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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000552 | 552 | Large ribosomal subunit protein eL42 | Ribosomal_eL44 | Family | 6,974 | false | false | A number of eukaryotic and archaeal ribosomal proteins can be grouped on the basis of sequence similarities. This protein family has been named eL42 (also known as L44e or L36A) and includes mammalian L44 [ ], Trypanosoma brucei and fungal L44, Caenorhabditis elegans rpl-36.A, and Haloarcula marismortui LA [ ]. eL42 an... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PROSITE",
"PANTHER"
] | [
"MF_01476",
"PF00935",
"PS01172",
"PTHR10369"
] | [
"Ribosomal_L44e",
"Ribosomal_L44",
"RIBOSOMAL_L44E",
""
] | [
1394,
6915,
5849,
6433
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00902",
"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:PDOC00902",
"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... | 70 | [
"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"... | 586 | [
"PUB00000650",
"PUB00001108",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00162566"
] | [
"8504167",
"3396452",
"11297922",
"11290319",
"11114498",
"30306205"
] | [
"HL35e and HLA: primary structure of two very basic and cysteine-rich ribosomal proteins from Haloarcula marismortui.",
"Primary structure of rat ribosomal protein L36a.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal... | [
1993,
1988,
2001,
2001,
2000,
2018
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
902,
2,
6036,
34
] | 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... | [
5,
1,
1,
3,
8,
4,
1,
12,
6,
2,
1,
13
] | 12 | true | Family | Large ribosomal subunit protein eL42 | Large ribosomal subunit protein eL42 | Ribosomal_eL44 | 7 |
IPR000554 | 554 | Small ribosomal subunit protein eS7 | Ribosomal_eS7 | Family | 6,488 | false | false | A number of eukaryotic ribosomal proteins can be grouped on the basis of sequence similarities [ ]. This entry represents the small ribosomal subunit protein eS7 (also referred to as S7) [ , , , ]. These proteins have about 200 amino acids. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in al... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF01251",
"PTHR11278"
] | [
"Ribosomal_S7e",
""
] | [
6478,
6270
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00730",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-6791226",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
... | [
"PROSITEDOC:PDOC00730",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827"... | 106 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r"... | 584 | [
"PUB00004431",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00059102",
"PUB00080279",
"PUB00110894",
"PUB00151110"
] | [
"8371989",
"11297922",
"11290319",
"11114498",
"22096102",
"24524803",
"23636399",
"34516797"
] | [
"Sequence of a cDNA from the mosquito Anopheles gambiae encoding a homologue of human ribosomal protein S7.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The structure of the eukaryotic ribosome at 3.0 ... | [
1993,
2001,
2001,
2000,
2011,
2014,
2013,
2021
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
6483
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
1,
3,
4,
2,
1,
11,
8,
2,
1,
24
] | 12 | true | Family | Small ribosomal subunit protein eS7 | Small ribosomal subunit protein eS7 | Ribosomal_eS7 | 7 |
IPR000555 | 555 | JAB1/MPN/MOV34 metalloenzyme domain | JAMM/MPN+_dom | Domain | 54,067 | false | false | This domain is known as the MPN domain [ ], PAD-1-like domain [ ], JABP1 domain [ ] or JAMM domain [ ]. Proteins with this domain include proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. They are metalloenzymes that function as the ubiquitin isopept... | [
"GO:0005515",
"GO:0008233",
"GO:0008237"
] | [
"protein binding",
"peptidase activity",
"metallopeptidase activity"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF01398",
"SM00232"
] | [
"JAB",
"JAB_MPN"
] | [
45707,
46155
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1169091",
"R-BTA-1234176",
"R-BTA-1236978",
"R-BTA-156827",
"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-450408",
"R-BT... | [
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1236978",
"REACTOME:R-BTA-156827",
"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",
"REACTOME:R-BTA-... | 413 | [
"2kcq",
"2kks",
"2o95",
"2o96",
"2og4",
"2p87",
"2p8r",
"2znr",
"2znv",
"3j8b",
"3j8c",
"3jb9",
"3jck",
"3jcm",
"3jco",
"3jcp",
"3jcr",
"3rzu",
"3rzv",
"3sbg",
"3zef",
"4bgd",
"4cr2",
"4cr3",
"4cr4",
"4d10",
"4d18",
"4e0q",
"4f7o",
"4i43",
"4ilg",
"4jxe"... | 337 | [
"PUB00005480",
"PUB00019876",
"PUB00034476",
"PUB00057398",
"PUB00057434",
"PUB00069770",
"PUB00069779"
] | [
"9644972",
"10369758",
"16859499",
"20838651",
"12183636",
"22970855",
"17209031"
] | [
"The PCI domain: a common theme in three multiprotein complexes.",
"Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer.",
"The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.",
"... | [
1998,
1999,
2006,
2010,
2002,
2012,
2007
] | 7 | [
"IPR037518"
] | [
"IPR044098"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
383,
6361,
46965,
118,
240
] | 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... | [
65,
9,
26,
17,
74,
36,
8,
56,
49,
4,
7,
125
] | 12 | true | Domain | JAB1/MPN/MOV34 metalloenzyme domain | JAB1/MPN/MOV34 metalloenzyme domain | JAMM/MPN+_dom | 5 |
IPR000556 | 556 | Glycoside hydrolase, 48F | Glyco_hydro_48F | Family | 1,860 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0008810",
"GO:0030245"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"cellulase activity",
"cellulose catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF02011",
"PR00844"
] | [
"Glyco_hydro_48",
"GLHYDRLASE48"
] | [
1860,
1776
] | 2 | [
"CAZY"
] | [
"GH48"
] | [
"CAZY:GH48"
] | 1 | [
"1f9d",
"1f9o",
"1fae",
"1fbo",
"1fbw",
"1fce",
"1g9g",
"1g9j",
"1l1y",
"1l2a",
"2qno",
"4el8",
"4fus",
"4jjj",
"4l0g",
"4l6x",
"4txt",
"4xwl",
"4xwm",
"4xwn",
"5bv9",
"5cvy",
"5vma",
"5yj6",
"6d5d",
"7kw6",
"8zu1"
] | 27 | [
"PUB00000145",
"PUB00004870",
"PUB00005266"
] | [
"7612247",
"7624375",
"8535779"
] | [
"celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995,
1995
] | 3 | [] | [
"IPR048103"
] | 0 | 1 | 0 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"uncultured organism"
] | [
1654,
5,
148,
53
] | 4 | [] | [] | 0 | true | Family | Glycoside hydrolase, 48F | Glycoside hydrolase, 48F | Glyco_hydro_48F | 4 |
IPR000557 | 557 | Calponin repeat | Calponin_repeat | Repeat | 8,991 | false | false | Calponin [ , ] is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin MgATPase activity. Calponin is a basic protein ... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE"
] | [
"PF00402",
"PS01052",
"PS51122"
] | [
"Calponin",
"CALPONIN_1",
"CALPONIN_2"
] | [
8935,
7766,
8828
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00808",
"R-BTA-114608",
"R-BTA-6798695",
"R-HSA-114608",
"R-HSA-6798695",
"R-HSA-8950505",
"R-HSA-9927432",
"R-MMU-114608",
"R-MMU-6798695",
"R-RNO-114608"
] | [
"PROSITEDOC:PDOC00808",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8950505",
"REACTOME:R-HSA-9927432",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-114608"
] | 10 | [] | 0 | [
"PUB00000772",
"PUB00000985",
"PUB00002836",
"PUB00003078",
"PUB00003620"
] | [
"8015377",
"8130072",
"8144658",
"7929573",
"7935620"
] | [
"The identification of NP25: a novel protein that is differentially expressed by neuronal subpopulations.",
"Calponin: thin filament-linked regulation of smooth muscle contraction.",
"Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle.",
"The Caenorhabditis elegan... | [
1994,
1993,
1994,
1994,
1994
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadota",
"bird metagenome"
] | [
8987,
3,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
15,
4,
33,
19,
25
] | 6 | true | Repeat | Calponin repeat | Calponin repeat | Calponin_repeat | 3 |
IPR000559 | 559 | Formate-tetrahydrofolate ligase, FTHFS | Formate_THF_ligase | Family | 21,203 | false | false | Formate--tetrahydrofolate ligase ( ) (formyltetrahydrofolate synthetase) (FTHFS) is one of the enzymes participating in the transfer of one-carbon units, an essential element of various biosynthetic pathways. FTHFS catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrof... | [
"GO:0004329",
"GO:0005524"
] | [
"formate-tetrahydrofolate ligase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP",
"PFAM",
"CDD"
] | [
"MF_01543",
"PF01268",
"cd00477"
] | [
"FTHFS",
"FTHFS",
"FTHFS"
] | [
16533,
21203,
16140
] | 3 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4.3",
"GenProp1216",
"GenProp1613",
"PWY-1722",
"PWY-2161",
"PWY-2201",
"PWY-3841",
"PWY-8303",
"PDOC00595",
"R-BTA-196757",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:6.3.4.3",
"GP:GenProp1216",
"GP:GenProp1613",
"METACYC:PWY-1722",
"METACYC:PWY-2161",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-8303",
"PROSITEDOC:PDOC00595",
"REACTOME:R-BTA-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-... | 16 | [
"1eg7",
"1fp7",
"1fpm",
"3do6",
"3qus",
"4ioj",
"4iok",
"4iol",
"4iom",
"4jim",
"4jjk",
"4jjz",
"4jki",
"5a4j",
"5a5g",
"7c11",
"7xzn",
"7xzo",
"7xzp"
] | 19 | [
"PUB00000324",
"PUB00002486",
"PUB00006525",
"PUB00021607"
] | [
"2200509",
"2836393",
"10747779",
"11087401"
] | [
"Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum.",
"Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase.",
"The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moor... | [
1990,
1988,
2000,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes code 15 clade",
"Eukaryota",
"unclassified sequences"
] | [
182,
11637,
2,
8683,
699
] | 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... | [
8,
1,
7,
5,
21,
7,
2,
4,
16,
2,
2,
5
] | 12 | true | Family | Formate-tetrahydrofolate ligase, FTHFS | Formate-tetrahydrofolate ligase, FTHFS | Formate_THF_ligase | 6 |
IPR000560 | 560 | Histidine phosphatase superfamily, clade-2 | His_Pase_clade-2 | Family | 47,231 | false | false | This entry represents the clade 2 of histidine phosphatase superfamily. Included in this group are: Escherichia coli pH 2.5 acid phosphatase (gene appA). E. coli glucose-1-phosphatase ( ) (gene agp). Yeast constitutive and repressible acid phosphatases (genes PHO3 and PHO5). Schizosaccharomyces pombe acid phosphatase (... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF00328",
"cd07061"
] | [
"His_Phos_2",
"HP_HAP_like"
] | [
47127,
39285
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"3.1.3",
"GenProp1229",
"GenProp1395",
"GenProp1574",
"GenProp1692",
"PDOC00538",
"R-BTA-1483166",
"R-BTA-1855167",
"R-BTA-6798695",
"R-CEL-1855167",
"R-CEL-6798695",
"R-DDI-1483166",
"R-DDI-1855231",
"R-DDI-6798695",
"R-DME-1855167",
"R-DRE-1971475",
"R-HSA-1483166",
"R-HSA-185516... | [
"EC:3.1.3",
"GP:GenProp1229",
"GP:GenProp1395",
"GP:GenProp1574",
"GP:GenProp1692",
"PROSITEDOC:PDOC00538",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-1855167",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-1855167",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-1483166",
"REACTOME:R-DDI-1855231",
... | 34 | [
"1cvi",
"1dkl",
"1dkm",
"1dkn",
"1dko",
"1dkp",
"1dkq",
"1ihp",
"1nd5",
"1nd6",
"1nt4",
"1qfx",
"1qwo",
"1rpa",
"1rpt",
"1sk8",
"1sk9",
"1ska",
"1skb",
"2gfi",
"2hpa",
"2wnh",
"2wni",
"2wu0",
"3it0",
"3it1",
"3it2",
"3it3",
"3k4p",
"3k4q",
"3ntl",
"3zhc"... | 81 | [
"PUB00053493",
"PUB00078599",
"PUB00078604"
] | [
"18092946",
"8387447",
"25132310"
] | [
"The histidine phosphatase superfamily: structure and function.",
"Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger.",
"Fungal phytases: characteristics and amelioration of nutritional quality and growth of non-ruminants."
] | [
2008,
1993,
2015
] | 3 | [] | [
"IPR016274",
"IPR037446"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4518,
42700,
7,
6
] | 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",... | [
23,
26,
85,
21,
2,
47,
25,
7,
13,
48,
6,
5,
38
] | 13 | true | Family | Histidine phosphatase superfamily, clade-2 | Histidine phosphatase superfamily, clade-2 | His_Pase_clade-2 | 9 |
IPR000562 | 562 | Fibronectin type II domain | FN_type2_dom | Domain | 17,420 | false | false | Fibronectin is a multi-domain glycoprotein, found in a soluble form in plasma, and in an insoluble form in loose connective tissue and basement membranes, that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in a number of important functions e.g.... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00040",
"PS00023",
"PS51092",
"SM00059",
"cd00062"
] | [
"fn2",
"FN2_1",
"FN2_2",
"FN2",
"FN2"
] | [
17302,
12308,
17212,
17237,
16122
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00022",
"R-BTA-1433557",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1482788",
"R-BTA-1482801",
"R-BTA-1482839",
"R-BTA-1482922",
"R-BTA-1482925",
"R-BTA-1483166",
"R-BTA-1592389",
"R-BTA-3928665",
"R-BTA-6798695",
"R-BTA-9009391",
"R-GGA-114608",
"R-GGA-1442490",
"R-GGA-1474228",
... | [
"PROSITEDOC:PDOC00022",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1482788",
"REACTOME:R-BTA-1482801",
"REACTOME:R-BTA-1482839",
"REACTOME:R-BTA-1482922",
"REACTOME:R-BTA-1482925",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-1592389",
"REACTOME:... | 158 | [
"1ck7",
"1cxw",
"1e88",
"1e8b",
"1eak",
"1gxd",
"1h8p",
"1j7m",
"1ks0",
"1l6j",
"1pdc",
"1qo6",
"2fn2",
"2v5o",
"2v5p",
"3m7p",
"3mql",
"5ao5",
"5ao6",
"5e4k",
"5e4l",
"5ew6",
"5xts",
"5xtw",
"6inn",
"6ino",
"6inu",
"6inv",
"6ioe",
"6szw",
"6um1",
"6um2"... | 44 | [
"PUB00000084",
"PUB00000461",
"PUB00001346",
"PUB00002483",
"PUB00002562",
"PUB00002776",
"PUB00002849",
"PUB00004209",
"PUB00004633"
] | [
"1323236",
"3606570",
"3780752",
"2834383",
"2373685",
"7683665",
"8294398",
"7753172",
"3031656"
] | [
"Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors.",
"Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin.",
"Complete primary structure of bovine plasma fibronectin.",
"H-ras oncogene-... | [
1992,
1987,
1986,
1988,
1990,
1993,
1994,
1995,
1987
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae sp. ChoanoV1",
"Pseudomonadota",
"metagenomes"
] | [
17368,
1,
47,
4
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
44,
49,
47
] | 4 | true | Domain | Fibronectin type II domain | Fibronectin type II domain | FN_type2_dom | 3 |
IPR000563 | 563 | Flagellar assembly protein FliH | Flag_FliH | Family | 4,809 | false | false | Many flagellar proteins are exported by a flagellum-specific export pathway. Attempts have been made to characterise the apparatus responsible for this process, by designing assays to screen for mutants with export defects. Experiments involving filament removal from temperature-sensitive flagellar mutants of Salmonell... | [
"GO:0003774",
"GO:0071973",
"GO:0009288"
] | [
"cytoskeletal motor activity",
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01003"
] | [
"FLGFLIH"
] | [
4809
] | 1 | [] | [] | [] | 0 | [
"5b0o"
] | 1 | [
"PUB00002143"
] | [
"1646201"
] | [
"Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4745,
25,
39
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar assembly protein FliH | Flagellar assembly protein FliH | Flag_FliH | 6 |
IPR000565 | 565 | DNA topoisomerase, type IIA, subunit B | Topo_IIA_B | Family | 58,316 | false | false | Type IIA topoisomerases together manage chromosome integrity and topology in cells. Topoisomerase II (called gyrase in bacteria) primarily introduces negative supercoils into DNA. In bacteria, topoisomerase II consists of two polypeptide subunits, gyrA and gyrB, which form a heterotetramer: (BA)2. In most eukaryotes, t... | [
"GO:0003677",
"GO:0003918",
"GO:0005524",
"GO:0006265"
] | [
"DNA binding",
"DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity",
"ATP binding",
"DNA topological change"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR01159"
] | [
"DNAGYRASEB"
] | [
58316
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"5.6.2.2",
"R-HSA-9638771",
"R-HSA-9913143"
] | [
"EC:5.6.2.2",
"REACTOME:R-HSA-9638771",
"REACTOME:R-HSA-9913143"
] | 3 | [
"1aj6",
"1ei1",
"1kij",
"2xco",
"2xcq",
"2xcr",
"2zjt",
"3cwv",
"3g75",
"3g7b",
"3ig0",
"3m4i",
"3nuh",
"3zkb",
"3zkd",
"3zm7",
"4bae",
"4duh",
"4em7",
"4emv",
"4gee",
"4gfn",
"4ggl",
"4hxw",
"4hz5",
"4i3h",
"4juo",
"4k4o",
"4ksg",
"4ksh",
"4ktn",
"4lp0"... | 116 | [
"PUB00005437",
"PUB00016842",
"PUB00020793",
"PUB00020794",
"PUB00020795",
"PUB00020802",
"PUB00020803"
] | [
"7770916",
"11395412",
"12596227",
"12042765",
"7980433",
"16023670",
"8982450"
] | [
"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",
"Structure and function of type II DNA topoisomerases.",
"The structural basis for substrate... | [
1995,
2001,
2003,
2002,
1994,
2005,
1996
] | 7 | [
"IPR001241"
] | [
"IPR005740",
"IPR011557"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
598,
55598,
31,
1167,
922
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
1,
3,
7
] | 4 | true | Family | DNA topoisomerase, type IIA, subunit B | DNA topoisomerase, type IIA, subunit B | Topo_IIA_B | 6 |
IPR000566 | 566 | Lipocalin/cytosolic fatty-acid binding domain | Lipocln_cytosolic_FA-bd_dom | Domain | 39,370 | false | false | This entry represents the lipocalin/cytosolic fatty-acid binding domain of a group of proteins that belong to the calycin superfamily. Proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids share limited regions of sequence homology and a common tertiary structure architect... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF00061",
"PF08212"
] | [
"Lipocalin",
"Lipocalin_2"
] | [
25246,
14260
] | 2 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1236",
"GenProp1321",
"GenProp1603",
"GenProp1703",
"R-BTA-163560",
"R-BTA-2162123",
"R-BTA-5362517",
"R-BTA-5365859",
"R-BTA-6798695",
"R-CEL-159418",
"R-CEL-163560",
"R-CEL-189483",
"R-CEL-2453902",
"R-CEL-5362517",
"R-CEL-5365859",
"R-CEL-6798695",
"R-CEL-975634",
"R-GGA... | [
"GP:GenProp1236",
"GP:GenProp1321",
"GP:GenProp1603",
"GP:GenProp1703",
"REACTOME:R-BTA-163560",
"REACTOME:R-BTA-2162123",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-5365859",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-159418",
"REACTOME:R-CEL-163560",
"REACTOME:R-CEL-189483",
"REACTOME:R-CEL-... | 73 | [
"1a18",
"1a2d",
"1a3y",
"1a57",
"1ab0",
"1acd",
"1adl",
"1ael",
"1alb",
"1aqb",
"1b0o",
"1b4m",
"1b56",
"1b8e",
"1bbp",
"1beb",
"1bj7",
"1blr",
"1bm5",
"1brp",
"1brq",
"1bso",
"1bsq",
"1bsy",
"1bwy",
"1cbi",
"1cbq",
"1cbr",
"1cbs",
"1cj5",
"1crb",
"1dc9"... | 1,052 | [
"PUB00000205",
"PUB00001391",
"PUB00001451",
"PUB00001491",
"PUB00002777",
"PUB00003778",
"PUB00004508",
"PUB00004787",
"PUB00004981",
"PUB00005013",
"PUB00005238",
"PUB00005340",
"PUB00005379"
] | [
"1834059",
"2026162",
"7514123",
"3622999",
"8486691",
"1707134",
"3064105",
"1608945",
"2217163",
"7684291",
"8069623",
"3238752",
"1723819"
] | [
"Mouse oncogene protein 24p3 is a member of the lipocalin protein family.",
"Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin.",
"Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins.",
"Hom... | [
1991,
1991,
1994,
1987,
1993,
1991,
1988,
1992,
1990,
1993,
1993,
1988,
1991
] | 13 | [] | [
"IPR000463",
"IPR047202"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
9045,
30199,
41,
85
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
5,
44,
11,
1,
88,
121,
9,
167,
8
] | 10 | true | Domain | Lipocalin/cytosolic fatty-acid binding domain | Lipocalin/cytosolic fatty-acid binding domain | Lipocln_cytosolic_FA-bd_dom | 8 |
IPR000568 | 568 | ATP synthase, F0 complex, subunit A | ATP_synth_F0_asu | Family | 82,463 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [
"GO:0015078",
"GO:0015986",
"GO:0045259"
] | [
"proton transmembrane transporter activity",
"proton motive force-driven ATP synthesis",
"proton-transporting ATP synthase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS",
"NCBIFAM"
] | [
"MF_01393",
"PF00119",
"PR00123",
"TIGR01131"
] | [
"ATP_synth_a_bact",
"ATP-synt_A",
"ATPASEA",
"ATP_synt_6_or_A"
] | [
