasing factor (CRF) family of neuropeptides in vertebrates."
] | [
1990,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2815
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
2,
5,
6,
10
] | 5 | true | Domain | Corticotropin-releasing factor | Corticotropin-releasing factor | CRF | 7 |
IPR000189 | 189 | Prokaryotic transglycosylase, active site | Transglyc_AS | Active_site | 29,353 | false | false | Bacterial lytic transglycosylases degrade murein via cleavage of the beta-1,4- glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine, with the concomitant formation of a 1,6-anhydrobond in the muramic acid residue. Escherichia coli has at least three different lytic transglycosylases: two soluble isozyme... | [
"GO:0008933",
"GO:0000270",
"GO:0016020"
] | [
"peptidoglycan lytic transglycosylase activity",
"peptidoglycan metabolic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00922"
] | [
"TRANSGLYCOSYLASE"
] | [
29353
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00713"
] | [
"PROSITEDOC:PDOC00713"
] | 1 | [
"1qsa",
"1qte",
"1sly",
"2y8p",
"3t36",
"4c5f",
"4hjv",
"4owd",
"4oxv",
"4oyv",
"4oz9",
"4p0g",
"4p11",
"5a5x",
"5aa1",
"5aa2",
"5aa3",
"5aa4",
"6cf8",
"6cf9",
"6cfc",
"6ghz",
"6gi4",
"6yt5",
"7eyb",
"7k5c",
"7lam",
"7laq",
"8gez",
"8gf0",
"8gf1",
"8gfb"... | 50 | [
"PUB00000408",
"PUB00002156",
"PUB00004171",
"PUB00005413"
] | [
"7548026",
"1938883",
"8107871",
"8203016"
] | [
"Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism.",
"Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase.",
"Doughnut-shaped... | [
1995,
1991,
1994,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
28574,
31,
402,
346
] | 4 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Active_site | Prokaryotic transglycosylase, active site | Prokaryotic transglycosylase, active site | Transglyc_AS | 4 |
IPR000190 | 190 | Angiotensin II receptor type 1 | ATII_AT1_rcpt | Family | 948 | false | false | Angiotensin II is a blood-borne hormone produced in the circulation, it is also formed in many tissues such as the brain, kidney, heart, and blood vessels, where angiotensin II functions as a paracrine and autocrine hormone. The known actions of angiotensin II are mediated through two angiotensin receptor subtypes, Ang... | [
"GO:0004945",
"GO:0007186",
"GO:0019229",
"GO:0016020"
] | [
"angiotensin type II receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of vasoconstriction",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00635"
] | [
"ANGIOTENSN1R"
] | [
948
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"34",
"R-BTA-375276",
"R-BTA-416476",
"R-BTA-8856825",
"R-BTA-8856828",
"R-GGA-375276",
"R-GGA-416476",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-375276",
"R-RNO-416476",
"R-RNO-8856825... | [
"IUPHAR:34",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-416476",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-375276",
... | 23 | [
"4yay",
"4zud",
"6do1",
"6os0",
"6os1",
"6os2",
"8th3",
"8th4",
"9eah",
"9eai",
"9eaj"
] | 11 | [
"PUB00063358",
"PUB00063362",
"PUB00063363",
"PUB00063364"
] | [
"17346243",
"9039129",
"9879743",
"16286564"
] | [
"Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology.",
"Angiotensin II signaling in vascular smooth muscle. New concepts.",
"Angiotensin II signal transduction pathways.",
"The angiotensin II type 2 receptor causes constitutive growth of cardiomyocy... | [
2007,
1997,
1998,
2005
] | 4 | [
"IPR000248"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
948
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
5,
6,
4
] | 4 | true | Family | Angiotensin II receptor type 1 | Angiotensin II receptor type 1 | ATII_AT1_rcpt | 4 |
IPR000192 | 192 | Aminotransferase class V domain | Aminotrans_V_dom | Domain | 180,872 | false | false | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [ ] into subfamilies. This entry represents an aminotransfer... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00266"
] | [
"Aminotran_5"
] | [
180872
] | 1 | [
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp0701",
"GenProp1747",
"PDOC00514",
"R-BTA-2408508",
"R-BTA-947581",
"R-CEL-947581",
"R-CEL-977347",
"R-DDI-1362409",
"R-DDI-389661",
"R-DDI-9033241",
"R-DDI-947581",
"R-DDI-977347",
"R-DDI-9865881",
"R-DME-1362409",
"R-DME-389661",
"R-DME-9033241",
"R-DME-947581",
"R-DME-97... | [
"GP:GenProp0701",
"GP:GenProp1747",
"PROSITEDOC:PDOC00514",
"REACTOME:R-BTA-2408508",
"REACTOME:R-BTA-947581",
"REACTOME:R-CEL-947581",
"REACTOME:R-CEL-977347",
"REACTOME:R-DDI-1362409",
"REACTOME:R-DDI-389661",
"REACTOME:R-DDI-9033241",
"REACTOME:R-DDI-947581",
"REACTOME:R-DDI-977347",
"REA... | 53 | [
"1bjn",
"1bjo",
"1bt4",
"1c0n",
"1ecx",
"1eg5",
"1elq",
"1elu",
"1h0c",
"1i29",
"1iug",
"1j04",
"1jf9",
"1kmj",
"1kmk",
"1m32",
"1n2t",
"1n31",
"1p3w",
"1t3i",
"1vjo",
"1w23",
"1w3u",
"2bhx",
"2bi1",
"2bi2",
"2bi3",
"2bi5",
"2bi9",
"2bia",
"2bie",
"2big"... | 238 | [
"PUB00001654"
] | [
"8482384"
] | [
"Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3889,
137562,
35964,
69,
3388
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
6,
17,
8,
4,
37,
24,
8,
30,
32,
3,
5,
46
] | 13 | true | Domain | Aminotransferase class V domain | Aminotransferase class V domain | Aminotrans_V_dom | 4 |
IPR000194 | 194 | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | ATPase_F1/V1/A1_a/bsu_nucl-bd | Domain | 181,849 | 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:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00006"
] | [
"ATP-synt_ab"
] | [
181849
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"7.1.2.2",
"PWY-7980",
"PDOC00137",
"R-BTA-1222556",
"R-BTA-77387",
"R-BTA-917977",
"R-BTA-9639288",
"R-BTA-983712",
"R-CEL-1222556",
"R-CEL-1268020",
"R-CEL-163210",
"R-CEL-77387",
"R-CEL-8949613",
"R-CEL-917977",
"R-CEL-9639288",
"R-CEL-983712",
"R-CEL-9837999",
"R-CFA-1268020",
... | [
"EC:7.1.2.2",
"METACYC:PWY-7980",
"PROSITEDOC:PDOC00137",
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-917977",
"REACTOME:R-BTA-9639288",
"REACTOME:R-BTA-983712",
"REACTOME:R-CEL-1222556",
"REACTOME:R-CEL-1268020",
"REACTOME:R-CEL-163210",
"REACTOME:R-CEL-77387",
"REACTO... | 81 | [
"1bmf",
"1cow",
"1e1q",
"1e1r",
"1e79",
"1efr",
"1fx0",
"1h8e",
"1h8h",
"1kmh",
"1mab",
"1nbm",
"1ohh",
"1pv4",
"1pvo",
"1qo1",
"1sky",
"1vdz",
"1w0j",
"1w0k",
"1xpo",
"1xpr",
"1xpu",
"2c61",
"2ck3",
"2dpy",
"2f43",
"2hld",
"2ht1",
"2jdi",
"2jiz",
"2jj1"... | 592 | [
"PUB00004187",
"PUB00009752",
"PUB00020603",
"PUB00020604",
"PUB00020609",
"PUB00020611",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"8065448",
"11309608",
"15473999",
"15078220",
"15629643",
"12745923",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.",
"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.",
"Mechan... | [
1994,
2001,
2004,
2004,
2005,
2003,
2010,
2008,
1992,
1998
] | 10 | [] | [
"IPR033732",
"IPR041703"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2247,
106703,
70754,
2145
] | 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",... | [
47,
6,
8,
19,
4,
30,
10,
4,
47,
26,
3,
4,
71
] | 13 | true | Domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain | ATPase_F1/V1/A1_a/bsu_nucl-bd | 6 |
IPR000195 | 195 | Rab-GAP-TBC domain | Rab-GAP-TBC_dom | Domain | 119,009 | false | false | The ~200 amino acid TBC/rab GTPase-activating protein (GAP) domain is well conserved across species and has been found in a wide range of different proteins from plant adhesion molecules to mammalian oncogenes. The name TBC derives from the name of the murine protein Tbc1 in which this domain was first identified based... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00566",
"PF23436",
"PS50086",
"SM00164"
] | [
"RabGAP-TBC",
"RabGap-TBC_2",
"TBC_RABGAP",
"TBC"
] | [
114242,
3405,
115137,
105233
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50086",
"R-BTA-204005",
"R-BTA-8854214",
"R-CEL-8854214",
"R-DME-6798695",
"R-DME-8854214",
"R-HSA-1445148",
"R-HSA-204005",
"R-HSA-432722",
"R-HSA-6798695",
"R-HSA-6811440",
"R-HSA-8854214",
"R-MMU-204005",
"R-MMU-432722",
"R-MMU-6798695",
"R-MMU-6811440",
"R-MMU-8854214",
"R... | [
"PROSITEDOC:PDOC50086",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-8854214",
"REACTOME:R-CEL-8854214",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-8854214",
"REACTOME:R-HSA-1445148",
"REACTOME:R-HSA-204005",
"REACTOME:R-HSA-432722",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6811440",
"REACTOME:R-H... | 24 | [
"1fkm",
"2g77",
"2qfz",
"2qq8",
"3hzj",
"3qwl",
"3qyb",
"3qye",
"4hl4",
"4hlq",
"4nc6",
"4p17",
"4z6y",
"5ejc",
"5hjn",
"5hjq",
"5tub",
"5tuc",
"6d0s",
"6jl7",
"7dl2",
"9ce3",
"9qzc",
"9qzf"
] | 24 | [
"PUB00004496",
"PUB00005468",
"PUB00014098",
"PUB00018101",
"PUB00018102"
] | [
"7566974",
"9255064",
"11013213",
"10508155",
"8654926"
] | [
"Molecular cloning of a cDNA with a novel domain present in the tre-2 oncogene and the yeast cell cycle regulators BUB2 and cdc16.",
"A shared domain between a spindle assembly checkpoint protein and Ypt/Rab-specific GTPase-activators.",
"Crystal structure of the GAP domain of Gyp1p: first insights into interac... | [
1995,
1997,
2000,
1999,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Bacillota",
"Eukaryota",
"bird metagenome"
] | [
5,
119003,
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... | [
143,
32,
174,
64,
195,
126,
12,
56,
179,
11,
13,
211
] | 12 | true | Domain | Rab-GAP-TBC domain | Rab-GAP-TBC domain | Rab-GAP-TBC_dom | 9 |
IPR000196 | 196 | Large ribosomal subunit protein eL19 domain | Ribosomal_eL19_dom | Domain | 7,662 | false | false | This entry represents a structural domain of large ribosomal subunit protein eL19, found in archaea and eukaryotes [ , , ]. | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM",
"SMART"
] | [
"MF_01475",
"NF006343",
"SM01416"
] | [
"Ribosomal_eL19",
"PRK08570.1",
"Ribosomal_L19e"
] | [
5561,
6288,
7662
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00455",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CFA-156827",
"R-CFA-1799339",
"R-CFA-6791226",
"R-CFA-72689... | [
"PROSITEDOC:PDOC00455",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 77 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 657 | [
"PUB00006505",
"PUB00030943",
"PUB00080279"
] | [
"10381320",
"15184028",
"24524803"
] | [
"The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.",
"The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit.",
"A new system for naming ribosomal proteins."
] | [
1999,
2004,
2014
] | 3 | [] | [
"IPR033935",
"IPR033936"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
949,
3,
6671,
39
] | 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... | [
13,
1,
1,
1,
10,
3,
1,
4,
10,
2,
2,
19
] | 12 | true | Domain | Large ribosomal subunit protein eL19 domain | Large ribosomal subunit protein eL19 domain | Ribosomal_eL19_dom | 7 |
IPR000197 | 197 | Zinc finger, TAZ-type | Znf_TAZ | Domain | 11,872 | false | false | TAZ (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases ( ) that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regu... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF02135",
"PS50134",
"SM00551"
] | [
"zf-TAZ",
"ZF_TAZ",
"ZnF_TAZ"
] | [
11508,
10156,
11580
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1.48",
"PDOC50134",
"R-CEL-1234158",
"R-CEL-201722",
"R-CEL-3899300",
"R-CEL-5250924",
"R-CEL-5689901",
"R-CEL-8936459",
"R-CEL-8939243",
"R-CEL-8939246",
"R-CEL-8951936",
"R-CEL-9617629",
"R-CEL-9701898",
"R-CEL-9759194",
"R-CEL-9856649",
"R-HSA-1234158",
"R-HSA-1368108",
"R-... | [
"EC:2.3.1.48",
"PROSITEDOC:PDOC50134",
"REACTOME:R-CEL-1234158",
"REACTOME:R-CEL-201722",
"REACTOME:R-CEL-3899300",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-5689901",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-8939243",
"REACTOME:R-CEL-8939246",
"REACTOME:R-CEL-8951936",
"REACTOME:R-CEL-961762... | 132 | [
"1f81",
"1l3e",
"1l8c",
"1p4q",
"1r8u",
"1u2n",
"2k8f",
"2ka4",
"2ka6",
"2kje",
"2lww",
"2mh0",
"2mzd",
"3io2",
"3p57",
"3t92",
"5hou",
"5hp0",
"5hpd",
"6fgn",
"6fgs",
"7lvs",
"7qgs",
"7xez",
"7xfg",
"8e1d",
"8hag",
"8hah",
"8hai",
"8haj",
"8hak",
"8hal"... | 34 | [
"PUB00005449",
"PUB00014077",
"PUB00020590",
"PUB00020592",
"PUB00026905",
"PUB00029716",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00037826",
"PUB00082643"
] | [
"8848831",
"12665246",
"11023789",
"14594809",
"11959990",
"12778114",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"15641773",
"19054356"
] | [
"ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins.",
"Zinc fingers--folds for many occasions.",
"Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP.",
"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: reg... | [
1996,
2002,
2000,
2004,
2002,
2003,
2007,
2005,
2005,
1999,
2001,
2005,
2009
] | 13 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"White spot syndrome virus",
"viral metagenome"
] | [
11861,
10,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
59,
9,
62,
4,
17,
7,
16,
10,
58
] | 9 | true | Domain | Zinc finger, TAZ-type | Zinc finger, TAZ-type | Znf_TAZ | 9 |
IPR000198 | 198 | Rho GTPase-activating protein domain | RhoGAP_dom | Domain | 150,062 | false | false | Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form. The active conformat... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00620",
"PS50238",
"SM00324"
] | [
"RhoGAP",
"RHOGAP",
"RhoGAP"
] | [
147564,
148881,
141595
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GenProp1229",
"GenProp1395",
"GenProp1509",
"GenProp1605",
"PDOC50238",
"R-BTA-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-1266695",
"R-BTA-1433557",
"R-BTA-1660499",
"R-BTA-180292",
"R-BTA-186763",
"R-BTA-193648",
"R-BTA-1963642",
"R-BTA-1982... | [
"GP:GenProp1229",
"GP:GenProp1395",
"GP:GenProp1509",
"GP:GenProp1605",
"PROSITEDOC:PDOC50238",
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1... | 412 | [
"1am4",
"1f7c",
"1grn",
"1ow3",
"1pbw",
"1rgp",
"1tx4",
"1xa6",
"2ee4",
"2ee5",
"2mbg",
"2ngr",
"2osa",
"2ovj",
"2qv2",
"2xs6",
"3byi",
"3cxl",
"3eap",
"3fk2",
"3iug",
"3kuq",
"3msx",
"3qis",
"3w6r",
"3wpq",
"3wps",
"5c2j",
"5c2k",
"5c5s",
"5hpy",
"5irc"... | 66 | [
"PUB00004251",
"PUB00004258",
"PUB00004880"
] | [
"9009196",
"9262406",
"8962058"
] | [
"The structure of the GTPase-activating domain from p50rhoGAP.",
"Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.",
"Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit."
