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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR002016 | 2,016 | Haem peroxidase | Haem_peroxidase | Domain | 81,794 | false | false | null | [
"GO:0004601",
"GO:0020037",
"GO:0006979"
] | [
"peroxidase activity",
"heme binding",
"response to oxidative stress"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00141",
"PR00458",
"PS50873"
] | [
"peroxidase",
"PEROXIDASE",
"PEROXIDASE_4"
] | [
80059,
73729,
79471
] | 3 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME"
] | [
"1.11.1",
"1.11.1.21",
"PWY-5506",
"PDOC00394",
"R-HSA-1222387"
] | [
"EC:1.11.1",
"EC:1.11.1.21",
"METACYC:PWY-5506",
"PROSITEDOC:PDOC00394",
"REACTOME:R-HSA-1222387"
] | 5 | [
"1a2f",
"1a2g",
"1aa4",
"1ac4",
"1ac8",
"1aeb",
"1aed",
"1aee",
"1aef",
"1aeg",
"1aeh",
"1aej",
"1aek",
"1aem",
"1aen",
"1aeo",
"1aeq",
"1aes",
"1aet",
"1aeu",
"1aev",
"1apx",
"1arp",
"1aru",
"1arv",
"1arw",
"1arx",
"1ary",
"1atj",
"1b80",
"1b82",
"1b85"... | 505 | [
"PUB00000617",
"PUB00001259",
"PUB00001743",
"PUB00005246"
] | [
"1954228",
"8062820",
"8167033",
"7922023"
] | [
"Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily.",
"Peroxidasin: a novel enzyme-matrix protein of Drosophila development.",
"Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium.",
"Structural variation in heme enzymes: a com... | [
1991,
1994,
1994,
1994
] | 4 | [] | [
"IPR033905"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mouse coronavirus",
"unclassified sequences"
] | [
437,
14652,
66479,
1,
225
] | 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)",
"Zea mays"
] | [
360,
1,
4,
528,
1,
624
] | 6 | true | Domain | Haem peroxidase | Haem peroxidase | Haem_peroxidase | 5 |
IPR002017 | 2,017 | Spectrin repeat | Spectrin_repeat | Repeat | 59,555 | false | false | Spectrin repeats are found in several proteins involved in cytoskeletal structure and in proteins with a more regulatory role mostly in animals [ , ]. This entry includes spectrin alpha and beta subunits, alpha-actinin and dystrophin [ , , ]. | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00435"
] | [
"Spectrin"
] | [
59555
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-114608",
"R-BTA-390522",
"R-BTA-438066",
"R-BTA-446388",
"R-BTA-5673001",
"R-BTA-9013405",
"R-BTA-9013418",
"R-BTA-9035034",
"R-CEL-375165",
"R-CEL-5673001",
"R-CEL-6807878",
"R-CEL-9913351",
"R-DDI-114608",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9013418",
"R-DDI-9013420",
... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-390522",
"REACTOME:R-BTA-438066",
"REACTOME:R-BTA-446388",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-9013405",
"REACTOME:R-BTA-9013418",
"REACTOME:R-BTA-9035034",
"REACTOME:R-CEL-375165",
"REACTOME:R-CEL-5673001",
"REACTOME:R-CEL-6807878",
"REACTOME:R-C... | 162 | [
"1aj3",
"1cun",
"1g8x",
"1hci",
"1owa",
"1quu",
"1s35",
"1sjj",
"1u4q",
"1u5p",
"1wlx",
"2iak",
"2spc",
"3edu",
"3edv",
"3f31",
"3f57",
"3fb2",
"3kbt",
"3kbu",
"3lbx",
"3pdy",
"3pe0",
"3uul",
"3uum",
"3uun",
"4d1e",
"4pd3",
"5i4e",
"5j4o",
"5jlh",
"5m6s"... | 42 | [
"PUB00005178",
"PUB00029619",
"PUB00030394",
"PUB00030886",
"PUB00099886"
] | [
"8266097",
"12672815",
"10481917",
"15062087",
"11911890"
] | [
"Crystal structure of the repetitive segments of spectrin.",
"Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.",
"Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments.",
"Structural insights into the stability and flexibility of unusual ... | [