43298,
82269,
76379,
77986
] | 4 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0128",
"PDOC00420",
"R-BTA-163210",
"R-BTA-5419276",
"R-BTA-8949613",
"R-BTA-9837999",
"R-CEL-163210",
"R-CEL-5419276",
"R-CEL-8949613",
"R-CEL-9837999",
"R-DDI-9837999",
"R-DME-163210",
"R-DME-5419276",
"R-DME-8949613",
"R-DME-9837999",
"R-DRE-163210",
"R-DRE-8949613",
"R-... | [
"GP:GenProp0128",
"PROSITEDOC:PDOC00420",
"REACTOME:R-BTA-163210",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-8949613",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-163210",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-8949613",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-1632... | 40 | [
"1c17",
"5ara",
"5are",
"5arh",
"5ari",
"5dn6",
"5fij",
"5fik",
"5fil",
"5lqx",
"5lqy",
"5lqz",
"5t4o",
"5t4p",
"5t4q",
"6b2z",
"6b8h",
"6cp3",
"6cp5",
"6cp6",
"6cp7",
"6f36",
"6fkf",
"6fkh",
"6fki",
"6j54",
"6j5a",
"6j5i",
"6j5j",
"6j5k",
"6n2d",
"6n2y"... | 234 | [
"PUB00009752",
"PUB00020603",
"PUB00020604",
"PUB00020607",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"11309608",
"15473999",
"15078220",
"16045926",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Structure of the F1-binding... | [
2001,
2004,
2004,
2005,
2010,
2008,
1992,
1998
] | 8 | [] | [
"IPR045082",
"IPR045083"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Pseudomonas phage PPAT",
"Stenosarchaea group",
"unclassified sequences"
] | [
25183,
56682,
1,
28,
569
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
8,
2,
18,
1,
1502,
9,
2,
9,
7,
1,
1,
7
] | 13 | true | Family | ATP synthase, F0 complex, subunit A | ATP synthase, F0 complex, subunit A | ATP_synth_F0_asu | 3 |
IPR000569 | 569 | HECT domain | HECT_dom | Domain | 88,037 | false | false | The HECT (Homologous to the E6-AP Carboxyl Terminus) domain is an around 350 amino acids motif that has been identified in proteins that all belong to a particular E3 ubiquitin-protein ligase family [ ]. HECT domain containing proteins accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester ... | [
"GO:0004842"
] | [
"ubiquitin-protein transferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00632",
"PS50237",
"SM00119",
"cd00078"
] | [
"HECT",
"HECT",
"HECTc",
"HECTc"
] | [
84753,
86660,
77627,
58681
] | 4 | [
"EC",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REAC... | [
"2.3.2.26",
"GenProp1754",
"PWY-7511",
"PDOC50237",
"R-BTA-983168",
"R-CEL-1253288",
"R-CEL-2672351",
"R-CEL-4641258",
"R-CEL-8948751",
"R-CEL-9013406",
"R-CEL-9013420",
"R-CEL-983168",
"R-DME-1169408",
"R-DME-1253288",
"R-DME-201451",
"R-DME-2122948",
"R-DME-2173788",
"R-DME-21737... | [
"EC:2.3.2.26",
"GP:GenProp1754",
"METACYC:PWY-7511",
"PROSITEDOC:PDOC50237",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-1253288",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-8948751",
"REACTOME:R-CEL-9013406",
"REACTOME:R-CEL-9013420",
"REACTOME:R-CEL-983168",
"REACTOME... | 125 | [
"1c4z",
"1d5f",
"1nd7",
"1zvd",
"2oni",
"2xbb",
"2xbf",
"3g1n",
"3h1d",
"3jvz",
"3jw0",
"3olm",
"3pt3",
"3tug",
"4bbn",
"4be8",
"4lcd",
"4y07",
"5c7j",
"5c7m",
"5c91",
"5hpk",
"5hpl",
"5hps",
"5hpt",
"5lp8",
"5tj7",
"5tj8",
"5tjq",
"5w87",
"5xmc",
"6fx4"... | 106 | [
"PUB00004858",
"PUB00018224",
"PUB00081573"
] | [
"7708685",
"9182527",
"9153201"
] | [
"A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase.",
"Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases.",
"Physical interaction between specific E2 and Hect E3 enzymes determines functio... | [
1995,
1997,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
149,
87854,
16,
18
] | 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... | [
35,
29,
317,
72,
144,
104,
11,
33,
127,
5,
7,
192
] | 12 | true | Domain | HECT domain | HECT domain | HECT_dom | 6 |
IPR000571 | 571 | Zinc finger, CCCH-type | Znf_CCCH | Domain | 188,778 | false | false | This entry represents C-x8-C-x5-C-x3-H (CCCH) type Zinc finger (Znf) domains. Proteins containing CCCH Znf domains include Znf proteins from eukaryotes involved in cell cycle or growth phase-related regulation, e.g. human TIS11B (butyrate response factor 1, also known as mRNA decay activator protein ZFP36L1), a probabl... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00642",
"PF25542",
"PS50103",
"SM00356"
] | [
"zf-CCCH",
"zf-CCCH_12",
"ZF_C3H1",
"ZnF_C3H1"
] | [
88762,
1730,
188137,
133906
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-159231",
"R-BTA-159236",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72187",
"R-BTA-72203",
"R-BTA-73856",
"R-BTA-77595",
"R-BTA-9629569",
"R-CEL-198323",
"R-CEL-450385",
"R-CEL-450513",
"R-CEL-8948751",
"R-CEL-983168",
"R-DDI-9629569",
"R-DME-159231",
"R-DME-159236",
"R-DME-450385... | [
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72165",
"REACTOME:R-BTA-72187",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-73856",
"REACTOME:R-BTA-77595",
"REACTOME:R-BTA-9629569",
"REACTOME:R-CEL-198323",
"REACTOME:R-CEL-450385",
"REACTOME:R-CEL-450513",... | 168 | [
"1m9o",
"1rgo",
"2cqe",
"2d9m",
"2d9n",
"2e5s",
"2fc6",
"2rhk",
"2rpp",
"3d2n",
"3d2q",
"3d2s",
"3jb9",
"3tp2",
"3u1l",
"3u1m",
"3u9g",
"4c3b",
"4c3d",
"4c3e",
"4cs7",
"4cs8",
"4cs9",
"4csa",
"4cyk",
"4ii1",
"4txa",
"4yh8",
"5elh",
"5elk",
"5gm6",
"5gmk"... | 125 | [
"PUB00005945",
"PUB00005946",
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"9703499",
"10330172",
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin.",
"Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA.",
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fi... | [
1998,
1999,
2002,
2007,
2005,
2005,
1999,
2001
] | 8 | [] | [
"IPR041367",
"IPR054361",
"IPR054429",
"IPR057674"
] | 0 | 4 | 0 | [
"Bacteria",
"Eukaryota",
"Pyrobaculum ferrireducens",
"Viruses",
"metagenomes"
] | [
39,
188029,
1,
646,
63
] | 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... | [
359,
54,
243,
157,
198,
190,
17,
167,
237,
10,
14,
567
] | 12 | true | Domain | Zinc finger, CCCH-type | Zinc finger, CCCH-type | Znf_CCCH | 4 |
IPR000572 | 572 | Oxidoreductase, molybdopterin-binding domain | OxRdtase_Mopterin-bd_dom | Domain | 46,050 | false | false | A number of different eukaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [ ] to share a few regions of sequence similarity. These enzymes include xanthine dehydrogenase ( ), aldehyde oxidase ( ), nitrate reductase ( ), and sulphite oxidase ( ). The multidomain redox enzyme NAD(P)H... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00174"
] | [
"Oxidored_molyb"
] | [
46050
] | 1 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.8.5.-",
"GenProp1554",
"PDOC00484",
"R-DME-1614517",
"R-HSA-1614517",
"R-MMU-1614517",
"R-RNO-1614517"
] | [
"EC:1.8.5.-",
"GP:GenProp1554",
"PROSITEDOC:PDOC00484",
"REACTOME:R-DME-1614517",
"REACTOME:R-HSA-1614517",
"REACTOME:R-MMU-1614517",
"REACTOME:R-RNO-1614517"
] | 7 | [
"1ogp",
"1sox",
"1xdq",
"1xdy",
"2a99",
"2a9a",
"2a9b",
"2a9c",
"2a9d",
"2bih",
"2bii",
"2blf",
"2bpb",
"2c9x",
"2ca3",
"2ca4",
"2xts",
"3hbg",
"3hbp",
"3hbq",
"3hc2",
"3r18",
"3r19",
"4pw3",
"4pw9",
"5k3x",
"5wa0",
"6y0k",
"7kom",
"7kos",
"7kou",
"7rkb"... | 33 | [
"PUB00000608",
"PUB00005356",
"PUB00007725"
] | [
"2015248",
"2204158",
"9428520"
] | [
"Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains.",
"Functional domains of assimilatory nitrate reductases and nitrite reductases.",
"Molecular basis of sulfite oxidase deficiency from the structure of sulfite o... | [
1991,
1990,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
1279,
34808,
9451,
2,
510
] | 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",... | [
17,
2,
4,
1,
1,
3,
1,
3,
13,
3,
27
] | 11 | true | Domain | Oxidoreductase, molybdopterin-binding domain | Oxidoreductase, molybdopterin-binding domain | OxRdtase_Mopterin-bd_dom | 6 |
IPR000573 | 573 | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | AconitaseA/IPMdHydase_ssu_swvl | Domain | 74,024 | false | false | This entry represents the 'swivel' domain found at the C-terminal of eukaryotic mAcn, cAcn/IPR1 and IRP2, and bacterial AcnA. This domain has a three layer β/β/α structure, and in cytosolic Acn is known to rotate between the cAcn and IRP1 forms of the enzyme. This domain is also found in the small subunit of isopropylm... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF00694",
"PF27512"
] | [
"Aconitase_C",
"LeuD"
] | [
73974,
17541
] | 2 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"4.2.1",
"4.2.1.33",
"R-BTA-71403",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-389542",
"R-CEL-71403",
"R-CEL-917937",
"R-CEL-9837999",
"R-CEL-9854311",
"R-DDI-389542",
"R-DDI-71403",
"R-DDI-917937",
"R-DDI-9837999",
"R-DDI-9854311",
"R-HSA-1268020",
"R-HSA-389542",
"R-HSA-71403",
... | [
"EC:4.2.1",
"EC:4.2.1.33",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-389542",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-917937",
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9854311",
"REACTOME:R-DDI-389542",
"REACTOME:R-DDI-71403",
"REACTOME:R-DD... | 39 | [
"1aco",
"1ami",
"1amj",
"1b0j",
"1b0k",
"1b0m",
"1c96",
"1c97",
"1fgh",
"1nis",
"1nit",
"1v7l",
"2b3x",
"2b3y",
"2hcu",
"2pkp",
"3h5e",
"3h5h",
"3h5j",
"3q3w",
"3sn2",
"3snp",
"3vba",
"5acn",
"6acn",
"6vcd",
"7acn",
"8acn"
] | 28 | [
"PUB00005471",
"PUB00036013",
"PUB00036014",
"PUB00162127"
] | [
"9020582",
"10087914",
"15877277",
"7026530"
] | [
"The aconitase family: three structural variations on a common theme.",
"Moonlighting proteins.",
"Single-gene disorders: what role could moonlighting enzymes play?",
"Wild-type isopropylmalate isomerase in Salmonella typhimurium is composed of two different subunits."
] | [
1997,
1999,
2005,
1981
] | 4 | [] | [
"IPR033940",
"IPR039386",
"IPR044137"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2071,
53102,
17646,
1205
] | 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",... | [
21,
2,
5,
9,
3,
22,
6,
4,
13,
15,
4,
5,
76
] | 13 | true | Domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain | AconitaseA/IPMdHydase_ssu_swvl | 8 |
IPR000574 | 574 | Tymovirus coat protein | Tymo_coat | Domain | 456 | false | false | This signature is found in coat proteins from the related tymoviruses. The coat protein is also known as the virion protein. The virus coat is composed of 180 copies of the coat protein arranged in an icosahedral shell. | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00983"
] | [
"Tymo_coat"
] | [
456
] | 1 | [] | [] | [] | 0 | [
"1auy",
"1ddl",
"1e57",
"1qjz",
"1w39",
"2fz1",
"2fz2",
"2wws",
"2xpj",
"7sqy",
"7sqz"
] | 11 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Riboviria"
] | [
2,
454
] | 2 | [] | [] | 0 | true | Domain | Tymovirus coat protein | Tymovirus coat protein | Tymo_coat | 2 |
IPR000577 | 577 | Carbohydrate kinase, FGGY | Carb_kinase_FGGY | Family | 85,401 | false | false | This entry represents FGGY carbohydrate kinase family. FGGY carbohydrate kinases carry out ATP-dependent phosphorylation on one out of at least nine distinct sugar substrates [ ]. These enzymes include L-ribulokinase ( ) (gene araB); Erythriol kinase ( ) (gene eryA); L-fucolokinase ( ) (gene fucK); gluconokinase ( ) (g... | [
"GO:0016301",
"GO:0005975"
] | [
"kinase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF000538"
] | [
"GlpK"
] | [
85401
] | 1 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"2.7.1.30",
"PWY-4261",
"PDOC00408",
"R-BTA-5661270",
"R-BTA-75109",
"R-CEL-5661270",
"R-CEL-75109",
"R-DDI-75109",
"R-HSA-5661270",
"R-HSA-75109",
"R-MMU-5661270",
"R-MMU-75109",
"R-RNO-5661270",
"R-RNO-75109"
] | [
"EC:2.7.1",
"EC:2.7.1.30",
"METACYC:PWY-4261",
"PROSITEDOC:PDOC00408",
"REACTOME:R-BTA-5661270",
"REACTOME:R-BTA-75109",
"REACTOME:R-CEL-5661270",
"REACTOME:R-CEL-75109",
"REACTOME:R-DDI-75109",
"REACTOME:R-HSA-5661270",
"REACTOME:R-HSA-75109",
"REACTOME:R-MMU-5661270",
"REACTOME:R-MMU-75109... | 15 | [
"1bo5",
"1bot",
"1bu6",
"1bwf",
"1gla",
"1glb",
"1glc",
"1gld",
"1gle",
"1glf",
"1glj",
"1gll",
"1r59",
"1xup",
"2d4w",
"2dpn",
"2itm",
"2nlx",
"2w40",
"2w41",
"2zf5",
"3d7e",
"3ezw",
"3flc",
"3g25",
"3gbt",
"3ge1",
"3gg4",
"3h3n",
"3h3o",
"3h45",
"3h46"... | 74 | [
"PUB00056209",
"PUB00080793"
] | [
"17274596",
"22215998"
] | [
"Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria.",
"The FGGY carbohydrate kinase family: insights into the evolution of functional specificities."
] | [
2007,
2011
] | 2 | [] | [
"IPR005999",
"IPR006000",
"IPR006002",
"IPR006003",
"IPR013450",
"IPR033676",
"IPR037444"
] | 0 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
676,
71523,
12441,
761
] | 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,
3,
23,
11,
6,
12,
15,
1,
6,
33,
7
] | 11 | true | Family | Carbohydrate kinase, FGGY | Carbohydrate kinase, FGGY | Carb_kinase_FGGY | 9 |
IPR000579 | 579 | Cation-transporting P-type ATPase A/B | Cation-trans_P-type_ATPase_A/B | Family | 406 | false | false | P-ATPases (also known as E1-E2 ATPases) ( ) are found in bacteria and in a number of eukaryotic plasma membranes and organelles [ ]. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of ... | [
"GO:0019829",
"GO:0006812",
"GO:0016020"
] | [
"ATPase-coupled monoatomic cation transmembrane transporter activity",
"monoatomic cation transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00940"
] | [
"CATPATPASEA"
] | [
406
] | 1 | [
"EC"
] | [
"7.2.2"
] | [
"EC:7.2.2"
] | 1 | [] | 0 | [
"PUB00009616",
"PUB00020660",
"PUB00084374",
"PUB00160065",
"PUB00160066"
] | [
"9419228",
"16269744",
"25967101",
"37264943",
"37838176"
] | [
"Evolution of substrate specificities in the P-type ATPase superfamily.",
"New findings on evolution of metal homeostasis genes: evidence from comparative genome analysis of bacteria and archaea.",
"CtpA, a putative Mycobacterium tuberculosis P-type ATPase, is stimulated by copper (I) in the mycobacterial plasm... | [
1998,
2005,
2015,
2023,
2023
] | 5 | [
"IPR027256"
] | [] | 1 | 0 | 1 | [
"Actinomycetes"
] | [
406
] | 1 | [] | [] | 0 | true | Family | Cation-transporting P-type ATPase A/B | Cation-transporting P-type ATPase A/B | Cation-trans_P-type_ATPase_A/B | 8 |
IPR000581 | 581 | Dihydroxy-acid/6-phosphogluconate dehydratase, N-terminal | ILV_EDD_N | Domain | 54,864 | false | false | This is the N-terminal domain of Ilv/ED dehydratase protein family which includes dihydroxy-acid/6-phosphogluconate dehydratases, and pentonate dehydratases [ ]. This domain is composed of a β-sheet with four parallel β-strands surrounded by four α-helices and forms a binding site for a [2Fe-2S] cluster and a Mg2+ ion ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00920"
] | [
"ILVD_EDD_N"
] | [
54864
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"4.2.1",
"4.2.1.9",
"GenProp1342",
"GenProp1405",
"GenProp1557",
"GenProp1691",
"PWY-5101",
"PWY-5103",
"PWY-5104",
"PWY-7111",
"PDOC00690"
] | [
"EC:4.2.1",
"EC:4.2.1.9",
"GP:GenProp1342",
"GP:GenProp1405",
"GP:GenProp1557",
"GP:GenProp1691",
"METACYC:PWY-5101",
"METACYC:PWY-5103",
"METACYC:PWY-5104",
"METACYC:PWY-7111",
"PROSITEDOC:PDOC00690"
] | 11 | [
"2gp4",
"5j83",
"5j84",
"5j85",
"5oyn",
"5ym0",
"5ze4",
"6nte",
"6ovt",
"7m3k",
"8ej0",
"8epz",
"8hs0",
"8ikz",
"8imu",
"9evv",
"9ix7",
"9jpi",
"9jsq",
"9l8r"
] | 20 | [
"PUB00001841",
"PUB00002191",
"PUB00086863",
"PUB00159907",
"PUB00159908"
] | [
"8299945",
"1624451",
"23233208",
"29339766",
"28574691"
] | [
"Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from Saccharomyces cerevisiae.",
"Molecular characterization of the Entner-Doudoroff pathway in Escherichia coli: sequence analysis and localization of promoters for the edd-eda operon.",
"Biosynthesis of ethylene glycol in Escherichia coli.",
"Th... | [
1993,
1992,
2013,
2018,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
869,
47095,
5989,
2,
909
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
3,
4,
2,
3,
1,
1,
19
] | 7 | true | Domain | Dihydroxy-acid/6-phosphogluconate dehydratase, N-terminal | Dihydroxy-acid/6-phosphogluconate dehydratase, N-terminal | ILV_EDD_N | 2 |
IPR000582 | 582 | Acyl-CoA-binding protein, ACBP | Acyl-CoA-binding_protein | Domain | 24,105 | false | false | Acyl-CoA-binding protein (ACBP) is a small (10 Kd) protein that binds medium-and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters [ ]. ACBP is also known as diazepam binding inhibitor (DBI) or endozepine (EP) because of its ability to displace diazepam f... | [
"GO:0000062"
] | [
"fatty-acyl-CoA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE",
"CDD"
] | [
"PF00887",
"PR00689",
"PS51228",
"cd00435"
] | [
"ACBP",
"ACOABINDINGP",
"ACB_2",
"ACBP"
] | [
23505,
16605,
23731,
4958
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00686",
"R-BTA-390918",
"R-BTA-77289",
"R-CEL-390918",
"R-CFA-77289",
"R-DDI-77289",
"R-DRE-390918",
"R-DRE-77289",
"R-DRE-8980692",
"R-DRE-9603798",
"R-HSA-390247",
"R-HSA-390918",
"R-HSA-432722",
"R-HSA-77289",
"R-HSA-8980692",
"R-HSA-9013106",
"R-HSA-9033241",
"R-HSA-960379... | [
"PROSITEDOC:PDOC00686",
"REACTOME:R-BTA-390918",
"REACTOME:R-BTA-77289",
"REACTOME:R-CEL-390918",
"REACTOME:R-CFA-77289",
"REACTOME:R-DDI-77289",
"REACTOME:R-DRE-390918",
"REACTOME:R-DRE-77289",
"REACTOME:R-DRE-8980692",
"REACTOME:R-DRE-9603798",
"REACTOME:R-HSA-390247",
"REACTOME:R-HSA-390918... | 39 | [
"1aca",
"1hb6",
"1hb8",
"1hbk",
"1nti",
"1nvl",
"1st7",
"2abd",
"2cb8",
"2cop",
"2cqu",
"2fdq",
"2fj9",
"2lbb",
"2wh5",
"3epy",
"3flv",
"3fp5",
"5h3g",
"5h3i",
"5ijm",
"6kf8",
"7des",
"7fc7",
"7wfs"
] | 25 | [
"PUB00000679",
"PUB00003552",
"PUB00003711",
"PUB00004768",
"PUB00021736",
"PUB00035335"
] | [
"10354522",
"1649940",
"8898349",
"1454809",
"11491287",
"16018771"
] | [
"Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor.",
"Diazepam binding inhibitor (DBI): a peptide with multiple biological actions.",
"A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells.",
"Molecular cloning of the gene for the yea... | [
1999,
1991,
1996,
1992,
2001,
2005
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"metagenomes"
] | [
2920,
21108,
8,
8,
61
] | 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... | [
35,
11,
38,
11,
52,
37,
2,
9,
40,
1,
1,
48
] | 12 | true | Domain | Acyl-CoA-binding protein, ACBP | Acyl-CoA-binding protein, ACBP | Acyl-CoA-binding_protein | 3 |
IPR000584 | 584 | Voltage-dependent calcium channel, L-type, beta subunit | VDCC_L_bsu | Family | 10,700 | false | false | This entry represents the beta subunits found in L-type voltage-gated calcium channels. Co-expression of beta subunit mRNA with alpha-1 subunit mRNA in xenopus oocytes produces increased calcium currents, which are accompanied by a shift in the voltage-dependence of activation to more negative membrane potentials. Conv... | [
"GO:0005245",
"GO:0070588",
"GO:0005891"
] | [
"voltage-gated calcium channel activity",
"calcium ion transmembrane transport",
"voltage-gated calcium channel complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01626"
] | [
"LCACHANNELB"
] | [
10700
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-112308",
"R-BTA-422356",
"R-BTA-5576892",
"R-BTA-5576893",
"R-HSA-112308",
"R-HSA-400042",
"R-HSA-419037",
"R-HSA-422356",
"R-HSA-5576892",
"R-HSA-5576893",
"R-HSA-9662360",
"R-HSA-9856532",
"R-MMU-112308",
"R-MMU-422356",
"R-MMU-5576892",
"R-MMU-5576893",
"R-RNO-112308",
"R... | [
"REACTOME:R-BTA-112308",
"REACTOME:R-BTA-422356",
"REACTOME:R-BTA-5576892",
"REACTOME:R-BTA-5576893",
"REACTOME:R-HSA-112308",
"REACTOME:R-HSA-400042",
"REACTOME:R-HSA-419037",
"REACTOME:R-HSA-422356",
"REACTOME:R-HSA-5576892",
"REACTOME:R-HSA-5576893",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HS... | 20 | [
"1t0h",
"1t0j",
"1t3l",
"1t3s",
"1vyt",
"1vyu",
"1vyv",
"3jbr",
"4dex",
"4dey",
"4zw2",
"5gjv",
"5gjw",
"5v2p",
"5v2q",
"6hw2",
"6jp5",
"6jp8",
"6jpa",
"6jpb",
"7mix",
"7miy",
"7uhf",
"7uhg",
"7vfs",
"7vfu",
"7vfv",
"7vfw",
"7xlq",
"7yg5",
"8dam",
"8e0e"... | 50 | [
"PUB00007090",
"PUB00036034"
] | [
"9153247",
"14657414"
] | [
"Beta subunit heterogeneity in neuronal L-type Ca2+ channels.",
"International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels."