] | [
1997,
1997,
1996
] | 3 | [] | [
"IPR028557",
"IPR037858",
"IPR037860",
"IPR041852",
"IPR046990",
"IPR047078",
"IPR047886",
"IPR047941",
"IPR049592",
"IPR061285"
] | 0 | 10 | 0 | [
"Bacteria",
"Eukaryota",
"Klebsiella phage vB_Kpn_K42PH8",
"Methanobacteriati",
"metagenomes"
] | [
370,
149674,
1,
5,
12
] | 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,
59,
642,
84,
381,
232,
14,
43,
366,
11,
10,
177
] | 12 | true | Domain | Rho GTPase-activating protein domain | Rho GTPase-activating protein domain | RhoGAP_dom | 8 |
IPR000199 | 199 | Peptidase C3A/C3B, picornaviral | Peptidase_C3A/C3B_picornavir | Domain | 12,371 | false | false | Viruses in the order Picornavirales infect different vertebrate, invertebrate, and plant hosts and are responsible for a variety of human, animal, and plant diseases. These viruses have a single-stranded, positive sense RNA genome that generally translates a large precursor polyprotein which is proteolytically cleaved ... | [
"GO:0004197",
"GO:0006508"
] | [
"cysteine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00548"
] | [
"Peptidase_C3"
] | [
12371
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.22",
"3.4.22.28",
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:2.7.7.48",
"EC:3.4.22",
"EC:3.4.22.28",
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 9 | [
"1cqq",
"1l1n",
"2b0f",
"2bhg",
"2ijd",
"2in2",
"2j92",
"2vb0",
"2wv4",
"2wv5",
"2xya",
"2ztx",
"2zty",
"2ztz",
"2zu1",
"2zu3",
"3osy",
"3q3x",
"3q3y",
"3qzq",
"3qzr",
"3r0f",
"3ruo",
"3sj8",
"3sj9",
"3sji",
"3sjk",
"3sjo",
"3zv8",
"3zv9",
"3zva",
"3zvb"... | 212 | [
"PUB00032759",
"PUB00050441",
"PUB00056357",
"PUB00056400",
"PUB00094816",
"PUB00094817"
] | [
"15654079",
"19144641",
"21835784",
"21795339",
"18293057",
"22534091"
] | [
"Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity.",
"Structural basis of inhibition specificities of 3C and 3C-like proteases by zinc-coordinating and peptidomimetic compounds.",
"Structural basis for antiviral inhibition of the main ... | [
2005,
2009,
2011,
2011,
2008,
2012
] | 6 | [
"IPR044067"
] | [] | 1 | 0 | 1 | [
"Bilateria",
"Viruses"
] | [
26,
12345
] | 2 | [] | [] | 0 | true | Domain | Peptidase C3A/C3B, picornaviral | Peptidase C3A/C3B, picornaviral | Peptidase_C3A/C3B_picornavir | 2 |
IPR000200 | 200 | Peptidase C10, streptopain | Peptidase_C10 | Family | 1,514 | false | false | This group of cysteine peptidases belong to MEROPS peptidase family C10 (streptopain family, clan CA). Streptopain is a cysteine protease found in Streptococcus pyogenes that shows some structural and functional similarity to papain (family C1) [ , ]. The order of the catalytic cysteine/histidine dyad is the same and t... | [
"GO:0008234",
"GO:0006508"
] | [
"cysteine-type peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF01640",
"PR00797"
] | [
"Peptidase_C10",
"STREPTOPAIN"
] | [
1514,
1024
] | 2 | [
"EC"
] | [
"3.4.22.10"
] | [
"EC:3.4.22.10"
] | 1 | [
"1dki",
"1pvj",
"2jtc",
"2uzj",
"3bb7",
"3bba",
"4d8b",
"4d8e",
"4d8i",
"4rkx",
"6ukd",
"6uqd"
] | 12 | [
"PUB00000271",
"PUB00002375",
"PUB00003577",
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00076953"
] | [
"4683008",
"1270417",
"7845226",
"11517925",
"9891971",
"14725770",
"7044372"
] | [
"On the mechanism of action of streptococcal proteinase. II. Comparison of the kinetics of proteinase- and papain-catalyzed hydrolysis of N-acylamino acid esters.",
"Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain.",
... | [
1973,
1976,
1994,
2001,
1998,
2004,
1982
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Sphagnum jensenii",
"unclassified sequences"
] | [
1460,
1,
53
] | 3 | [] | [] | 0 | true | Family | Peptidase C10, streptopain | Peptidase C10, streptopain | Peptidase_C10 | 5 |
IPR000201 | 201 | Hepadnaviral P protein, N-terminal | DNApol_viral_N | Domain | 13,417 | false | false | This domain is at the N terminus of hepadnavirus P proteins and covers the so-called terminal protein and the spacer region of the protein. This domain is always associated with and . | [
"GO:0003677",
"GO:0003887",
"GO:0006260"
] | [
"DNA binding",
"DNA-directed DNA polymerase activity",
"DNA replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00242"
] | [
"DNA_pol_viral_N"
] | [
13417
] | 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 | [
"Revtraviricetes"
] | [
13417
] | 1 | [] | [] | 0 | true | Domain | Hepadnaviral P protein, N-terminal | Hepadnaviral P protein, N-terminal | DNApol_viral_N | 2 |
IPR000202 | 202 | GPCR, family 3, metabotropic glutamate receptor 5 | GPCR_3_mGluR5 | Family | 1,922 | false | false | The mRNA for GRM5 is widespread in the brain, with a unique distribution; it is found in high levels in the striatum, cerebral cortex, hippocampus and olfactory bulb. GRM5 activates the phosphoinositide pathway. It plays an important role in the regulation of synaptic plasticity and the modulation of the neural network... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01055"
] | [
"MTABOTROPC5R"
] | [
1922
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"293",
"R-HSA-416476",
"R-HSA-420499",
"R-HSA-6794361",
"R-MMU-416476",
"R-MMU-420499",
"R-MMU-6794361",
"R-RNO-416476",
"R-RNO-420499",
"R-RNO-6794361"
] | [
"IUPHAR:293",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-420499",
"REACTOME:R-HSA-6794361",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-420499",
"REACTOME:R-MMU-6794361",
"REACTOME:R-RNO-416476",
"REACTOME:R-RNO-420499",
"REACTOME:R-RNO-6794361"
] | 10 | [
"3lmk",
"6n4x",
"6n4y",
"6n50",
"6n51",
"6n52",
"7fd8",
"7fd9",
"8t6j",
"8t7h",
"8t8m",
"8tao",
"8x0b",
"8x0c",
"8x0d",
"8x0e",
"8x0f",
"8x0g",
"8x0h"
] | 19 | [
"PUB00002720",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816",
"PUB00100441",
"PUB00100442",
"PUB00100443",
"PUB001004... | [
"1320017",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293",
"20055706",
"7908515",
"25042998",
"34469715"
] | [
"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,
2010,
1994,
2014,
2021
] | 19 | [
"IPR000162"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
1922
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
8,
6,
5
] | 4 | true | Family | GPCR, family 3, metabotropic glutamate receptor 5 | GPCR, family 3, metabotropic glutamate receptor 5 | GPCR_3_mGluR5 | 9 |
IPR000203 | 203 | GPS motif | GPS | Conserved_site | 49,037 | false | false | The GPS motif is an integral part, and the most conserved region, of a much larger (320-residue approximately) domain that has been termed GPCR-Autoproteolysis INducing (GAIN) domain. The GAIN domain represents an autoproteolytic fold whose function is relevant for GPCR signalling and may regulate this process [ , ]. T... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01825",
"SM00303"
] | [
"GPS",
"GPS"
] | [
46026,
46180
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50221",
"R-DME-350368",
"R-DME-350376",
"R-DME-350379",
"R-DME-350411",
"R-DME-350480",
"R-DME-373080",
"R-DME-450728",
"R-DME-6798695",
"R-DRE-9619665",
"R-HSA-373080",
"R-HSA-5620916",
"R-HSA-5683826",
"R-HSA-6798695",
"R-HSA-9619665",
"R-MMU-373080",
"R-MMU-5620916",
"R-MMU... | [
"PROSITEDOC:PDOC50221",
"REACTOME:R-DME-350368",
"REACTOME:R-DME-350376",
"REACTOME:R-DME-350379",
"REACTOME:R-DME-350411",
"REACTOME:R-DME-350480",
"REACTOME:R-DME-373080",
"REACTOME:R-DME-450728",
"REACTOME:R-DME-6798695",
"REACTOME:R-DRE-9619665",
"REACTOME:R-HSA-373080",
"REACTOME:R-HSA-56... | 22 | [
"4dlo",
"4dlq",
"5kvm",
"6v55",
"6vhh",
"7d76",
"7d77",
"7qu8",
"7wu3",
"7wu4",
"7wu5",
"7wui",
"7wxu",
"7wxw",
"7wy0",
"7wy5",
"7wy8",
"7wyb",
"7wz7",
"7x10",
"7x2v",
"7xke",
"7yp7",
"8hc0",
"8ikj",
"8jmt",
"8oek",
"8vti",
"8vy2",
"8x9s",
"8x9t",
"8x9u"... | 36 | [
"PUB00005835",
"PUB00008017",
"PUB00018218",
"PUB00058430",
"PUB00100163",
"PUB00101119"
] | [
"9830014",
"10469603",
"10026162",
"22333914",
"23850273",
"22938866"
] | [
"alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis.",
"A latrophilin/CL-1-like GPS domain in polycystin-1.",
"A novel ubiquitously expressed alpha-latrotoxin receptor is a member of the... | [
1998,
1999,
1999,
2012,
2013,
2012
] | 6 | [] | [] | 0 | 0 | null | [
"Candidatus Giovannonibacteria bacterium RIFCSPHIGHO2_01_FULL_45_23",
"Eukaryota",
"organismal metagenomes"
] | [
1,
49027,
9
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
481,
14,
151,
107,
172
] | 6 | true | Conserved_site | GPS motif | GPS motif | GPS | 6 |
IPR000204 | 204 | Orexin receptor family | Orexin_rcpt | Family | 1,141 | false | false | The neuropeptide hormone orexin stimulates appetite and food consumption [ ], and is found in the hypothalamus, which has been shown to be the 'feeding centre' and plays a central role in the integrated control of feeding and energy homeostasis [ ]. It also has a prominent role in promoting wakefulness [ , , ]. The ore... | [
"GO:0016499",
"GO:0007186",
"GO:0007631",
"GO:0016020"
] | [
"orexin receptor activity",
"G protein-coupled receptor signaling pathway",
"feeding behavior",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01064"
] | [
"OREXINR"
] | [
1141
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-389397",
"R-BTA-416476",
"R-CFA-389397",
"R-CFA-416476",
"R-HSA-389397",
"R-HSA-416476",
"R-MMU-389397",
"R-MMU-416476",
"R-RNO-389397",
"R-RNO-416476",
"R-SSC-389397",
"R-SSC-416476"
] | [
"REACTOME:R-BTA-389397",
"REACTOME:R-BTA-416476",
"REACTOME:R-CFA-389397",
"REACTOME:R-CFA-416476",
"REACTOME:R-HSA-389397",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-389397",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-389397",
"REACTOME:R-RNO-416476",
"REACTOME:R-SSC-389397",
"REACTOME:R-SSC-416... | 12 | [
"4s0v",
"4zj8",
"4zjc",
"5wqc",
"5ws3",
"6to7",
"6tod",
"6tos",
"6tot",
"6tp3",
"6tp4",
"6tp6",
"6tpg",
"6tpj",
"6tpn",
"6tq4",
"6tq6",
"6tq7",
"6tq9",
"6v9s",
"7l1u",
"7l1v",
"7sqo",
"7sr8",
"7xrr"
] | 25 | [
"PUB00000959",
"PUB00004488",
"PUB00063338",
"PUB00063339",
"PUB00063340",
"PUB00063342"
] | [
"9491897",
"9656726",
"10458611",
"10615891",
"10481909",
"16507882"
] | [
"Orexins and orexin receptors: a family of hypothalamic neuropeptides and G protein-coupled receptors that regulate feeding behavior.",
"Orexins: a newly discovered family of hypothalamic regulators of food intake.",
"The sleep disorder canine narcolepsy is caused by a mutation in the hypocretin (orexin) recept... | [
1998,
1998,
1999,
2000,
1999,
2006
] | 6 | [
"IPR000276"
] | [
"IPR004059",
"IPR004060"
] | 1 | 2 | 0 | [
"Bilateria"
] | [
1141
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
8,
5,
7
] | 4 | true | Family | Orexin receptor family | Orexin receptor family | Orexin_rcpt | 1 |
IPR000206 | 206 | Large ribosomal subunit protein bL12 | Ribosomal_bL12 | Family | 32,202 | false | false | This family represents the large ribosomal subunit protein bL12, formerly known as L7/L12 in E. coli (L7 and L12 are identical except that L7 is acetylated at the N terminus) [ ]. This protein is present in each 50S subunit in four copies organised as two dimers. The L8 protein complex consisting of two dimers of bL12 ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00368",
"PTHR45987",
"TIGR00855",
"cd00387"
] | [
"Ribosomal_bL12",
"",
"L12",
"Ribosomal_L7_L12"
] | [
29020,
31867,
26306,
30119
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9837999",
"R-BTA-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9837999",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9837999",
"R-MMU-9937383",
"R-SCE-9837999",
"R-SPO-9837999"
] | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOM... | 15 | [
"1ctf",
"1dd3",
"1dd4",
"1rqs",
"1rqu",
"1rqv",
"2bcw",
"2ftc",
"2zjq",
"3j7z",
"3j9y",
"4v42",
"4v4p",
"4v4v",
"4v4w",
"4v5m",
"4v5n",
"4v6f",
"4v7b",
"4v7d",
"4v85",
"4v89",
"4v9j",
"4v9k",
"4v9l",
"4v9m",
"4v9o",
"4w29",
"5kcs",
"6gaw",
"6gb2",
"6gsl"... | 109 | [
"PUB00003217",
"PUB00006172",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00010619",
"PUB00016781",
"PUB00025269",
"PUB00037548",
"PUB00038823",
"PUB00039608",
"PUB00045897",
"PUB00079605",
"PUB00079606",
"PUB00079607",
"PUB00079608",
"PUB00079609",
"PUB00079610",
"PUB000796... | [
"3309338",
"10488095",
"11297922",
"11290319",
"11114498",
"11231892",
"9175862",
"11283358",
"14960595",
"15989950",
"16337596",
"17599351",
"17574829",
"12370014",
"12867082",
"16292341",
"17932030",
"17889453",
"12369843",
"12705832",
"348499",
"24524803"
] | [
"Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A.",
"Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding.",
"Atomic structures at last: the ribosome in 2000.... | [
1987,
1999,
2001,
2001,
2000,
2001,
1997,
2001,
2004,
2005,
2005,
2007,
2007,
2002,
2003,
2005,
2007,
2007,
2002,
2003,
1978,
2014
] | 22 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
23817,
7939,
2,
443,
1
] | 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",... | [
32,
1,
2,
2,
1,
3,
1,
1,
16,
2,
1,
1,
26
] | 13 | true | Family | Large ribosomal subunit protein bL12 | Large ribosomal subunit protein bL12 | Ribosomal_bL12 | 2 |
IPR000207 | 207 | Alpha 2B adrenoceptor | ADRA2B_rcpt | Family | 804 | false | false | The adrenoceptors (or adrenergic receptors) are rhodopsin-like G protein-coupled receptors that are targets of the catecholamines, especially norepinephrine (noradrenaline) and epinephrine (adrenaline). Many cells possess these receptors, and the binding of a catecholamine to the receptor will generally stimulate the s... | [
"GO:0004938",
"GO:0006940",
"GO:0007186",
"GO:0019229",
"GO:0030168",
"GO:0016020"
] | [
"alpha2-adrenergic receptor activity",
"regulation of smooth muscle contraction",
"G protein-coupled receptor signaling pathway",
"regulation of vasoconstriction",
"platelet activation",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PRINTS"
] | [
"PR00559"
] | [
"ADRENRGCA2BR"
] | [
804
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"26",
"R-HSA-390696",
"R-HSA-392023",
"R-HSA-418594",
"R-HSA-418597",
"R-MMU-390696",
"R-MMU-392023",
"R-MMU-418594",
"R-MMU-418597",
"R-RNO-390696",
"R-RNO-392023",
"R-RNO-418594",
"R-RNO-418597"
] | [
"IUPHAR:26",
"REACTOME:R-HSA-390696",
"REACTOME:R-HSA-392023",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-418597",
"REACTOME:R-MMU-390696",
"REACTOME:R-MMU-392023",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-418597",
"REACTOME:R-RNO-390696",
"REACTOME:R-RNO-392023",
"REACTOME:R-RNO-418594",
"REA... | 13 | [] | 0 | [
"PUB00066376",
"PUB00066377",
"PUB00066395",
"PUB00066396",
"PUB00066462",
"PUB00066463",
"PUB00066464",
"PUB00066465",
"PUB00066466",
"PUB00066467",
"PUB00066468",
"PUB00066471",
"PUB00066990"
] | [
"18882199",
"2855960",
"2887122",
"9280371",
"9605427",
"9760042",
"9824686",
"8670422",
"15684247",
"2574568",
"10215710",
"7812219",
"19912818"
] | [
"A study of the adrenotropic receptors.",
"Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.",
"Coronary vasoconstriction mediated by alpha 1- and alpha 2-adrenoceptors in conscious dogs.",
"Alpha-adrenoceptors in equine digital veins: evidence for the presence of ... | [
1948,
1988,