1993,
2003,
1999,
2004,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
2,
59551,
2
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
327,
74,
229,
158,
170
] | 6 | true | Repeat | Spectrin repeat | Spectrin repeat | Spectrin_repeat | 7 |
IPR002018 | 2,018 | Carboxylesterase, type B | CarbesteraseB | Domain | 106,559 | false | false | Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters ( ). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00135"
] | [
"COesterase"
] | [
106559
] | 1 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.1",
"GenProp1703",
"PDOC00112",
"R-BTA-422085",
"R-BTA-9749641",
"R-CEL-112311",
"R-CEL-1483191",
"R-CEL-192456",
"R-CEL-2022377",
"R-CEL-211945",
"R-CEL-5578768",
"R-CEL-6794361",
"R-CEL-9749641",
"R-DDI-112311",
"R-DDI-1483191",
"R-DDI-2022377",
"R-DDI-211945",
"R-DDI-557876... | [
"EC:3.1.1",
"GP:GenProp1703",
"PROSITEDOC:PDOC00112",
"REACTOME:R-BTA-422085",
"REACTOME:R-BTA-9749641",
"REACTOME:R-CEL-112311",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-192456",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CEL-211945",
"REACTOME:R-CEL-5578768",
"REACTOME:R-CEL-6794361",
"REACTOM... | 51 | [
"1acj",
"1acl",
"1akn",
"1amn",
"1aql",
"1ax9",
"1b41",
"1c2b",
"1c2o",
"1c7i",
"1c7j",
"1cfj",
"1cle",
"1crl",
"1dx6",
"1e3q",
"1e66",
"1ea5",
"1eea",
"1eve",
"1f6w",
"1f8u",
"1fss",
"1gpk",
"1gpn",
"1gqr",
"1gqs",
"1gz7",
"1h22",
"1h23",
"1hbj",
"1j06"... | 547 | [
"PUB00003630",
"PUB00004750",
"PUB00005009"
] | [
"3163407",
"1862088",
"8453375"
] | [
"On the origins of esterases.",
"Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.",
"Relationship between sequence conservation and three-dimensional structure in a large family of esterases, ... | [
1988,
1991,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"Viruses",
"unclassified sequences"
] | [
18558,
87666,
11,
34,
290
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
57,
76,
113,
100,
75,
9,
104,
1,
4
] | 9 | true | Domain | Carboxylesterase, type B | Carboxylesterase, type B | CarbesteraseB | 7 |
IPR002019 | 2,019 | Urease, beta subunit-like | Urease_beta-like | Family | 14,170 | false | false | Urease is a nickel-dependent metalloenzyme that catalyses the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of th... | [
"GO:0043419",
"GO:0035550"
] | [
"urea catabolic process",
"urease complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"NCBIFAM",
"CDD"
] | [
"MF_01954",
"PF00699",
"TIGR00192",
"cd00407"
] | [
"Urease_beta",
"Urease_beta",
"urease_beta",
"Urease_beta"
] | [
10559,
14168,
13279,
13673
] | 4 | [
"EC",
"GP",
"METACYC"
] | [
"3.5.1.5",
"GenProp0051",
"PWY-5704"
] | [
"EC:3.5.1.5",
"GP:GenProp0051",
"METACYC:PWY-5704"
] | 3 | [
"1a5k",
"1a5l",
"1a5m",
"1a5n",
"1a5o",
"1e9y",
"1e9z",
"1ef2",
"1ejr",
"1ejs",
"1ejt",
"1eju",
"1ejv",
"1ejw",
"1ejx",
"1fwa",
"1fwb",
"1fwc",
"1fwd",
"1fwe",
"1fwf",
"1fwg",
"1fwh",
"1fwi",
"1fwj",
"1ie7",
"1kra",
"1krb",
"1krc",
"1s3t",
"1ubp",
"2kau"... | 84 | [
"PUB00010725",
"PUB00018934",
"PUB00018936",
"PUB00079461",
"PUB00079462"
] | [
"7565414",
"10865198",
"11373617",
"11996109",
"16173497"
] | [
"Molecular biology of microbial ureases.",
"Bacterial ureases in infectious diseases.",
"Supramolecular assembly and acid resistance of Helicobacter pylori urease.",
"Plant ureases: roles and regulation.",
"Staying alive overdosed: how does Helicobacter pylori control urease activity?"