] | [
1997,
2003
] | 2 | [] | [
"IPR005443",
"IPR005444",
"IPR008079"
] | 0 | 3 | 0 | [
"Opisthokonta",
"bird metagenome"
] | [
10699,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
43,
9,
56,
22,
33
] | 6 | true | Family | Voltage-dependent calcium channel, L-type, beta subunit | Voltage-dependent calcium channel, L-type, beta subunit | VDCC_L_bsu | 3 |
IPR000585 | 585 | Hemopexin-like domain | Hemopexin-like_dom | Domain | 22,288 | false | false | Hemopexin ( ) is a serum glycoprotein that binds haem and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation [ ]. Hemopexin prevents haem-mediated oxidative stress. Structurally hemopexin consists of two similar halves of approximately two hundred amino... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd00094"
] | [
"HX"
] | [
22288
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.24",
"PDOC00023",
"R-BTA-1433557",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1592389",
"R-BTA-3928665",
"R-BTA-6798695",
"R-BTA-9009391",
"R-CEL-1442490",
"R-CEL-1474228",
"R-CEL-1592389",
"R-CEL-210991",
"R-CEL-2168880",
"R-CEL-2179392",
"R-CEL-3928665",
"R-CEL-6798695",
"R-CF... | [
"EC:3.4.24",
"PROSITEDOC:PDOC00023",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-3928665",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9009391",
"REACTOME:R-CEL-1442490",
"REACTOME:R-CEL-1474228",
"REACTOME:R-CEL-1592389... | 96 | [
"1ck7",
"1fbl",
"1gen",
"1gxd",
"1hxn",
"1itv",
"1pex",
"1qhu",
"1qjs",
"1rtg",
"1su3",
"2clt",
"2jxy",
"2mqs",
"3ba0",
"3c7x",
"3lp9",
"3oyo",
"4auo",
"4fu4",
"4fvl",
"4g0d",
"4rt6",
"6clz",
"6cm1",
"6o5e",
"7rj9",
"7txr",
"7u68"
] | 29 | [
"PUB00013983",
"PUB00013984",
"PUB00013985"
] | [
"14619953",
"9572850",
"12042069"
] | [
"Structure and evolutionary aspects of matrix metalloproteinases: a brief overview.",
"Characterization of the ligand binding activities of vitronectin: interaction of vitronectin with lipids and identification of the binding domains for various ligands using recombinant domains.",
"Hemopexin: structure, functi... | [
2003,
1998,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Betanudivirus hezeae",
"Eukaryota"
] | [
72,
2,
22214
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
55,
10,
58,
60,
74
] | 6 | true | Domain | Hemopexin-like domain | Hemopexin-like domain | Hemopexin-like_dom | 9 |
IPR000586 | 586 | Somatostatin receptor family | Somatstn_rcpt | Family | 4,796 | false | false | Somatostatin (SST), also known as somatotropin release-inhibiting factor (SRIF), is a hypothalamic hormone, a pancreatic hormone, and a central and peripheral neurotransmitter. Somatostatin has a wide distribution throughout the central nervous system (CNS) as well as in peripheral tissues, for example in the pituitary... | [
"GO:0004994",
"GO:0007186",
"GO:0016020"
] | [
"somatostatin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00246"
] | [
"SOMATOSTATNR"
] | [
4796
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-375276",
"R-BTA-418594",
"R-CFA-375276",
"R-CFA-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-5620922",
"R-MMU-375276",
"R-MMU-418594",
"R-MMU-5620922",
"R-RNO-375276",
"R-RNO-418594",
"R-RNO-5620922",
"R-SSC-375276",
"R-SSC-418594"
] | [
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418594",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-5620922",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-5620922",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-4... | 15 | [
"7t10",
"7t11",
"7ul5",
"7wic",
"7wig",
"7wj5",
"7xat",
"7xau",
"7xav",
"7xmr",
"7xms",
"7xmt",
"7xn9",
"7xna",
"7y24",
"7y26",
"7y27",
"7yac",
"7yae",
"8x8l",
"8x8n",
"8xio",
"8xip",
"8xiq",
"8xir",
"8zbe",
"8zbi",
"8zbj",
"8zcj",
"9ik8",
"9ik9"
] | 31 | [
"PUB00013316",
"PUB00063572",
"PUB00063590",
"PUB00063595",
"PUB00063596",
"PUB00063597",
"PUB00063598",
"PUB00063599",
"PUB00063600",
"PUB00063601",
"PUB00063602",
"PUB00063603",
"PUB00063604",
"PUB00063605"
] | [
"14507421",
"10433861",
"7792934",
"8243278",
"8078491",
"7907795",
"1346068",
"8483934",
"15361490",
"10598790",
"1328199",
"7538774",
"9426226",
"8684611"
] | [
"Somatostatin receptors.",
"Somatostatin and its receptor family.",
"Classification and nomenclature of somatostatin receptors.",
"Tissue distribution of somatostatin receptor subtype messenger ribonucleic acid in the rat.",
"Characterization of cloned human somatostatin receptor SSTR5.",
"Stimulation of ... | [
2003,
1999,
1995,
1993,
1994,
1994,
1992,
1993,
2004,
1999,
1992,
1995,
1997,
1996
] | 14 | [
"IPR000276"
] | [
"IPR001116",
"IPR001184",
"IPR001512",
"IPR001856",
"IPR002074"
] | 1 | 5 | 0 | [
"Bilateria"
] | [
4796
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
20,
8,
9,
12,
15
] | 5 | true | Family | Somatostatin receptor family | Somatostatin receptor family | Somatstn_rcpt | 6 |
IPR000587 | 587 | Creatinase, N-terminal | Creatinase_N | Domain | 51,644 | false | false | Creatinase or creatine amidinohydrolase ( ) catalyses the conversion of creatine and water to sarcosine and urea. The enzyme works as a homodimer, and is induced by choline chloride. Each monomer of creatinase has two clearly defined domains, a small N-terminal domain, and a large C-terminal domain. The structure of th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01321"
] | [
"Creatinase_N"
] | [
51644
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.11.9",
"R-DDI-163125",
"R-HSA-163125",
"R-MMU-163125",
"R-RNO-163125",
"R-SCE-163125",
"R-SSC-163125"
] | [
"EC:3.4.11.9",
"REACTOME:R-DDI-163125",
"REACTOME:R-HSA-163125",
"REACTOME:R-MMU-163125",
"REACTOME:R-RNO-163125",
"REACTOME:R-SCE-163125",
"REACTOME:R-SSC-163125"
] | 7 | [
"1chm",
"1kp0",
"1pv9",
"1wn1",
"1wy2",
"2how",
"2zsg",
"3ctz",
"3i7m",
"3il0",
"3o5v",
"3ooo",
"3ovk",
"3peb",
"3pn9",
"3q6d",
"3qoc",
"4ege",
"4fkc",
"4r60",
"4rgz",
"4s2r",
"4s2t",
"4zng",
"5cde",
"5cdl",
"5cdv",
"5cik",
"5cnx",
"5e2c",
"5fcf",
"5fch"... | 43 | [
"PUB00000379",
"PUB00026792",
"PUB00044073",
"PUB00103861",
"PUB00103862"
] | [
"8471602",
"12136144",
"8146141",
"30536999",
"28179139"
] | [
"Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.",
"Structure of creatine amidinohydrolase from Actinobacillus.",
"Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a co... | [
1993,
2002,
1994,
2019,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1818,
39986,
9007,
2,
831
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
2,
18,
3,
1,
7,
10,
1,
11,
12,
1,
1,
15
] | 13 | true | Domain | Creatinase, N-terminal | Creatinase, N-terminal | Creatinase_N | 6 |
IPR000588 | 588 | Peptidase A3A, cauliflower mosaic virus-type | Pept_A3A | Domain | 408 | false | false | This aspartic peptidase domain is found in viral enzymatic polyproteins. It belongs to MEROPS peptidase family A3, subfamily A3A (cauliflower mosaic virus-type endopeptidase, clan AA). Cauliflower mosaic virus belongs to the Retro-transcribing viruses, which have a double-stranded DNA genome. The genome includes an ope... | [
"GO:0004190",
"GO:0006508"
] | [
"aspartic-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF02160",
"PR00731"
] | [
"Peptidase_A3",
"CAULIMOPTASE"
] | [
408,
209
] | 2 | [
"EC",
"EC"
] | [
"2.7.7.49",
"3.4.23.-"
] | [
"EC:2.7.7.49",
"EC:3.4.23.-"
] | 2 | [] | 0 | [
"PUB00000093",
"PUB00000349",
"PUB00000522",
"PUB00001330",
"PUB00003578",
"PUB00011023",
"PUB00011707",
"PUB00011867",
"PUB00021296",
"PUB00042504",
"PUB00065205",
"PUB00066803",
"PUB00076784",
"PUB00076785",
"PUB00076786"
] | [
"2194475",
"1851433",
"8439290",
"6795036",
"7674916",
"10331925",
"11566868",
"10557305",
"10864493",
"2682266",
"23254940",
"21765428",
"4912600",
"10497172",
"21751400"
] | [
"The structure and function of the aspartic proteinases.",
"Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.",
"Evolutionary families of peptidases.",
"Gastric proteinases--structure, function, evolution and mechanism of action.",
"Families of aspartic peptid... | [
1990,
1991,
1993,
1981,
1995,
1999,
2001,
1999,
2000,
1989,
2013,
2011,
1970,
1999,
2011
] | 15 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caulimoviridae",
"Eukaryota"
] | [
3,
183,
222
] | 3 | [] | [] | 0 | true | Domain | Peptidase A3A, cauliflower mosaic virus-type | Peptidase A3A, cauliflower mosaic virus-type | Pept_A3A | 5 |
IPR000589 | 589 | Small ribosomal subunit protein uS15 | Ribosomal_uS15 | Family | 48,050 | false | false | Small ribosomal subunit protein uS15 is one of the proteins from the small ribosomal subunit. In Escherichia coli, this protein binds to 16S ribosomal RNA and functions at early steps in ribosome assembly. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ ], groups bacterial an... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROSITE",
"SMART",
"CDD"
] | [
"PF00312",
"PS00362",
"SM01387",
"cd00353"
] | [
"Ribosomal_S15",
"RIBOSOMAL_S15",
"Ribosomal_S15",
"Ribosomal_S15p_S13e"
] | [
47872,
41767,
47648,
43052
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00313",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R... | [
"PROSITEDOC:PDOC00313",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827"... | 116 | [
"1a32",
"1ab3",
"1dk1",
"1eg0",
"1f7y",
"1fjg",
"1fka",
"1g1x",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1kuq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1vvj",
"1vy4"... | 1,932 | [
"PUB00004383",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"2263452",
"11297922",
"11290319",
"11114498"
] | [
"Structural and functional analyses of a yeast mitochondrial ribosomal protein homologous to ribosomal protein S15 of Escherichia coli.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
1990,
2001,
2001,
2000
] | 4 | [] | [
"IPR005290",
"IPR023029"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
934,
23257,
23349,
510
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
1,
2,
3,
1,
2,
4,
2,
23,
13,
2,
2,
24
] | 13 | true | Family | Small ribosomal subunit protein uS15 | Small ribosomal subunit protein uS15 | Ribosomal_uS15 | 1 |
IPR000590 | 590 | Hydroxymethylglutaryl-coenzyme A synthase, active site | HMG_CoA_synt_AS | Active_site | 4,676 | false | false | Hydroxymethylglutaryl-CoA synthase ( ) catalyses the condensation of acetyl-CoA with acetoacetyl-CoA to produce HMG-CoA and CoA, the second reaction in the mevalonate-dependent isoprenoid biosynthesis pathway. HMG-CoA synthase contains an important catalytic cysteine residue that acts as a nucleophile in the first step... | [
"GO:0004421",
"GO:0008299"
] | [
"hydroxymethylglutaryl-CoA synthase activity",
"isoprenoid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS01226"
] | [
"HMG_COA_SYNTHASE"
] | [
4676
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"2.3.3.10",
"PWY-6174",
"PWY-7391",
"PWY-7524",
"PWY-7571",
"PWY-8125",
"PWY-922",
"PDOC00942",
"R-BTA-77111",
"R-BTA-9837999",
"R-CEL-191273",
"R-CEL-77111",
"R-CEL-9837999",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-77111",
"R-HSA-9837999",
"R-MMU-191273",
"R-M... | [
"EC:2.3.3.10",
"METACYC:PWY-6174",
"METACYC:PWY-7391",
"METACYC:PWY-7524",
"METACYC:PWY-7571",
"METACYC:PWY-8125",
"METACYC:PWY-922",
"PROSITEDOC:PDOC00942",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-191273",
"REACTOME:R-CEL-77111",
"REACTOME:R-CEL-9837999",
"REACTO... | 32 | [
"2f82",
"2f9a",
"2fa0",
"2fa3",
"2p8u",
"2wya",
"7cqt"
] | 7 | [
"PUB00036056",
"PUB00036057",
"PUB00036058",
"PUB00036059",
"PUB00036060"
] | [
"15498869",
"15546978",
"16640729",
"17128980",
"16245942"
] | [
"3-hydroxy-3-methylglutaryl-CoA synthase intermediate complex observed in \"real-time\".",
"An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthase.",
"Isolation, endocrine regulation and mRNA distribution of the 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMG-S) gene from the pine engrave... | [
2004,
2004,
2006,
2006,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4676
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
1,
3,
1,
4,
9,
1,
8,
7,
1,
1,
11
] | 12 | true | Active_site | Hydroxymethylglutaryl-coenzyme A synthase, active site | Hydroxymethylglutaryl-coenzyme A synthase, active site | HMG_CoA_synt_AS | 3 |
IPR000591 | 591 | DEP domain | DEP_dom | Domain | 46,137 | false | false | This entry represents the DEP (Dishevelled, Egl-10 and Pleckstrin) domain, a globular domain of about 80 residues that is found in over 50 proteins involved in G-protein signalling pathways. It was named after the three proteins it was initially found in: Dishevelled (Dsh and Dvl), which play a key role in the transduc... | [
"GO:0035556"
] | [
"intracellular signal transduction"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00610",
"PS50186",
"SM00049"
] | [
"DEP",
"DEP",
"DEP"
] | [
42603,
42911,
43189
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50186",
"R-BTA-418594",
"R-BTA-6814122",
"R-CEL-201688",
"R-CEL-2028269",
"R-CEL-354192",
"R-CEL-381676",
"R-CEL-392517",
"R-CEL-4086400",
"R-CEL-418594",
"R-CEL-4641258",
"R-CEL-4641262",
"R-CEL-5099900",
"R-CEL-5663220",
"R-CEL-6814122",
"R-CEL-8856825",
"R-CEL-8856828",
"R-... | [
"PROSITEDOC:PDOC50186",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6814122",
"REACTOME:R-CEL-201688",
"REACTOME:R-CEL-2028269",
"REACTOME:R-CEL-354192",
"REACTOME:R-CEL-381676",
"REACTOME:R-CEL-392517",
"REACTOME:R-CEL-4086400",
"REACTOME:R-CEL-418594",
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-... | 165 | [
"1fsh",
"1o7f",
"1uhw",
"1v3f",
"1w4m",
"2byv",
"2cso",
"2pbi",
"2ysr",
"3ml6",
"4f7z",
"5lnp",
"5suy",
"5suz",
"6ces",
"6cet",
"6h7e",
"6n9g",
"6pcv",
"6vsk",
"7dkl",
"7ewp",
"7ewr",
"7owg",
"7pe7",
"7pe8",
"7pe9",
"7pea",
"7peb",
"7pec",
"7ped",
"7rx9"... | 64 | [
"PUB00015163",
"PUB00018182"
] | [
"10987813",
"11101902"
] | [
"Regulators of G protein signaling: a bestiary of modular protein binding domains.",
"Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway."
] | [
2000,
2000
] | 2 | [] | [
"IPR037335",
"IPR037336",
"IPR037367",
"IPR037368",
"IPR037369",
"IPR037371",
"IPR037378"
] | 0 | 7 | 0 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
203,
45930,
4
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
24,
126,
14,
114,
74,
5,
6,
102,
5,
5,
7
] | 12 | true | Domain | DEP domain | DEP domain | DEP_dom | 8 |
IPR000592 | 592 | Small ribosomal subunit protein eS27 | Ribosomal_eS27 | Family | 9,087 | false | false | S27 is involved in rRNa processing, direct binding to mRNA and degradation of damaged mRNAs. S27 is a C4 zinc finger protein of the CX2CX14-16CX2C class. Zinc finger motifs in ribosomal proteins mediate protein-RNA interactions, however it has been suggested the zinc finger in S27 possibly has no functional importance ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PROSITE",
"PANTHER"
] | [
"MF_00371",
"PF01667",
"PS01168",
"PTHR11594"
] | [
"Ribosomal_eS27",
"Ribosomal_S27e",
"RIBOSOMAL_S27E",
""
] | [
7760,
8930,
6523,
8154
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00898",
"R-BTA-141444",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-5663220",
"R-BTA-6791226",
"R-BTA-68877",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-9648025",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827... | [
"PROSITEDOC:PDOC00898",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-5663220",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-68877",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72... | 108 | [
"1qxf",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q"... | 622 | [
"PUB00004441",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00030432"
] | [
"8441676",
"11297922",
"11290319",
"11114498",
"15096641"
] | [
"Zinc finger-like motifs in rat ribosomal proteins S27 and S29.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of A... | [
1993,
2001,
2001,
2000,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
866,
12,
8183,
26
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
12,
1,
4,
1,
6,
8,
1,
7,
21,
2,
1,
8
] | 12 | true | Family | Small ribosomal subunit protein eS27 | Small ribosomal subunit protein eS27 | Ribosomal_eS27 | 8 |
IPR000593 | 593 | IQGAP, helical domain | IQGAP_helical | Domain | 8,207 | false | false | This helical domain can be found towards the C terminus of the IQGAP family members, including human IQGAP1/2/3 and its fungal homologues, S. cerevisiae Iqg1 and S. pombe Rng2. Some members function in cytoskeletal remodelling [ ]. Human IQGAP1 is a scaffolding protein that can assemble multi-protein complexes involved... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF03836"
] | [
"RasGAP_C"
] | [
8207
] | 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-DDI-5626467",
"R-DDI-6798695",
"R-DDI-9013149",
"R-DDI-9013404",
"R-DDI-9013406",
"R-DDI-9013408",
"R-DDI-9013420",
"R-DDI-9013424",
"R-HSA-373753",
"R-HSA-381676",
"R-HSA-5626467",
"R-HSA-5674135",
"R-HSA-6798695",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955... | [
"REACTOME:R-DDI-5626467",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-9013149",
"REACTOME:R-DDI-9013404",
"REACTOME:R-DDI-9013406",
"REACTOME:R-DDI-9013408",
"REACTOME:R-DDI-9013420",
"REACTOME:R-DDI-9013424",
"REACTOME:R-HSA-373753",
"REACTOME:R-HSA-381676",
"REACTOME:R-HSA-5626467",
"REACTOME:... | 58 | [] | 0 | [
"PUB00078917",
"PUB00078918",
"PUB00078919",
"PUB00078920"
] | [
"20335501",
"11112700",
"11854008",
"9635188"
] | [
"The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network.",
"Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins.",
"Plakins: a... | [
2010,
2001,
2002,
1998
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8207
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
6,
13,
14,
2,
9,
1,
2
] | 8 | true | Domain | IQGAP, helical domain | IQGAP, helical domain | IQGAP_helical | 5 |
IPR000594 | 594 | THIF-type NAD/FAD binding fold | ThiF_NAD_FAD-bd | Domain | 100,109 | false | false | This domain is a NAD/FAD-binding fold found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [ , , ]. ThiF/MoeB/HesA are involved in molybdopterin and thiamine biosynthesis. The common reaction mechanism catalysed by MoeB and ThiF, li... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00899"
] | [
"ThiF"
] | [
100109
] | 1 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1311",
"GenProp1461",
"GenProp1711",
"R-BTA-3065676",
"R-BTA-3065678",
"R-BTA-8866652",
"R-BTA-947581",
"R-BTA-983168",
"R-CEL-3065676",
"R-CEL-3065678",
"R-CEL-8951664",
"R-CEL-947581",
"R-CEL-983168",
"R-DDI-1169408",
"R-DDI-1632852",
"R-DDI-3065676",
"R-DDI-3065678",
"R-... | [
"GP:GenProp1311",
"GP:GenProp1461",
"GP:GenProp1711",
"REACTOME:R-BTA-3065676",
"REACTOME:R-BTA-3065678",
"REACTOME:R-BTA-8866652",
"REACTOME:R-BTA-947581",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-3065676",
"REACTOME:R-CEL-3065678",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-947581",
"REACTO... | 94 | [
"1jw9",
"1jwa",
"1jwb",
"1r4m",
"1r4n",
"1tt5",
"1y8q",
"1y8r",
"1yov",
"1zfn",
"1zkm",
"1zud",
"2nvu",
"3cmm",
"3dbh",
"3dbl",
"3dbr",
"3guc",
"3gzn",
"3h5a",
"3h5n",
"3h5r",
"3h8v",
"3h9g",
"3h9j",
"3h9q",
"3kyc",
"3kyd",
"3rui",
"3t7e",
"3vh1",
"3vh2"... | 138 | [
"PUB00000623",
"PUB00005373",
"PUB00011756",
"PUB00015619",
"PUB00015620",
"PUB00015621",
"PUB00015625",
"PUB00038452",
"PUB00075384",
"PUB00099202"
] | [
"1647207",
"1656558",
"11713534",
"15454246",
"14998368",
"15556404",
"15196553",
"15660128",
"18662542",
"9632726"
] | [
"Genetic analysis of the ubiquitin system.",
"The ubiquitin pathway for protein degradation.",
"Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.",
"The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.",
"Getting into position: t... | [
1991,
1991,
2001,
2004,
2004,
2004,
2004,
2005,
2008,
1998
] | 10 | [] | [
"IPR030468"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1173,
50685,
47222,
55,
974
] | 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",... | [
60,
11,
23,
21,
3,
54,
34,
12,
44,
59,
8,
8,
155
] | 13 | true | Domain | THIF-type NAD/FAD binding fold | THIF-type NAD/FAD binding fold | ThiF_NAD_FAD-bd | 1 |
IPR000595 | 595 | Cyclic nucleotide-binding domain | cNMP-bd_dom | Domain | 266,036 | false | false | Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues [ , , ]. The best studied of these proteins is the prokaryotic catabolite gene activator (also known as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three α-helices and a distinct... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00027",
"PS50042",
"SM00100",
"cd00038"
] | [
"cNMP_binding",
"CNMP_BINDING_3",
"cNMP",
"CAP_ED"
] | [
227698,
245119,
191514,
245798
] | 4 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1352",
"PDOC00691",
"R-BTA-1296072",
"R-BTA-163615",
"R-BTA-164378",
"R-BTA-180024",
"R-BTA-2485179",
"R-BTA-2514859",
"R-BTA-392517",
"R-BTA-418457",
"R-BTA-432040",
"R-BTA-442720",
"R-BTA-5610787",
"R-BTA-5673001",
"R-BTA-9634597",
"R-BTA-983231",
"R-BTA-9856530",
"R-CEL-... | [
"GP:GenProp1352",
"PROSITEDOC:PDOC00691",
"REACTOME:R-BTA-1296072",
"REACTOME:R-BTA-163615",
"REACTOME:R-BTA-164378",
"REACTOME:R-BTA-180024",
"REACTOME:R-BTA-2485179",
"REACTOME:R-BTA-2514859",
"REACTOME:R-BTA-392517",
"REACTOME:R-BTA-418457",
"REACTOME:R-BTA-432040",
"REACTOME:R-BTA-442720",... | 189 | [
"1cgp",
"1cx4",
"1ft9",
"1g6n",
"1hw5",
"1i5z",
"1i6x",
"1j59",
"1lb2",
"1ne4",
"1ne6",
"1o3q",
"1o3r",
"1o3s",
"1o3t",
"1o5l",
"1o7f",
"1q3e",
"1q43",
"1q5o",
"1rgs",
"1rl3",
"1run",
"1ruo",
"1u12",
"1vp6",
"1wgp",
"1zrc",
"1zrd",
"1zre",
"1zrf",
"1zyb"... | 477 | [
"PUB00005543",
"PUB00013967",
"PUB00013968"
] | [
"1710853",
"14638413",
"10550204"
] | [
"The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium.",
"Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs.",
"Transcription activation by catabolite activator protein (CAP... | [
1991,
2003,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
213,
147557,
116268,
49,
1949
] | 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",... | [
180,
34,
287,
86,
3,
135,
111,
4,
94,
156,
3,
3,
219
] | 13 | true | Domain | Cyclic nucleotide-binding domain | Cyclic nucleotide-binding domain | cNMP-bd_dom | 8 |
IPR000596 | 596 | Cholecystokinin receptor type A | Cholcy_rcpt_A | Family | 584 | 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:0004951",
"GO:0007186",
"GO:0016020"
] | [
"cholecystokinin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00524"
] | [
"CCYSTOKNINAR"
] | [
584
] | 1 | [
"GP",
"GP",
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp2096",
"GenProp2098",
"76",
"R-HSA-375276",
"R-HSA-416476",
"R-MMU-375276",
"R-MMU-416476",
"R-RNO-375276",
"R-RNO-416476"
] | [
"GP:GenProp2096",
"GP:GenProp2098",
"IUPHAR:76",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476"
] | 9 | [
"7ezh",
"7ezk",
"7ezm",
"7mbx",
"7mby",
"7xou",
"7xov",
"9bkj",
"9bkk"
] | 9 | [
"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 | [
"IPR009126"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
584
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3
] | 3 | true | Family | Cholecystokinin receptor type A | Cholecystokinin receptor type A | Cholcy_rcpt_A | 1 |
IPR000599 | 599 | G protein-coupled receptor 12 | GPR12 | Family | 675 | false | false | G protein-coupled receptor 12 (GPR12) was initially isolated from a rat pituitary library, and is found in discrete regions of the brain, pituitary and testis, but is absent in other tissues [ , ]. Three human homologues (GPR12, GPR6 and GPR3) have also been isolated [ ]. The 3 genes have been localised to human chromo... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PRINTS"
] | [
"PR00650"
] | [
"GPR12ORPHANR"
] | [
675
] | 1 | [] | [] | [] | 0 | [
"7y3g"
] | 1 | [
"PUB00001626",
"PUB00001967"
] | [
"1840531",
"8530049"
] | [
"Cloning, sequencing and tissue distribution of a candidate G protein-coupled receptor from rat pituitary gland.",
"Molecular cloning and chromosomal localization of human genes encoding three closely related G protein-coupled receptors."