1987,
1997,
1998,
1998,
1998,
1996,
2004,
1989,
1999,
1994,
1991
] | 13 | [
"IPR002233"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
804
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2
] | 3 | true | Family | Alpha 2B adrenoceptor | Alpha 2B adrenoceptor | ADRA2B_rcpt | 3 |
IPR000208 | 208 | RNA-directed RNA polymerase, fingers/palm subdomains, flavivirus | Flavi_RdRp_fingers/palm | Domain | 13,510 | false | false | Flaviviruses produce a polyprotein from the ssRNA genome. The polyprotein is cleaved to a number of products one of which is NS5. Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity. NS5 is the largest mature viral protein and contains a N-terminal me... | [
"GO:0003968",
"GO:0005524"
] | [
"RNA-directed RNA polymerase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00972"
] | [
"Flavi_NS5"
] | [
13510
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.56",
"2.1.1.57",
"2.7.7.48",
"3.4.21.91",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"PWY-7375",
"PWY-7379"
] | [
"EC:2.1.1.56",
"EC:2.1.1.57",
"EC:2.7.7.48",
"EC:3.4.21.91",
"EC:3.6.1.15",
"EC:3.6.4.13",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"METACYC:PWY-7375",
"METACYC:PWY-7379"
] | 13 | [
"1l9k",
"1r6a",
"2hcn",
"2hcs",
"2hfz",
"2j7u",
"2j7w",
"2p1d",
"2p3l",
"2p3o",
"2p3q",
"2p40",
"2p41",
"3lkz",
"3vws",
"4c11",
"4hdg",
"4hdh",
"4hhj",
"4k6m",
"4mtp",
"4v0q",
"4v0r",
"5ccv",
"5dto",
"5f3t",
"5f3z",
"5f41",
"5hmw",
"5hmx",
"5hmy",
"5hmz"... | 147 | [
"PUB00005614",
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625",
"PUB00095857",
"PUB00098521",
"PUB00103480"
] | [
"8607261",
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187",
"28345656",
"32313955",
"30951555"
] | [
"Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity.",
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependen... | [
1996,
1998,
1997,
1989,
1996,
2001,
2000,
2017,
2020,
2019
] | 10 | [] | [] | 0 | 0 | null | [
"Ecdysozoa",
"Viruses"
] | [
14,
13496
] | 2 | [] | [] | 0 | true | Domain | RNA-directed RNA polymerase, fingers/palm subdomains, flavivirus | RNA-directed RNA polymerase, fingers/palm subdomains, flavivirus | Flavi_RdRp_fingers/palm | 5 |
IPR000209 | 209 | Peptidase S8/S53 domain | Peptidase_S8/S53_dom | Domain | 185,612 | false | false | These proteins contain a domain found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin) and S53 (sedolisin), both of which are members of clan SB [ ]. The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subt... | [
"GO:0008236",
"GO:0006508"
] | [
"serine-type peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00082"
] | [
"Peptidase_S8"
] | [
185612
] | 1 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"3.4.21",
"3.4.21.-",
"PWY-7884",
"PDOC00125",
"R-CEL-1592389",
"R-CEL-186797",
"R-CEL-2173789",
"R-CEL-2173796",
"R-CEL-983168",
"R-DDI-1369007",
"R-DDI-159418",
"R-DDI-193368",
"R-DDI-382556",
"R-DDI-9754706",
"R-DDI-9757110",
"R-DME-1592389",
"R-DME-186797",
"R-DME-2173789",
"... | [
"EC:3.4.21",
"EC:3.4.21.-",
"METACYC:PWY-7884",
"PROSITEDOC:PDOC00125",
"REACTOME:R-CEL-1592389",
"REACTOME:R-CEL-186797",
"REACTOME:R-CEL-2173789",
"REACTOME:R-CEL-2173796",
"REACTOME:R-CEL-983168",
"REACTOME:R-DDI-1369007",
"REACTOME:R-DDI-159418",
"REACTOME:R-DDI-193368",
"REACTOME:R-DDI-... | 110 | [
"1a2q",
"1af4",
"1ah2",
"1ak9",
"1aqn",
"1au9",
"1av7",
"1avt",
"1be6",
"1be8",
"1bfk",
"1bfu",
"1bh6",
"1bjr",
"1c3l",
"1c9j",
"1c9m",
"1c9n",
"1cnm",
"1cse",
"1dbi",
"1dui",
"1ea7",
"1egq",
"1ga1",
"1ga4",
"1ga6",
"1gci",
"1gns",
"1gnv",
"1gt9",
"1gtg"... | 647 | [
"PUB00000522",
"PUB00003576",
"PUB00006225",
"PUB00011905",
"PUB00101920"
] | [
"8439290",
"7845208",
"9070434",
"12673349",
"24367091"
] | [
"Evolutionary families of peptidases.",
"Families of serine peptidases.",
"Subtilases: the superfamily of subtilisin-like serine proteases.",
"Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.",
"Neisseria meningitidis NalP cleaves human complement C3, facilitating d... | [
1993,
1994,
1997,
2003,
2014
] | 5 | [] | [
"IPR030400",
"IPR033857",
"IPR034041",
"IPR034045",
"IPR034051",
"IPR034054",
"IPR034056",
"IPR034058",
"IPR034061",
"IPR034063",
"IPR034065",
"IPR034067",
"IPR034073",
"IPR034074",
"IPR034075",
"IPR034080",
"IPR034084",
"IPR034176",
"IPR034182",
"IPR034185",
"IPR034187",
"... | 0 | 28 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid pAD1",
"Viruses",
"unclassified sequences"
] | [
2361,
91223,
90660,
1,
114,
1253
] | 6 | [
"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... | [
265,
5,
30,
13,
61,
41,
11,
194,
42,
4,
4,
291
] | 12 | true | Domain | Peptidase S8/S53 domain | Peptidase S8/S53 domain | Peptidase_S8/S53_dom | 9 |
IPR000210 | 210 | BTB/POZ domain | BTB/POZ_dom | Domain | 348,814 | false | false | The BTB domain (Broad-Complex, Tramtrack and Bric a brac) is also known as the POZ domain (POxvirus and Zinc finger). It is a homodimerisation domain occurring at the N terminus of proteins containing multiple copies of either zinc fingers of the C2H2 type or Kelch repeats [ , ]. Many BTB proteins are transcriptional r... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00651",
"PS50097",
"SM00225"
] | [
"BTB",
"BTB",
"BTB"
] | [
275440,
285767,
294333
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50097",
"R-BTA-114608",
"R-BTA-1296072",
"R-BTA-5576894",
"R-BTA-5632684",
"R-BTA-8951664",
"R-BTA-983168",
"R-CEL-5632684",
"R-CEL-8951664",
"R-CEL-9706019",
"R-CEL-983168",
"R-DDI-114608",
"R-DDI-8951664",
"R-DDI-983168",
"R-DME-1296072",
"R-DME-210671",
"R-DME-216167",
"R-D... | [
"PROSITEDOC:PDOC50097",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1296072",
"REACTOME:R-BTA-5576894",
"REACTOME:R-BTA-5632684",
"REACTOME:R-BTA-8951664",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-5632684",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-9706019",
"REACTOME:R-CEL-983168",
"REACTOME:R-D... | 128 | [
"1a68",
"1buo",
"1cs3",
"1dsx",
"1eod",
"1eoe",
"1eof",
"1exb",
"1nn7",
"1qdv",
"1qdw",
"1r28",
"1r29",
"1r2b",
"1s1g",
"1t1d",
"2a79",
"2i2r",
"2if5",
"2ihc",
"2nn2",
"2nz0",
"2ppi",
"2q81",
"2r9r",
"2vkp",
"2vpk",
"2yy9",
"2z8h",
"3b84",
"3bim",
"3drx"... | 481 | [
"PUB00001918",
"PUB00004829",
"PUB00004917"
] | [
"7958847",
"7938017",
"9770450"
] | [
"The POZ domain: a conserved protein-protein interaction motif.",
"The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila.",
"Crystal structure of the BTB domain from PLZF."
] | [
1994,
1994,
1998
] | 3 | [] | [
"IPR003131",
"IPR028764",
"IPR029851",
"IPR030104",
"IPR030404",
"IPR030562",
"IPR030563",
"IPR030565",
"IPR030566",
"IPR030570",
"IPR030571",
"IPR030577",
"IPR030584",
"IPR030586",
"IPR030588",
"IPR030589",
"IPR030596",
"IPR030597",
"IPR030599",
"IPR030601",
"IPR030603",
"... | 0 | 41 | 0 | [
"Bacteria",
"Eukaryota",
"Sulfolobus acidocaldarius",
"Viruses",
"metagenomes"
] | [
208,
347412,
4,
1158,
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... | [
346,
172,
579,
225,
554,
516,
12,
400,
579,
3,
3,
352
] | 12 | true | Domain | BTB/POZ domain | BTB/POZ domain | BTB/POZ_dom | 3 |
IPR000211 | 211 | Geminivirus BL1 movement protein | Gemini_BL | Family | 1,764 | false | false | The movement of bipartite Geminiviruses such as squash leaf curl virus (SqLCV) requires the cooperative interaction of two essential virus-encoded movement proteins, BR1 and BL1. Recent studies of SqLCV and bean dwarf mosaic virus have shown that BR1 and BL1 act in a cooperative manner to move the viral genome intracel... | [
"GO:0003677",
"GO:0046740",
"GO:0033644"
] | [
"DNA binding",
"transport of virus in host, cell to cell",
"host cell membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00845"
] | [
"Gemini_BL1"
] | [
1764
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009554"
] | [
"9765472"
] | [
"The bipartite geminivirus coat protein aids BR1 function in viral movement by affecting the accumulation of viral single-stranded DNA."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Mesangiospermae",
"Viruses"
] | [
82,
1682
] | 2 | [] | [] | 0 | true | Family | Geminivirus BL1 movement protein | Geminivirus BL1 movement protein | Gemini_BL | 1 |
IPR000213 | 213 | Vitamin D-binding protein | VitD-bd | Family | 755 | false | false | A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [ , , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs - its main function ... | [
"GO:0005499",
"GO:0090482",
"GO:0051180",
"GO:0005615"
] | [
"vitamin D binding",
"vitamin transmembrane transporter activity",
"vitamin transport",
"extracellular space"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00804"
] | [
"VITAMNDBNDNG"
] | [
755
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196791",
"R-MMU-196791",
"R-RNO-196791"
] | [
"REACTOME:R-HSA-196791",
"REACTOME:R-MMU-196791",
"REACTOME:R-RNO-196791"
] | 3 | [
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9"
] | 6 | [
"PUB00000582",
"PUB00002430",
"PUB00002857",
"PUB00003407"
] | [
"2423133",
"2419332",
"7517938",
"2481749"
] | [
"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.",
"Rat vitamin D binding protein. Determination of the full-length primary structure from cloned cDNA.",
"Afamin is a new member of t... | [
1986,
1986,
1994,
1989
] | 4 | [
"IPR000264"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
755
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
6
] | 4 | true | Family | Vitamin D-binding protein | Vitamin D-binding protein | VitD-bd | 7 |
IPR000215 | 215 | Serpin family | Serpin_fam | Family | 54,588 | false | false | Protein protease inhibitors constitute a very important mechanism for regulating proteolytic activity. Serpins (SERine Proteinase INhibitors) belong to MEROPS inhibitor family I4, clan ID. Most serpin family members are indeed serine protease inhibitors, but several have additional cross-class inhibition functions and ... | [
"GO:0004867",
"GO:0005615"
] | [
"serine-type endopeptidase inhibitor activity",
"extracellular space"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR11461"
] | [
""
] | [
54588
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00256",
"R-BTA-114608",
"R-BTA-1650814",
"R-BTA-194002",
"R-BTA-2022377",
"R-BTA-204005",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-416476",
"R-BTA-418594",
"R-BTA-5694530",
"R-BTA-6798695",
"R-BTA-75205",
"R-BTA-8957275",
"R-BTA-9757110",
"R-DME-114608",
"R-DME-140837",
"R-DME-1... | [
"PROSITEDOC:PDOC00256",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-194002",
"REACTOME:R-BTA-2022377",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-5694530",
"REACTOME:R-BTA-6... | 105 | [
"1a7c",
"1ant",
"1as4",
"1ath",
"1att",
"1atu",
"1azx",
"1b3k",
"1br8",
"1by7",
"1c5g",
"1c8o",
"1d5s",
"1db2",
"1dvm",
"1dvn",
"1dzg",
"1dzh",
"1e03",
"1e04",
"1e05",
"1ezx",
"1f0c",
"1hle",
"1hp7",
"1imv",
"1iz2",
"1jjo",
"1jmj",
"1jmo",
"1jrr",
"1jti"... | 281 | [
"PUB00001649",
"PUB00002863",
"PUB00011889",
"PUB00014154",
"PUB00067344",
"PUB00067346",
"PUB00067347",
"PUB00067348",
"PUB00067349",
"PUB00067350",
"PUB00097183"
] | [
"8417965",
"8034697",
"12824063",
"12411597",
"18539447",
"11435447",
"12475206",
"15638455",
"7851535",
"21781239",
"25525260"
] | [
"The ovalbumin family of serpin proteins.",
"Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition.",
"Serpins: structure, function and molecular evolution.",
"Serpins in prokaryotes.",
"A serpin in the cellulosome of the anaerobic fungus Pi... | [
1993,
1994,
2003,
2002,
2008,
2001,
2002,
2004,
1995,
2011,
2015
] | 11 | [] | [
"IPR000227",
"IPR000240"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
243,
3816,
49887,
523,
119
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
74,
11,
62,
81,
206,
174,
53,
158,
17
] | 9 | true | Family | Serpin family | Serpin family | Serpin_fam | 4 |
IPR000217 | 217 | Tubulin | Tubulin | Family | 94,365 | false | false | Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [ , ]. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta... | [
"GO:0007017",
"GO:0005874"
] | [
"microtubule-based process",
"microtubule"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR01161",
"PTHR11588"
] | [
"TUBULIN",
""
] | [
87586,
74528
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00199",
"R-BTA-114608",
"R-BTA-190840",
"R-BTA-2132295",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-2565942",
"R-BTA-3371497",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-5610787",
"R-BTA-5617833",
"R-BTA-5620912",
"R-BTA-5620924",
"R-BTA-5626467",
"R-... | [
"PROSITEDOC:PDOC00199",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-190840",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
"REACTOME:R-BTA... | 234 | [
"1ffx",
"1ia0",
"1jff",
"1sa0",
"1sa1",
"1tub",
"1tvk",
"1z2b",
"1z5v",
"1z5w",
"2bto",
"2btq",
"2hxf",
"2hxh",
"2p4n",
"2wbe",
"2xrp",
"3cb2",
"3dco",
"3du7",
"3e22",
"3edl",
"3hkb",
"3hkc",
"3hkd",
"3hke",
"3iz0",
"3j1t",
"3j1u",
"3j2u",
"3j6e",
"3j6f"... | 784 | [
"PUB00000039",
"PUB00000721",
"PUB00000978",
"PUB00002443",
"PUB00006112",
"PUB00039756",
"PUB00072957",
"PUB00072959",
"PUB00099927"
] | [
"3896122",
"8274140",
"2194680",
"3680207",
"8102497",
"15967998",
"12486237",
"25169981",
"26234217"
] | [
"Molecular biology and genetics of tubulin.",
"Gamma-tubulin: the hub of cellular microtubule assemblies.",
"Diversity among tubulin subunits: toward what functional end?",
"Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate.",
"Localization of an exchangeable GT... | [
1985,
1993,
1990,
1987,
1993,
2005,
2002,
2014,
2015
] | 9 | [] | [
"IPR002452",
"IPR002453",
"IPR002454",
"IPR002967",
"IPR004057",
"IPR004058"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
25,
52,
94286,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
45,
20,
37,
31,
144,
50,
4,
40,
79,
4,
4,
212
] | 12 | true | Family | Tubulin | Tubulin | Tubulin | 4 |
IPR000218 | 218 | Large ribosomal subunit protein uL14 | Ribosomal_uL14 | Family | 49,572 | false | false | This entry represents the large ribosomal subunit protein uL14 (formerly known as L14) from all domains of life. In eubacteria, uL14 is known to bind directly to the 23S rRNA. It belongs to a family of ribosomal proteins, which have been grouped on the basis of sequence similarities. Based on amino-acid sequence homolo... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"SMART"
] | [
"MF_01367",
"PF00238",
"PTHR11761",
"SM01374"
] | [
"Ribosomal_uL14",
"Ribosomal_L14",
"",
"Ribosomal_L14"
] | [
47881,
49476,
47375,
49239
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00048",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"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",... | [
"PROSITEDOC:PDOC00048",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 89 | [
"1c04",
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 1,944 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00015240"
] | [
"11297922",
"11290319",
"11114498",
"15299380"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Crystallization and preliminary X-ray diffraction studies of bacterial ribosomal protein L14."