] | [
1995,
2000,
2001,
2000,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
188,
11188,
2684,
110
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
1,
1,
12
] | 5 | true | Family | Urease, beta subunit-like | Urease, beta subunit-like | Urease_beta-like | 3 |
IPR002020 | 2,020 | Citrate synthase | Citrate_synthase | Family | 65,615 | false | false | Citrate synthase is a member of a small family of enzymes that can directly form a carbon-carbon bond without the presence of metal ion cofactors. It catalyses the first reaction in the Krebs' cycle, namely the conversion of oxaloacetate and acetyl-coenzyme A into citrate and coenzyme A. This reaction is important for ... | [
"GO:0046912"
] | [
"acyltransferase activity, acyl groups converted into alkyl on transfer"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER",
"PANTHER"
] | [
"PF00285",
"PR00143",
"PTHR11739",
"PTHR23118"
] | [
"Citrate_synt",
"CITRTSNTHASE",
"",
""
] | [
64641,
53411,
33943,
6548
] | 4 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"2.3.3",
"2.3.3.16",
"GenProp1265",
"GenProp1267",
"GenProp1687",
"GenProp1693",
"GenProp1710",
"PDOC00422",
"R-BTA-6798695",
"R-BTA-71403",
"R-BTA-75105",
"R-BTA-9837999",
"R-BTA-9854311",
"R-CEL-6798695",
"R-CEL-71403",
"R-CEL-75105",
"R-CEL-9837999",
"R-DDI-6798695",
"R-DDI-71... | [
"EC:2.3.3",
"EC:2.3.3.16",
"GP:GenProp1265",
"GP:GenProp1267",
"GP:GenProp1687",
"GP:GenProp1693",
"GP:GenProp1710",
"PROSITEDOC:PDOC00422",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71403",
"REACTOME:R-BTA-75105",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9854311",
"REACTOME:R-CEL-6798695... | 52 | [
"1a59",
"1aj8",
"1al6",
"1amz",
"1csc",
"1csh",
"1csi",
"1csr",
"1css",
"1cts",
"1iom",
"1ixe",
"1nxe",
"1nxg",
"1o7x",
"1owb",
"1owc",
"1vgm",
"1vgp",
"2c6x",
"2csc",
"2cts",
"2h12",
"2ibp",
"2ifc",
"2p2w",
"2r26",
"2r9e",
"3csc",
"3enj",
"3hwk",
"3msu"... | 152 | [
"PUB00013490",
"PUB00042604",
"PUB00042605",
"PUB00042606",
"PUB00042607",
"PUB00090961",
"PUB00094532",
"PUB00094533"
] | [
"9579066",
"15147839",
"17087502",
"16952946",
"16007201",
"28956599",
"17973657",
"29420286"
] | [
"Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships.",
"Investigating the accessibility of the closed domain conformation of citrate synthase using essential dynamics sampling.",
"Structure of a NADH-insensitive hexameric citrate synthase that resists acid inact... | [
1998,
2004,
2006,
2006,
2005,
2017,
2008,
2018
] | 8 | [] | [
"IPR010109",
"IPR014608",
"IPR024176"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
870,
47886,
16018,
5,
836
] | 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",... | [
30,
24,
14,
9,
2,
25,
11,
3,
17,
17,
3,
2,
51
] | 13 | true | Family | Citrate synthase | Citrate synthase | Citrate_synthase | 9 |
IPR002021 | 2,021 | Paramyxovirus nucleocapsid protein | Paramyx_ncap | Family | 3,532 | false | false | The nucleocapsid protein is referred to as NP. NP is is the major structural component of the nucleocapsid. The protein is approx. 58kDa. 2600 NP molecules go to tightly encapsidate the viral RNA. NP interacts with several other viral encoded proteins, all of which are involved in controlling replication: NP-NP, NP-P, ... | [
"GO:0005198",
"GO:0019013"
] | [
"structural molecule activity",
"viral nucleocapsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00973"
] | [
"Paramyxo_ncap"
] | [
3532
] | 1 | [] | [] | [] | 0 | [
"4co6",
"4uft",
"4xjn",
"5e4v",
"5wkn",
"6h5q",
"6h5s",
"6jc3",
"6m7d",
"7ev8",
"7ewq",
"7exa",
"7nt5",
"7nt6",
"7oi3",
"7ozr",
"8c4h",
"8cbw"
] | 18 | [
"PUB00000174",
"PUB00003503",
"PUB00005616"
] | [
"9125045",
"8396656",
"8806522"
] | [
"Protein interaction domains of the measles virus nucleocapsid protein (NP).",
"The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly.",
"The Sendai virus V protein interacts with the NP protein to regulate viral genome RNA replication."