] | [
1991,
1995
] | 2 | [
"IPR000723"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
675
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
2
] | 4 | true | Family | G protein-coupled receptor 12 | G protein-coupled receptor 12 | GPR12 | 9 |
IPR000600 | 600 | ROK family | ROK | Family | 112,579 | false | false | A family of bacterial proteins has been described which groups transcriptional repressors, sugar kinases and yet uncharacterised open reading frames [ ]. This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylos... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF00480",
"PTHR18964"
] | [
"ROK",
""
] | [
111787,
106648
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"GenProp1394",
"GenProp1463",
"GenProp1565",
"GenProp1599",
"GenProp1737",
"PDOC00866",
"R-HSA-4085001",
"R-HSA-4085011",
"R-MMU-4085001",
"R-RNO-4085001"
] | [
"EC:2.7.1",
"GP:GenProp1394",
"GP:GenProp1463",
"GP:GenProp1565",
"GP:GenProp1599",
"GP:GenProp1737",
"PROSITEDOC:PDOC00866",
"REACTOME:R-HSA-4085001",
"REACTOME:R-HSA-4085011",
"REACTOME:R-MMU-4085001",
"REACTOME:R-RNO-4085001"
] | 11 | [
"1woq",
"1xc3",
"1z05",
"1z6r",
"2aa4",
"2ap1",
"2gup",
"2hoe",
"2qm1",
"2yhw",
"2yhy",
"2yi1",
"3bp8",
"3eo3",
"3htv",
"3lm2",
"3lm9",
"3mcp",
"3ohr",
"3r8e",
"3vgk",
"3vgl",
"3vgm",
"3vov",
"4db3",
"4htl",
"4ija",
"5f7p",
"5f7q",
"5f7r",
"5nck",
"6jda"... | 46 | [
"PUB00003590"
] | [
"7952186"
] | [
"Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria."
] | [
1994
] | 1 | [] | [
"IPR004654",
"IPR023505",
"IPR023945",
"IPR030883",
"IPR054618",
"IPR054671"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
593,
108527,
2225,
1,
1233
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
7,
5,
9,
7
] | 5 | true | Family | ROK family | ROK family | ROK | 5 |
IPR000602 | 602 | Glycoside hydrolase family 38, N-terminal domain | Glyco_hydro_38_N | Domain | 29,113 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004559",
"GO:0006013"
] | [
"alpha-mannosidase activity",
"mannose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01074"
] | [
"Glyco_hydro_38N"
] | [
29113
] | 1 | [
"CAZY",
"EC",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GH38",
"3.2.1.24",
"GenProp1299",
"GenProp1444",
"GenProp1524",
"R-BTA-6798695",
"R-BTA-8853383",
"R-DDI-6798695",
"R-DDI-8853383",
"R-DME-975578",
"R-HSA-6798695",
"R-HSA-6811438",
"R-HSA-8853383",
"R-HSA-9694548",
"R-HSA-975578",
"R-MMU-6798695",
"R-MMU-8853383",
"R-MMU-975578",... | [
"CAZY:GH38",
"EC:3.2.1.24",
"GP:GenProp1299",
"GP:GenProp1444",
"GP:GenProp1524",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8853383",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-8853383",
"REACTOME:R-DME-975578",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-6811438",
"REACTOME:R-HSA-8853383",
"... | 22 | [
"1hty",
"1hww",
"1hxk",
"1o7d",
"1ps3",
"1qwn",
"1qwu",
"1qx1",
"1r33",
"1r34",
"1tqs",
"1tqt",
"1tqu",
"1tqv",
"1tqw",
"2alw",
"2f18",
"2f1a",
"2f1b",
"2f7o",
"2f7p",
"2f7q",
"2f7r",
"2fyv",
"2ow6",
"2ow7",
"2wyh",
"2wyi",
"3blb",
"3bub",
"3bud",
"3bui"... | 84 | [
"PUB00004870",
"PUB00005266"
] | [
"7624375",
"8535779"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1995,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
125,
11920,
16924,
2,
142
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
29,
4,
21,
17,
1,
25,
19,
1,
13,
26,
1,
1,
55
] | 13 | true | Domain | Glycoside hydrolase family 38, N-terminal domain | Glycoside hydrolase family 38, N-terminal domain | Glyco_hydro_38_N | 9 |
IPR000603 | 603 | Movement protein | MPV | Family | 1,916 | false | false | This entry includes movement proteins from various viruses, including Movement protein (also known as Protein 3A) from Bromoviruses and Cucumoviruses, whose genomes contain 3 RNA segments. The third segment (RNA 3) contains two proteins, the coat protein and the 3A protein. Protein 3A has been shown to be involved in c... | [
"GO:0046740"
] | [
"transport of virus in host, cell to cell"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00803"
] | [
"3A"
] | [
1916
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005623",
"PUB00099796"
] | [
"9356336",
"19481775"
] | [
"Characterization of cucumber mosaic virus. IV. Movement protein and coat protein are both essential for cell-to-cell movement of cucumber mosaic virus.",
"Identification of domains of the Tomato spotted wilt virus NSm protein involved in tubule formation, movement and symptomatology."
] | [
1997,
2009
] | 2 | [] | [
"IPR006889"
] | 0 | 1 | 0 | [
"Viruses"
] | [
1916
] | 1 | [] | [] | 0 | true | Family | Movement protein | Movement protein | MPV | 5 |
IPR000604 | 604 | Major outer membrane protein, Chlamydia | Major_OMP_Chlamydia | Family | 2,724 | false | false | The major outer membrane protein of Chlamydia contains four symmetrically spaced variable domains (VDs I to IV). This protein maintains the structural rigidity of the outer membrane and facilitates porin formation, permitting diffusion of solutes through the intracellular reticulate body membrane. It is believed to pla... | [
"GO:0005198",
"GO:0015288",
"GO:0009279"
] | [
"structural molecule activity",
"porin activity",
"cell outer membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF01308",
"PR01334"
] | [
"Chlam_OMP",
"CHLAMIDIAOMP"
] | [
2724,
2198
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
2723,
1
] | 2 | [] | [] | 0 | true | Family | Major outer membrane protein, Chlamydia | Major outer membrane protein, Chlamydia | Major_OMP_Chlamydia | 5 |
IPR000605 | 605 | Helicase, superfamily 3, single-stranded DNA/RNA virus | Helicase_SF3_ssDNA/RNA_vir | Domain | 21,794 | false | false | Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A (phosphate-binding loop or P-loop) and Walker B (Mg2+-binding aspartic acid) motifs. Superfamily 3 consists of helicases encoded mainly by small DNA viruses and some larg... | [
"GO:0003723",
"GO:0003724"
] | [
"RNA binding",
"RNA helicase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00910"
] | [
"RNA_helicase"
] | [
21794
] | 1 | [
"EC",
"EC",
"EC"
] | [
"2.7.7.48",
"3.4.22",
"3.6.1"
] | [
"EC:2.7.7.48",
"EC:3.4.22",
"EC:3.6.1"
] | 3 | [
"5gq1",
"5grb",
"5z3q",
"6s3a",
"6t3w",
"7e6v",
"7lar",
"7las",
"7xt3",
"8x3v",
"8xms",
"9r34"
] | 12 | [
"PUB00014778",
"PUB00027539",
"PUB00033628",
"PUB00033629",
"PUB00033630"
] | [
"15037234",
"12774115",
"11689653",
"2156730",
"15718137"
] | [
"Evolutionary history and higher order classification of AAA+ ATPases.",
"Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen.",
"Common origin of four diverse families of large eukaryotic DNA viruses.",
"A new superfamily of putative NTP-binding domains encoded by genomes of sm... | [
2004,
2003,
2001,
1990,
2005
] | 5 | [] | [
"IPR014759"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3,
546,
381,
20831,
33
] | 5 | [] | [] | 0 | true | Domain | Helicase, superfamily 3, single-stranded DNA/RNA virus | Helicase, superfamily 3, single-stranded DNA/RNA virus | Helicase_SF3_ssDNA/RNA_vir | 2 |
IPR000608 | 608 | Ubiquitin-conjugating (UBC), catalytic core domain | UBC | Domain | 142,588 | false | false | This entry represents the catalytic core domain of E2 ubiquitin-conjugating enzymes and similar sequences mainly found in eukaryotes. It is an α/β domain. Ubiquitin-conjugating enzymes (UBC or E2 enzymes) ( ) [ , , ] catalyse the covalent attachment of ubiquitin to target proteins. Ubiquitinylation is an ATP-dependent ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00179",
"PS50127"
] | [
"UQ_con",
"UBC_2"
] | [
140078,
141489
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"2.3.2",
"2.3.2.23",
"GenProp1311",
"GenProp1754",
"PWY-7511",
"PDOC00163",
"R-BTA-110314",
"R-BTA-1169408",
"R-BTA-1234176",
"R-BTA-141430",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-174184",
"R-BTA-176407",
"R-BTA-176408",
"R-BTA-176409",
"R-BTA-176... | [
"EC:2.3.2",
"EC:2.3.2.23",
"GP:GenProp1311",
"GP:GenProp1754",
"METACYC:PWY-7511",
"PROSITEDOC:PDOC00163",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-141430",
"REACTOME:R-BTA-174048",
"REACTOME:R-BTA-174084",
"REACTOME:R-BTA-174154",
"REACT... | 472 | [
"1a3s",
"1ayz",
"1c4z",
"1fbv",
"1fxt",
"1fzy",
"1i7k",
"1j74",
"1j7d",
"1jas",
"1jat",
"1jbb",
"1kps",
"1pzv",
"1q34",
"1qcq",
"1tte",
"1u9a",
"1u9b",
"1ur6",
"1w4u",
"1wzv",
"1wzw",
"1x23",
"1y6l",
"1y8x",
"1yf9",
"1yh2",
"1yla",
"1yrv",
"1z2u",
"1z3d"... | 471 | [
"PUB00000623",
"PUB00005354",
"PUB00005373",
"PUB00015620",
"PUB00015626"
] | [
"1647207",
"2193438",
"1656558",
"14998368",
"15545318"
] | [
"Genetic analysis of the ubiquitin system.",
"Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells.",
"The ubiquitin pathway for protein degradation.",
"Getting into position: the catalytic mechanisms of protein ubiquitylation.",
"Ubiquitin charging of human class III ubiquitin-conjugating en... | [
1991,
1990,
1991,
2004,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
24,
158,
141944,
205,
257
] | 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... | [
192,
32,
93,
72,
174,
155,
19,
142,
178,
14,
14,
396
] | 12 | true | Domain | Ubiquitin-conjugating (UBC), catalytic core domain | Ubiquitin-conjugating (UBC), catalytic core domain | UBC | 8 |
IPR000609 | 609 | 7TM GPCR, serpentine receptor class g (Srg) | 7TM_GPCR_serpentine_rcpt_Srg | Family | 2,193 | 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:0004888",
"GO:0007606",
"GO:0016020"
] | [
"transmembrane signaling receptor activity",
"sensory perception of chemical stimulus",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF02118",
"PR00698"
] | [
"Srg",
"TMPROTEINSRG"
] | [
2150,
589
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000924",
"PUB00001946",
"PUB00004961",
"PUB00007387",
"PUB00044128",
"PUB00044129",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"7585938",
"9582190",
"8170923",
"10580986",
"18050473",
"15618405",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Divergent seven transmembrane receptors are candidate chemosensory receptors in C. elegans.",
"Two large families of chemoreceptor genes in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae reveal extensive gene duplication, diversification, movement, and intron loss.",
"Fingerprinting G-protein... | [
1995,
1998,
1994,
1999,
2006,
2005,
2003,
1994,
2005,
2009,
2006,
2013
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria"
] | [
2,
2191
] | 2 | [
"Caenorhabditis elegans"
] | [
70
] | 1 | true | Family | 7TM GPCR, serpentine receptor class g (Srg) | 7TM GPCR, serpentine receptor class g (Srg) | 7TM_GPCR_serpentine_rcpt_Srg | 4 |
IPR000610 | 610 | 5-Hydroxytryptamine 1A receptor | 5HT1A_rcpt | Family | 900 | false | false | 5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n... | [
"GO:0004993",
"GO:0007186",
"GO:0019229",
"GO:0046883",
"GO:0050795",
"GO:0005886"
] | [
"G protein-coupled serotonin receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of vasoconstriction",
"regulation of hormone secretion",
"regulation of behavior",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PRINTS"
] | [
"PR00512"
] | [
"5HT1ARECEPTR"
] | [
900
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1",
"R-HSA-390666",
"R-MMU-390666",
"R-RNO-390666"
] | [
"IUPHAR:1",
"REACTOME:R-HSA-390666",
"REACTOME:R-MMU-390666",
"REACTOME:R-RNO-390666"
] | 4 | [
"7e2x",
"7e2y",
"7e2z",
"8fy8",
"8fye",
"8fyl",
"8fyt",
"8fyx",
"8jsp",
"8jt6",
"8pjk",
"8pkm",
"8w8b",
"9dyd",
"9dye",
"9dyf",
"9gl2",
"9md1",
"9vj5",
"9vj6",
"9vje",
"9vjf",
"9vjg",
"9vmy",
"9vnf"
] | 25 | [
"PUB00064376",
"PUB00064380",
"PUB00064381",
"PUB00064382",
"PUB00064383",
"PUB00064384",
"PUB00064385",
"PUB00064386",
"PUB00064387",
"PUB00064388",
"PUB00064389",
"PUB00064390",
"PUB00064391",
"PUB00064392",
"PUB00064393",
"PUB00064394",
"PUB00064395",
"PUB00064396",
"PUB000643... | [
"18476671",
"9935065",
"18761712",
"8430834",
"12480158",
"8841890",
"7796165",
"2156831",
"1531498",
"8416603",
"2649317",
"9169298",
"9724773",
"1796057",
"2883013",
"12404310",
"9844013",
"15574737",
"15743927",
"1819150",
"16455061",
"17702902",
"11989819"
] | [
"Serotonin receptors.",
"Localization of 5-HT1A receptors in the living human brain using [carbonyl-11C]WAY-100635: PET with anatomic standardization technique.",
"Serotonin 1A receptors in human and monkey prefrontal cortex are mainly expressed in pyramidal neurons and in a GABAergic interneuron subpopulation:... | [
2008,
1999,
2008,
1993,
2003,
1996,
1995,
1990,
1992,
1993,
1989,
1997,
1998,
1991,
1987,
2000,
1998,
2004,
2005,
1991,
2006,
2007,
2002
] | 23 | [
"IPR002231"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
900
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
2,
3
] | 4 | true | Family | 5-Hydroxytryptamine 1A receptor | 5-Hydroxytryptamine 1A receptor | 5HT1A_rcpt | 2 |
IPR000611 | 611 | Neuropeptide Y receptor family | NPY_rcpt | Family | 13,346 | false | false | Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01012"
] | [
"NRPEPTIDEYR"
] | [
13346
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-375276",
"R-BTA-416476",
"R-BTA-418594",
"R-CFA-375276",
"R-CFA-418594",
"R-DME-416476",
"R-GGA-375276",
"R-GGA-418594",
"R-HSA-375276",
"R-HSA-389397",
"R-HSA-416476",
"R-HSA-418555",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-418555",
"R-MMU-418594",
"R-RNO-375... | [
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-418594",
"REACTOME:R-DME-416476",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-389397",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418... | 22 | [
"7vgx",
"7x9a",
"7x9b",
"7x9c",
"7yon",
"7yoo",
"8k6m",
"8k6n",
"8k6o",
"8wz2",
"8zh8"
] | 11 | [
"PUB00063739",
"PUB00063740",
"PUB00063741",
"PUB00063742",
"PUB00063743",
"PUB00063744",
"PUB00063745",
"PUB00063746",
"PUB00063747",
"PUB00063748",
"PUB00063749",
"PUB00063750",
"PUB00063751",
"PUB00063752",
"PUB00063753",
"PUB00063754",
"PUB00063755",
"PUB00063756",
"PUB000637... | [
"6549409",
"16874931",
"6547387",
"6549039",
"2821236",
"8395947",
"16190896",
"7529442",
"7644568",
"15337373",
"8685245",
"8369959",
"11287113",
"7629398",
"6133408",
"3855566",
"12678499",
"17222466",
"8013354",
"9833945",
"9389418",
"9446690",
"2453065",
"1661086",
... | [
"Neuropeptide Y: a potent inducer of consummatory behavior in rats.",
"Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.",
"Neuropeptide Y and human pancreatic polypeptide stimulate feeding behavior in rats.",
"Neuropeptide Y: stimulation of feeding and drinking by injection into the... | [
1984,
2006,
1984,
1984,
1987,
1993,
2005,
1994,
1995,
2004,
1996,
1993,
2001,
1995,
1982,
1985,
2003,
2007,
1994,
1998,
1997,
1998,
1988,
1991,
1995,
2003,
2007,
1998,
2004,
2007,
2007,
2007,
2006,
2007,
2006,
2007,
2008,
1996,
1996,
1998... | 41 | [
"IPR000276"
] | [
"IPR000351",
"IPR000393",
"IPR000986",
"IPR001358",
"IPR001933"
] | 1 | 5 | 0 | [
"Eumetazoa"
] | [
13346
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
24,
18,
12,
22,
22,
24
] | 6 | true | Family | Neuropeptide Y receptor family | Neuropeptide Y receptor family | NPY_rcpt | 9 |
IPR000612 | 612 | Proteolipid membrane potential modulator | PMP3 | Family | 14,470 | false | false | Proteolipid membrane potential modulator is an evolutionarily conserved proteolipid in the plasma membrane which, in S. pombe, is transcriptionally regulated by the Spc1 stress MAPK (mitogen-activated protein kinases) pathway. It functions to modulate the membrane potential, particularly to resist high cellular cation ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROSITE",
"PANTHER"
] | [
"PF01679",
"PS01309",
"PTHR21659"
] | [
"Pmp3",
"UPF0057",
""
] | [
14455,
8469,
11258
] | 3 | [
"PROSITEDOC"
] | [
"PDOC01013"
] | [
"PROSITEDOC:PDOC01013"
] | 1 | [
"7ueb",
"8gwa"
] | 2 | [
"PUB00001129",
"PUB00100132"
] | [
"9588799",
"16603158"
] | [
"Low molecular weight proteins: a challenge for post-genomic research.",
"The fission yeast stress MAPK cascade regulates the pmp3+ gene that encodes a highly conserved plasma membrane protein."
] | [
1998,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Ignicoccus islandicus DSM 13165",
"Viruses",
"unclassified sequences"
] | [
5822,
8597,
1,
6,
44
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / AT... | [
25,
15,
1,
4,
17,
4,
2,
24
] | 8 | true | Family | Proteolipid membrane potential modulator | Proteolipid membrane potential modulator | PMP3 | 4 |
IPR000614 | 614 | Free Met sulfoxide reductase conserved site | FRMsr_CS | Conserved_site | 7,253 | false | false | Free methionine-R-sulfoxide reductases are a family of GAF domain-containing proteins that have been shown to catalyse the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine [ ]. This entry represents a conserved site within the GAF domain section of these proteins. | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01320"
] | [
"UPF0067"
] | [
7253
] | 1 | [
"PROSITEDOC"
] | [
"PDOC01024"
] | [
"PROSITEDOC:PDOC01024"
] | 1 | [
"1f5m",
"1vhm",
"3ko6",
"3ksf",
"3ksg",
"3ksh",
"3ksi",
"5hl6",
"8dgd"
] | 9 | [
"PUB00062207"
] | [
"19049972"
] | [
"Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5879,
1342,
32
] | 3 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1,
1
] | 3 | true | Conserved_site | Free Met sulfoxide reductase conserved site | Free Met sulfoxide reductase conserved site | FRMsr_CS | 8 |
IPR000615 | 615 | Bestrophin | Bestrophin | Family | 8,930 | false | false | This entry represents the Bestrophin family that includes four paralogous genes in mammals (BEST1, BEST2, BEST3, BEST4) encoding integral membrane calcium (Ca2+)-activated chloride (Cl-) channels. In humans, they are widely distributed in various organs including the airways, colon, kidney, pancreas and central nervous... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR10736"
] | [
""
] | [
8930
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2672351",
"R-HSA-2672351",
"R-MMU-2672351",
"R-SSC-2672351"
] | [
"REACTOME:R-BTA-2672351",
"REACTOME:R-HSA-2672351",
"REACTOME:R-MMU-2672351",
"REACTOME:R-SSC-2672351"
] | 4 | [
"4rdq",
"5t5n",
"6n23",
"6n24",
"6n25",
"6n26",
"6n27",
"6n28",
"6vx5",
"6vx6",
"6vx7",
"6vx8",
"6vx9",
"8d1e",
"8d1f",
"8d1g",
"8d1h",
"8d1i",
"8d1j",
"8d1k",
"8d1l",
"8d1m",
"8d1n",
"8d1o",
"8ecy",
"9ctq",
"9ctr",
"9cts",
"9ctt",
"9dyh",
"9dyi",
"9dyj"... | 45 | [
"PUB00011864",
"PUB00011865",
"PUB00096747",
"PUB00096748",
"PUB00096752",
"PUB00153737",
"PUB00153738",
"PUB00153739"
] | [
"12032738",
"12058047",
"12907679",
"18400985",
"25337878",
"28153808",
"29063836",
"35789156"
] | [
"Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family.",
"Bestrophin interacts physically and functionally with protein phosphatase 2A.",
"Structure-function analysis of the bestrophin family of anion channels.",
"Bestrophin Cl- channels are highly permeable to HCO3... | [
2002,
2002,
2003,
2008,
2014,
2017,
2017,
2022
] | 8 | [
"IPR021134"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
8930
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
11,
9,
23,
5,
10
] | 6 | true | Family | Bestrophin | Bestrophin | Bestrophin | 2 |
IPR000618 | 618 | Insect cuticle protein | Insect_cuticle | Family | 38,648 | false | false | Insect cuticle is composed of proteins and chitin. The cuticular proteins seem to be specific to the type of cuticle (flexible or stiff) that occur at stages of the insect development. The proteins found in the flexible cuticle of larva and pupa of different insects share a conserved C-terminal section [ ] such a regio... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00379",
"PR00947",
"PS51155"
] | [
"Chitin_bind_4",
"CUTICLE",
"CHIT_BIND_RR_2"
] | [
37847,
20927,
38193
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00206"
] | [
"PROSITEDOC:PDOC00206"
] | 1 | [
"9l0p"
] | 1 | [
"PUB00001387",
"PUB00002037",
"PUB00002038",
"PUB00003233",
"PUB00007094"
] | [
"1997327",
"9014336",
"9066122",
"2462055",
"11520687"
] | [
"Determination of the covalent structure of an N- and C-terminally blocked glycoprotein from endocuticle of Locusta migratoria. Combined use of plasma desorption mass spectrometry and Edman degradation to study post-translationally modified proteins.",
"Purification and characterization of five cuticular proteins... | [
1991,
1996,
1997,
1988,
2001
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
62,
38585,
1
] | 3 | [
"Drosophila melanogaster"
] | [
202
] | 1 | true | Family | Insect cuticle protein | Insect cuticle protein | Insect_cuticle | 7 |
IPR000620 | 620 | EamA domain | EamA_dom | Domain | 302,615 | false | false | EamA (named after the O-acetyl-serine/cysteine export gene in E. coli) domain is found in a wide range of proteins including the Erwinia chrysanthemi PecM protein, which is involved in pectinase, cellulase and blue pigment regulation, the Salmonella typhimurium PagO protein (function unknown), some eukaryotic members o... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF00892"
] | [
"EamA"
] | [
302615
] | 1 | [] | [] | [] | 0 | [
"5i20",
"7b0k",
"7paf"
] | 3 | [
"PUB00020858",
"PUB00106529"
] | [
"11432728",
"21569384"
] | [
"The drug/metabolite transporter superfamily.",
"Functional specialization in nucleotide sugar transporters occurred through differentiation of the gene cluster EamA (DUF6) before the radiation of Viridiplantae."