] | [
2001,
2001,
2000,
1994
] | 4 | [] | [
"IPR005745",
"IPR019971"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
909,
23235,
24942,
486
] | 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",... | [
19,
2,
3,
3,
1,
15,
3,
2,
15,
13,
3,
3,
34
] | 13 | true | Family | Large ribosomal subunit protein uL14 | Large ribosomal subunit protein uL14 | Ribosomal_uL14 | 3 |
IPR000219 | 219 | Dbl homology domain | DH_dom | Domain | 150,683 | false | false | The Rho family GTPases Rho, Rac and CDC42 regulate a diverse array of cellular processes. Like all members of the Ras superfamily, the Rho proteins cycle between active GTP-bound and inactive GDP-bound conformational states. Activation of Rho proteins through release of bound GDP and subsequent binding of GTP, is catal... | [
"GO:0005085"
] | [
"guanyl-nucleotide exchange factor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00621",
"PS50010",
"SM00325",
"cd00160"
] | [
"RhoGEF",
"DH_2",
"RhoGEF",
"RhoGEF"
] | [
147290,
150164,
139169,
124250
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00605",
"R-BTA-114604",
"R-BTA-1257604",
"R-BTA-1433557",
"R-BTA-193648",
"R-BTA-2029482",
"R-BTA-2871796",
"R-BTA-2871809",
"R-BTA-389359",
"R-BTA-416482",
"R-BTA-4420097",
"R-BTA-512988",
"R-BTA-5218920",
"R-BTA-6811558",
"R-BTA-8980692",
"R-BTA-9013106",
"R-BTA-9013148",
"R... | [
"PROSITEDOC:PDOC00605",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-193648",
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-2871796",
"REACTOME:R-BTA-2871809",
"REACTOME:R-BTA-389359",
"REACTOME:R-BTA-416482",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BT... | 390 | [
"1by1",
"1dbh",
"1f5x",
"1foe",
"1ki1",
"1kz7",
"1kzg",
"1lb1",
"1nty",
"1rj2",
"1txd",
"1x86",
"1xcg",
"1xd4",
"1xdv",
"2dfk",
"2dx1",
"2kr9",
"2nz8",
"2pz1",
"2rgn",
"2vrw",
"2z0q",
"3bji",
"3eo2",
"3gf9",
"3jv3",
"3jzy",
"3ksy",
"3ky9",
"3kz1",
"3mpx"... | 144 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sylvanvirus sp.",
"organismal metagenomes"
] | [
5,
91,
150584,
1,
2
] | 5 | [
"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... | [
65,
868,
137,
429,
265,
7,
378,
6,
8
] | 9 | true | Domain | Dbl homology domain | Dbl homology domain | DH_dom | 5 |
IPR000221 | 221 | Protamine P1 | Protamine_P1 | Family | 432 | false | false | Protamines are small, highly basic proteins, that substitute for histones in sperm chromatin during the haploid phase of spermatogenesis. They pack sperm DNA into a highly condensed, stable and inactive complex [ , ], creating a more hydrodynamic sperm head for efficient swimming and protects the DNA from UV radiation ... | [
"GO:0003677",
"GO:0007283",
"GO:0035092",
"GO:0000786",
"GO:0005634"
] | [
"DNA binding",
"spermatogenesis",
"sperm DNA condensation",
"nucleosome",
"nucleus"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"PFAM",
"PROSITE"
] | [
"PF00260",
"PS00048"
] | [
"Protamine_P1",
"PROTAMINE_P1"
] | [
202,
398
] | 2 | [
"PROSITEDOC",
"REACTOME"
] | [
"PDOC00047",
"R-HSA-9821993"
] | [
"PROSITEDOC:PDOC00047",
"REACTOME:R-HSA-9821993"
] | 2 | [] | 0 | [
"PUB00002517",
"PUB00075474",
"PUB00100028"
] | [
"2808336",
"17903313",
"32392345"
] | [
"Quail (Coturnix japonica) protamine, full-length cDNA sequence, and the function and evolution of vertebrate protamines.",
"The protamine family of sperm nuclear proteins.",
"Protamine loops DNA in multiple steps."
] | [
1989,
2007,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Psilogramma increta granulovirus"
] | [
431,
1
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
2
] | 3 | true | Family | Protamine P1 | Protamine P1 | Protamine_P1 | 8 |
IPR000222 | 222 | PPM-type phosphatase, divalent cation binding | PP2C_BS | Binding_site | 53,214 | false | false | Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg(2+)- or Mn(2+)-depen... | [
"GO:0043169"
] | [
"cation binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01032"
] | [
"PPM_1"
] | [
53214
] | 1 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.3",
"3.1.3.16",
"PDOC00792",
"R-BTA-1169408",
"R-BTA-204174",
"R-BTA-2173795",
"R-BTA-380972",
"R-BTA-70895",
"R-CEL-1169408",
"R-CEL-2173795",
"R-CEL-380972",
"R-HSA-1169408",
"R-HSA-1660661",
"R-HSA-204174",
"R-HSA-2173795",
"R-HSA-380972",
"R-HSA-70895",
"R-HSA-8878166",
... | [
"EC:3.1.3",
"EC:3.1.3.16",
"PROSITEDOC:PDOC00792",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-204174",
"REACTOME:R-BTA-2173795",
"REACTOME:R-BTA-380972",
"REACTOME:R-BTA-70895",
"REACTOME:R-CEL-1169408",
"REACTOME:R-CEL-2173795",
"REACTOME:R-CEL-380972",
"REACTOME:R-HSA-1169408",
"REACTOME:R-... | 33 | [
"1a6q",
"2i0o",
"2iq1",
"2p8e",
"2pnq",
"3fxj",
"3fxk",
"3fxl",
"3fxm",
"3fxo",
"3jrq",
"3kb3",
"3kdj",
"3mq3",
"3nmn",
"3nmt",
"3nmv",
"3qn1",
"3rt0",
"3ujg",
"3ujk",
"3ujl",
"3zvu",
"4da1",
"4ds8",
"4jnd",
"4la7",
"4lg5",
"4lga",
"4lgb",
"4n0g",
"4oic"... | 72 | [
"PUB00001297",
"PUB00056982",
"PUB00074808",
"PUB00074809"
] | [
"9003755",
"22115775",
"9869399",
"22668558"
] | [
"Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.",
"Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis.",
"Protein phosphatase 2C (PP2C) function in higher plants.",
"Function analysis of conserved amino acid residues in a Mn(2+... | [
1996,
2011,
1998,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nucleocytoviricota",
"metagenomes"
] | [
95,
53071,
33,
15
] | 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... | [
153,
8,
43,
26,
55,
33,
4,
114,
49,
5,
4,
278
] | 12 | true | Binding_site | PPM-type phosphatase, divalent cation binding | PPM-type phosphatase, divalent cation binding | PP2C_BS | 7 |
IPR000223 | 223 | Peptidase S26A, signal peptidase I | Pept_S26A_signal_pept_1 | Family | 57,263 | false | false | This group of serine peptidases belong to MEROPS peptidase family S26 (signal peptidase I family, clan SF), subfamily S26A. At least 3 eubacterial leader peptidases are known: murein prelipoprotein peptidase, which cleaves the leader peptide from a component of the bacterial outer membrane; type IV prepilin leader pept... | [
"GO:0008236",
"GO:0006508",
"GO:0016020"
] | [
"serine-type peptidase activity",
"proteolysis",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PR00727",
"PTHR43390",
"TIGR02227"
] | [
"LEADERPTASE",
"",
"sigpep_I_bact"
] | [
55125,
48378,
51073
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"3.4.21.89",
"PDOC00418",
"R-HSA-9760173"
] | [
"EC:3.4.21.89",
"PROSITEDOC:PDOC00418",
"REACTOME:R-HSA-9760173"
] | 3 | [
"1b12",
"1kn9",
"1t7d",
"3iiq",
"3s04",
"4k8w",
"4me8",
"4n31",
"4nv4",
"4wvg",
"4wvh",
"4wvi",
"4wvj",
"6b88"
] | 14 | [
"PUB00003576"
] | [
"7845208"
] | [
"Families of serine peptidases."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
9,
45978,
10488,
5,
783
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
2,
4,
5,
1,
7,
2,
2,
20,
10,
2,
2,
59
] | 13 | true | Family | Peptidase S26A, signal peptidase I | Peptidase S26A, signal peptidase I | Pept_S26A_signal_pept_1 | 1 |
IPR000225 | 225 | Armadillo | Armadillo | Repeat | 136,609 | false | false | This entry represents proteins that contain the Armadillo repeat mainly from eukaryotes. These proteins include: Vacuolar protein 8, Importins, Catenins, Junction plakoglobin and related proteins. The armadillo (Arm) repeat is an approximately 40 amino acid long tandemly repeated sequence motif first identified in the ... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00514",
"PS50176",
"SM00185"
] | [
"Arm",
"ARM_REPEAT",
"ARM"
] | [
75774,
92875,
126800
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50176",
"R-BTA-140342",
"R-BTA-177504",
"R-BTA-195253",
"R-BTA-196299",
"R-BTA-201681",
"R-BTA-201722",
"R-BTA-204005",
"R-BTA-2132295",
"R-BTA-3134973",
"R-BTA-351906",
"R-BTA-3769402",
"R-BTA-4086398",
"R-BTA-416993",
"R-BTA-418990",
"R-BTA-437239",
"R-BTA-4641262",
"R-BTA-5... | [
"PROSITEDOC:PDOC50176",
"REACTOME:R-BTA-140342",
"REACTOME:R-BTA-177504",
"REACTOME:R-BTA-195253",
"REACTOME:R-BTA-196299",
"REACTOME:R-BTA-201681",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-3134973",
"REACTOME:R-BTA-351906",
"REACTOME:R-BTA-37... | 354 | [
"1bk5",
"1bk6",
"1ee4",
"1ee5",
"1ejl",
"1ejy",
"1g3j",
"1i7w",
"1i7x",
"1ial",
"1iq1",
"1jdh",
"1jpp",
"1jpw",
"1luj",
"1m1e",
"1m5n",
"1pjm",
"1pjn",
"1q1s",
"1q1t",
"1qgk",
"1qgr",
"1qz7",
"1t08",
"1th1",
"1ukl",
"1un0",
"1v18",
"1wa5",
"1xm9",
"1y2a"... | 430 | [
"PUB00000951",
"PUB00015440",
"PUB00015441"
] | [
"9298899",
"9770300",
"12946625"
] | [
"Three-dimensional structure of the armadillo repeat region of beta-catenin.",
"The armadillo family of structural proteins.",
"Armadillo repeat proteins: beyond the animal kingdom."
] | [
1997,
1999,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
173,
836,
135575,
3,
22
] | 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... | [
380,
23,
276,
44,
221,
146,
5,
209,
191,
4,
7,
452
] | 12 | true | Repeat | Armadillo | Armadillo | Armadillo | 3 |
IPR000227 | 227 | Angiotensinogen | Angiotensinogen | Family | 955 | false | false | Angiotensinogen is a component of the renin-angiotensin system (RAS), a hormone system that regulates blood pressure and fluid balance. It is also known as the renin substrate, and is a non-inhibitory member of the serpin family of proteinase inhibitors (MEROPS inhibitor family I4, clan ID, MEROPS identifier I04.953). ... | [
"GO:0003081"
] | [
"regulation of systemic arterial blood pressure by renin-angiotensin"
] | [
"biological_process"
] | 1 | [
"PRINTS"
] | [
"PR00654"
] | [
"ANGIOTENSNGN"
] | [
955
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp2085",
"R-BTA-2022377",
"R-BTA-375276",
"R-BTA-416476",
"R-BTA-418594",
"R-HSA-1989781",
"R-HSA-2022377",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-418594",
"R-MMU-2022377",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-418594",
"R-RNO-2022377",
"R-RNO-375276",
"R-RNO-416476",
"R-RNO... | [
"GP:GenProp2085",
"REACTOME:R-BTA-2022377",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2022377",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-2022377",
"REACTOME:R-MMU-375276... | 18 | [
"2wxw",
"2wxx",
"2wxy",
"2wxz",
"2wy0",
"2wy1",
"2x0b",
"5m3x",
"5m3y",
"6i3f",
"6i3i",
"8h55"
] | 12 | [
"PUB00003892",
"PUB00067351",
"PUB00067352",
"PUB00067353",
"PUB00067354",
"PUB00067355",
"PUB00067356",
"PUB00067360",
"PUB00067361",
"PUB00067362",
"PUB00067363"
] | [
"8513325",
"10969042",
"2476171",
"15010016",
"1132082",
"18026570",
"15283675",
"23",
"9",
"467805",
"4675"
] | [
"A molecular variant of angiotensinogen associated with preeclampsia.",
"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9.",
"Angiotensin-converting enzyme: new concepts concerning its biological role.",
"Newly recognized physiologic and pathophys... | [
1993,
2000,
1989,
2004,
1975,
2008,
2004,
1975,
1975,
1979,
1976
] | 11 | [
"IPR000215"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
955
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
18,
4,
4
] | 4 | true | Family | Angiotensinogen | Angiotensinogen | Angiotensinogen | 9 |
IPR000228 | 228 | RNA 3'-terminal phosphate cyclase | RNA3'_term_phos_cyc | Family | 10,587 | false | false | RNA cyclases are a family of RNA-modifying enzymes that are conserved in eukaryotes, bacteria and archaea. Type 1 RNA 3'-terminal phosphate cyclases ( ) [ , ] catalyse the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA: ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2'... | [
"GO:0006396"
] | [
"RNA processing"
] | [
"biological_process"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF005378",
"PTHR11096"
] | [
"RNA3'_term_phos_cycl_euk",
""
] | [
5494,
10587
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.5.1.4",
"PDOC00989",
"R-BTA-6791226",
"R-CEL-6791226",
"R-DDI-6791226",
"R-DME-6791226",
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"EC:6.5.1.4",
"PROSITEDOC:PDOC00989",
"REACTOME:R-BTA-6791226",
"REACTOME:R-CEL-6791226",
"REACTOME:R-DDI-6791226",
"REACTOME:R-DME-6791226",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 11 | [
"1qmh",
"1qmi",
"3kgd",
"3pqv",
"3tut",
"3tux",
"3tv1",
"3tw3",
"4clq",
"4o89",
"4o8j",
"5jpq",
"5oql",
"5tzs",
"5wlc",
"5wyj",
"5wyk",
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6rxt",
"6rxu",
"6rxv",
"6rxx",
"6rxy",
"6rxz",
"6zqa"... | 65 | [
"PUB00001300",
"PUB00003565",
"PUB00042947"
] | [
"9184239",
"2199762",
"10790377"
] | [
"The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea.",
"RNA 3'-terminal phosphate cyclase from HeLa cells.",
"Rcl1p, the yeast protein similar to the RNA 3'-phosphate cyclase, associates with U3 snoRNP and is required for 18S rRNA bioge... | [
1997,
1990,
2000
] | 3 | [] | [
"IPR016443",
"IPR017770"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
649,
1830,
8053,
55
] | 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",... | [
5,
1,
2,
3,
1,
8,
12,
2,
3,
10,
1,
1,
7
] | 13 | true | Family | RNA 3'-terminal phosphate cyclase | RNA 3'-terminal phosphate cyclase | RNA3'_term_phos_cyc | 5 |
IPR000229 | 229 | Nucleocapsid protein, arenaviridae | Nucleocapsid_arenaviridae | Family | 763 | false | false | Arenaviridae are single stranded RNA viruses. The arenaviridae S RNAs that have been characterised include conserved terminal sequences, an ambisense arrangement of the coding regions for the precursor glycoprotein (GPC) and nucleocapsid (N) proteins and an intergenic region capable of forming a base-paired "hairpin" s... | [
"GO:0019013"
] | [
"viral nucleocapsid"
] | [
"cellular_component"
] | 1 | [
"HAMAP",
"PIRSF"
] | [
"MF_04085",
"PIRSF004029"
] | [
"ARENA_NCAP",
"N_ArenaV"
] | [
726,
763
] | 2 | [
"EC"
] | [
"3.1.13.-"
] | [
"EC:3.1.13.-"
] | 1 | [
"3mwp",
"3mwt",
"3mx2",
"3mx5",
"3r3l"
] | 5 | [
"PUB00005615",
"PUB00006263"
] | [
"8599223",
"2042397"
] | [
"Oliveros virus: a novel arenavirus from Argentina.",
"Nucleotide sequence of the S RNA of Lassa virus (Nigerian strain) and comparative analysis of arenavirus gene products."