] | [
1997,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Bifidobacterium breve",
"Eupercaria",
"Mononegavirales"
] | [
1,
3,
3528
] | 3 | [] | [] | 0 | true | Family | Paramyxovirus nucleocapsid protein | Paramyxovirus nucleocapsid protein | Paramyx_ncap | 9 |
IPR002022 | 2,022 | Pectate lyase | Pec_lyase | Domain | 25,365 | false | false | Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. Pectate lyase is responsible for the eliminative cleavage of pectate, yielding oligosaccharides with 4-deoxy-alpha-D-mann-4-enuronosyl groups at their non-reducing ends. The protein is maximally expressed late in pollen development.... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00544",
"SM00656"
] | [
"Pectate_lyase_4",
"Amb_all"
] | [
24496,
24781
] | 2 | [
"EC",
"EC"
] | [
"4.2.2",
"4.2.2.2"
] | [
"EC:4.2.2",
"EC:4.2.2.2"
] | 2 | [
"1air",
"1bn8",
"1idj",
"1idk",
"1jrg",
"1jta",
"1o88",
"1o8d",
"1o8e",
"1o8f",
"1o8g",
"1o8h",
"1o8i",
"1o8j",
"1o8k",
"1o8l",
"1o8m",
"1ooc",
"1pcl",
"1pe9",
"1plu",
"1pxz",
"1qcx",
"1vbl",
"2bsp",
"2ewe",
"2nzm",
"2o04",
"2o0v",
"2o0w",
"2o17",
"2o1d"... | 47 | [
"PUB00004536",
"PUB00005163",
"PUB00007170",
"PUB00085875"
] | [
"1983191",
"8502994",
"11926834",
"25978036"
] | [
"Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia.",
"New domain motif: the structure of pectate lyase C, a secreted plant virulence factor.",
"Folding kinetics of the protein pectate lyase C reveal fast-forming in... | [
1990,
1993,
2002,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
7,
7488,
17813,
4,
53
] | 5 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
119,
1,
33,
59
] | 4 | true | Domain | Pectate lyase | Pectate lyase | Pec_lyase | 3 |
IPR002023 | 2,023 | NADH-quinone oxidoreductase subunit E-like | NuoE-like | Family | 24,760 | false | false | Respiratory-chain NADH dehydrogenase ( ) [ ] (also known as complex I or NADH-ubiquinone oxidoreductase) is an oligomeric enzymatic complex located in the inner mitochondrial membrane which also seems to exist in the chloroplast and in cyanobacteria (as a NADH-plastoquinone oxidoreductase). Among the 25 to 30 polypepti... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PROSITE",
"NCBIFAM"
] | [
"PIRSF000216",
"PS01099",
"TIGR01958"
] | [
"NADH_DH_24kDa",
"COMPLEX1_24K",
"nuoE_fam"
] | [
19894,
16102,
16537
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1.-",
"GenProp0135",
"GenProp1198",
"GenProp1230",
"GenProp1254",
"GenProp1341",
"GenProp1537",
"GenProp1583",
"GenProp1608",
"GenProp1637",
"GenProp1751",
"PDOC00843",
"R-BTA-611105",
"R-BTA-6799198",
"R-DDI-6799198",
"R-HSA-611105",
"R-HSA-6799198",
"R-MMU-611105",
"R-MMU-... | [
"EC:7.1.1.-",
"GP:GenProp0135",
"GP:GenProp1198",
"GP:GenProp1230",
"GP:GenProp1254",
"GP:GenProp1341",