] | [
2001,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
4639,
251447,
42192,
2,
28,
4307
] | 6 | [
"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... | [
241,
16,
2,
11,
12,
10,
1,
172,
19,
2,
217
] | 11 | true | Domain | EamA domain | EamA domain | EamA_dom | 2 |
IPR000621 | 621 | Melanocortin 5 receptor | Melancort_rcpt_5 | Family | 1,003 | 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"
] | [
"PR01063"
] | [
"MELNOCORTN5R"
] | [
1003
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"286",
"R-BTA-375276",
"R-BTA-418555",
"R-HSA-375276",
"R-HSA-418555",
"R-HSA-9856649",
"R-MMU-375276",
"R-MMU-418555",
"R-RNO-375276"
] | [
"IUPHAR:286",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418555",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-375276"
] | 9 | [
"8inr",
"8iod",
"9k3h"
] | 3 | [
"PUB00000131",
"PUB00000233",
"PUB00000234",
"PUB00000530",
"PUB00002477",
"PUB00002830",
"PUB00004827",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"8179577",
"8185570",
"8172596",
"2830256",
"8463333",
"8415620",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"Molecular cloning and characterization of the rat fifth melanocortin receptor.",
"Molecular cloning, expression, and characterization of a fifth melanocortin receptor.",
"Molecular cloning, functional expression and pharmacological characterization of a mouse melanocorti... | [
1990,
1994,
1994,
1994,
1988,
1993,
1993,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 15 | [
"IPR001908"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1003
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
3,
2
] | 4 | true | Family | Melanocortin 5 receptor | Melanocortin 5 receptor | Melancort_rcpt_5 | 2 |
IPR000622 | 622 | K/Cl co-transporter 1 | KCC1 | Family | 1,168 | false | false | The K-Cl co-transporter (KCC) mediates the coupled movement of K + and Cl - ions across the plasma membrane of many animal cells. This transport is involved in the regulatory volume decrease in response to cell swelling in red blood cells, and has been proposed to play a role in the vectorial movement of Cl - across ki... | [
"GO:0022857",
"GO:0006811",
"GO:0016020"
] | [
"transmembrane transporter activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01082"
] | [
"KCLTRNSPORT1"
] | [
1168
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-426117",
"R-MMU-426117",
"R-RNO-426117"
] | [
"REACTOME:R-HSA-426117",
"REACTOME:R-MMU-426117",
"REACTOME:R-RNO-426117"
] | 3 | [
"6kkr",
"6kkt",
"6kku",
"6m1y",
"6m22",
"6y5r",
"6y5v",
"7ain",
"7aio",
"7aip",
"7aiq",
"7air",
"7ngb",
"7tth",
"7tti"
] | 15 | [
"PUB00002955",
"PUB00002956",
"PUB00004291",
"PUB00044874"
] | [
"8663127",
"8663311",
"9930699",
"10600773"
] | [
"Molecular cloning and functional expression of the K-Cl cotransporter from rabbit, rat, and human. A new member of the cation-chloride cotransporter family.",
"Molecular characterization of a putative K-Cl cotransporter in rat brain. A neuronal-specific isoform.",
"The K+/Cl- co-transporter KCC2 renders GABA h... | [
1996,
1996,
1999,
1999
] | 4 | [
"IPR000076"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1168
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
13,
7
] | 4 | true | Family | K/Cl co-transporter 1 | K/Cl co-transporter 1 | KCC1 | 2 |
IPR000623 | 623 | Shikimate kinase/Threonine synthase-like 1 | Shikimate_kinase/TSH1 | Family | 32,058 | false | false | Shikimate kinase ( ) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [ ]. The enzyme catalyses the following reaction: ATP + shikimate = ADP + shikimate-3-phosphate The protein is found in bacteria (gene aroK or aroL), plants and fungi (where it is ... | [] | [] | [] | 0 | [
"HAMAP",
"CDD"
] | [
"MF_00109",
"cd00464"
] | [
"Shikimate_kinase",
"SK"
] | [
31786,
31463
] | 2 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME"
] | [
"2.7.1.71",
"PWY-6163",
"PDOC00868",
"R-MTU-964903"
] | [
"EC:2.7.1.71",
"METACYC:PWY-6163",
"PROSITEDOC:PDOC00868",
"REACTOME:R-MTU-964903"
] | 4 | [
"1e6c",
"1kag",
"1l4u",
"1l4y",
"1shk",
"1u8a",
"1via",
"1we2",
"1zuh",
"1zui",
"1zyu",
"2dfn",
"2dft",
"2g1j",
"2g1k",
"2iyq",
"2iyr",
"2iys",
"2iyt",
"2iyu",
"2iyv",
"2iyw",
"2iyx",
"2iyy",
"2iyz",
"2pt5",
"2shk",
"3baf",
"3hr7",
"3mrs",
"3muf",
"3n2e"... | 44 | [
"PUB00001125",
"PUB00003386",
"PUB00005018"
] | [
"7612934",
"9600856",
"7703851"
] | [
"The gene (aroK) encoding shikimate kinase I from Escherichia coli.",
"The three-dimensional structure of shikimate kinase.",
"Protein structural similarities predicted by a sequence-structure compatibility method."
] | [
1995,
1998,
1994
] | 3 | [
"IPR031322"
] | [
"IPR027544"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
151,
26929,
4406,
572
] | 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)... | [
11,
1,
2,
1,
2,
1,
7,
2,
1,
1,
14
] | 11 | true | Family | Shikimate kinase/Threonine synthase-like 1 | Shikimate kinase/Threonine synthase-like 1 | Shikimate_kinase/TSH1 | 3 |
IPR000625 | 625 | Anti-repression trans-activator protein, REV protein | REV_protein | Family | 43,771 | false | false | REV is a viral anti-repression trans-activator protein, which appears to act post-transcriptionally [ ] to relieve negative repression of GAG and ENV production. It is a phosphoprotein [ , ] whose state of phosphorylation is mediated by a specific serine kinase activity present in the nucleus [ ]. REV accumulates in th... | [
"GO:0003700",
"GO:0006355",
"GO:0042025"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"host cell nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM"
] | [
"MF_04077",
"PF00424"
] | [
"REV_HIV1",
"REV"
] | [
14776,
43771
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-165054",
"R-HSA-173107",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180746",
"R-HSA-180910"
] | [
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-165054",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-175474",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177... | 15 | [
"2x7l",
"3lph",
"4pmi",
"5dhv",
"5dhx",
"5dhy",
"5dhz",
"6bsy",
"6cf2",
"7u0f",
"7wbn",
"8urj",
"8x3o",
"8x3p"
] | 14 | [
"PUB00033175",
"PUB00033176",
"PUB00033177",
"PUB00033178"
] | [
"2550674",
"2741343",
"2846891",
"2656990"
] | [
"Functional significance of phosphorylation to the human immunodeficiency virus Rev protein.",
"The human immunodeficiency virus rev protein is a nuclear phosphoprotein.",
"Phosphorylation of the rev gene product of human immunodeficiency virus type 1.",
"Structural and functional characterization of the huma... | [
1989,
1989,
1988,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Lentivirus",
"Ophiocordyceps unilateralis",
"Streptomyces"
] | [
43768,
1,
2
] | 3 | [] | [] | 0 | true | Family | Anti-repression trans-activator protein, REV protein | Anti-repression trans-activator protein, REV protein | REV_protein | 7 |
IPR000626 | 626 | Ubiquitin-like domain | Ubiquitin-like_dom | Domain | 159,743 | false | false | Ubiquitin is expressed as three different precursors: a polymeric head-to-tail concatemer of identical units (polyubiquitin), and two N-terminal ubiquitin moieties, UbL40 and UbS27, that are fused to the ribosomal polypeptides L40 and S27, respectively. Specific endopeptidases cleave these precursor molecules [ ] to re... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00240",
"PF14560",
"PS50053",
"SM00213"
] | [
"ubiquitin",
"Ubiquitin_2",
"UBIQUITIN_2",
"UBQ"
] | [
107900,
7514,
152643,
102243
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00271",
"R-BTA-110312",
"R-BTA-110314",
"R-BTA-110320",
"R-BTA-1169091",
"R-BTA-1169408",
"R-BTA-1234176",
"R-BTA-1253288",
"R-BTA-1295596",
"R-BTA-1358803",
"R-BTA-156827",
"R-BTA-168638",
"R-BTA-174048",
"R-BTA-174084",
"R-BTA-174113",
"R-BTA-174154",
"R-BTA-174178",
"R-BTA-... | [
"PROSITEDOC:PDOC00271",
"REACTOME:R-BTA-110312",
"REACTOME:R-BTA-110314",
"REACTOME:R-BTA-110320",
"REACTOME:R-BTA-1169091",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1234176",
"REACTOME:R-BTA-1253288",
"REACTOME:R-BTA-1295596",
"REACTOME:R-BTA-1358803",
"REACTOME:R-BTA-156827",
"REACTOME:R-BT... | 1,711 | [
"1a5r",
"1aar",
"1bt0",
"1c3t",
"1cmx",
"1d3z",
"1euv",
"1f9j",
"1fxt",
"1g6j",
"1gjz",
"1iyf",
"1j8c",
"1l2n",
"1lm8",
"1lqb",
"1m94",
"1mg8",
"1nbf",
"1ndd",
"1ogw",
"1oqy",
"1otr",
"1p0r",
"1p1a",
"1p3q",
"1p98",
"1p9d",
"1q0w",
"1q5w",
"1qze",
"1r4m"... | 2,003 | [
"PUB00015619",
"PUB00020517",
"PUB00032266",
"PUB00042453",
"PUB00043569",
"PUB00083511",
"PUB00083514",
"PUB00083519"
] | [
"15454246",
"9857030",
"15479240",
"17491593",
"12826404",
"15571815",
"16185873",
"12729753"
] | [
"The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.",
"Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes.",
"Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional ... | [
2004,
1998,
2004,
2007,
2003,
2004,
2005,
2003
] | 8 | [] | [
"IPR019956",
"IPR022617",
"IPR033882",
"IPR039540",
"IPR044743",
"IPR045172",
"IPR047406",
"IPR047468",
"IPR047877",
"IPR047991"
] | 0 | 10 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
39,
579,
158558,
340,
227
] | 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... | [
395,
40,
137,
67,
265,
157,
14,
215,
238,
14,
18,
351
] | 12 | true | Domain | Ubiquitin-like domain | Ubiquitin-like domain | Ubiquitin-like_dom | 9 |
IPR000627 | 627 | Intradiol ring-cleavage dioxygenase, C-terminal | Intradiol_dOase_C | Domain | 32,324 | false | false | This entry represents the C-terminal domain common to several intradiol ring-cleavage dioxygenases. Dioxygenases catalyse the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms. Cleavage of aromatic rings is one of the most important functions of dioxygenases, which p... | [
"GO:0003824",
"GO:0008199"
] | [
"catalytic activity",
"ferric iron binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROSITE"
] | [
"PF00775",
"PS00083"
] | [
"Dioxygenase_C",
"INTRADIOL_DIOXYGENAS"
] | [
32305,
14561
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"1.13.11",
"PDOC00079"
] | [
"EC:1.13.11",
"PROSITEDOC:PDOC00079"
] | 2 | [
"1dlm",
"1dlq",
"1dlt",
"1dmh",
"1eo2",
"1eo9",
"1eoa",
"1eob",
"1eoc",
"1s9a",
"1tmx",
"1ykk",
"1ykl",
"1ykm",
"1ykn",
"1yko",
"1ykp",
"2azq",
"2boy",
"2bum",
"2buq",
"2bur",
"2but",
"2buu",
"2buv",
"2buw",
"2bux",
"2buy",
"2buz",
"2bv0",
"2pcd",
"2xsr"... | 94 | [
"PUB00015256",
"PUB00015258"
] | [
"10730195",
"15060064"
] | [
"Catechol dioxygenases.",
"Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP."
] | [
1999,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid pEMT3",
"unclassified sequences"
] | [
14,
24686,
7521,
1,
102
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
4
] | 1 | true | Domain | Intradiol ring-cleavage dioxygenase, C-terminal | Intradiol ring-cleavage dioxygenase, C-terminal | Intradiol_dOase_C | 2 |
IPR000628 | 628 | Vasopressin V1B receptor | Vprs_rcpt_V1B | Family | 593 | 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:0005000",
"GO:0007186",
"GO:0016020"
] | [
"vasopressin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00897"
] | [
"VASOPRSNV1BR"
] | [
593
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"367",
"R-HSA-388479",
"R-HSA-416476",
"R-HSA-5619099",
"R-MMU-388479",
"R-MMU-416476"
] | [
"IUPHAR:367",
"REACTOME:R-HSA-388479",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-5619099",
"REACTOME:R-MMU-388479",
"REACTOME:R-MMU-416476"
] | 6 | [] | 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 | [
"IPR001817"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
593
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
3
] | 3 | true | Family | Vasopressin V1B receptor | Vasopressin V1B receptor | Vprs_rcpt_V1B | 1 |
IPR000629 | 629 | ATP-dependent RNA helicase DEAD-box, conserved site | RNA-helicase_DEAD-box_CS | Conserved_site | 175,828 | false | false | A number of eukaryotic and prokaryotic proteins involved in ATP-dependent, nucleic-acid unwinding have been characterised [ , , ] on the basis of their structural similarity. All these proteins share a number of conserved sequence motifs. Some of them are specific to this family while others are shared by other ATP-bin... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00039"
] | [
"DEAD_ATP_HELICASE"
] | [
175828
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.13",
"PDOC00039",
"R-BTA-1169408",
"R-BTA-156827",
"R-BTA-159236",
"R-BTA-2565942",
"R-BTA-3108214",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-429947",
"R-BTA-5620912",
"R-BTA-5696394",
"R-BTA-5696395",
"R-BTA-6791226",
"R-BTA-72163",
"R-BTA-7218... | [
"EC:3.6.4.13",
"PROSITEDOC:PDOC00039",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3108214",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
"REACTOME:R-BTA-380320",
"REACTOME:R-BTA-429947",
... | 183 | [
"1fuu",
"1hv8",
"1m39",
"1qde",
"1qva",
"1s2m",
"1vec",
"1wrb",
"1xtk",
"2a4j",
"2db3",
"2g9n",
"2ggm",
"2gxq",
"2gxs",
"2gxu",
"2hxy",
"2hyi",
"2i4i",
"2j0q",
"2j0s",
"2j0u",
"2k2i",
"2kbe",
"2obh",
"2oxc",
"2pl3",
"2vso",
"2vsx",
"2xb2",
"2zu6",
"3b7g"... | 223 | [
"PUB00003826",
"PUB00004037",
"PUB00004089"
] | [
"1552844",
"2563148",
"1825133"
] | [
"D-E-A-D protein family of putative RNA helicases.",
"Birth of the D-E-A-D box.",
"RNA splicing. Alive with DEAD proteins."
] | [
1992,
1989,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
301,
64145,
110423,
16,
943
] | 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",... | [
136,
36,
95,
53,
5,
141,
88,
20,
58,
100,
20,
19,
329
] | 13 | true | Conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | ATP-dependent RNA helicase DEAD-box, conserved site | RNA-helicase_DEAD-box_CS | 8 |
IPR000630 | 630 | Small ribosomal subunit protein uS8 | Ribosomal_uS8 | Family | 49,632 | false | false | This entry includes small ribosomal subunit protein uS8 from bacteria, archaea and eukaryotes (in yeast, these proteins are also known as S22 and in vertebrates S15A) [ ]. In Escherichia coli, uS8 is known to bind directly to 16S ribosomal RNA. Ribosomes are the particles that catalyse mRNA-directed protein synthesis i... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"HAMAP",
"NCBIFAM",
"PFAM",
"PANTHER"
] | [
"MF_01302_A",
"MF_01302_B",
"NF001109",
"PF00410",
"PTHR11758"
] | [
"Ribosomal_uS8_A",
"Ribosomal_uS8_B",
"PRK00136.1",
"Ribosomal_S8",
""
] | [
3172,
37499,
37660,
49324,
47573
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00052",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DDI-72706",
"R-DDI-975956",
"... | [
"PROSITEDOC:PDOC00052",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-DDI-156827"... | 91 | [
"1an7",
"1eg0",
"1emi",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i6u",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1s03",
"1sei",
"1vvj",
"1vy4",
"1vy5"... | 1,847 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279",
"PUB00104061"
] | [
"11297922",
"11290319",
"11114498",
"24524803",
"9061793"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system for naming ribosomal proteins.",
"Crystallization and preliminary crystallographic analysis of ribosomal protein S8 from Thermus thermophilus."
] | [
2001,
2001,
2000,
2014,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
936,
23595,
24617,
484
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
20,
3,
1,
3,
1,
10,
5,
2,
13,
12,
3,
3,
21
] | 13 | true | Family | Small ribosomal subunit protein uS8 | Small ribosomal subunit protein uS8 | Ribosomal_uS8 | 8 |
IPR000631 | 631 | ATP/ADP-dependent (S)-NAD(P)H-hydrate dehydratase | CARKD | Domain | 32,026 | false | false | Hydration of NAD(P)H to NAD(P)HX, which inhibits several dehydrogenases, is corrected by an ATP-dependent dehydratase and an epimerase. The ATP-dependent dehydratase has been identified as the product of the vertebrate Carkd (carbohydrate kinase domain) gene [ , ]. Variants of this enzyme leads to deficient NADHX repai... | [
"GO:0016836"
] | [
"hydro-lyase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PROFILE",
"NCBIFAM",
"CDD"
] | [
"MF_01965",
"PF01256",
"PS51383",
"TIGR00196",
"cd01171"
] | [
"NADHX_dehydratase",
"Carb_kinase",
"YJEF_C_3",
"yjeF_cterm",
"YXKO-related"
] | [
29959,
31744,
31830,
27812,
31032
] | 5 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.2.1",
"GenProp1736",
"PDOC00806",
"R-BTA-196807",
"R-CEL-196807",
"R-DDI-196807",
"R-DME-196807",
"R-DRE-196807",
"R-HSA-196807",
"R-MMU-196807",
"R-RNO-196807",
"R-SCE-196807",
"R-SPO-196807"
] | [
"EC:4.2.1",
"GP:GenProp1736",
"PROSITEDOC:PDOC00806",
"REACTOME:R-BTA-196807",
"REACTOME:R-CEL-196807",
"REACTOME:R-DDI-196807",
"REACTOME:R-DME-196807",
"REACTOME:R-DRE-196807",
"REACTOME:R-HSA-196807",
"REACTOME:R-MMU-196807",
"REACTOME:R-RNO-196807",
"REACTOME:R-SCE-196807",
"REACTOME:R-S... | 13 | [
"1kyh",
"2ax3",
"2r3b",
"2r3e",
"3bgk",
"3k5w",
"3rph",
"3rpz",
"3rq2",
"3rq5",
"3rq6",
"3rq8",
"3rqh",
"3rqq",
"3rqx",
"3rrb",
"3rre",
"3rrf",
"3rrj",
"3rs8",
"3rs9",
"3rsf",
"3rsg",
"3rsq",
"3rss",
"3rt7",
"3rt9",
"3rta",
"3rtb",
"3rtc",
"3rtd",
"3rte"... | 37 | [
"PUB00060794",
"PUB00073185",
"PUB00100876"
] | [
"21994945",
"24611804",
"30576410"
] | [
"Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.",
"Occurrence and subcellular distribution of the NADPHX repair system in mammals.",
"NAD(P)HX dehydratase (NAXD) deficiency: a novel neurodegenerative disorder exacerbated by febrile illnesses."
] | [
2011,
2014,
2019
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1016,
24989,
5376,
645
] | 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",... | [
3,
1,
16,
1,
1,
9,
5,
1,
3,
8,
1,
1,
3
] | 13 | true | Domain | ATP/ADP-dependent (S)-NAD(P)H-hydrate dehydratase | ATP/ADP-dependent (S)-NAD(P)H-hydrate dehydratase | CARKD | 8 |
IPR000634 | 634 | Serine/threonine dehydratase, pyridoxal-phosphate-binding site | Ser/Thr_deHydtase_PyrdxlP-BS | Binding_site | 63,582 | false | false | Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [ , , ]. PLP-dependent enzymes are primarily involved in the biosynthesis of a... | [
"GO:0030170",
"GO:0006520"
] | [
"pyridoxal phosphate binding",
"amino acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00165"
] | [
"DEHYDRATASE_SER_THR"
] | [
63582
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.3.1",
"PDOC00149",
"R-BTA-977347",
"R-DDI-8849175",
"R-DDI-977347",
"R-HSA-8849175",
"R-HSA-977347",
"R-MMU-8849175",
"R-MMU-977347",
"R-RNO-8849175",
"R-RNO-977347",
"R-SCE-8849175",
"R-SCE-977347"
] | [
"EC:4.3.1",
"PROSITEDOC:PDOC00149",
"REACTOME:R-BTA-977347",
"REACTOME:R-DDI-8849175",
"REACTOME:R-DDI-977347",
"REACTOME:R-HSA-8849175",
"REACTOME:R-HSA-977347",
"REACTOME:R-MMU-8849175",
"REACTOME:R-MMU-977347",
"REACTOME:R-RNO-8849175",
"REACTOME:R-RNO-977347",
"REACTOME:R-SCE-8849175",
"... | 13 | [
"1e5x",
"1kl7",
"1p5j",
"1pwe",
"1pwh",
"1tdj",
"1uim",
"1uin",
"1v7c",
"1vb3",
"1ve5",
"2c2b",
"2c2g",
"2d1f",
"2gn0",
"2gn1",
"2gn2",
"2rkb",
"2zsj",
"3aex",
"3aey",
"3hmk",
"3iau",
"3l6b",
"3l6c",
"3l6r",
"3r0x",
"3r0z",
"3ss7",
"3ss9",
"3v7n",
"4f4f"... | 50 | [
"PUB00002510",
"PUB00004637",
"PUB00006322",
"PUB00015327",
"PUB00035504",
"PUB00035505",
"PUB00035506",
"PUB00035507",
"PUB00035508"
] | [
"2674117",
"3540965",
"7748903",
"3098560",
"15581583",
"8690703",
"15189147",
"17109392",
"16763894"
] | [
"Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources.",
"Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases.",
"Pyridoxal phosphate-dependent enzymes.",
"Evolution of biosyntheti... | [
1989,
1987,
1995,
1986,
2005,
1995,
2004,
2006,
2006
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
1652,
49908,
11228,
3,
791
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae ... | [
13,
1,
4,
4,
11,
6,
3,
10,
6,
5,
2,
18
] | 12 | true | Binding_site | Serine/threonine dehydratase, pyridoxal-phosphate-binding site | Serine/threonine dehydratase, pyridoxal-phosphate-binding site | Ser/Thr_deHydtase_PyrdxlP-BS | 4 |
IPR000635 | 635 | Viral ssDNA-binding protein | Viral_ssDNA-bd | Family | 656 | false | false | This entry includes the major DNA-binding protein (DBP, UL57 or ICP8) from Herpesviruses. DBP binds single-stranded DNA, and the region encompassing residues 368-902 contains the DNA-binding site [ ]. UL5, UL8 and UL52 genes encode an essential heterotrimeric DNA helicase-primase that is responsible for concomitant DNA... | [
"GO:0003697",
"GO:0006260",
"GO:0042025"
] | [
"single-stranded DNA binding",
"DNA replication",
"host cell nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM"
] | [
"MF_04007",
"PF00747"
] | [
"HSV_DNBI",
"Viral_DNA_bp"
] | [
578,
656
] | 2 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9609690",
"R-HSA-9610379"
] | [
"REACTOME:R-HSA-9609690",
"REACTOME:R-HSA-9610379"
] | 2 | [
"1urj",
"9byp",
"9byq",
"9byr"
] | 4 | [
"PUB00006411",
"PUB00006455",
"PUB00084220",
"PUB00084221"
] | [
"9593724",
"10529391",
"8230421",
"26676794"
] | [
"Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA.",
"Photoaffinity labeling of the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) with oligodeoxyribonucleotides.",
"Eleven loci enco... | [
1998,
1999,
1993,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Herpesvirales",
"Homo sapiens"
] | [
655,
1
] | 2 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Viral ssDNA-binding protein | Viral ssDNA-binding protein | Viral_ssDNA-bd | 5 |
IPR000637 | 637 | HMG-I/HMG-Y, DNA-binding, conserved site | HMGI/Y_DNA-bd_CS | Conserved_site | 8,106 | false | false | High mobility group (HMG) proteins are a family of relatively low molecular weight non-histone components in chromatin [ ]. HMG-I and HMG-Y (HMGA) are proteins of about 100 amino acid residues which are produced by the alternative splicing of a single gene. HMG-I/Y proteins bind preferentially to the minor groove of AT... | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS00354"
] | [
"HMGI_Y"
] | [
8106
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00306",
"R-CFA-2559584",
"R-HSA-162592",
"R-HSA-164843",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-2559584",
"R-HSA-3214841",
"R-HSA-5617472",
"R-HSA-8936459",
"R-HSA-9772755",
"R-HSA-9818564",
"R-HSA-9841922",
"R-MMU-2559584",
"R-MMU-3214841",
"R-... | [
"PROSITEDOC:PDOC00306",
"REACTOME:R-CFA-2559584",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177539",
"REACTOME:R-HSA-180689",
"REACTOME:R-HSA-180910",
"REACTOME:R-HSA-2559584",
"REACTOME:R-HSA-3214841",
"REACTOME:R-HSA-5617472",
"REACTOME:R-HSA-... | 20 | [] | 0 | [
"PUB00002624",
"PUB00004432",
"PUB00044075"
] | [
"1692833",
"8414980",
"11406267"
] | [
"The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure.",
"Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene.",
"HMGI/Y proteins: flexible regulators of transcription and ... | [
1990,
1993,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanothrix harundinacea (strain 6Ac)",
"Viruses",
"ecological metagenomes"
] | [
1410,
6686,
1,
6,
3
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
39,
40,
19,
3,
6,
16,
12
] | 9 | true | Conserved_site | HMG-I/HMG-Y, DNA-binding, conserved site | HMG-I/HMG-Y, DNA-binding, conserved site | HMGI/Y_DNA-bd_CS | 5 |
IPR000638 | 638 | Gas vesicle protein GvpA-like | Gas-vesicle_GvpA-like | Family | 7,664 | false | false | Gas vesicles (GVs) are small, hollow, gas filled protein structures found in several cyanobacterial and archaebacterial microorganisms [ , , , ]. They allow the positioning of the bacteria at the favourable depth for growth. Gas vesicles are hollow cylindrical tubes, closed by a hollow, conical cap at each end. Both th... | [
"GO:0005198",
"GO:0012506"
] | [
"structural molecule activity",
"vesicle membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00741"
] | [
"Gas_vesicle"
] | [
7664
] | 1 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0460",
"PDOC00207"
] | [
"GP:GenProp0460",
"PROSITEDOC:PDOC00207"
] | 2 | [
"7r1c",
"8gbs"
] | 2 | [
"PUB00000481",
"PUB00001807",
"PUB00151154",
"PUB00151155",
"PUB00151157",
"PUB00151158"
] | [
"2513809",
"1864501",
"33711860",
"2586485",
"37040766",
"36868215"
] | [
"Gas vesicle proteins.",
"Structure and organization of the gas vesicle gene cluster on the Halobacterium halobium plasmid pNRC100.",
"Growth competition between <i>Halobacterium salinarium</i> strain PHH1 and mutants affected in gas vesicle synthesis.",
"Expression of two gas vacuole protein genes in Halobac... | [
1989,
1991,
1997,
1989,
2023,
2023
] | 6 | [] | [
"IPR047870"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211)",
"ecological metagenomes"
] | [
492,
7166,
2,
4
] | 4 | [] | [] | 0 | true | Family | Gas vesicle protein GvpA-like | Gas vesicle protein GvpA-like | Gas-vesicle_GvpA-like | 5 |
IPR000639 | 639 | Epoxide hydrolase-like | Epox_hydrolase-like | Family | 137,672 | false | false | The α/β hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an α/β-sheet (rather than a barrel), containing 8 strands connected by helices [ ]. The enzymes are believed to have diverged from a common ancestor, preserving t... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00412"
] | [
"EPOXHYDRLASE"
] | [
137672
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-69273",
"R-CEL-69273",
"R-HSA-211945",
"R-HSA-2142670",
"R-HSA-426048",
"R-HSA-9018682",
"R-HSA-9033241",
"R-MMU-211945",
"R-MMU-2142670",
"R-MMU-426048",
"R-MMU-69273",
"R-MMU-9018682",
"R-MMU-9033241",
"R-RNO-211945",
"R-RNO-2142670",
"R-RNO-426048",
"R-RNO-9018682",
"R-RN... | [
"REACTOME:R-BTA-69273",
"REACTOME:R-CEL-69273",
"REACTOME:R-HSA-211945",
"REACTOME:R-HSA-2142670",
"REACTOME:R-HSA-426048",
"REACTOME:R-HSA-9018682",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-211945",
"REACTOME:R-MMU-2142670",
"REACTOME:R-MMU-426048",
"REACTOME:R-MMU-69273",
"REACTOME:R-MMU-90... | 22 | [
"1a7u",
"1a88",
"1a8q",
"1a8s",
"1a8u",
"1b6g",
"1be0",
"1bee",
"1bez",
"1bn6",
"1bn7",
"1bro",
"1brt",
"1cij",
"1cqw",
"1cqz",
"1cr6",
"1cv2",
"1d07",
"1edb",
"1edd",
"1ede",
"1ehy",
"1ek1",
"1ek2",
"1g42",
"1g4h",
"1g5f",
"1hde",
"1hkh",
"1hl7",
"1iun"... | 462 | [
"PUB00001119",
"PUB00002948",
"PUB00004149",
"PUB00004958"
] | [
"7832993",
"7713895",
"8515812",
"1409539"
] | [
"Gene evolution of epoxide hydrolases and recommended nomenclature.",
"Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase.",
"Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase.",
"The alpha/be... | [
1995,
1995,
1993,
1992
] | 4 | [] | [
"IPR016292",
"IPR017209",
"IPR017727",
"IPR023489",
"IPR023594",
"IPR023791"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1086,
97020,
38498,
12,
1056
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
81,
6,
18,
19,
1,
21,
24,
3,
58,
31,
106
] | 11 | true | Family | Epoxide hydrolase-like | Epoxide hydrolase-like | Epox_hydrolase-like | 6 |
IPR000640 | 640 | Elongation factor EFG, domain V-like | EFG_V-like | Domain | 129,601 | false | false | Elongation factor 2 (EF2 or EFG) is folded into five domains, with domains I and II forming the N-terminal block, domains IV and V forming the C-terminal block, and domain III providing the covalently-linked flexible connection between the two [ ]. This entry represents the domain V of EF2 of both prokaryotes and eukar... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00679",
"SM00838"
] | [
"EFG_C",
"EFG_C"
] | [
129310,
100746
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156902",
"R-BTA-5358493",
"R-BTA-5419276",
"R-BTA-6798695",
"R-BTA-8876725",
"R-CEL-156902",
"R-CEL-5358493",
"R-CEL-5389840",
"R-CEL-6798695",
"R-DDI-156902",
"R-DDI-5358493",
"R-DDI-6798695",
"R-DME-156902",
"R-DME-5358493",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-6798695",... | [
"REACTOME:R-BTA-156902",
"REACTOME:R-BTA-5358493",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8876725",
"REACTOME:R-CEL-156902",
"REACTOME:R-CEL-5358493",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-156902",
"REACTOME:R-DDI-5358493",
"REACTOME:R... | 57 | [
"1dar",
"1efg",
"1elo",
"1fnm",
"1jqm",
"1jqs",
"1ktv",
"1n0u",
"1n0v",
"1pn6",
"1u2r",
"1wdt",
"1zm2",
"1zm3",
"1zm4",
"1zm9",
"1zn0",
"2bm0",
"2bm1",
"2bv3",
"2dy1",
"2e1r",
"2efg",
"2j7k",
"2mzw",
"2npf",
"2om7",
"2p8w",
"2p8x",
"2p8y",
"2p8z",
"2rdo"... | 334 | [
"PUB00011746",
"PUB00014828"
] | [
"11054294",
"12471894"
] | [
"Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.",
"Translational elongation factor G: a GTP-driven motor of the ribosome."