] | [
1996,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Arenaviridae"
] | [
763
] | 1 | [] | [] | 0 | true | Family | Nucleocapsid protein, arenaviridae | Nucleocapsid protein, arenaviridae | Nucleocapsid_arenaviridae | 5 |
IPR000231 | 231 | Large ribosomal subunit protein eL30 | Ribosomal_eL30 | Family | 3,626 | false | false | This family represents the large ribosomal subunit protein eL30 family of proteins, which includes: Mammalian eL30 [ , ]. Thermococcus celer eL30 [ ]. Methanococcus vannielii eL30 [ ]. Sulfolobus acidocaldarius eL30 [ ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The cod... | [
"GO:0003723",
"GO:0003735",
"GO:0022625"
] | [
"RNA binding",
"structural constituent of ribosome",
"cytosolic large ribosomal subunit"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_00481"
] | [
"Ribosomal_eL30"
] | [
3626
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00588",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-GGA-1799339",
"R-GGA-72689",
"R-GGA-72706",
"R-GGA-975956",
"R-GGA-975957",
"R-HSA-156827",
"R-HSA-156902",
"R-HSA-1799339",
"R-HSA-192823",
"R-HSA-240855... | [
"PROSITEDOC:PDOC00588",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-GGA-1799339",
"REACTOME:R-GGA-72689",
"REACTOME:R-GGA-72706",
"REACTOME:R-GGA-97595... | 40 | [
"1go0",
"1go1",
"1h7m",
"1w3e",
"1w40",
"1w41",
"1w42",
"2bo1",
"3cpq",
"3j7o",
"3j7p",
"3j7q",
"3j7r",
"3j92",
"3lfo",
"3n4y",
"3n4z",
"3ra5",
"3ra6",
"3vi6",
"4d5y",
"4d67",
"4ug0",
"4ujc",
"4ujd",
"4uje",
"4v4n",
"4v5z",
"4v6u",
"4v6w",
"4v6x",
"5aj0"... | 251 | [
"PUB00001749",
"PUB00003405",
"PUB00004357",
"PUB00004394",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00101554"
] | [
"3840111",
"2475640",
"2501756",
"1840672",
"11297922",
"11290319",
"11114498",
"32669547"
] | [
"Molecular cloning and nucleotide sequences of cDNAs specific for rat liver ribosomal proteins S17 and L30.",
"Organization and nucleotide sequence of a transcriptional unit of Methanococcus vannielii comprising genes for protein synthesis elongation factors and ribosomal proteins.",
"Organization and nucleotid... | [
1985,
1989,
1989,
1991,
2001,
2001,
2000,
2020
] | 8 | [
"IPR039109"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Eukaryota",
"Nocardioides humilatus",
"ecological metagenomes"
] | [
378,
3240,
1,
7
] | 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",
"Zea mays"
] | [
2,
1,
1,
3,
2,
4,
1,
4,
3,
8
] | 10 | true | Family | Large ribosomal subunit protein eL30 | Large ribosomal subunit protein eL30 | Ribosomal_eL30 | 9 |
IPR000233 | 233 | Cadherin, Y-type LIR-motif | Cadherin_Y-type_LIR | Domain | 25,727 | false | false | Cadherins (CADHs) are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation [ ]. CADHs also have a crucial role in epithelial-to-mesenchymal transition (EMT), involved in migration properties of tumour cells. CADH6 is an EMT marker in thyroid cancer that interacts with ... | [
"GO:0005509",
"GO:0007156"
] | [
"calcium ion binding",
"homophilic cell-cell adhesion"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01049"
] | [
"CADH_Y-type_LIR"
] | [
25727
] | 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-418990",
"R-CFA-1474228",
"R-CFA-216083",
"R-CFA-351906",
"R-CFA-418990",
"R-CFA-6805567",
"R-CFA-6809371",
"R-CFA-9764561",
"R-CFA-9766229",
"R-CFA-9768727",
"R-DME-1474228",
"R-DME-216083",
"R-DME-351906",
"R-DME-381426",
"R-DME-418990",
"R-DME-5218920",
"R-DME-525793",
"R... | [
"REACTOME:R-BTA-418990",
"REACTOME:R-CFA-1474228",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-351906",
"REACTOME:R-CFA-418990",
"REACTOME:R-CFA-6805567",
"REACTOME:R-CFA-6809371",
"REACTOME:R-CFA-9764561",
"REACTOME:R-CFA-9766229",
"REACTOME:R-CFA-9768727",
"REACTOME:R-DME-1474228",
"REACTOME:R-... | 109 | [
"1i7w",
"1i7x",
"1q55",
"1q5a",
"1q5b",
"1q5c",
"3ifq"
] | 7 | [
"PUB00003086",
"PUB00007071",
"PUB00096942",
"PUB00096943"
] | [
"9566976",
"3061804",
"27375021",
"32587856"
] | [
"The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn.",
"Cell binding function of E-cadherin is regulated by the cytoplasmic domain.",
"Cadherin-6 promotes EMT and cancer metastasis by restraining autophagy.",
"Structure a... | [
1998,
1988,
2017,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
25727
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
92,
9,
69,
46,
65
] | 5 | true | Domain | Cadherin, Y-type LIR-motif | Cadherin, Y-type LIR-motif | Cadherin_Y-type_LIR | 4 |
IPR000234 | 234 | Herpesvirus Glycoprotein B | Herpes_Glycoprot_B | Family | 921 | false | false | Glycoprotein B is an envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells [ , , ]. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_04032"
] | [
"HSV_GB"
] | [
921
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9609690",
"R-HSA-9610379"
] | [
"REACTOME:R-HSA-9609690",
"REACTOME:R-HSA-9610379"
] | 2 | [
"5v2s",
"6bm8",
"6vn1",
"6z9m",
"7k1s",
"7kdd",
"7kdp",
"8rgz",
"8rh0",
"9ih8",
"9jme",
"9q9l",
"9q9n",
"9q9s"
] | 14 | [
"PUB00085345",
"PUB00085346",
"PUB00155380"
] | [
"23736286",
"27573107",
"26365435"
] | [
"Human cytomegalovirus (HCMV) glycoprotein gB promotes virus entry in trans acting as the viral fusion protein rather than as a receptor-binding protein.",
"Platelet-derived growth factor-α receptor is the cellular receptor for human cytomegalovirus gHgLgO trimer.",
"Structure of HCMV glycoprotein B in the post... | [
2013,
2016,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Herpesvirales",
"Homo sapiens",
"Salmonella enterica"
] | [
919,
1,
1
] | 3 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Herpesvirus Glycoprotein B | Herpesvirus Glycoprotein B | Herpes_Glycoprot_B | 4 |
IPR000235 | 235 | Small ribosomal subunit protein uS7 | Ribosomal_uS7 | Family | 57,372 | false | false | This entry includes the small ribosomal subunit protein uS7, formerly referred to as 30S ribosomal proteins S7 (bacterial, archaeal, plastid, mitochondrial), and eukaryotic 40S ribosomal proteins S5 (cytoplasmic) [ , , , ]. 30S ribosomal protein S7 contacts ribosomal proteins S9 and S11. It is also one of the primary r... | [
"GO:0006412"
] | [
"translation"
] | [
"biological_process"
] | 1 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF002122",
"PTHR11205"
] | [
"RPS7p_RPS7a_RPS5e_RPS7o",
""
] | [
53599,
57045
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00051",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"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-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419... | [
"PROSITEDOC:PDOC00051",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"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-97595... | 117 | [
"1dv4",
"1eg0",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1hus",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1iqv",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1rss",
"1vvj",
"1vy4",
"1vy5",
"1vy6"... | 1,895 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00059258",
"PUB00110894",
"PUB00151110"
] | [
"11297922",
"11290319",
"11114498",
"11160889",
"23636399",
"34516797"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Ribosomal protein S7 from Escherichia coli uses the same determinants to bind 16S ribosomal RNA and its messenger RNA.",
"Structures of the human and Drosophi... | [
2001,
2001,
2000,
2001,
2013,
2021
] | 6 | [] | [
"IPR005716",
"IPR005717"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
911,
23438,
32569,
454
] | 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",... | [
14,
2,
4,
6,
1,
11,
4,
2,
15,
8,
2,
3,
17
] | 13 | true | Family | Small ribosomal subunit protein uS7 | Small ribosomal subunit protein uS7 | Ribosomal_uS7 | 4 |
IPR000236 | 236 | Transactivation protein X | Transactivation_prot_X | Family | 14,326 | false | false | The Hepatitis B virus (HBV) X gene shares sequences with both the polymerase and precore genes, carries several regulatory signals critical to the replicative cycle, and its product has a transactivating function [ ]. The transactivating function is probably associated with a tumourigenic potential of HBx, since x gene... | [
"GO:0019079"
] | [
"viral genome replication"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PFAM"
] | [
"MF_04074",
"PF00739"
] | [
"HBV_X",
"X"
] | [
8871,
14326
] | 2 | [] | [] | [] | 0 | [
"5b1z",
"5fcg",
"8gtx",
"8wls",
"9j6j",
"9j6k"
] | 6 | [
"PUB00006332",
"PUB00006490"
] | [
"7561749",
"8530810"
] | [
"The hepatitis B virus X gene: analysis of functional domain variation and gene phylogeny using multiple sequences.",
"Transactivating function and expression of the x gene of hepatitis B virus."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Hepadnaviridae",
"Marmota monax",
"Streptomyces griseicoloratus"
] | [
14323,
2,
1
] | 3 | [] | [] | 0 | true | Family | Transactivation protein X | Transactivation protein X | Transactivation_prot_X | 3 |
IPR000237 | 237 | GRIP domain | GRIP_dom | Domain | 14,698 | false | false | The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain [ , , ] is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi [ ]. The GRIP domain contains a completely conserved tyrosine residue. | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01465",
"PS50913",
"SM00755"
] | [
"GRIP",
"GRIP",
"Grip"
] | [
10595,
14582,
9776
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50913",
"R-CEL-6811440",
"R-HSA-5620924",
"R-HSA-6811438",
"R-HSA-6811440",
"R-HSA-9673768",
"R-HSA-9703465",
"R-HSA-9725370",
"R-MMU-6811440",
"R-RNO-6811440",
"R-SCE-6811440"
] | [
"PROSITEDOC:PDOC50913",
"REACTOME:R-CEL-6811440",
"REACTOME:R-HSA-5620924",
"REACTOME:R-HSA-6811438",
"REACTOME:R-HSA-6811440",
"REACTOME:R-HSA-9673768",
"REACTOME:R-HSA-9703465",
"REACTOME:R-HSA-9725370",
"REACTOME:R-MMU-6811440",
"REACTOME:R-RNO-6811440",
"REACTOME:R-SCE-6811440"
] | 11 | [
"1r4a",
"1upt"
] | 2 | [
"PUB00001040",
"PUB00001041",
"PUB00001042",
"PUB00031855"
] | [
"10209120",
"10209123",
"10209125",
"14580338"
] | [
"The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins.",
"A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins.",
"A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins.",
"Structural basis for Arl1-... | [
1999,
1999,
1999,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
35,
14662,
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... | [
4,
6,
12,
19,
38,
16,
2,
3,
18,
2,
3,
3
] | 12 | true | Domain | GRIP domain | GRIP domain | GRIP_dom | 2 |
IPR000238 | 238 | Ribosome-binding factor A | RbfA | Family | 26,080 | false | false | Ribosome-binding factor A [ ] (gene rbfA) is a bacterial protein that associates with free 30S ribosomal subunits. It does not associate with 30S subunits that are part of 70S ribosomes or polysomes. It is essential for efficient processing of 16S rRNA. Ribosome-binding factor A is a protein of from 13 to 15 Kd which i... | [
"GO:0006364"
] | [
"rRNA processing"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00003",
"PF02033",
"PTHR33515",
"TIGR00082"
] | [
"RbfA",
"RBFA",
"",
"rbfA"
] | [
23965,
26048,
23893,
23319
] | 4 | [
"PROSITEDOC"
] | [
"PDOC01023"
] | [
"PROSITEDOC:PDOC01023"
] | 1 | [
"1jos",
"1kkg",
"1pa4",
"2dyj",
"2e7g",
"2kzf",
"2r1c",
"6ye5",
"7afl",
"7afq",
"7bog",
"7boh",
"7nav",
"7pnt",
"7pnu",
"7pnv",
"7pnx",
"7pny",
"7pnz",
"7po0",
"7x9u",
"8bxa",
"8byv",
"8csr",
"8css",
"8cst",
"8csu",
"9g5b",
"9g5c",
"9g5d"
] | 30 | [
"PUB00002319",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"9422595",
"11297922",
"11290319",
"11114498"
] | [
"RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1998,
2001,
2001,
2000
] | 4 | [] | [
"IPR039212"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
2,
23546,
2013,
2,
517
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
3,
2,
3,
1,
1,
1,
2,
2,
4,
2
] | 10 | true | Family | Ribosome-binding factor A | Ribosome-binding factor A | RbfA | 8 |
IPR000239 | 239 | GPCR kinase | GPCR_kinase | Family | 10,478 | false | false | Rapid regulation of G-protein-coupled receptors (GPCRs) involves agonist- promoted receptor phosphorylation by GPCR kinases (GRKs) [ ]. This process is followed by arrestin binding and transient receptor internalisation. It has been shown that beta-adrenergic receptor kinase (beta ARK-1 or GRK2) follows a similar patte... | [
"GO:0004703",
"GO:0005524",
"GO:0006468",
"GO:0007165"
] | [
"G protein-coupled receptor kinase activity",
"ATP binding",
"protein phosphorylation",
"signal transduction"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR00717"
] | [
"GPCRKINASE"
] | [
10478
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11",
"R-BTA-111933",
"R-BTA-2514859",
"R-BTA-416476",
"R-BTA-418555",
"R-BTA-5635838",
"R-BTA-8856825",
"R-CEL-111933",
"R-CEL-2514859",
"R-CEL-416476",
"R-DME-111933",
"R-DME-416476",
"R-DME-418555",
"R-DME-5635838",
"R-DRE-2514859",
"R-HSA-111933",
"R-HSA-2514859",
"R-HSA-41... | [
"EC:2.7.11",
"REACTOME:R-BTA-111933",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-5635838",
"REACTOME:R-BTA-8856825",
"REACTOME:R-CEL-111933",
"REACTOME:R-CEL-2514859",
"REACTOME:R-CEL-416476",
"REACTOME:R-DME-111933",
"REACTOME:R-DME-416476",
... | 34 | [
"1omw",
"1ym7",
"2acx",
"2bcj",
"3c4w",
"3c4x",
"3c4y",
"3c4z",
"3c50",
"3c51",
"3cik",
"3krw",
"3krx",
"3nyn",
"3nyo",
"3psc",
"3pvu",
"3pvw",
"3qc9",
"3t8o",
"3uzs",
"3uzt",
"3v5w",
"4l9i",
"4mk0",
"4pni",
"4pnk",
"4tnb",
"4tnd",
"4wbo",
"4wnk",
"4yhj"... | 74 | [
"PUB00003012"
] | [
"9092483"
] | [
"Beta-adrenergic receptor kinase (GRK2) colocalizes with beta-adrenergic receptors during agonist-induced receptor internalization."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
10478
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
24,
4,
24,
21,
34
] | 6 | true | Family | GPCR kinase | GPCR kinase | GPCR_kinase | 3 |
IPR000240 | 240 | Serpin B9/maspin | Serpin_B9/Maspin | Family | 1,788 | false | false | This family consists of serpin B5 (Maspin) and serpin B9. They are members of the serpin (SERine Protease INhibitor) family (MEROPS inhibitor family I4, clan ID). | [
"GO:0004867"
] | [
"serine-type endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00676"
] | [
"MASPIN"
] | [
1788
] | 1 | [
"REACTOME"
] | [
"R-MMU-75205"
] | [
"REACTOME:R-MMU-75205"
] | 1 | [
"1wz9",
"1xqg",
"1xqj",
"1xu8",
"8zcr"
] | 5 | [
"PUB00005180",
"PUB00014133",
"PUB00014143"
] | [
"8290962",
"14705960",
"12792516"
] | [
"Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells.",
"Evolutionary families of peptidase inhibitors.",
"Serine proteinase inhibitor-9, an endogenous blocker of granzyme B/perforin lytic pathway, is hyperexpressed during acute rejection of renal allografts."
] | [
1994,
2004,
2003
] | 3 | [
"IPR000215"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1788
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
5,
13,
11
] | 4 | true | Family | Serpin B9/maspin | Serpin B9/maspin | Serpin_B9/Maspin | 3 |
IPR000241 | 241 | Ribosomal RNA large subunit methyltransferase K/L-like, methyltransferase domain | RlmKL-like_Mtase | Domain | 27,834 | false | false | This entry represents the methyltransferase domain found in ribosomal RNA large subunit methyltransferase K/L from Escherichia coli (RmlKL) and tRNA (guanine(10)-N2)-dimethyltransferase from Methanocaldococcus jannaschii which is associated with the THUMP domain ( ) RmlKL specifically methylates the guanine in position... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01170"
] | [
"UPF0020"
] | [
27834
] | 1 | [
"EC",
"EC",
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"2.1.1",
"2.1.1.173",
"2.1.1.264",
"PDOC00969",
"R-HSA-6782315"
] | [
"EC:2.1.1",
"EC:2.1.1.173",
"EC:2.1.1.264",
"PROSITEDOC:PDOC00969",
"REACTOME:R-HSA-6782315"
] | 5 | [
"3k0b",
"3ldg",
"3ldu",
"3tlj",
"3tm4",
"3tm5",
"3tma",
"3v8v",
"3v97",
"5e71",
"5e72",
"6zxv",
"6zxw",
"6zxy"
] | 14 | [
"PUB00007072",
"PUB00039897",
"PUB00100798",
"PUB00100799"
] | [
"11295541",
"16343540",
"22362734",
"17010378"
] | [
"THUMP--a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases.",
"Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain.",
"Structure of the bifunctional methyltransferase YcbY (RlmKL) that adds the m7... | [
2001,
2006,
2012,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Bodo saltans virus",
"Eukaryota",
"unclassified sequences"
] | [
1111,
18419,
1,
8076,
227
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
2,
9,
1,
1,
8,
6,
1,
1,
18,
1,
1,
4
] | 13 | true | Domain | Ribosomal RNA large subunit methyltransferase K/L-like, methyltransferase domain | Ribosomal RNA large subunit methyltransferase K/L-like, methyltransferase domain | RlmKL-like_Mtase | 7 |
IPR000243 | 243 | Peptidase T1A, proteasome beta-subunit | Pept_T1A_subB | Family | 18,453 | false | false | The proteasome (or macropain) ( ) [ , , , , ] is a multicatalytic proteinase complex in eukaryotes and archaea, and in some bacteria, that seems to be involved in an ATP/ubiquitin-dependent nonlysosomal proteolytic pathway. In eukaryotes the proteasome is composed of 28 distinct subunits which form a highly ordered rin... | [
"GO:0004298",
"GO:0030163",
"GO:0005839"
] | [
"threonine-type endopeptidase activity",
"protein catabolic process",
"proteasome core complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00141"
] | [
"PROTEASOME"
] | [
18453
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.25.1",
"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-4... | [
"EC:3.4.25.1",
"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",
... | 367 | [
"1fnt",
"1g0u",
"1g65",
"1iru",
"1j2q",
"1jd2",
"1pma",
"1ryp",
"1ya7",
"1yar",
"1yau",
"1z7q",
"2f16",
"2fak",
"2gpl",
"2zcy",
"3bdm",
"3c91",
"3c92",
"3d29",
"3dy3",
"3dy4",
"3e47",
"3gpj",
"3gpt",
"3gpw",
"3h4p",
"3hye",
"3ipm",
"3j9i",
"3jco",
"3jcp"... | 562 | [
"PUB00000148",
"PUB00000524",
"PUB00001329",
"PUB00004123",
"PUB00005460",
"PUB00030848",
"PUB00065662"
] | [
"2643381",
"7682410",
"7697118",
"1317508",
"8882582",
"9087403",
"22341445"
] | [
"The multicatalytic proteinase of mammalian cells.",
"Proteasomes: multicatalytic proteinase complexes.",
"Proteasomes. Multicatalytic proteinase complexes.",
"Proteolysis, proteasomes and antigen presentation.",
"Proteasomes: destruction as a programme.",
"Structure of 20S proteasome from yeast at 2.4 A ... | [
1989,
1993,
1993,
1992,
1996,
1997,
2012
] | 7 | [
"IPR023333"
] | [
"IPR019983"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1317,
1622,
15443,
71
] | 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... | [
17,
4,
14,
17,
26,
16,
3,
11,
27,
3,
2,
19
] | 12 | true | Family | Peptidase T1A, proteasome beta-subunit | Peptidase T1A, proteasome beta-subunit | Pept_T1A_subB | 8 |
IPR000244 | 244 | Large ribosomal subunit protein bL9 | Ribosomal_bL9 | Family | 28,043 | false | false | This entry represents the large ribosomal subunit protein bL9. In Escherichia coli, bL9 is known to bind directly to the 23S rRNA. It belongs to a family of ribosomal proteins grouped on the basis of sequence similarities [ ]. The crystal structure of Bacillus stearothermophilus bL9 shows the 149-residue protein compri... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER"
] | [
"PTHR21368"
] | [
""
] | [
28043
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00560",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383",
"R-RNO-5389840",
"R-RNO-5419276",
"R-RNO-9937383"
... | [
"PROSITEDOC:PDOC00560",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:... | 17 | [
"1cqu",
"1div",
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2hba",
"2hbb",
"2hvf",
"2j28",
"2rdo",
"3bbx",
"3iy9",
"3j5l",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce",
"3jcj"... | 1,047 | [
"PUB00001252",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00007073"
] | [
"8306963",
"11297922",
"11290319",
"11114498",
"12051860"
] | [
"Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"pH-dependent stability and folding kinetics of a protein with an unu... | [
1994,
2001,
2001,
2000,
2002
] | 5 | [] | [
"IPR020594"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
23616,
3907,
520
] | 3 | [
"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,
1,
1,
1,
7,
4,
1,
5,
9,
14
] | 11 | true | Family | Large ribosomal subunit protein bL9 | Large ribosomal subunit protein bL9 | Ribosomal_bL9 | 1 |
IPR000245 | 245 | V-ATPase proteolipid subunit | ATPase_proteolipid_csu | Family | 16,340 | false | false | This entry represents the 16kDa proteolipid subunit c that is part of the V0 complex of V-ATPase in eukaryotic organelles and in certain bacteria. There are three proteolipid subunits (known as c, c' and c'' in yeast) that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is e... | [
"GO:0046961",
"GO:1902600",
"GO:0033179"
] | [
"proton-transporting ATPase activity, rotational mechanism",
"proton transmembrane transport",
"proton-transporting V-type ATPase, V0 domain"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00122"
] | [
"VACATPASE"
] | [
16340
] | 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-1222556",
"R-BTA-77387",
"R-BTA-917977",
"R-BTA-9639288",
"R-BTA-983712",
"R-CEL-1222556",
"R-CEL-6798695",
"R-CEL-77387",
"R-CEL-917977",
"R-CEL-9639288",
"R-CEL-983712",
"R-DDI-1222556",
"R-DDI-6798695",
"R-DDI-77387",
"R-DDI-917977",
"R-DDI-9639288",
"R-DME-1222556",
"R-D... | [
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-917977",
"REACTOME:R-BTA-9639288",
"REACTOME:R-BTA-983712",
"REACTOME:R-CEL-1222556",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-77387",
"REACTOME:R-CEL-917977",
"REACTOME:R-CEL-9639288",
"REACTOME:R-CEL-983712",
"REACTOME:R-DDI-... | 51 | [
"2bl2",
"2cyd",
"2db4",
"3aou",
"3j9t",
"3j9u",
"3j9v",
"5gar",
"5gas",
"5tj5",
"5tsj",
"5vox",
"5voy",
"5voz",
"5y5x",
"5y5z",
"5y60",
"6c6l",
"6ly9",
"6m0r",
"6m0s",
"6o7t",
"6o7u",
"6o7v",
"6o7w",
"6o7x",
"6pe4",
"6pe5",
"6qum",
"6r0w",
"6r0y",
"6r0z"... | 104 | [
"PUB00007886",
"PUB00020603",
"PUB00020604",
"PUB00020608",
"PUB00020609",
"PUB00020629",
"PUB00020631",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789",
"PUB00160299"
] | [
"11533110",
"15473999",
"15078220",
"15907459",
"15629643",
"15951435",
"14635779",
"20450191",
"18937357",
"1385979",
"9741106",
"9874757"
] | [
"Structure-function relationships of A-, F- and V-ATPases.",
"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.",
"A new view of an old pore.",
"A structural model of the vac... | [
2001,
2004,
2004,
2005,
2005,
2005,
2003,
2010,
2008,
1992,
1998,
1992
] | 12 | [] | [
"IPR011555"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
328,
1313,
14641,
58
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
19,
3,
3,
11,
6,
13,
3,
13,
8,
3,
3,
36
] | 12 | true | Family | V-ATPase proteolipid subunit | V-ATPase proteolipid subunit | ATPase_proteolipid_csu | 7 |
IPR000247 | 247 | Cucumovirus coat protein | Cucumovirus_coat | Family | 1,286 | false | false | Cucumoviruses are tripartite RNA plant viruses believed to share a close evolutionary relationship with Brome mosaic virus (BMV). The cucumoviruses include: Cucumber mosaic virus [ ], Peanut stunt virus [ ] and Tomato aspermy virus [ ]. The viral coat proteins show a high degree of sequence similarity [ ]. | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00222"
] | [
"CUCUMOCOAT"
] | [
1286
] | 1 | [] | [] | [] | 0 | [
"1f15",
"1laj",
"5ow6"
] | 3 | [
"PUB00003131",
"PUB00003135",
"PUB00005580"
] | [
"2230731",
"1990057",
"1926787"
] | [
"Nucleotide sequence and evolutionary relationships of cucumber mosaic virus (CMV) strains: CMV RNA 3.",
"Tomato aspermy virus has an evolutionary relationship with other tripartite RNA plant viruses.",
"Nucleotide sequence of RNA 3 of peanut stunt cucumovirus."
] | [
1990,
1991,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
1286
] | 1 | [] | [] | 0 | true | Family | Cucumovirus coat protein | Cucumovirus coat protein | Cucumovirus_coat | 9 |
IPR000248 | 248 | Angiotensin II receptor family | ATII_rcpt | Family | 3,449 | false | false | Angiotensin II is a blood-borne hormone produced in the circulation, it is also formed in many tissues such as the brain, kidney, heart, and blood vessels, where angiotensin II functions as a paracrine and autocrine hormone. The known actions of angiotensin II are mediated through two angiotensin receptor subtypes, Ang... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00241"
] | [
"ANGIOTENSINR"
] | [
3449
] | 1 | [
"GP",
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GenProp2085",
"35",
"R-BTA-375276",
"R-BTA-416476",
"R-BTA-8856825",
"R-BTA-8856828",
"R-DRE-375276",
"R-DRE-418594",
"R-GGA-375276",
"R-GGA-416476",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-444821",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-375276",
"R-MMU-416476",
... | [
"GP:GenProp2085",
"IUPHAR:35",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-DRE-375276",
"REACTOME:R-DRE-418594",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-416476",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME... | 31 | [
"4yay",
"4zud",
"5unf",
"5ung",
"5unh",
"5xjm",
"6do1",
"6jod",
"6os0",
"6os1",
"6os2",
"7c6a",
"7jni",
"7yj4",
"7yk6",
"7yk7",
"8th3",
"8th4",
"9eah",
"9eai",
"9eaj"
] | 21 | [
"PUB00063358",
"PUB00082340",
"PUB00082341"
] | [
"17346243",
"14522967",
"16750822"
] | [
"Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology.",
"Identification of relaxin-3/INSL7 as a ligand for GPCR142.",
"Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular de... | [
2007,
2003,
2006
] | 3 | [
"IPR050119"
] | [
"IPR000147",
"IPR000190"
] | 1 | 2 | 0 | [
"Avipoxvirus",
"Vertebrata"
] | [
13,
3436
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
8,
10,
8
] | 4 | true | Family | Angiotensin II receptor family | Angiotensin II receptor family | ATII_rcpt | 6 |
IPR000250 | 250 | Peptidase G1 | Peptidase_G1 | Family | 3,696 | false | false | The peptidases in family G1 form a subset of what were formerly termed 'pepstatin-insensitive carboxyl proteinases'. After its discovery in about 1970, the pentapeptide pepstatin soon came to be thought of as a very general inhibitor of the endopeptidases that are active at acidic pH. But more recently several acid-act... | [
"GO:0070007",
"GO:0006508"
] | [
"glutamic-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF01828",
"PR00977",
"PTHR37536"
] | [
"Peptidase_A4",
"SCYTLDPTASE",
""
] | [
3695,
2321,
3397
] | 3 | [] | [] | [] | 0 | [
"1s2b",
"1s2k",
"1y43",
"2ifr",
"2ifw",
"3trs"
] | 6 | [
"PUB00002659",
"PUB00003579",
"PUB00015132",
"PUB00041696"
] | [
"1918060",
"7674922",
"14993599",
"17069854"
] | [
"The gene and deduced protein sequences of the zymogen of Aspergillus niger acid proteinase A.",
"Evolutionary families of metallopeptidases.",
"The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.",
"Crystal structure of scytalidoglutamic peptidase with i... | [
1991,
1995,
2004,
2007
] | 4 | [] | [
"IPR033863"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
24,
654,
3014,
4
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Family | Peptidase G1 | Peptidase G1 | Peptidase_G1 | 1 |
IPR000253 | 253 | Forkhead-associated (FHA) domain | FHA_dom | Domain | 155,797 | false | false | The forkhead-associated (FHA) domain [ ] is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-s... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00498",
"PS50006",
"SM00240"
] | [
"FHA",
"FHA_DOMAIN",
"FHA"
] | [
143780,
129956,
110320
] | 3 | [
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1508",
"GenProp1763",
"PDOC50006",
"R-BTA-5693565",
"R-BTA-5693571",
"R-BTA-5693607",
"R-BTA-69473",
"R-BTA-9645460",
"R-CEL-6811434",
"R-CEL-983189",
"R-DDI-111932",
"R-DDI-442729",
"R-DDI-5693565",
"R-DDI-6804760",
"R-DDI-69473",
"R-DDI-69601",
"R-DDI-75035",
"R-DME-56935... | [
"GP:GenProp1508",
"GP:GenProp1763",
"PROSITEDOC:PDOC50006",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-5693571",
"REACTOME:R-BTA-5693607",
"REACTOME:R-BTA-69473",
"REACTOME:R-BTA-9645460",
"REACTOME:R-CEL-6811434",
"REACTOME:R-CEL-983189",
"REACTOME:R-DDI-111932",
"REACTOME:R-DDI-442729",
"RE... | 140 | [
"1dmz",
"1fhq",
"1fhr",
"1g3g",
"1g6g",
"1gxc",
"1j4k",
"1j4l",
"1j4o",
"1j4p",
"1j4q",
"1k2m",
"1k2n",
"1k3j",
"1k3n",
"1k3q",
"1lgp",
"1lgq",
"1mzk",
"1qu5",
"1r21",
"1uht",
"1wln",
"2a0t",
"2aff",
"2csw",
"2eh0",
"2fez",
"2ff4",
"2g1l",
"2jkd",
"2jpe"... | 126 | [
"PUB00005445",
"PUB00007074"
] | [
"7482699",
"11911881"
] | [
"The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors.",
"The FHA domain."
] | [
1995,
2002
] | 2 | [] | [
"IPR032030",
"IPR047398",
"IPR049779",
"IPR061279"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
370,
58061,
96364,
125,
877
] | 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... | [
86,
31,
364,
59,
181,
94,
13,
58,
142,
15,
8,
168
] | 12 | true | Domain | Forkhead-associated (FHA) domain | Forkhead-associated (FHA) domain | FHA_dom | 1 |
IPR000254 | 254 | Cellulose-binding domain | CBD | Domain | 19,434 | false | false | This entry represents the cellulose-binding domain (CBD) in monooxygenase, exoglucanase, cellobiohydrolase, endoglucanases and related enzymes, mainly from fungi. The microbial degradation of cellulose and xylans requires several types of enzymes, such as endoglucanases ( ), cellobiohydrolases ( ) (exoglucanases), or x... | [
"GO:0030248",
"GO:0005975",
"GO:0005576"
] | [
"cellulose binding",
"carbohydrate metabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00734",
"PS00562",
"PS51164",
"SM00236"
] | [
"CBM_1",
"CBM1_1",
"CBM1_2",
"fCBD"
] | [
18891,
14991,
18446,
18754
] | 4 | [
"EC",
"PROSITEDOC"
] | [
"3.2.1",
"PDOC00486"
] | [
"EC:3.2.1",
"PROSITEDOC:PDOC00486"
] | 2 | [
"1az6",
"1azh",
"1azj",
"1azk",
"1cbh",
"2cbh",
"2mwj",
"2mwk",
"4bmf",
"4qi4",
"4qi5",
"4qi6",
"4qi7",
"5mrj",
"5x34",
"5x35",
"5x36",
"5x37",
"5x38",
"5x39",
"5x3c",
"6mvi",
"6mvj",
"6q8m",
"6q8n",
"6rv8",
"7yhf",
"7yhg",
"7yhh",
"7yhi"
] | 30 | [
"PUB00003608"
] | [
"1886523"
] | [
"Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteroidota",
"Ectocarpus siliculosus virus 1 (isolate New Zealand/Kaikoura/1988)",
"Eukaryota",
"viral metagenome"
] | [
8,
1,
19424,
1
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
22,
1
] | 2 | true | Domain | Cellulose-binding domain | Cellulose-binding domain | CBD | 1 |
IPR000256 | 256 | Influenza A virus NS1 protein | NS1A | Family | 58,019 | false | false | NS1 is a homodimeric RNA-binding protein found in influenza virus that is required for viral replication. NS1 binds polyA tails of mRNA keeping them in the nucleus. NS1 inhibits pre-mRNA splicing by tightly binding to a specific stem-bulge of U6 snRNA [ ]. | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00600"
] | [
"Flu_NS1"
] | [
58019
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1012",
"R-HSA-1169408",
"R-HSA-168276",
"R-HSA-168315",
"R-HSA-168888",
"R-HSA-169131",
"R-HSA-192823",
"R-HSA-5213460",
"R-HSA-9686347",
"R-HSA-9833482"
] | [
"GP:GenProp1012",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-168276",
"REACTOME:R-HSA-168315",
"REACTOME:R-HSA-168888",
"REACTOME:R-HSA-169131",
"REACTOME:R-HSA-192823",
"REACTOME:R-HSA-5213460",
"REACTOME:R-HSA-9686347",
"REACTOME:R-HSA-9833482"
] | 10 | [
"1ail",
"1ns1",
"2gx9",
"2kkz",
"2n74",
"2rhk",
"2z0a",
"2zko",
"3d6r",
"3ee8",
"3ee9",
"3f5t",
"3kwg",
"3kwi",
"3l4q",
"3m5r",
"3m8a",
"3o9q",
"3o9r",
"3o9s",
"3o9t",
"3o9u",
"3oa9",
"3p31",
"3p38",
"3p39",
"3rvc",
"4opa",
"4oph",
"5bxz",
"5by1",
"5h5n"... | 48 | [
"PUB00003954"
] | [
"9360601"
] | [
"A novel RNA-binding motif in influenza A virus non-structural protein 1."