] | [
2000,
2000
] | 2 | [] | [
"IPR035649",
"IPR035650",
"IPR035651",
"IPR035654",
"IPR035655"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
943,
93150,
33650,
13,
1845
] | 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",... | [
57,
8,
25,
10,
3,
19,
32,
5,
38,
21,
6,
6,
52
] | 13 | true | Domain | Elongation factor EFG, domain V-like | Elongation factor EFG, domain V-like | EFG_V-like | 5 |
IPR000641 | 641 | CbxX/CfxQ | CbxX/CfxQ | Family | 16,340 | false | false | The Cfx genes in Ralstonia eutropha (Alcaligenes eutrophus) encode a number of Calvin cycle enzymes. The observed sizes of two of the gene products, CfxX and CfxY, are 35kDa and 27kDa respectively [ ]. No functions could be assigned to CfxX and CfxY, but CfxQ is required for the expression of rubisco. These proteins sh... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00819"
] | [
"CBXCFQXSUPER"
] | [
16340
] | 1 | [] | [] | [] | 0 | [
"3syk",
"3syl",
"3zuh"
] | 3 | [
"PUB00002204",
"PUB00003809"
] | [
"1429456",
"1787791"
] | [
"The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus.",
"Sequential activation of dual promoters by different sigma factors maintains spoVJ expression during successive developmental stages of Bacillus subtilis."
] | [
1992,
1991
] | 2 | [] | [
"IPR000470",
"IPR014232",
"IPR023835"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
62,
12090,
3909,
65,
214
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
3,
14
] | 4 | true | Family | CbxX/CfxQ | CbxX/CfxQ | CbxX/CfxQ | 7 |
IPR000642 | 642 | Peptidase M41 | Peptidase_M41 | Domain | 60,846 | false | false | This group of metallopeptidases belong to MEROPS peptidase family M41 (FtsH endopeptidase family, clan MA(E)). The predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH. The peptidase M41 family belong to a larger family of zinc metalloprotease... | [
"GO:0004176",
"GO:0004222",
"GO:0005524",
"GO:0006508"
] | [
"ATP-dependent peptidase activity",
"metalloendopeptidase activity",
"ATP binding",
"proteolysis"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF01434"
] | [
"Peptidase_M41"
] | [
60846
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24.-",
"PWY-8119",
"R-BTA-8949664",
"R-BTA-9837999",
"R-CEL-8949664",
"R-CEL-9837999",
"R-DME-8949664",
"R-DME-9837999",
"R-HSA-8949664",
"R-HSA-9837999",
"R-HSA-9840373",
"R-MMU-8949664",
"R-MMU-9837999",
"R-MMU-9840373",
"R-RNO-8949664",
"R-RNO-9837999",
"R-RNO-9840373",
"R-... | [
"EC:3.4.24.-",
"METACYC:PWY-8119",
"REACTOME:R-BTA-8949664",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-8949664",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DME-8949664",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-8949664",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9840373",
"REACTOME:R-MMU-8949664",... | 21 | [
"2ce7",
"2cea",
"2dhr",
"2di4",
"3kds",
"4eiw",
"4ww0",
"4z8x",
"6az0",
"6gcn",
"6gco",
"6nyy",
"7tdo",
"7vhp",
"7wi3",
"7wi4",
"7zbh",
"8vw9",
"8vwa",
"8vwb",
"8vwc",
"8xks",
"8xku",
"8xkv",
"8xqw",
"8xqx",
"9cz2"
] | 27 | [
"PUB00003579"
] | [
"7674922"
] | [
"Evolutionary families of metallopeptidases."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina mazei",
"Viruses",
"unclassified sequences"
] | [
35897,
23981,
1,
25,
942
] | 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",... | [
65,
4,
8,
6,
1,
26,
12,
2,
24,
20,
3,
2,
94
] | 13 | true | Domain | Peptidase M41 | Peptidase M41 | Peptidase_M41 | 7 |
IPR000643 | 643 | Iodothyronine deiodinase | Iodothyronine_deiodinase | Family | 4,102 | false | false | Iodothyronine deiodinase ( ) (DI) [ ] is the vertebrate enzyme responsible for the deiodination of the prohormone thyroxine (T4 or 3,5,3',5'-tetraiodothyronine) into the biologically active hormone T3 (3,5,3'-triiodothyronine) and of T3 into the inactive metabolite T2 (3,3'-diiodothyronine). All known DI are proteins o... | [
"GO:0004800"
] | [
"thyroxine 5'-deiodinase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF00837",
"PIRSF001330",
"PTHR11781"
] | [
"T4_deiodinase",
"IOD",
""
] | [
4047,
919,
3841
] | 3 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.21.99.3",
"1.21.99.4",
"PWY-6260",
"PWY-6261",
"R-BTA-350864",
"R-CFA-350864",
"R-HSA-350864",
"R-HSA-9844594",
"R-MMU-350864",
"R-RNO-350864",
"R-SSC-350864"
] | [
"EC:1.21.99.3",
"EC:1.21.99.4",
"METACYC:PWY-6260",
"METACYC:PWY-6261",
"REACTOME:R-BTA-350864",
"REACTOME:R-CFA-350864",
"REACTOME:R-HSA-350864",
"REACTOME:R-HSA-9844594",
"REACTOME:R-MMU-350864",
"REACTOME:R-RNO-350864",
"REACTOME:R-SSC-350864"
] | 11 | [
"4tr3",
"4tr4",
"9h48"
] | 3 | [
"PUB00002931",
"PUB00076675"
] | [
"7592917",
"8187873"
] | [
"Cloning of a cDNA for the type II iodothyronine deiodinase.",
"Activation and inactivation of thyroid hormone by type I iodothyronine deiodinase."
] | [
1995,
1994
] | 2 | [] | [
"IPR027252"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes",
"unclassified Klosneuvirinae"
] | [
164,
3900,
7,
29,
2
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
20,
14,
9
] | 4 | true | Family | Iodothyronine deiodinase | Iodothyronine deiodinase | Iodothyronine_deiodinase | 4 |
IPR000644 | 644 | CBS domain | CBS_dom | Domain | 335,156 | false | false | CBS domains are evolutionarily conserved structural domains found in a variety of non functionally-related proteins from all kingdoms of life. These domains pair together to form a intramolecular dimeric structure (CBS pair), termed Bateman domain [ , , , ]. CBS domains have been shown to bind mainly ligands with an ad... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00571",
"PS51371",
"SM00116"
] | [
"CBS",
"CBS",
"CBS"
] | [
323303,
323577,
234206
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1632852",
"R-BTA-2672351",
"R-BTA-380972",
"R-BTA-5628897",
"R-BTA-6798695",
"R-BTA-6804756",
"R-BTA-73817",
"R-BTA-9748787",
"R-CEL-2672351",
"R-CEL-6798695",
"R-CEL-73817",
"R-CEL-9748787",
"R-CFA-2672351",
"R-DDI-1614603",
"R-DDI-1632852",
"R-DDI-163680",
"R-DDI-200425",
... | [
"REACTOME:R-BTA-1632852",
"REACTOME:R-BTA-2672351",
"REACTOME:R-BTA-380972",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-73817",
"REACTOME:R-BTA-9748787",
"REACTOME:R-CEL-2672351",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-73817",
"REACTOME:R-C... | 90 | [
"1ak5",
"1b3o",
"1jcn",
"1jr1",
"1me7",
"1me8",
"1me9",
"1meh",
"1mei",
"1mew",
"1nf7",
"1nfb",
"1o50",
"1pbj",
"1pvm",
"1vr9",
"1vrd",
"1xkf",
"1y5h",
"1zfj",
"2cu0",
"2d4z",
"2ef7",
"2emq",
"2j9l",
"2ja3",
"2nyc",
"2nye",
"2o16",
"2oox",
"2ooy",
"2oux"... | 333 | [
"PUB00000457",
"PUB00014845",
"PUB00019266",
"PUB00019267",
"PUB00043686",
"PUB00099758",
"PUB00099759",
"PUB00099760"
] | [
"10200156",
"14722619",
"11524006",
"14722609",
"16275737",
"29037129",
"19153081",
"24161944"
] | [
"Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.",
"CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.",
"Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytical... | [
1999,
2004,
2001,
2004,
2005,
2017,
2009,
2013
] | 8 | [] | [
"IPR044725",
"IPR044729",
"IPR044751",
"IPR046353"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
12128,
247761,
71286,
17,
3964
] | 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",... | [
122,
45,
82,
24,
10,
90,
66,
9,
122,
81,
10,
5,
261
] | 13 | true | Domain | CBS domain | CBS domain | CBS_dom | 2 |
IPR000645 | 645 | Type II secretion system protein GspN, conserved site | T2SS_GspN_CS | Conserved_site | 220 | false | false | GspN is a cytoplasmic membrane component of the type II secretion system (T2SS). It is present in T2SS operons of a subset of Gram-negative speciesI, such as Aeromonas hydrophila (gene exeN); Erwinia carotovora (gene outN); Klebsiella pneumoniae (gene pulN); or Vibrio cholerae (gene epsN) [ ]. The size of the 'N' prote... | [
"GO:0015628",
"GO:0015627"
] | [
"protein secretion by the type II secretion system",
"type II protein secretion system complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS01142"
] | [
"T2SP_N"
] | [
220
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00879"
] | [
"PROSITEDOC:PDOC00879"
] | 1 | [] | 0 | [
"PUB00093998"
] | [
"30767847"
] | [
"Architecture, Function, and Substrates of the Type II Secretion System."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
216,
2,
2
] | 3 | [] | [] | 0 | true | Conserved_site | Type II secretion system protein GspN, conserved site | Type II secretion system protein GspN, conserved site | T2SS_GspN_CS | 8 |
IPR000646 | 646 | Pre-hexon-linking protein VIII | Adeno_PVIII | Family | 395 | false | false | This family includes the minor capsid protein VIII from adenoviruses. Protein VIII is a structural component of the virion that lashes peripentonal hexons to the hexons situated in the facets through its interaction with the capsid vertex protein [ ]. Adenoviruses are responsible for diseases such as pneumonia, cystiti... | [
"GO:0031423",
"GO:0019028"
] | [
"hexon binding",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM"
] | [
"MF_04049",
"PF01310"
] | [
"ADV_CAP8",
"Adeno_PVIII"
] | [
348,
395
] | 2 | [] | [] | [] | 0 | [
"3zif",
"6b1t",
"6cgv",
"6qi5",
"6yba",
"6z7n",
"7rd1",
"7s78",
"7tau",
"8roq",
"9lr9"
] | 11 | [
"PUB00005244",
"PUB00076673"
] | [
"7704534",
"20798312"
] | [
"Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution.",
"Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks."
] | [
1994,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Adenoviridae"
] | [
395
] | 1 | [] | [] | 0 | true | Family | Pre-hexon-linking protein VIII | Pre-hexon-linking protein VIII | Adeno_PVIII | 2 |
IPR000647 | 647 | CTF transcription factor/nuclear factor 1 | CTF/NFI | Family | 11,206 | false | false | Nuclear factor I (NF-I) or CCAAT box-binding transcription factor (CTF) [ , , ] (also known as TGGCA-binding proteins) are a family of vertebrate nuclear proteins which recognise and bind, as dimers, the palindromic DNA sequence 5'-TGGCANNNTGCCA-3'. This family was first described for its role in stimulating the initia... | [
"GO:0003700",
"GO:0006355",
"GO:0005634"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF00859",
"PTHR11492"
] | [
"CTF_NFI",
""
] | [
9555,
11145
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC00361",
"R-HSA-73980",
"R-HSA-749476"
] | [
"PROSITEDOC:PDOC00361",
"REACTOME:R-HSA-73980",
"REACTOME:R-HSA-749476"
] | 3 | [
"7qqd",
"7qqe",
"9qky"
] | 3 | [
"PUB00000833",
"PUB00001922",
"PUB00004374",
"PUB00004597",
"PUB00097185",
"PUB00097186"
] | [
"2504497",
"8543151",
"2339052",
"6216480",
"19584245",
"28962832"
] | [
"The proline-rich transcriptional activator of CTF/NF-I is distinct from the replication and DNA binding domain.",
"A proline-rich TGF-beta-responsive transcriptional activator interacts with histone H3.",
"Chicken NFI/TGGCA proteins are encoded by at least three independent genes: NFI-A, NFI-B and NFI-C with h... | [
1989,
1995,
1990,
1982,
2009,
2017
] | 6 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
11206
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
149,
2,
62,
31,
44
] | 6 | true | Family | CTF transcription factor/nuclear factor 1 | CTF transcription factor/nuclear factor 1 | CTF/NFI | 7 |
IPR000648 | 648 | Oxysterol-binding protein | Oxysterol-bd | Family | 45,159 | false | false | A number of eukaryotic proteins that seem to be involved with sterol synthesis and/or its regulation have been found [ ] to be evolutionary related. These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds a variety of oxysterols (oxygenated derivatives of choleste... | [
"GO:0008289"
] | [
"lipid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF01237",
"PTHR10972"
] | [
"Oxysterol_BP",
""
] | [
43985,
44356
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00774",
"R-DDI-1482801",
"R-DDI-192105",
"R-DDI-9013407",
"R-HSA-1482801",
"R-HSA-1660661",
"R-HSA-192105",
"R-HSA-2132295",
"R-HSA-9013407",
"R-MMU-1482801",
"R-MMU-192105",
"R-MMU-2132295",
"R-MMU-9013407",
"R-RNO-192105",
"R-RNO-2132295",
"R-SCE-1482801",
"R-SCE-192105",
"R... | [
"PROSITEDOC:PDOC00774",
"REACTOME:R-DDI-1482801",
"REACTOME:R-DDI-192105",
"REACTOME:R-DDI-9013407",
"REACTOME:R-HSA-1482801",
"REACTOME:R-HSA-1660661",
"REACTOME:R-HSA-192105",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-9013407",
"REACTOME:R-MMU-1482801",
"REACTOME:R-MMU-192105",
"REACTOME:R-M... | 20 | [
"1zht",
"1zhw",
"1zhx",
"1zhy",
"1zhz",
"1zi7",
"2d9x",
"3spw",
"4b2z",
"4f4b",
"4fes",
"4ic4",
"4inq",
"4jch",
"4ph7",
"5h2d",
"5wvr",
"5zm5",
"5zm6",
"5zm7",
"5zm8",
"7cyz",
"7dei",
"7dej",
"7v62",
"8p7a",
"9hdh",
"9hdk"
] | 28 | [
"PUB00005653",
"PUB00100201",
"PUB00100202",
"PUB00100203",
"PUB00100204",
"PUB00100205",
"PUB00100206",
"PUB00100237"
] | [
"8017104",
"17428193",
"16897474",
"15746430",
"34283201",
"11238399",
"29487131",
"30051576"
] | [
"A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein.",
"The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket.",
"Identification and characterization of PiORP1, a Petunia oxys... | [
1994,
2007,
2006,
2005,
2021,
2001,
2018,
2018
] | 8 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
45158,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
66,
12,
143,
22,
80,
57,
7,
24,
69,
7,
6,
138
] | 12 | true | Family | Oxysterol-binding protein | Oxysterol-binding protein | Oxysterol-bd | 6 |
IPR000649 | 649 | Initiation factor 2B-related | IF-2B-related | Family | 32,766 | false | false | Initiation factor 2 binds to Met-tRNA, GTP and the small ribosomal subunit. The eukaryotic translation initiation factor EIF-2B is a complex made up of five different subunits, alpha, beta, gamma, delta and epsilon, and catalyses the exchange of EIF-2-bound GDP for GTP. This family includes initiation factor 2B alpha, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01008"
] | [
"IF-2B"
] | [
32766
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
... | [
"5.3.1",
"5.3.1.23",
"PWY-4361",
"PWY-7174",
"PWY-8130",
"PWY-8131",
"PWY-8132",
"R-BTA-72731",
"R-CEL-1237112",
"R-CEL-72731",
"R-DDI-72731",
"R-DME-1237112",
"R-DRE-1237112",
"R-HSA-1237112",
"R-HSA-72731",
"R-MMU-1237112",
"R-MMU-72731",
"R-RNO-1237112",
"R-RNO-72731",
"R-SC... | [
"EC:5.3.1",
"EC:5.3.1.23",
"METACYC:PWY-4361",
"METACYC:PWY-7174",
"METACYC:PWY-8130",
"METACYC:PWY-8131",
"METACYC:PWY-8132",
"REACTOME:R-BTA-72731",
"REACTOME:R-CEL-1237112",
"REACTOME:R-CEL-72731",
"REACTOME:R-DDI-72731",
"REACTOME:R-DME-1237112",
"REACTOME:R-DRE-1237112",
"REACTOME:R-H... | 24 | [
"1t5o",
"1t9k",
"1vb5",
"1w2w",
"2a0u",
"2yrf",
"2yvk",
"3a11",
"3a9c",
"3ecs",
"3vm6",
"4ldq",
"4ldr",
"4zem",
"4zeo",
"5b04",
"5dbo",
"5yfj",
"5yfs",
"5yft",
"5yfu",
"5yfv",
"5yfw",
"5yfx",
"5yg5",
"5yg6",
"5yg7",
"5yg8",
"5yg9",
"5yga",
"6a34",
"6a35"... | 65 | [
"PUB00016714",
"PUB00016716"
] | [
"15215245",
"14551435"
] | [
"Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits.",
"A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO."