] | [
1997
] | 1 | [
"IPR004208"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Influenza A virus"
] | [
8,
58011
] | 2 | [] | [] | 0 | true | Family | Influenza A virus NS1 protein | Influenza A virus NS1 protein | NS1A | 6 |
IPR000257 | 257 | Uroporphyrinogen decarboxylase (URO-D) | Uroporphyrinogen_deCOase | Domain | 35,785 | false | false | Uroporphyrinogen decarboxylase (URO-D), the fifth enzyme of the haem biosynthetic pathway, catalyses the sequential decarboxylation of the four acetyl side chains of uroporphyrinogen to yield coproporphyrinogen [ ]. URO-D deficiency is responsible for the human genetic diseases familial porphyria cutanea tarda (fPCT) a... | [
"GO:0004853",
"GO:0006779"
] | [
"uroporphyrinogen decarboxylase activity",
"porphyrin-containing compound biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE",
"PROSITE"
] | [
"PF01208",
"PS00906",
"PS00907"
] | [
"URO-D",
"UROD_1",
"UROD_2"
] | [
35782,
24217,
22996
] | 3 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.1.37",
"GenProp1447",
"PWY-5531",
"PWY-7159",
"PWY-7766",
"PDOC00705",
"R-DDI-189451",
"R-DME-189451",
"R-DRE-189451",
"R-HSA-189451",
"R-MMU-189451",
"R-RNO-189451",
"R-SCE-189451",
"R-SPO-189451"
] | [
"EC:4.1.1.37",
"GP:GenProp1447",
"METACYC:PWY-5531",
"METACYC:PWY-7159",
"METACYC:PWY-7766",
"PROSITEDOC:PDOC00705",
"REACTOME:R-DDI-189451",
"REACTOME:R-DME-189451",
"REACTOME:R-DRE-189451",
"REACTOME:R-HSA-189451",
"REACTOME:R-MMU-189451",
"REACTOME:R-RNO-189451",
"REACTOME:R-SCE-189451",
... | 14 | [
"1j93",
"1jph",
"1jpi",
"1jpk",
"1r3q",
"1r3r",
"1r3s",
"1r3t",
"1r3v",
"1r3w",
"1r3y",
"1uro",
"2eja",
"2inf",
"2q6z",
"2q71",
"3cyv",
"3gvq",
"3gvr",
"3gvv",
"3gvw",
"3gw0",
"3gw3",
"4ay7",
"4ay8",
"4exq",
"4wsh",
"4zr8",
"6w2o"
] | 29 | [
"PUB00001413",
"PUB00006407"
] | [
"1576986",
"9564029"
] | [
"Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene sequence and evidence for two conserved glycines essential for enzymatic activity.",
"Crystal structure of human uroporphyrinogen decarboxylase."
] | [
1992,
1998
] | 2 | [] | [
"IPR006360"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
978,
27205,
6432,
2,
1168
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
9,
1,
3,
1,
18,
2,
1,
6,
3,
1,
1,
48
] | 12 | true | Domain | Uroporphyrinogen decarboxylase (URO-D) | Uroporphyrinogen decarboxylase (URO-D) | Uroporphyrinogen_deCOase | 2 |
IPR000258 | 258 | Bacterial ice-nucleation, octamer repeat | Ice_nucleatn | Repeat | 310 | false | false | Certain Gram-negative bacteria express proteins that enable them to promote nucleation of ice at relatively high temperatures (above -5C) [ , ]. These proteins are localised at the outer membrane surface and can cause frost damage to many plants. The primary structure of the proteins contains a highly repetitive domain... | [
"GO:0009279"
] | [
"cell outer membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE"
] | [
"PF00818",
"PR00327",
"PS00314"
] | [
"Ice_nucleation",
"ICENUCLEATN",
"ICE_NUCLEATION"
] | [
281,
216,
274
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00283"
] | [
"PROSITEDOC:PDOC00283"
] | 1 | [] | 0 | [
"PUB00001519",
"PUB00005501"
] | [
"8224607",
"1366726"
] | [
"Bacterial ice nucleation: significance and molecular basis.",
"Detection of bacteria by transduction of ice nucleation genes."
] | [
1993,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"uncultured Caudovirales phage"
] | [
295,
11,
4
] | 3 | [] | [] | 0 | true | Repeat | Bacterial ice-nucleation, octamer repeat | Bacterial ice-nucleation, octamer repeat | Ice_nucleatn | 4 |
IPR000259 | 259 | Fimbrial-type adhesion domain | Adhesion_dom_fimbrial | Domain | 41,225 | false | false | This domain is found in bacterial proteins that are involved in regulation of length and mediation of adhesion of fimbriae. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers, that enable bacteria to colonize the epithelium of specific host or... | [
"GO:0007155",
"GO:0009289"
] | [
"cell adhesion",
"pilus"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00419"
] | [
"Fimbrial"
] | [
41225
] | 1 | [
"REACTOME"
] | [
"R-HSA-9638630"
] | [
"REACTOME:R-HSA-9638630"
] | 1 | [
"1kiu",
"1klf",
"1n0l",
"1n12",
"1pdk",
"1qun",
"1ze3",
"2jmr",
"2jty",
"2m5g",
"2n7h",
"2uy6",
"2uy7",
"2w07",
"3bwu",
"3jwn",
"3rfz",
"3sqb",
"4dwh",
"4j3o",
"4xo9",
"4xoa",
"4xob",
"4xod",
"4xoe",
"5afo",
"5cyl",
"5flu",
"5jqi",
"5jr4",
"5lp9",
"5mts"... | 78 | [
"PUB00006174",
"PUB00006175",
"PUB00006176"
] | [
"10066469",
"1681580",
"2890081"
] | [
"Fimbriae-mediated host-pathogen cross-talk.",
"Bacterial adhesion: genetics, biogenesis, and role in pathogenesis of fimbrial adhesins of Escherichia coli.",
"Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae."
] | [
1998,
1991,
1987
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
41145,
57,
23
] | 3 | [
"Escherichia coli (strain K12)"
] | [
28
] | 1 | true | Domain | Fimbrial-type adhesion domain | Fimbrial-type adhesion domain | Adhesion_dom_fimbrial | 7 |
IPR000260 | 260 | NADH:ubiquinone oxidoreductase chain 4, N-terminal | NADH4_N | Domain | 31,967 | false | false | This entry represents the N-terminal domain of ADH:ubiquinone oxidoreductase (complex I) chain 4. This domain is found upstream of . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01059"
] | [
"Oxidored_q5_N"
] | [
31967
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"7.1.1.2",
"PWY-3781",
"PWY-4302",
"PWY-5083",
"PWY-6692",
"R-BTA-5419276",
"R-BTA-611105",
"R-BTA-6799198",
"R-DME-5419276",
"R-DME-611105",
"R-DME-6799198",
"R-DRE-611105",
"R-GGA-5419276",
"R-GGA-611105",
"R-GGA-6799198",
"R-HSA-5419276",
"R-HSA-611105",
"R-HSA-6799198",
"R-MM... | [
"EC:7.1.1.2",
"METACYC:PWY-3781",
"METACYC:PWY-4302",
"METACYC:PWY-5083",
"METACYC:PWY-6692",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DRE-611105",
"REACTOME:R-GGA-541... | 27 | [
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtc",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6q9b",
"6qa9",
"6qbx",
"6qc2",
"6qc3",
"6qc4",
"6qc5",
"6qc6",
"6qc7",
"6qc8",
"6qc9",
"6qca",
"6qcf",
"6zka",
"6zkb",
"6zkc",
"6zkd",
"6zke",
"6zkf"... | 209 | [
"PUB00005074",
"PUB00043561",
"PUB00045437"
] | [
"1470679",
"10940377",
"18394423"
] | [
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.",
"Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)."
] | [
1992,
2000,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
116,
3554,
28130,
167
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
21,
703,
11,
10
] | 5 | true | Domain | NADH:ubiquinone oxidoreductase chain 4, N-terminal | NADH:ubiquinone oxidoreductase chain 4, N-terminal | NADH4_N | 8 |
IPR000261 | 261 | EH domain | EH_dom | Domain | 34,841 | false | false | The EH (for Eps15 Homology) domain is a protein-protein interaction module of approximately 95 residues which was originally identified as a repeated sequence present in three copies at the N terminus of the tyrosine kinase substrates Eps15 and Eps15R [ , ]. The EH domain was subsequently found in several proteins impl... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF12763",
"PS50031",
"SM00027",
"cd00052"
] | [
"EH",
"EH",
"EH",
"EH"
] | [
33666,
33998,
32289,
31834
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50031",
"R-BTA-983231",
"R-DDI-193648",
"R-DDI-8856825",
"R-DDI-8856828",
"R-DDI-9013148",
"R-DDI-9013406",
"R-DDI-9013408",
"R-DDI-9013420",
"R-HSA-182971",
"R-HSA-193648",
"R-HSA-3928662",
"R-HSA-416482",
"R-HSA-6807004",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-8875360",
"R... | [
"PROSITEDOC:PDOC50031",
"REACTOME:R-BTA-983231",
"REACTOME:R-DDI-193648",
"REACTOME:R-DDI-8856825",
"REACTOME:R-DDI-8856828",
"REACTOME:R-DDI-9013148",
"REACTOME:R-DDI-9013406",
"REACTOME:R-DDI-9013408",
"REACTOME:R-DDI-9013420",
"REACTOME:R-HSA-182971",
"REACTOME:R-HSA-193648",
"REACTOME:R-HS... | 57 | [
"1c07",
"1eh2",
"1f8h",
"1ff1",
"1fi6",
"1iq3",
"1q80",
"1qjt",
"2jq6",
"2jxc",
"2kff",
"2kfg",
"2kfh",
"2kgr",
"2khn",
"2ksp",
"2mx7",
"2qpt",
"2scp",
"3fia",
"4cid",
"5mtv",
"5mvf",
"6yet",
"6yeu",
"6yig",
"7sox"
] | 27 | [
"PUB00006280",
"PUB00006290",
"PUB00007075",
"PUB00007076",
"PUB00007077",
"PUB00007078",
"PUB00007079",
"PUB00007080",
"PUB00007081",
"PUB00007082",
"PUB00007084"
] | [
"1339314",
"7689153",
"7568168",
"11911876",
"9397678",
"10021353",
"9303539",
"9822599",
"9721102",
"10757979",
"11389591"
] | [
"Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast.",
"eps15, a novel tyrosine kinase substrate, exhibits transforming activity.",
"A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution.",
"The Eps15 homology (EH) doma... | [
1992,
1993,
1995,
2002,
1997,
1999,
1997,
1998,
1998,
2000,
2001
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
139,
34688,
9
] | 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... | [
22,
15,
95,
20,
72,
62,
4,
11,
61,
5,
5,
84
] | 12 | true | Domain | EH domain | EH domain | EH_dom | 3 |
IPR000262 | 262 | FMN-dependent dehydrogenase | FMN-dep_DH | Domain | 50,522 | false | false | A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown [ , , ] to be structurally related. These enzymes are: Lactate dehydrogenase ( ), which consists of a dehydrogenase domain and a haem-binding domain called cytochrome b2 and which catalyses the convers... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01070"
] | [
"FMN_dh"
] | [
50522
] | 1 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1662",
"GenProp1747",
"R-BTA-390918",
"R-BTA-9033241",
"R-DDI-389661",
"R-DDI-390918",
"R-DDI-9033241",
"R-HSA-389661",
"R-HSA-390918",
"R-HSA-9033241",
"R-MMU-389661",
"R-MMU-390918",
"R-MMU-9033241",
"R-RNO-389661",
"R-RNO-390918",
"R-RNO-9033241"
] | [
"GP:GenProp1662",
"GP:GenProp1747",
"REACTOME:R-BTA-390918",
"REACTOME:R-BTA-9033241",
"REACTOME:R-DDI-389661",
"REACTOME:R-DDI-390918",
"REACTOME:R-DDI-9033241",
"REACTOME:R-HSA-389661",
"REACTOME:R-HSA-390918",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-389661",
"REACTOME:R-MMU-390918",
"RE... | 16 | [
"1al7",
"1al8",
"1fcb",
"1gox",
"1gyl",
"1huv",
"1kbi",
"1kbj",
"1lco",
"1ldc",
"1ltd",
"1p0k",
"1p0n",
"1p4c",
"1p5b",
"1qcw",
"1sze",
"1szf",
"1szg",
"1tb3",
"1vcf",
"1vcg",
"2a7n",
"2a7p",
"2a85",
"2cdh",
"2du2",
"2e77",
"2j6x",
"2nli",
"2nzl",
"2oz0"... | 128 | [
"PUB00000334",
"PUB00002533",
"PUB00002617",
"PUB00002664"
] | [
"2271624",
"2644287",
"2324094",
"1939137"
] | [
"Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.",
"The active site of spinach glycolate oxidase.",
"L-lactate 2-monooxygenase from Myco... | [
1990,
1989,
1990,
1991
] | 4 | [] | [
"IPR037396"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
731,
28680,
20587,
524
] | 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",... | [
35,
2,
7,
4,
1,
4,
6,
4,
10,
4,
1,
1,
42
] | 13 | true | Domain | FMN-dependent dehydrogenase | FMN-dependent dehydrogenase | FMN-dep_DH | 6 |
IPR000263 | 263 | Geminivirus AR1/BR1 coat protein | GV_A/BR1_coat | Family | 9,502 | false | false | Geminiviruses are characterised by a genome of circular single-stranded DNA encapsidated in twinned (geminate) quasi-isometric particles, from which the group derives its name [ ]. Most geminiviruses can be divided into 2 subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous p... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF00844",
"PR00223"
] | [
"Gemini_coat",
"GEMCOATARBR1"
] | [
9502,
7678
] | 2 | [] | [] | [] | 0 | [
"6ek5",
"6f2s",
"8ugq",
"8uh4"
] | 4 | [
"PUB00001145",
"PUB00003169"
] | [
"16453696",
"9191917"
] | [
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"Maize streak virus coat protein binds single- and double-stranded DNA in vitro."
] | [
1986,
1997
] | 2 | [] | [
"IPR000143",
"IPR000650",
"IPR001530"
] | 0 | 3 | 0 | [
"Actinomycetes",
"Mesangiospermae",
"Viruses"
] | [
4,
61,
9437
] | 3 | [] | [] | 0 | true | Family | Geminivirus AR1/BR1 coat protein | Geminivirus AR1/BR1 coat protein | GV_A/BR1_coat | 5 |
IPR000264 | 264 | ALB/AFP/VDB | ALB/AFP/VDB | Family | 2,921 | false | false | A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [ , , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs - its main function ... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR00802",
"PTHR11385"
] | [
"SERUMALBUMIN",
""
] | [
2838,
2920
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00186",
"R-BTA-381426",
"R-BTA-8957275",
"R-HSA-114608",
"R-HSA-159418",
"R-HSA-189451",
"R-HSA-189483",
"R-HSA-196791",
"R-HSA-2168880",
"R-HSA-381426",
"R-HSA-8957275",
"R-HSA-8964058",
"R-HSA-9707564",
"R-HSA-9749641",
"R-HSA-9757110",
"R-HSA-9793528",
"R-MMU-114608",
"R-MM... | [
"PROSITEDOC:PDOC00186",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-159418",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-2168880",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8... | 44 | [
"1ao6",
"1bj5",
"1bke",
"1bm0",
"1e78",
"1e7a",
"1e7b",
"1e7c",
"1e7e",
"1e7f",
"1e7g",
"1e7h",
"1e7i",
"1gni",
"1gnj",
"1h9z",
"1ha2",
"1hk1",
"1hk2",
"1hk3",
"1hk4",
"1hk5",
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9",
"1n5u",
"1o9x",
"1tf0",
"1uor"... | 242 | [
"PUB00000582",
"PUB00002857",
"PUB00003407",
"PUB00004128"
] | [
"2423133",
"7517938",
"2481749",
"1630489"
] | [
"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.",
"Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.",
"Amphibian albumins as memb... | [
1986,
1994,
1989,
1992
] | 4 | [] | [
"IPR000213",
"IPR021177"
] | 0 | 2 | 0 | [
"Bacteria",
"Opisthokonta"
] | [
2,
2919
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
23,
13,
27
] | 4 | true | Family | ALB/AFP/VDB | ALB/AFP/VDB | ALB/AFP/VDB | 3 |
IPR000265 | 265 | Prostanoid EP3 receptor | Prostglndn_EP3_rcpt | Family | 1,002 | 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:0004957",
"GO:0007186",
"GO:0016020"
] | [
"prostaglandin E receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00582"
] | [
"PRSTNOIDEP3R"
] | [
1002
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"342",
"R-BTA-391908",
"R-BTA-418594",
"R-HSA-391908",
"R-HSA-418594",
"R-MMU-391908",
"R-MMU-418594",
"R-RNO-391908",
"R-RNO-418594",
"R-SSC-391908",
"R-SSC-418594"
] | [
"IUPHAR:342",
"REACTOME:R-BTA-391908",
"REACTOME:R-BTA-418594",
"REACTOME:R-HSA-391908",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-391908",
"REACTOME:R-RNO-418594",
"REACTOME:R-SSC-391908",
"REACTOME:R-SSC-418594"
] | 11 | [
"6ak3",
"7wu9",
"8gdc"
] | 3 | [
"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 | [
"IPR001244"
] | [
"IPR000154",
"IPR001481",
"IPR003304"
] | 1 | 3 | 0 | [
"Gnathostomata"
] | [
1002
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
8,
3,
12
] | 4 | true | Family | Prostanoid EP3 receptor | Prostanoid EP3 receptor | Prostglndn_EP3_rcpt | 2 |
IPR000266 | 266 | Small ribosomal subunit protein uS17 | Ribosomal_uS17 | Family | 35,778 | false | false | This family includes small ribosomal subunit protein uS17 (formerly known as 30S ribosomal protein S17 and 40S ribosomal protein S11) [ ]. The ribosomal proteins catalyse ribosome assembly and stabilise the rRNA, tuning the structure of the ribosome for optimal function. Evidence suggests that, in prokaryotes, the pept... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00366",
"PR00973",
"PTHR10744"
] | [
"Ribosomal_S17",
"RIBOSOMALS17",
""
] | [
35606,
31703,
33534
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00055",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"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-BTA-9937383",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72695"... | [
"PROSITEDOC:PDOC00055",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"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-97595... | 94 | [
"1eg0",
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1rip",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo",
"1xmq",
"1xnq"... | 1,918 | [
"PUB00003381",
"PUB00004907",
"PUB00080279"
] | [
"9281425",
"9371771",
"24524803"
] | [
"A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data.",
"Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique.",
"A new system for naming ribosomal proteins."