] | [
2004,
2003
] | 2 | [] | [
"IPR011559"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1834,
10209,
20271,
452
] | 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... | [
39,
5,
8,
8,
15,
16,
5,
18,
24,
4,
4,
44
] | 12 | true | Family | Initiation factor 2B-related | Initiation factor 2B-related | IF-2B-related | 8 |
IPR000650 | 650 | Geminivirus AR1 coat protein | Gem_coat_AR1 | Family | 6,281 | 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 two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00224"
] | [
"GEMCOATAR1"
] | [
6281
] | 1 | [] | [] | [] | 0 | [
"6ek5",
"6f2s"
] | 2 | [
"PUB00001133",
"PUB00001145",
"PUB00003142",
"PUB00003143",
"PUB00004348",
"PUB00004397",
"PUB00005574",
"PUB00005578"
] | [
"6526009",
"16453696",
"1919519",
"1588314",
"2829117",
"1840676",
"1984668",
"1926771"
] | [
"The nucleotide sequence of maize streak virus DNA.",
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"The nucleotide sequence and genome structure of the geminivirus miscanthus streak virus.",
"The nucleotide sequence of an infectious insect-transmissible clone of t... | [
1984,
1986,
1991,
1992,
1988,
1991,
1991,
1991
] | 8 | [
"IPR000263"
] | [] | 1 | 0 | 1 | [
"Actinomycetes",
"Malvaceae",
"Viruses"
] | [
2,
10,
6269
] | 3 | [] | [] | 0 | true | Family | Geminivirus AR1 coat protein | Geminivirus AR1 coat protein | Gem_coat_AR1 | 4 |
IPR000651 | 651 | Ras-like guanine nucleotide exchange factor, N-terminal | Ras-like_Gua-exchang_fac_N | Domain | 49,004 | false | false | The N-terminal domain of guanine nucleotide exchange factor (GEF) for Ras-like GTPases is also called REM domain (Ras exchanger motif). REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyr... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00618",
"PS50212",
"SM00229",
"cd06224"
] | [
"RasGEF_N",
"RASGEF_NTER",
"RasGEFN",
"REM"
] | [
43578,
48241,
40314,
43675
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00594",
"R-BTA-354192",
"R-BTA-392517",
"R-BTA-5673001",
"R-CEL-1433557",
"R-CEL-1433559",
"R-CEL-179812",
"R-CEL-180336",
"R-CEL-186763",
"R-CEL-193648",
"R-CEL-1963640",
"R-CEL-2179392",
"R-CEL-354192",
"R-CEL-354194",
"R-CEL-375165",
"R-CEL-381676",
"R-CEL-392517",
"R-CEL-4... | [
"PROSITEDOC:PDOC00594",
"REACTOME:R-BTA-354192",
"REACTOME:R-BTA-392517",
"REACTOME:R-BTA-5673001",
"REACTOME:R-CEL-1433557",
"REACTOME:R-CEL-1433559",
"REACTOME:R-CEL-179812",
"REACTOME:R-CEL-180336",
"REACTOME:R-CEL-186763",
"REACTOME:R-CEL-193648",
"REACTOME:R-CEL-1963640",
"REACTOME:R-CEL-... | 228 | [
"1bkd",
"1nvu",
"1nvv",
"1nvw",
"1nvx",
"1xd2",
"1xd4",
"1xdv",
"2byv",
"2ii0",
"3cf6",
"3ksy",
"4f7z",
"4jgw",
"4l9m",
"4mgi",
"4mgk",
"4mgy",
"4mgz",
"4mh0",
"4nyi",
"4nyj",
"4nym",
"4uru",
"4urv",
"4urw",
"4urx",
"4ury",
"4urz",
"4us0",
"4us1",
"4us2"... | 112 | [
"PUB00000728",
"PUB00004150",
"PUB00004162",
"PUB00006190",
"PUB00029235",
"PUB00039810",
"PUB00080062",
"PUB00080063"
] | [
"7786285",
"8479541",
"8259209",
"9690470",
"12628188",
"16452984",
"18541156",
"18236214"
] | [
"Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins.",
"Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling.",
"Proteins regulating Ras and its relatives.",
"The structural basis of the activation of Ras by Sos.",
"Str... | [
1995,
1993,
1993,
1998,
2003,
2006,
2008,
2007
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Iteradensovirus sp.",
"metagenomes"
] | [
66,
48934,
1,
3
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
17,
235,
32,
140,
123,
4,
133,
5,
2
] | 9 | true | Domain | Ras-like guanine nucleotide exchange factor, N-terminal | Ras-like guanine nucleotide exchange factor, N-terminal | Ras-like_Gua-exchang_fac_N | 9 |
IPR000652 | 652 | Triosephosphate isomerase | Triosephosphate_isomerase | Family | 44,424 | false | false | Triosephosphate isomerase ( ) (TIM) [ ] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, highly conserved in prokaryotes and euk... | [
"GO:0004807"
] | [
"triose-phosphate isomerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PF00121",
"PS51440",
"PTHR21139",
"TIGR00419",
"cd00311"
] | [
"TIM",
"TIM_2",
"",
"tim",
"TIM"
] | [
44292,
44344,
42072,
35894,
42322
] | 5 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"5.3.1.1",
"GenProp0120",
"GenProp0691",
"GenProp1306",
"GenProp1344",
"GenProp1407",
"GenProp1599",
"GenProp1612",
"PWY-1042",
"PWY-5484",
"PWY-6142",
"PWY-7003",
"PWY-8404",
"PDOC00155",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",... | [
"EC:5.3.1.1",
"GP:GenProp0120",
"GP:GenProp0691",
"GP:GenProp1306",
"GP:GenProp1344",
"GP:GenProp1407",
"GP:GenProp1599",
"GP:GenProp1612",
"METACYC:PWY-1042",
"METACYC:PWY-5484",
"METACYC:PWY-6142",
"METACYC:PWY-7003",
"METACYC:PWY-8404",
"PROSITEDOC:PDOC00155",
"REACTOME:R-CEL-70171",
... | 40 | [
"1ag1",
"1amk",
"1aw1",
"1aw2",
"1b9b",
"1btm",
"1ci1",
"1dkw",
"1hg3",
"1hti",
"1i45",
"1if2",
"1iig",
"1iih",
"1kv5",
"1lyx",
"1lzo",
"1m6j",
"1m7o",
"1m7p",
"1ml1",
"1mo0",
"1mss",
"1n55",
"1ney",
"1nf0",
"1o5x",
"1qds",
"1r2r",
"1r2s",
"1r2t",
"1spq"... | 265 | [
"PUB00000326",
"PUB00004091",
"PUB00014239",
"PUB00027646",
"PUB00029041",
"PUB00099868"
] | [
"2204417",
"2005961",
"12023819",
"12206759",
"12509510",
"31878282"
] | [
"Structure of yeast triosephosphate isomerase at 1.9-A resolution.",
"Enzyme catalysis: not different, just better.",
"Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease.",
"One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequen... | [
1990,
1991,
2002,
2002,
2003,
2019
] | 6 | [] | [
"IPR022891",
"IPR022896"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
981,
29050,
13627,
1,
765
] | 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,
1,
3,
2,
1,
8,
2,
2,
11,
14,
1,
1,
48
] | 13 | true | Family | Triosephosphate isomerase | Triosephosphate isomerase | Triosephosphate_isomerase | 6 |
IPR000653 | 653 | DegT/DnrJ/EryC1/StrS aminotransferase | DegT/StrS_aminotransferase | Family | 63,235 | false | false | This entry represents the 3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn) that are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. Members of the family have the same structural fold as members of the pyridoxal phosphate (PLP)-dependent aspartate amino... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"PF01041",
"PIRSF000390",
"PTHR30244",
"cd00616"
] | [
"DegT_DnrJ_EryC1",
"PLP_StrS",
"",
"AHBA_syn"
] | [
63186,
53648,
61604,
52088
] | 4 | [
"EC",
"GP",
"GP",
"GP"
] | [
"2.6.1",
"GenProp1403",
"GenProp1468",
"GenProp1534"
] | [
"EC:2.6.1",
"GP:GenProp1403",
"GP:GenProp1468",
"GP:GenProp1534"
] | 4 | [
"1b9h",
"1b9i",
"1mdo",
"1mdx",
"1mdz",
"1o61",
"1o62",
"1o69",
"1qz9",
"2c7t",
"2c81",
"2fn6",
"2fni",
"2fnu",
"2gms",
"2gmu",
"2oga",
"2oge",
"2po3",
"2r0t",
"3b8x",
"3bb8",
"3bcx",
"3bn1",
"3dr4",
"3dr7",
"3frk",
"3gr9",
"3ju7",
"3nu7",
"3nu8",
"3nub"... | 87 | [
"PUB00006322",
"PUB00006531",
"PUB00008019",
"PUB00016775",
"PUB00016898",
"PUB00023569",
"PUB00028947",
"PUB00035507",
"PUB00039920",
"PUB00042185",
"PUB00050697",
"PUB00070977",
"PUB00079514",
"PUB00079515"
] | [
"7748903",
"10800595",
"9238101",
"10223296",
"9914259",
"10433690",
"12429098",
"17109392",
"16894611",
"17456741",
"18247575",
"10673430",
"17504214",
"11933250"
] | [
"Pyridoxal phosphate-dependent enzymes.",
"The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes.",
"Identification of stsC, the gene encoding the L-glutamine:scyllo-inosose aminotransferase from streptomycin-producing Streptomycetes.",
"Common structural elements in the architecture of the cofa... | [
1995,
2000,
1997,
1999,
1998,
1999,
2002,
2006,
2006,
2007,
2008,
2000,
2007,
2001
] | 14 | [] | [
"IPR012749",
"IPR020026",
"IPR022850",
"IPR026385",
"IPR030967"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1267,
58481,
1239,
77,
2171
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | DegT/DnrJ/EryC1/StrS aminotransferase | DegT/DnrJ/EryC1/StrS aminotransferase | DegT/StrS_aminotransferase | 5 |
IPR000654 | 654 | G-protein alpha subunit, group Q | Gprotein_alpha_Q | Family | 4,737 | false | false | Guanine nucleotide binding proteins (G-proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian cells, regulating systems as diverse as sensory perce... | [
"GO:0001664",
"GO:0003924",
"GO:0007186"
] | [
"G protein-coupled receptor binding",
"GTPase activity",
"G protein-coupled receptor signaling pathway"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS"
] | [
"PR00442"
] | [
"GPROTEINAQ"
] | [
4737
] | 1 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"GenProp2096",
"GenProp2098",
"R-BTA-112043",
"R-BTA-202040",
"R-BTA-399997",
"R-BTA-416476",
"R-BTA-418592",
"R-BTA-428930",
"R-BTA-434316",
"R-BTA-456926",
"R-BTA-6814122",
"R-BTA-9856530",
"R-BTA-9860927",
"R-CFA-112043",
"R-CFA-202040",
"R-CFA-399997",
"R-CFA-416476",
"R-CFA-41... | [
"GP:GenProp2096",
"GP:GenProp2098",
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418592",
"REACTOME:R-BTA-428930",
"REACTOME:R-BTA-434316",
"REACTOME:R-BTA-456926",
"REACTOME:R-BTA-6814122",
"REACTOME:R-BTA-9856530",
"REA... | 76 | [
"2bcj",
"2rgn",
"3ah8",
"4ekc",
"4ekd",
"4gnk",
"4qj3",
"4qj4",
"4qj5",
"5do9",
"6oij",
"6vu5",
"7dfl",
"7ezm",
"7f6g",
"7f6h",
"7f6i",
"7f8w",
"7rkf",
"7sq2",
"7try",
"7w3z",
"7w40",
"7xow",
"7xxh",
"8ia7",
"8iys",
"8jpb",
"8jpc",
"8jpe",
"8qeg",
"8qeh"... | 41 | [
"PUB00005142",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172",
"PUB00015180"
] | [
"1902986",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385",
"12554647"
] | [
"Diversity of G proteins in signal transduction.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"G protein signaling: insights from new structures.",
"Regulation of G prote... | [
1991,
2004,
2004,
2004,
2001,
1997,
2002,
2003
] | 8 | [
"IPR001019"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4737
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
15,
4,
11,
10,
17
] | 6 | true | Family | G-protein alpha subunit, group Q | G-protein alpha subunit, group Q | Gprotein_alpha_Q | 8 |
IPR000655 | 655 | Regulatory protein cro-like | Cro-like | Family | 596 | false | false | Bacteriophage lambda encodes two repressors: the Cro repressor that acts to turn off early gene transcription during the lytic cycle, and the lambda or cI repressor that is required to maintain lysogenic growth. Together the Cro and cI repressors form a helix-turn-helix (HTH) superfamily. The lambda Cro repressor binds... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS"
] | [
"PF09048",
"PIRSF003217",
"PR00030"
] | [
"Cro",
"Cro_protein",
"HTHCRO"
] | [
533,
299,
124
] | 3 | [] | [] | [] | 0 | [
"1cop",
"1d1l",
"1d1m",
"1orc",
"1zug",
"2a63",
"2cro",
"2cw1",
"2ecs",
"2orc",
"2ovg",
"2pij",
"3cro",
"3orc",
"4cro",
"5cro",
"5w8z",
"6cro"
] | 18 | [
"PUB00016684",
"PUB00016685",
"PUB00016686"
] | [
"9653036",
"2598646",
"15062080"
] | [
"Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity.",
"Reduced immune adherence of antigen/antibody complexes formed in the presence of complement in vivo and in vitro.",
"Secondary structure switching in Cro protein evolution."
] | [
1998,
1989,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Infirmifilum",
"Viruses",
"metagenomes"
] | [
539,
2,
53,
2
] | 4 | [] | [] | 0 | true | Family | Regulatory protein cro-like | Regulatory protein cro-like | Cro-like | 5 |
IPR000657 | 657 | Geminivirus AL3 coat protein | Gemini_AL3 | Family | 4,534 | 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 two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous... | [
"GO:0016032"
] | [
"viral process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF01407",
"PR00231"
] | [
"Gemini_AL3",
"GEMCOATAL3"
] | [
4534,
4258
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001133",
"PUB00001145",
"PUB00003142",
"PUB00003143",
"PUB00003527",
"PUB00004348",
"PUB00004397",
"PUB00005574",
"PUB00005578",
"PUB00005599"
] | [
"6526009",
"16453696",
"1919519",
"1588314",
"8794317",
"2829117",
"1840676",
"1984668",
"1926771",
"8030214"
] | [
"The nucleotide sequence of maize streak virus DNA.",
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"The nucleotide sequence and genome structure of the geminivirus miscanthus streak virus.",
"The nucleotide sequence of an infectious insect-transmissible clone of t... | [
1984,
1986,
1991,
1992,
1996,
1988,
1991,
1991,
1991,
1994
] | 10 | [] | [] | 0 | 0 | null | [
"Mesangiospermae",
"Viruses"
] | [
17,
4517
] | 2 | [] | [] | 0 | true | Family | Geminivirus AL3 coat protein | Geminivirus AL3 coat protein | Gemini_AL3 | 2 |
IPR000659 | 659 | Pyridoxamine 5'-phosphate oxidase | Pyridox_Oxase | Family | 24,756 | false | false | Pyridoxamine 5'-phosphate oxidase ( ) is an enzyme that is involved in the de novo synthesis of pyridoxine (vitamin B6) and pyridoxal phosphate. It oxidizes pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P. The enzyme requires the presence of flavin mononucleotide (FMN) as a cofactor, although there is ... | [
"GO:0004733",
"GO:0010181",
"GO:0008615"
] | [
"pyridoxamine phosphate oxidase activity",
"FMN binding",
"pyridoxine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_01629",
"PIRSF000190",
"PTHR10851",
"TIGR00558"
] | [
"PdxH",
"Pyd_amn-ph_oxd",
"",
"pdxH"
] | [
17968,
20185,
24650,
19064
] | 4 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.4.3.5",
"GenProp1604",
"GenProp1633",
"PWY-7204",
"PWY-7282",
"PDOC00815",
"R-BTA-964975",
"R-CEL-964975",
"R-DDI-964975",
"R-HSA-964975",
"R-MMU-964975",
"R-RNO-964975",
"R-SCE-964975",
"R-SPO-964975"
] | [
"EC:1.4.3.5",
"GP:GenProp1604",
"GP:GenProp1633",
"METACYC:PWY-7204",
"METACYC:PWY-7282",
"PROSITEDOC:PDOC00815",
"REACTOME:R-BTA-964975",
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-964975",
"REACTOME:R-HSA-964975",
"REACTOME:R-MMU-964975",
"REACTOME:R-RNO-964975",
"REACTOME:R-SCE-964975",
"... | 14 | [
"1ci0",
"1dnl",
"1g76",
"1g77",
"1g78",
"1g79",
"1jnw",
"1nrg",
"1t9m",
"1ty9",
"1wv4",
"2a2j",
"3hy8",
"4hms",
"4hmt",
"4hmu",
"4hmv",
"4hmw",
"4hmx",
"6h00",
"6ylz",
"6ymh",
"8qyt",
"8qyw",
"8ros"
] | 25 | [
"PUB00001735",
"PUB00002199",
"PUB00002264",
"PUB00055044",
"PUB00155385"
] | [
"8586283",
"1356963",
"7896706",
"20675471",
"23897464"
] | [
"Molecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium. Pseudomonas aureofaciens 30-84.",
"Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations.",
"Sterol uptake induced by an impairment ... | [
1995,
1992,
1995,
2010,
2013
] | 5 | [] | [
"IPR021198",
"IPR024015"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
18998,
5409,
4,
345
] | 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",... | [
6,
1,
1,
5,
1,
6,
1,
1,
8,
2,
1,
1,
12
] | 13 | true | Family | Pyridoxamine 5'-phosphate oxidase | Pyridoxamine 5'-phosphate oxidase | Pyridox_Oxase | 3 |
IPR000662 | 662 | Capsid protein VP1,Polyomavirus | Capsid_VP1_Polyomavir | Family | 5,376 | false | false | This entry represents the major capsid protein VP1 (viral protein 1) from Polyomaviruses, such as Murine polyomavirus (strain P16 small-plaque) (MPyV) [ ]. Polyomaviruses are dsDNA viruses with no RNA stage in their life cycle. The virus capsid is composed of 72 icosahedral units, each of which is composed of five copi... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PIRSF"
] | [
"PF00718",
"PIRSF003376"
] | [
"Polyoma_coat",
"Capsid_VP1_Polyomavir"
] | [
5376,
997
] | 2 | [] | [] | [] | 0 | [
"1cn3",
"1sid",
"1sie",
"1sva",
"1vpn",
"1vps",
"3bwq",
"3bwr",
"3iys",
"3nxd",
"3nxg",
"3s7v",
"3s7x",
"4fmg",
"4fmh",
"4fmi",
"4fmj",
"4jcd",
"4jce",
"4jcf",
"4mbx",
"4mby",
"4mbz",
"4mj0",
"4mj1",
"4pcg",
"4pch",
"4poq",
"4por",
"4pos",
"4pot",
"4u5z"... | 101 | [
"PUB00006154",
"PUB00035621"
] | [
"9628860",
"12928495"
] | [
"Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry.",
"Chaperone-mediated in vitro assembly of Polyomavirus capsids."
] | [
1998,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Polyomaviridae"
] | [
5376
] | 1 | [] | [] | 0 | true | Family | Capsid protein VP1,Polyomavirus | Capsid protein VP1,Polyomavirus | Capsid_VP1_Polyomavir | 6 |
IPR000664 | 664 | Lethal(2) giant larvae protein | Lethal2_giant | Family | 9,367 | false | false | The lethal(2)giant larvae protein (Lgl) of Drosophila is essential for polarised epithelia development, for cell polarity associated with asymmetric cell division of neuroblasts during development and for oocyte polarity formation. As a result of alternative splicing Lgl has two isoforms that differ in their C-terminal... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00962"
] | [
"LETHAL2GIANT"
] | [
9367
] | 1 | [] | [] | [] | 0 | [
"6n8p",
"6n8q",
"6n8r",
"6n8s",
"8r3y",
"9ejk",
"9ejl",
"9ejm"
] | 8 | [
"PUB00000814",
"PUB00005948",
"PUB00094511",
"PUB00094512",
"PUB00094513"
] | [
"3036370",
"8389031",
"21856246",
"16170365",
"15983403"
] | [
"Structure of the l(2)gl gene of Drosophila and delimitation of its tumor suppressor domain.",
"The l(2)gl homologue of Drosophila pseudoobscura suppresses tumorigenicity in transgenic Drosophila melanogaster.",
"Lgl1 activation of rab10 promotes axonal membrane trafficking underlying neuronal polarization.",
... | [
1987,
1993,
2011,
2006,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9367
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
52,
6,
21,
12,
27
] | 6 | true | Family | Lethal(2) giant larvae protein | Lethal(2) giant larvae protein | Lethal2_giant | 1 |
IPR000667 | 667 | Peptidase S13, D-Ala-D-Ala carboxypeptidase C | Peptidase_S13 | Family | 18,035 | false | false | This family of serine peptidases belong to MEROPS peptidase family S13 (D-Ala-D-Ala carboxypeptidase C, clan SE). The active site residues occur in the motif SXXK. D-Ala-D-Ala carboxypeptidase C is involved in the metabolism of cell components [ , ]; it is synthesised with a leader peptide to target it to the cell memb... | [
"GO:0004185",
"GO:0006508"
] | [
"serine-type carboxypeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PF02113",
"PR00922",
"PTHR30023",
"TIGR00666"
] | [
"Peptidase_S13",
"DADACBPTASE3",
"",
"PBP4"
] | [
18009,
17149,
17939,
14808
] | 4 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.4.16.4",
"PWY-5265",
"PWY-6471"
] | [
"EC:3.4.16.4",
"METACYC:PWY-5265",
"METACYC:PWY-6471"
] | 3 | [
"1w5d",
"1w79",
"1w8q",
"1w8y",
"2ex2",
"2ex6",
"2ex8",
"2ex9",
"2exa",
"2exb",
"2j9p",
"2vgj",
"2vgk",
"2wke",
"2xdm",
"2xk1",
"2xln",
"2y4a",
"2y55",
"2y59",
"3a3d",
"3a3e",
"3a3f",
"3a3i",
"3v39",
"3zcz",
"3zvt",
"3zvw",
"4b4x",
"4b4z",
"4ben",
"5ceb"... | 35 | [
"PUB00000120",
"PUB00000522",
"PUB00003576",
"PUB00035543"
] | [
"1741619",
"8439290",
"7845208",
"16411754"
] | [
"Serine beta-lactamases and penicillin-binding proteins.",
"Evolutionary families of peptidases.",
"Families of serine peptidases.",
"Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics."