] | [
1997,
1997,
2014
] | 3 | [] | [
"IPR019984",
"IPR028333",
"IPR039193"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
908,
23485,
10927,
458
] | 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",... | [
19,
1,
3,
16,
1,
7,
10,
2,
16,
14,
3,
3,
24
] | 13 | true | Family | Small ribosomal subunit protein uS17 | Small ribosomal subunit protein uS17 | Ribosomal_uS17 | 9 |
IPR000268 | 268 | DNA-directed RNA polymerase subunit RPABC5/Rpb10 | RPABC5/Rpb10 | Family | 4,968 | false | false | In eukaryotes, there are three different forms of DNA-dependent RNA polymerases ( ) transcribing different sets of genes. Each class of RNA polymerase is an assemblage of ten to twelve different polypeptides. In archaebacteria, there is generally a single form of RNA polymerase which also consists of an oligomeric asse... | [
"GO:0003677",
"GO:0003899",
"GO:0006351"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER"
] | [
"MF_00250",
"PF01194",
"PIRSF005653",
"PTHR23431"
] | [
"RNApol_arch_Rpo10",
"RNA_pol_N",
"RNA_pol_N/8_sub",
""
] | [
4002,
4967,
3816,
4816
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"PDOC00856",
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-5250924",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73762",... | [
"EC:2.7.7.6",
"PROSITEDOC:PDOC00856",
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",... | 217 | [
"1ef4",
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 546 | [
"PUB00002250",
"PUB00004866",
"PUB00015096",
"PUB00015097",
"PUB00059148"
] | [
"8045907",
"7597027",
"10841539",
"11831707",
"19419240"
] | [
"Halobacterial S9 operon contains two genes encoding proteins homologous to subunits shared by eukaryotic RNA polymerases I, II, and III.",
"Transcription in archaea: similarity to that in eucarya.",
"Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum."... | [
1994,
1995,
2000,
1995,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
878,
2,
3752,
63,
273
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
1,
2,
1,
1,
1,
7,
4,
1,
1,
10
] | 12 | true | Family | DNA-directed RNA polymerase subunit RPABC5/Rpb10 | DNA-directed RNA polymerase subunit RPABC5/Rpb10 | RPABC5/Rpb10 | 6 |
IPR000269 | 269 | Copper amine oxidase | Cu_amine_oxidase | Family | 19,599 | false | false | This entry represents a family of copper amine oxidase enzymes. Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing ( ) and copper-containing ( ). Copp... | [
"GO:0005507",
"GO:0008131",
"GO:0048038",
"GO:0009308"
] | [
"copper ion binding",
"primary methylamine oxidase activity",
"quinone binding",
"amine metabolic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PANTHER"
] | [
"PTHR10638"
] | [
""
] | [
19599
] | 1 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3",
"1.4.3.21",
"PDOC00895",
"R-BTA-211945",
"R-HSA-211945",
"R-HSA-6798695",
"R-MMU-211945",
"R-MMU-6798695",
"R-RNO-211945",
"R-RNO-6798695",
"R-SSC-211945",
"R-SSC-6798695"
] | [
"EC:1.4.3",
"EC:1.4.3.21",
"PROSITEDOC:PDOC00895",
"REACTOME:R-BTA-211945",
"REACTOME:R-HSA-211945",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-211945",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-211945",
"REACTOME:R-RNO-6798695",
"REACTOME:R-SSC-211945",
"REACTOME:R-SSC-6798695"
] | 12 | [
"1a2v",
"1av4",
"1avk",
"1avl",
"1d6u",
"1d6y",
"1d6z",
"1dyu",
"1ekm",
"1iqx",
"1iqy",
"1iu7",
"1ivu",
"1ivv",
"1ivw",
"1ivx",
"1jrq",
"1ksi",
"1lvn",
"1n9e",
"1oac",
"1pu4",
"1qaf",
"1qak",
"1qal",
"1rjo",
"1rky",
"1sih",
"1sii",
"1spu",
"1tu5",
"1ui7"... | 151 | [
"PUB00005251",
"PUB00010699",
"PUB00010700",
"PUB00010701",
"PUB00016565"
] | [
"8591028",
"9048544",
"9405045",
"8805580",
"10576737"
] | [
"Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.",
"Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.",
"Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the... | [
1995,
1997,
1997,
1996,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"metagenomes"
] | [
58,
3635,
15835,
2,
69
] | 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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",... | [
46,
2,
1,
12,
19,
2,
28,
13,
2,
14
] | 10 | true | Family | Copper amine oxidase | Copper amine oxidase | Cu_amine_oxidase | 3 |
IPR000271 | 271 | Large ribosomal subunit protein bL34 | Ribosomal_bL34 | Family | 24,435 | false | false | Ribosomal protein L34 (also known as Large ribosomal subunit protein bL34) is one of the proteins from the large subunit of the ribosome from bacteria and eukaryotes. It is a small basic protein of 44 to 51 amino-acid residues [ ]. L34 belongs to a family of ribosomal proteins which, on the basis of sequence similariti... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00391",
"PF00468",
"PTHR14503",
"TIGR01030"
] | [
"Ribosomal_bL34",
"Ribosomal_L34",
"",
"rpmH_bact"
] | [
22546,
24425,
23115,
23548
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00626",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
] | [
"PROSITEDOC:PDOC00626",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:... | 14 | [
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xbp",
"2ftc",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3j3v",
"3j3w",
"3j5l",
"3j6b",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu"... | 1,270 | [
"PUB00004412",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"1461740",
"11297922",
"11290319",
"11114498"
] | [
"Nucleotide sequence of the Borrelia burgdorferi rpmH gene encoding ribosomal protein L34.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1992,
2001,
2001,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
20100,
4087,
1,
247
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
9,
2,
3,
1,
2,
1,
1,
5,
2,
1,
1,
8
] | 12 | true | Family | Large ribosomal subunit protein bL34 | Large ribosomal subunit protein bL34 | Ribosomal_bL34 | 7 |
IPR000272 | 272 | Ion-transport regulator, FXYD family | Ion-transport_regulator_FXYD | Family | 4,225 | false | false | The FXYD protein family contains at least seven members in mammals [ ]. Two other family members that are not obvious orthologs of any identified mammalian FXYD protein exist in zebrafish. All these proteins share a signature sequence of six conserved amino acids comprising the FXYD motif in the NH2-terminus, and two g... | [
"GO:0099106",
"GO:0043269",
"GO:0016020"
] | [
"ion channel regulator activity",
"regulation of monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF02038"
] | [
"ATP1G1_PLM_MAT8"
] | [
4225
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC01014",
"R-BTA-5578775",
"R-BTA-936837",
"R-HSA-5578775",
"R-HSA-936837",
"R-HSA-9679191",
"R-MMU-5578775",
"R-MMU-936837",
"R-RNO-5578775",
"R-RNO-936837",
"R-SSC-5578775",
"R-SSC-936837"
] | [
"PROSITEDOC:PDOC01014",
"REACTOME:R-BTA-5578775",
"REACTOME:R-BTA-936837",
"REACTOME:R-HSA-5578775",
"REACTOME:R-HSA-936837",
"REACTOME:R-HSA-9679191",
"REACTOME:R-MMU-5578775",
"REACTOME:R-MMU-936837",
"REACTOME:R-RNO-5578775",
"REACTOME:R-RNO-936837",
"REACTOME:R-SSC-5578775",
"REACTOME:R-SS... | 12 | [
"2jo1",
"2jp3",
"2mkv",
"2zxe",
"3a3y",
"3b8e",
"3kdp",
"3n23",
"3wgu",
"3wgv",
"4hqj",
"4hyt",
"4res",
"4ret",
"4xe5",
"5avq",
"5avr",
"5avs",
"5avt",
"5avu",
"5avv",
"5avw",
"5avx",
"5avy",
"5avz",
"5aw0",
"5aw1",
"5aw2",
"5aw3",
"5aw4",
"5aw5",
"5aw6"... | 78 | [
"PUB00010252",
"PUB00102458",
"PUB00102497"
] | [
"12538882",
"21228272",
"16288923"
] | [
"FXYD proteins: new tissue-specific regulators of the ubiquitous Na,K-ATPase.",
"FXYD proteins stabilize Na,K-ATPase: amplification of specific phosphatidylserine-protein interactions.",
"Correlation of gene and protein structures in the FXYD family proteins."
] | [
2003,
2011,
2005
] | 3 | [] | [
"IPR047281",
"IPR047282",
"IPR047283",
"IPR047284"
] | 0 | 4 | 0 | [
"Vertebrata",
"bird metagenome"
] | [
4223,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
35,
25,
22,
33
] | 4 | true | Family | Ion-transport regulator, FXYD family | Ion-transport regulator, FXYD family | Ion-transport_regulator_FXYD | 4 |
IPR000274 | 274 | Adenylate cyclase, class-I | Adenylate_cyclase_1 | Family | 3,695 | false | false | Adenylate cyclase is the enzyme responsible for the synthesis of cAMP from ATP. On the basis of sequence similarity, it has been proposed that there are three different classes of adenylate cyclases [ , ]. Class I cyclases are found in enterobacteria and related Gram-negative bacteria. | [
"GO:0004016",
"GO:0006171"
] | [
"adenylate cyclase activity",
"cAMP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF001444",
"PTHR38760"
] | [
"Adenylate_cycl",
""
] | [
3086,
3695
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"4.6.1.1",
"PDOC00837"
] | [
"EC:4.6.1.1",
"PROSITEDOC:PDOC00837"
] | 2 | [] | 0 | [
"PUB00000015",
"PUB00004943"
] | [
"8418825",
"7863008"
] | [
"Phylogeny of adenylyl cyclases.",
"Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes."
] | [
1993,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3645,
4,
46
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Adenylate cyclase, class-I | Adenylate cyclase, class-I | Adenylate_cyclase_1 | 5 |
IPR000275 | 275 | Coagulin | Coagulin | Family | 10 | false | false | This entry represents a family of coagulogen proteins from arthropods. Coagulogen is a gel-forming protein of hemolymph that hinders the spread of invaders by immobilising them [ , ]. The protein contains a single 175- residue polypeptide chain; this is cleaved after Arg-18 and Arg-46 by a clotting enzyme contained in ... | [
"GO:0042381",
"GO:0005576"
] | [
"hemolymph coagulation",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS"
] | [
"PF02035",
"PIRSF002379",
"PR00763"
] | [
"Coagulin",
"Coagulogen",
"COAGULIN"
] | [
10,
4,
10
] | 3 | [] | [] | [] | 0 | [
"1aoc"
] | 1 | [
"PUB00002323",
"PUB00002327",
"PUB00014988",
"PUB00023387"
] | [
"6469947",
"3905780",
"15170505",
"9003754"
] | [
"The amino acid sequence of coagulogen isolated from southeast Asian horseshoe crab, Tachypleus gigas.",
"The complete amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Carcinoscorpius rotundicauda.",
"Structure and function of coagulogen, a clottable protein in horseshoe crabs.",
... | [
1984,
1985,
2004,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Limulidae"
] | [
10
] | 1 | [] | [] | 0 | true | Family | Coagulin | Coagulin | Coagulin | 3 |
IPR000276 | 276 | G protein-coupled receptor, rhodopsin-like | GPCR_Rhodpsn | Family | 606,170 | false | false | This entry represents the G protein-coupled receptor, rhodopsin-like family. The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. ... | [
"GO:0004930",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PROSITE",
"SMART"
] | [
"PF00001",
"PR00237",
"PS00237",
"SM01381"
] | [
"7tm_1",
"GPCRRHODOPSN",
"G_PROTEIN_RECEP_F1_1",
"7TM_GPCR_Srsx"
] | [
432817,
556773,
414944,
132443
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00210",
"R-BTA-2187335",
"R-BTA-2453902",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-373076",
"R-BTA-375276",
"R-BTA-375281",
"R-BTA-376176",
"R-BTA-380095",
"R-BTA-380108",
"R-BTA-388479",
"R-BTA-389397",
"R-BTA-390648",
"R-BTA-390651",
"R-BTA-390696",
"R-BTA-391906",
"R-BTA-39... | [
"PROSITEDOC:PDOC00210",
"REACTOME:R-BTA-2187335",
"REACTOME:R-BTA-2453902",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-373076",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-375281",
"REACTOME:R-BTA-376176",
"REACTOME:R-BTA-380095",
"REACTOME:R-BTA-380108",
"REACTOME:R-BTA-... | 360 | [
"1f88",
"1gzm",
"1hll",
"1hof",
"1hzx",
"1jfp",
"1l9h",
"1ln6",
"1u19",
"2g87",
"2hpy",
"2i35",
"2i36",
"2i37",
"2j4y",
"2ks9",
"2ksa",
"2ksb",
"2lnl",
"2ped",
"2r4r",
"2r4s",
"2rh1",
"2vt4",
"2x72",
"2y00",
"2y01",
"2y02",
"2y03",
"2y04",
"2ycw",
"2ycx"... | 1,721 | [
"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 | [] | [
"IPR000018",
"IPR000025",
"IPR000142",
"IPR000204",
"IPR000356",
"IPR000371",
"IPR000405",
"IPR000499",
"IPR000503",
"IPR000586",
"IPR000611",
"IPR000670",
"IPR000723",
"IPR000725",
"IPR000820",
"IPR000826",
"IPR000921",
"IPR000929",
"IPR000995",
"IPR001069",
"IPR001350",
"... | 0 | 84 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
14,
605329,
819,
8
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
296,
1394,
251,
2220,
3001,
2854
] | 6 | true | Family | G protein-coupled receptor, rhodopsin-like | G protein-coupled receptor, rhodopsin-like | GPCR_Rhodpsn | 7 |
IPR000277 | 277 | Cys/Met metabolism, pyridoxal phosphate-dependent enzyme | Cys/Met-Metab_PyrdxlP-dep_enz | Family | 98,587 | false | false | A number of pyridoxal-dependent enzymes involved in the metabolism of cysteine, homocysteine and methionine have been shown [ , ] to be evolutionary related. These enzymes are proteins of about 400 amino-acid residues. The pyridoxal-P group is attached to a lysine residue located in the central section of these enzymes... | [
"GO:0030170",
"GO:0019346"
] | [
"pyridoxal phosphate binding",
"transsulfuration"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF01053",
"PIRSF001434",
"PTHR11808",
"cd00614"
] | [
"Cys_Met_Meta_PP",
"CGS",
"",
"CGS_like"
] | [
98273,
86005,
58540,
73724
] | 4 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1238",
"GenProp1507",
"GenProp1654",
"GenProp1685",
"PDOC00677",
"R-CEL-1614558",
"R-CEL-1614603",
"R-DDI-1614558",
"R-DDI-1614603",
"R-HSA-1614558",
"R-HSA-1614603",
"R-HSA-2408508",
"R-MMU-1614558",
"R-MMU-1614603",
"R-MTU-937250",
"R-RNO-1614558",
"R-RNO-1614603",
"R-SCE... | [
"GP:GenProp1238",
"GP:GenProp1507",
"GP:GenProp1654",
"GP:GenProp1685",
"PROSITEDOC:PDOC00677",
"REACTOME:R-CEL-1614558",
"REACTOME:R-CEL-1614603",
"REACTOME:R-DDI-1614558",
"REACTOME:R-DDI-1614603",
"REACTOME:R-HSA-1614558",
"REACTOME:R-HSA-1614603",
"REACTOME:R-HSA-2408508",
"REACTOME:R-MM... | 21 | [
"1cl1",
"1cl2",
"1cs1",
"1e5e",
"1e5f",
"1gc0",
"1gc2",
"1i41",
"1i43",
"1i48",
"1ibj",
"1n8p",
"1pff",
"1pg8",
"1qgn",
"1ukj",
"1y4i",
"2cb1",
"2ctz",
"2fq6",
"2gqn",
"2nmp",
"2o7c",
"2rfv",
"3acz",
"3aej",
"3ael",
"3aem",
"3aen",
"3aeo",
"3aep",
"3cog"... | 165 | [
"PUB00002177",
"PUB00005650",
"PUB00006322",
"PUB00035504",
"PUB00035505",
"PUB00035506",
"PUB00035507",
"PUB00035508",
"PUB00082323"
] | [
"1577698",
"8511966",
"7748903",
"15581583",
"8690703",
"15189147",
"17109392",
"16763894",
"26662839"
] | [
"Cloning and characterization of the CYS3 (CYI1) gene of Saccharomyces cerevisiae.",
"Physical localization of yeast CYS3, a gene whose product resembles the rat gamma-cystathionase and Escherichia coli cystathionine gamma-synthase enzymes.",
"Pyridoxal phosphate-dependent enzymes.",
"Reaction specificity in ... | [
1992,
1993,
1995,
2005,
1995,
2004,
2006,
2006,
2016
] | 9 | [] | [
"IPR006233",
"IPR006234",
"IPR006235",
"IPR006237",
"IPR006238",
"IPR011821",
"IPR044639"
] | 0 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1525,
76067,
19457,
20,
1518
] | 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",... | [
28,
5,
10,
2,
2,
1,
1,
7,
27,
5,
8,
4,
40
] | 13 | true | Family | Cys/Met metabolism, pyridoxal phosphate-dependent enzyme | Cys/Met metabolism, pyridoxal phosphate-dependent enzyme | Cys/Met-Metab_PyrdxlP-dep_enz | 4 |
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