] | [
1991,
1993,
1994,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
36,
17418,
133,
448
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Peptidase S13, D-Ala-D-Ala carboxypeptidase C | Peptidase S13, D-Ala-D-Ala carboxypeptidase C | Peptidase_S13 | 4 |
IPR000668 | 668 | Peptidase C1A, papain C-terminal | Peptidase_C1A_C | Domain | 74,967 | false | false | This entry represents the papain C-terminal of a group of proteins that belong to the cysteine peptidase family C1, sub-family C1A (papain family, clan CA). A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usual... | [
"GO:0008234",
"GO:0006508"
] | [
"cysteine-type peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"SMART"
] | [
"PF00112",
"PR00705",
"SM00645"
] | [
"Peptidase_C1",
"PAPAIN",
"Pept_C1"
] | [
74861,
44513,
66515
] | 3 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.4.22",
"GenProp1728",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1592389",
"R-BTA-1679131",
"R-BTA-2022377",
"R-BTA-204005",
"R-BTA-2132295",
"R-BTA-432720",
"R-BTA-5683826",
"R-BTA-5694530",
"R-BTA-6798695",
"R-BTA-8939242",
"R-CEL-1474228",
"R-CEL-1592389",
"R-CEL-2022377",
"R-C... | [
"EC:3.4.22",
"GP:GenProp1728",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-1679131",
"REACTOME:R-BTA-2022377",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-5683826",
"REACTOME:R-BTA-5694530",
"RE... | 102 | [
"1aec",
"1aim",
"1atk",
"1au0",
"1au2",
"1au3",
"1au4",
"1ayu",
"1ayv",
"1ayw",
"1bgo",
"1bp4",
"1bqi",
"1by8",
"1cjl",
"1cpj",
"1cqd",
"1cs8",
"1csb",
"1cte",
"1cvz",
"1deu",
"1ef7",
"1ewl",
"1ewm",
"1ewo",
"1ewp",
"1f29",
"1f2a",
"1f2b",
"1f2c",
"1fh0"... | 496 | [
"PUB00003577",
"PUB00011704",
"PUB00015451",
"PUB00020025",
"PUB00030423",
"PUB00076953",
"PUB00076965"
] | [
"7845226",
"11517925",
"12188906",
"9891971",
"14725770",
"7044372",
"1363350"
] | [
"Families of cysteine peptidases.",
"Evolutionary lines of cysteine peptidases.",
"Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidas... | [
1994,
2001,
2002,
1998,
2004,
1982,
1992
] | 7 | [] | [
"IPR039412",
"IPR039417"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
366,
4419,
69636,
264,
282
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
158,
38,
48,
17,
147,
80,
145,
78,
205
] | 9 | true | Domain | Peptidase C1A, papain C-terminal | Peptidase C1A, papain C-terminal | Peptidase_C1A_C | 7 |
IPR000669 | 669 | Mannitol dehydrogenase | Mannitol_DH | Family | 20,876 | false | false | Mannitol dehydrogenases catalyse the NAD-dependent reduction of mannitol-1-phosphates as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to form the corresponding sugar phosphates, which are then converted to glyco... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00084"
] | [
"MTLDHDRGNASE"
] | [
20876
] | 1 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC"
] | [
"1.1.1",
"1.1.1.17",
"PWY-6531",
"PDOC00751"
] | [
"EC:1.1.1",
"EC:1.1.1.17",
"METACYC:PWY-6531",
"PROSITEDOC:PDOC00751"
] | 4 | [
"1lj8",
"1m2w",
"3h2z",
"4im7",
"5itg",
"5jnm",
"7rk4",
"7rk5"
] | 8 | [
"PUB00002028",
"PUB00003120"
] | [
"1322373",
"8254318"
] | [
"Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system.",
"Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodo... | [
1992,
1993
] | 2 | [] | [
"IPR023028"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacterium salinarum",
"Viruses",
"metagenomes"
] | [
18888,
1901,
1,
3,
83
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
4,
1,
2
] | 3 | true | Family | Mannitol dehydrogenase | Mannitol dehydrogenase | Mannitol_DH | 2 |
IPR000670 | 670 | Urotensin II receptor | Urot_II_rcpt | Family | 1,783 | false | false | Urotensin II (UII) is a vasoactive somatostatin-like or cortistatin-like peptide hormone. However, despite the apparent structural similarity to these peptide hormones, they are not homologous to UII. Urotensin II was first identified in fish spinal cord but later found in humans and other mammals [ ]. In fish, UII is ... | [
"GO:0001604",
"GO:0007186",
"GO:0008217",
"GO:0097746",
"GO:0016020"
] | [
"urotensin II receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of blood pressure",
"blood vessel diameter maintenance",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00647"
] | [
"UROTENSIN2R"
] | [
1783
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"365",
"R-HSA-375276",
"R-HSA-416476",
"R-MMU-375276",
"R-MMU-416476",
"R-RNO-375276",
"R-RNO-416476"
] | [
"IUPHAR:365",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476"
] | 7 | [] | 0 | [
"PUB00000246",
"PUB00007095",
"PUB00007096",
"PUB00007097",
"PUB00063803",
"PUB00063804"
] | [
"7733947",
"10499587",
"11020490",
"11282300",
"15102493",
"3724202"
] | [
"A novel putative neuropeptide receptor expressed in neural tissue, including sensory epithelia.",
"Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14.",
"Human urotensin II mediates vasoconstriction via an increase in inositol phosphates.",
"Human urotensin-II, the most ... | [
1995,
1999,
2000,
2000,
2004,
1986
] | 6 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1783
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
1,
2,
2
] | 4 | true | Family | Urotensin II receptor | Urotensin II receptor | Urot_II_rcpt | 1 |
IPR000671 | 671 | Peptidase A31 family | Peptidase_A31 | Family | 10,792 | false | false | This group represents metallopeptidases of the MEROPS peptidase family A31 (HybD endopeptidase family). Peptidase family A31 includes endopeptidases involved in hydrogenase maturation. HycI (hydrogenase 3 maturation protease) is a protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase ... | [
"GO:0008047",
"GO:0008233"
] | [
"enzyme activator activity",
"peptidase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PF01750",
"PR00446",
"PTHR30302",
"TIGR00072"
] | [
"HycI",
"HYDRGNUPTAKE",
"",
"hydrog_prot"
] | [
9789,
8592,
10636,
10653
] | 4 | [] | [] | [] | 0 | [
"1cfz",
"2e85",
"2i8l",
"2kml",
"3pu6",
"5ija",
"5ttx",
"5zby"
] | 8 | [
"PUB00001457",
"PUB00011020",
"PUB00011021",
"PUB00011022",
"PUB00011023",
"PUB00011024",
"PUB00013568",
"PUB00013569",
"PUB00014601"
] | [
"7851435",
"10727938",
"8125094",
"10795682",
"10331925",
"8405419",
"11336840",
"12196162",
"10226043"
] | [
"Characterisation of a protease from Escherichia coli involved in hydrogenase maturation.",
"Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation.",
"Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed... | [
1995,
2000,
1994,
2000,
1999,
1993,
2001,
2002,
1999
] | 9 | [] | [
"IPR004411",
"IPR004419",
"IPR004420"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
779,
9790,
6,
217
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Family | Peptidase A31 family | Peptidase A31 family | Peptidase_A31 | 6 |
IPR000672 | 672 | Tetrahydrofolate dehydrogenase/cyclohydrolase | THF_DH/CycHdrlase | Family | 43,468 | false | false | Enzymes that participate in the transfer of one-carbon units require the coenzyme tetrahydrofolate (THF). Various reactions generate one-carbon derivatives of THF, which can be interconverted between different oxidation states by methylene-THF dehydrogenase ( ), methenyl-THF cyclohydrolase ( ) and formyl-THF synthetase... | [
"GO:0004488"
] | [
"methylenetetrahydrofolate dehydrogenase (NADP+) activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PRINTS"
] | [
"MF_01576",
"PR00085"
] | [
"THF_DHG_CYH",
"THFDHDRGNASE"
] | [
38230,
43225
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.5",
"3.5.4.9",
"PWY-1722",
"PWY-2201",
"PWY-3841",
"PWY-5030",
"PWY-5497",
"PWY-6613",
"PWY-7909",
"PWY-8303",
"PDOC00616",
"R-BTA-196757",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.5",
"EC:3.5.4.9",
"METACYC:PWY-1722",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"METACYC:PWY-6613",
"METACYC:PWY-7909",
"METACYC:PWY-8303",
"PROSITEDOC:PDOC00616",
"REACTOME:R-BTA-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"... | 18 | [
"1a4i",
"1b0a",
"1dia",
"1dib",
"1dig",
"1edz",
"1ee9",
"2c2x",
"2c2y",
"3l07",
"3ngl",
"3ngx",
"3p2o",
"4a26",
"4a5o",
"4b4u",
"4b4v",
"4b4w",
"4cjx",
"5nhs",
"5o22",
"5o28",
"5o2a",
"5tc4",
"5zf1",
"6ape",
"6de8",
"6deb",
"6ecp",
"6ecq",
"6ecr",
"6jib"... | 54 | [
"PUB00000304",
"PUB00000651"
] | [
"2541774",
"8485162"
] | [
"Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme.",
"The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
] | [
1989,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
688,
28853,
13152,
20,
755
] | 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",... | [
17,
1,
26,
7,
1,
25,
11,
3,
11,
20,
3,
3,
21
] | 13 | true | Family | Tetrahydrofolate dehydrogenase/cyclohydrolase | Tetrahydrofolate dehydrogenase/cyclohydrolase | THF_DH/CycHdrlase | 9 |
IPR000673 | 673 | Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase | Sig_transdc_resp-reg_Me-estase | Domain | 30,216 | false | false | This entry represents the signal transduction response regulator CheB involved in chemotaxis. CheB methylesterase is responsible for removing the methyl group from the gamma-glutamyl methyl ester residues in the methyl-accepting chemotaxis proteins (MCP). The enzyme catalyses the reaction: protein L-glutamate O-methyl ... | [
"GO:0000156",
"GO:0008984",
"GO:0000160",
"GO:0006935",
"GO:0005737"
] | [
"phosphorelay response regulator activity",
"protein-glutamate methylesterase activity",
"phosphorelay signal transduction system",
"chemotaxis",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM",
"PROFILE",
"CDD"
] | [
"PF01339",
"PS50122",
"cd16432"
] | [
"CheB_methylest",
"CHEB",
"CheB_Rec"
] | [
30215,
29961,
18496
] | 3 | [
"EC",
"EC",
"PROSITEDOC"
] | [
"3.1.1.61",
"3.5.1.44",
"PDOC50122"
] | [
"EC:3.1.1.61",
"EC:3.5.1.44",
"PROSITEDOC:PDOC50122"
] | 3 | [
"1a2o",
"1chd",
"3sft",
"6ymz",
"7esg"
] | 5 | [
"PUB00010651",
"PUB00011096",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"12372152",
"10966457",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis.",
"Specificity in two-component signal transduction pathways.... | [
2002,
2000,
2005,
2007,
2002,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
604,
29301,
23,
288
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase | Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase | Sig_transdc_resp-reg_Me-estase | 4 |
IPR000674 | 674 | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead | Ald_Oxase/Xan_DH_a/b | Domain | 66,596 | false | false | Aldehyde oxidase ( ) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase ( ) catalyses the hydrogenation of xanthine to urate, and also requires ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01315",
"SM01008"
] | [
"Ald_Xan_dh_C",
"Ald_Xan_dh_C"
] | [
52099,
66420
] | 2 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1236",
"GenProp1255",
"GenProp1469",
"GenProp1753",
"R-CEL-964975",
"R-DDI-74259",
"R-DDI-964975",
"R-DDI-9748787",
"R-DME-74259",
"R-DME-964975",
"R-DME-9748787",
"R-GGA-421178",
"R-HSA-74259",
"R-HSA-8851680",
"R-HSA-964975",
"R-HSA-9748787",
"R-MMU-74259",
"R-MMU-8851680... | [
"GP:GenProp1236",
"GP:GenProp1255",
"GP:GenProp1469",
"GP:GenProp1753",
"REACTOME:R-CEL-964975",
"REACTOME:R-DDI-74259",
"REACTOME:R-DDI-964975",
"REACTOME:R-DDI-9748787",
"REACTOME:R-DME-74259",
"REACTOME:R-DME-964975",
"REACTOME:R-DME-9748787",
"REACTOME:R-GGA-421178",
"REACTOME:R-HSA-7425... | 24 | [
"1dgj",
"1ffu",
"1ffv",
"1fiq",
"1fo4",
"1jro",
"1jrp",
"1n5w",
"1n5x",
"1n60",
"1n61",
"1n62",
"1n63",
"1rm6",
"1sb3",
"1sij",
"1t3q",
"1v97",
"1vdv",
"1vlb",
"1wyg",
"1zxi",
"2ckj",
"2e1q",
"2e3t",
"2w3r",
"2w3s",
"2w54",
"2w55",
"3am9",
"3amz",
"3an1"... | 86 | [
"PUB00005209",
"PUB00015693",
"PUB00019122",
"PUB00153681"
] | [
"7502041",
"7815950",
"10430865",
"5849820"
] | [
"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.",
"Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans.",
"Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur fla... | [
1995,
1994,
1999,
1965
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
969,
52227,
12352,
1048
] | 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",... | [
36,
3,
4,
7,
3,
6,
15,
1,
20,
23,
80
] | 11 | true | Domain | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead | Ald_Oxase/Xan_DH_a/b | 1 |
IPR000675 | 675 | Cutinase/acetylxylan esterase | Cutinase/axe | Family | 16,365 | false | false | Plant pathogenic fungi produce extracellular degradative enzymes [ ] that play an important role in pathogenesis. They include cutinase, which hydrolyses cutin, facilitating fungus penetration through the cuticle. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The prote... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01083",
"SM01110"
] | [
"Cutinase",
"Cutinase"
] | [
15867,
15858
] | 2 | [
"EC"
] | [
"3.1.1.74"
] | [
"EC:3.1.1.74"
] | 1 | [
"1agy",
"1bs9",
"1cex",
"1cua",
"1cub",
"1cuc",
"1cud",
"1cue",
"1cuf",
"1cug",
"1cuh",
"1cui",
"1cuj",
"1cus",
"1cuu",
"1cuv",
"1cuw",
"1cux",
"1cuy",
"1cuz",
"1ffa",
"1ffb",
"1ffc",
"1ffd",
"1ffe",
"1g66",
"1oxm",
"1qoz",
"1xza",
"1xzb",
"1xzc",
"1xzd"... | 71 | [
"PUB00003749",
"PUB00004118",
"PUB00030352",
"PUB00100716",
"PUB00100717",
"PUB00100718",
"PUB00100719"
] | [
"1557023",
"1560844",
"11243887",
"20103719",
"23843969",
"34705546",
"19225166"
] | [
"Cloning and analysis of CUT1, a cutinase gene from Magnaporthe grisea.",
"Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.",
"Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism... | [
1992,
1992,
2000,
2010,
2013,
2022,
2009
] | 7 | [] | [
"IPR011150"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
6,
7338,
197,
8815,
9
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
3
] | 1 | true | Family | Cutinase/acetylxylan esterase | Cutinase/acetylxylan esterase | Cutinase/axe | 7 |
IPR000677 | 677 | Chitinase-like | Chitinase-like | Family | 1,741 | false | false | This entry includes Chitinase 1/2 from Tulipa saxatilis subsp. bakeri. They are class IIIb chitinases [ ]. | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00551"
] | [
"2SGLOBULIN"
] | [
1741
] | 1 | [] | [] | [] | 0 | [
"1nar",
"3sim",
"4rl3",
"7xmh"
] | 4 | [
"PUB00095174"
] | [
"9692212"
] | [
"Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus Tulipa."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Fadolivirus FV1/VV64"
] | [
32,
1708,
1
] | 3 | [
"Homo sapiens",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
1,
7,
15
] | 3 | true | Family | Chitinase-like | Chitinase-like | Chitinase-like | 1 |
IPR000678 | 678 | Nuclear transition protein 2 | TP2 | Family | 153 | false | false | null | [
"GO:0003677",
"GO:0007283",
"GO:0000786",
"GO:0005634"
] | [
"DNA binding",
"spermatogenesis",
"nucleosome",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PFAM",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PF01254",
"PS00970",
"PS00971",
"PTHR17488"
] | [
"TP2",
"TP2_1",
"TP2_2",
""
] | [
147,
95,
93,
145
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00749"
] | [
"PROSITEDOC:PDOC00749"
] | 1 | [] | 0 | [
"PUB00000203"
] | [
"1930189"
] | [
"Mammalian spermatid specific protein, TP2, is a zinc metalloprotein with two finger motifs."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Euteleostomi"
] | [
5,
148
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
4
] | 3 | true | Family | Nuclear transition protein 2 | Nuclear transition protein 2 | TP2 | 8 |
IPR000679 | 679 | Zinc finger, GATA-type | Znf_GATA | Domain | 56,433 | false | false | This entry represents GATA-type zinc fingers (Znf). A number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins), specifically bind the DNA sequence (A/T)GATA(A/G) [ ] in the regulatory regions of genes. They are consequently termed GATA-binding transcription fa... | [
"GO:0043565",
"GO:0006355"
] | [
"sequence-specific DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00320",
"PR00619",
"PS00344",
"PS50114",
"SM00401",
"cd00202"
] | [
"GATA",
"GATAZNFINGER",
"GATA_ZN_FINGER_1",
"GATA_ZN_FINGER_2",
"ZnF_GATA",
"ZnF_GATA"
] | [
51407,
17021,
36861,
46763,
51065,
49441
] | 6 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00300",
"R-BTA-983231",
"R-CEL-5683826",
"R-CEL-8936459",
"R-CFA-983231",
"R-DDI-5689880",
"R-DDI-9018519",
"R-DME-5683826",
"R-DME-5689880",
"R-DME-8936459",
"R-DME-8939236",
"R-DME-9018519",
"R-DME-983231",
"R-DRE-9018519",
"R-DRE-983231",
"R-GGA-5683826",
"R-GGA-8939236",
"... | [
"PROSITEDOC:PDOC00300",
"REACTOME:R-BTA-983231",
"REACTOME:R-CEL-5683826",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CFA-983231",
"REACTOME:R-DDI-5689880",
"REACTOME:R-DDI-9018519",
"REACTOME:R-DME-5683826",
"REACTOME:R-DME-5689880",
"REACTOME:R-DME-8936459",
"REACTOME:R-DME-8939236",
"REACTOME:R-... | 71 | [
"1gat",
"1gau",
"1gnf",
"1y0j",
"2gat",
"2kae",
"2l6y",
"2l6z",
"2m9w",
"2vus",
"2vut",
"2vuu",
"3dfv",
"3dfx",
"3gat",
"3vd6",
"3vek",
"4gat",
"4hc7",
"4hc9",
"4hca",
"5gat",
"5o9b",
"6gat",
"6zfv",
"7ao8",
"7ao9",
"7aoa",
"7gat",
"8j48",
"8vg0",
"8vg1"... | 32 | [
"PUB00000834",
"PUB00001896",
"PUB00005167"
] | [
"2776214",
"2249770",
"8332909"
] | [
"The erythroid-specific transcription factor Eryf1: a new finger protein.",
"Activity and tissue-specific expression of the transcription factor NF-E1 multigene family.",
"NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1."
] | [
1989,
1990,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
170,
147,
56094,
8,
14
] | 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... | [
117,
35,
112,
27,
46,
61,
7,
79,
56,
10,
5,
154
] | 12 | true | Domain | Zinc finger, GATA-type | Zinc finger, GATA-type | Znf_GATA | 7 |
IPR000680 | 680 | Borrelia lipoprotein | Borrelia_lipo | Family | 3,029 | false | false | This family of lipoproteins is found in Borrelia spirochetes. They are known as variable large proteins (vlp). The function of these proteins is uncertain, but it may serve to avoid the host immune response by changing from one surface exposed variable major outer membrane lipoprotein to another [ ]. | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF00921"
] | [
"Lipoprotein_2"
] | [
3029
] | 1 | [] | [] | [] | 0 | [
"1l8w"
] | 1 | [
"PUB00081179"
] | [
"2385585"
] | [
"Juxtaposition of expressed variable antigen genes with a conserved telomere in the bacterium Borrelia hermsii."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Borreliaceae"
] | [
3029
] | 1 | [] | [] | 0 | true | Family | Borrelia lipoprotein | Borrelia lipoprotein | Borrelia_lipo | 4 |
IPR000681 | 681 | Beta 3 adrenoceptor | ADRB3_rcpt | Family | 257 | 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:0004939",
"GO:0007186",
"GO:0007189",
"GO:0016020"
] | [
"beta-adrenergic receptor activity",
"G protein-coupled receptor signaling pathway",
"adenylate cyclase-activating G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00563"
] | [
"ADRENRGCB3AR"
] | [
257
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"30",
"R-HSA-390696",
"R-HSA-418555",
"R-MMU-390696",
"R-MMU-418555",
"R-RNO-390696",
"R-SSC-390696",
"R-SSC-418555"
] | [
"IUPHAR:30",
"REACTOME:R-HSA-390696",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-390696",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-390696",
"REACTOME:R-SSC-390696",
"REACTOME:R-SSC-418555"
] | 8 | [
"7dh5",
"7xjh",
"7xji",
"9ijd",
"9ije"
] | 5 | [
"PUB00066376",
"PUB00066377",
"PUB00066533",
"PUB00066535",
"PUB00066557",
"PUB00066576",
"PUB00066577",
"PUB00066578",
"PUB00066579",
"PUB00066580",
"PUB00066581"
] | [
"18882199",
"2855960",
"11053129",
"15655528",
"12063255",
"8389717",
"7621895",
"16457637",
"15935402",
"9808702",
"2565118"
] | [
"A study of the adrenotropic receptors.",
"Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.",
"G(i)-dependent localization of beta(2)-adrenergic receptor signaling to L-type Ca(2+) channels.",
"The selectivity of beta-adrenoceptor antagonists at the human beta1, b... | [
1948,
1988,
2000,
2005,
2002,
1993,
1995,
2006,
2005,
1998,
1989
] | 11 | [
"IPR002233"
] | [] | 1 | 0 | 1 | [
"Amniota",
"Streptomyces citrinus"
] | [
256,
1
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
3,
3
] | 3 | true | Family | Beta 3 adrenoceptor | Beta 3 adrenoceptor | ADRB3_rcpt | 3 |
IPR000682 | 682 | Protein-L-isoaspartate(D-aspartate) O-methyltransferase | PCMT | Family | 36,233 | false | false | Protein-L-isoaspartate(D-aspartate) O-methyltransferase ( ) (PCMT) [ ] (which is also known as L-isoaspartyl protein carboxyl methyltransferase) is an enzyme that catalyses the transfer of a methyl group from S-adenosylmethionine to the free carboxyl groups of D-aspartyl or L-isoaspartyl residues in a variety of peptid... | [
"GO:0004719",
"GO:0036211"
] | [
"protein-L-isoaspartate (D-aspartate) O-methyltransferase activity",
"protein modification process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PROSITE",
"PANTHER",
"NCBIFAM"
] | [
"MF_00090",
"PS01279",
"PTHR11579",
"TIGR00080"
] | [
"PIMT",
"PCMT",
"",
"pimt"
] | [
11071,
16415,
35865,
17681
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.77",
"PDOC00985",
"R-CEL-5676934",
"R-DDI-5676934",
"R-DME-5676934",
"R-DRE-5676934",
"R-HSA-5676934",
"R-MMU-5676934",
"R-RNO-5676934",
"R-SPO-5676934",
"R-SSC-5676934"
] | [
"EC:2.1.1.77",
"PROSITEDOC:PDOC00985",
"REACTOME:R-CEL-5676934",
"REACTOME:R-DDI-5676934",
"REACTOME:R-DME-5676934",
"REACTOME:R-DRE-5676934",
"REACTOME:R-HSA-5676934",
"REACTOME:R-MMU-5676934",
"REACTOME:R-RNO-5676934",
"REACTOME:R-SPO-5676934",
"REACTOME:R-SSC-5676934"
] | 11 | [
"1dl5",
"1i1n",
"1jg1",
"1jg2",
"1jg3",
"1jg4",
"1kr5",
"1r18",
"1vbf",
"2pbf",
"2yxe",
"3lbf",
"4l7v",
"4o29",
"8qby",
"9oma",
"9omf"
] | 17 | [
"PUB00000999"
] | [
"9253175"
] | [
"Molecular phylogenetics of a protein repair methyltransferase."
] | [
1997
] | 1 | [] | [
"IPR026448",
"IPR027573"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1052,
24952,
9695,
5,
529
] | 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",... | [
23,
4,
16,
3,
1,
23,
19,
1,
8,
13,
1,
10
] | 12 | true | Family | Protein-L-isoaspartate(D-aspartate) O-methyltransferase | Protein-L-isoaspartate(D-aspartate) O-methyltransferase | PCMT | 7 |
IPR000683 | 683 | Gfo/Idh/MocA-like oxidoreductase, N-terminal | Gfo/Idh/MocA-like_OxRdtase_N | Domain | 209,981 | false | false | This entry represents the N-terminal domain of a group of enzymes that utilise NADP or NAD, known as the GFO/IDH/MOCA family (GFO: glucose--fructose oxidoreductase, IDH: inositol 2-dehydrogenase and MOCA which catalyses a dehydrogenase reaction involved in rhizopine catabolism) in UniProtKB/Swiss-Prot, which includes e... | [
"GO:0000166"
] | [
"nucleotide binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01408"
] | [
"GFO_IDH_MocA"
] | [
209981
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1271",
"GenProp1286",
"GenProp1468",
"GenProp1534",
"GenProp1591",
"R-HSA-189483",
"R-HSA-9013406",
"R-HSA-9707564",
"R-MMU-189483",
"R-MMU-9013406",
"R-MMU-9707564",
"R-RNO-189483",
"R-RNO-9707564",
"R-XTR-9013406"
] | [
"GP:GenProp1271",
"GP:GenProp1286",
"GP:GenProp1468",
"GP:GenProp1534",
"GP:GenProp1591",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-9013406",
"REACTOME:R-HSA-9707564",
"REACTOME:R-MMU-189483",
"REACTOME:R-MMU-9013406",
"REACTOME:R-MMU-9707564",
"REACTOME:R-RNO-189483",
"REACTOME:R-RNO-9707564... | 14 | [
"1evj",
"1gcu",
"1h6a",
"1h6b",
"1h6c",
"1h6d",
"1lc0",
"1lc3",
"1ofg",
"1ryd",
"1rye",
"1tlt",
"1xea",
"1ydw",
"1zh8",
"2glx",
"2h63",
"2ho5",
"2ixa",
"2ixb",
"2nvw",
"2o48",
"2o4u",
"2p2s",
"2poq",
"2q4e",
"3bio",
"3bts",
"3btu",
"3btv",
"3c1a",
"3cea"... | 167 | [
"PUB00094646"
] | [
"26749496"
] | [
"Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3914,
172958,
29687,
16,
3406
] | 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... | [
24,
9,
8,
6,
10,
11,
6,
11,
8,
2,
5,
29
] | 12 | true | Domain | Gfo/Idh/MocA-like oxidoreductase, N-terminal | Gfo/Idh/MocA-like oxidoreductase, N-terminal | Gfo/Idh/MocA-like_OxRdtase_N | 7 |
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