"GP:GenProp1537",
"GP:GenProp1583",
"GP:GenProp1608",
"GP:GenProp1637",
"GP:GenProp1751",
"PROSITEDOC:PDOC00843",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-DDI-679... | 21 | [
"2fug",
"2ybb",
"3i9v",
"3iam",
"3ias",
"3m9s",
"4hea",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6hl2",
"6hl3",
"6hl4",
"6hla",
"6hli",
"6hlj",
"6hlm",
"6i0d",
"6i1p",
"6q8o",
"6q8w"... | 373 | [
"PUB00000637",
"PUB00001392",
"PUB00003309"
] | [
"1445936",
"2029890",
"7690854"
] | [
"Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins.",
"The respiratory-chain NADH dehydrogenase (complex I) of mitochondria.",
"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes ... | [
1992,
1991,
1993
] | 3 | [
"IPR028431"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
82,
19453,
4625,
600
] | 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",... | [
4,
1,
1,
3,
1,
6,
1,
1,
3,
4,
1,
5
] | 12 | true | Family | NADH-quinone oxidoreductase subunit E-like | NADH-quinone oxidoreductase subunit E-like | NuoE-like | 4 |
IPR002024 | 2,024 | Bacterioferritin | Bacterioferritin | Family | 13,822 | false | false | Bacterioferritin (BFR; also known as cytochrome b1 or cytochrome b557) [ , ] of Escherichia coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter [ , ]. X-ray crystallographic studie... | [
"GO:0008199",
"GO:0006826",
"GO:0006879"
] | [
"ferric iron binding",
"iron ion transport",
"intracellular iron ion homeostasis"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PIRSF",
"PRINTS",
"NCBIFAM",
"CDD"
] | [
"PIRSF002560",
"PR00601",
"TIGR00754",
"cd00907"
] | [
"Bacterioferritin",
"BACFERRITIN",
"bfr",
"Bacterioferritin"
] | [
12779,
13757,
12286,
12530
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"1.16.3.1",
"PDOC00475",
"R-HSA-1222449"
] | [
"EC:1.16.3.1",
"PROSITEDOC:PDOC00475",
"REACTOME:R-HSA-1222449"
] | 3 | [
"1bcf",
"1bfr",
"1jgc",
"1nf4",
"1nf6",
"1nfv",
"1sof",
"2fkz",
"2fl0",
"2htn",
"2vxi",
"2wtl",
"2y3q",
"3bkn",
"3e1j",
"3e1l",
"3e1m",
"3e1n",
"3e1o",
"3e1p",
"3e1q",
"3e2c",
"3fvb",
"3ghq",
"3gvy",
"3is7",
"3is8",
"3ise",
"3isf",
"3qb9",
"3r2h",
"3r2k"... | 107 | [
"PUB00000540",
"PUB00000570",
"PUB00000615",
"PUB00000672",
"PUB00002921",
"PUB00003913",
"PUB00019549"
] | [
"8526846",
"2276500",
"1904771",
"8695634",
"7559480",
"7664064",
"9889981"
] | [
"Identification of the ferroxidase centre of Escherichia coli bacterioferritin.",
"Genetic and structural characterization of the bacterioferritin of Escherichia coli.",
"Physical, chemical and immunological properties of the bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and Azotobacter vineland... | [
1995,
1990,
1991,
1996,
1995,
1994,
1998
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctOAa14",
"unclassified sequences"
] | [
57,
13652,
36,
1,
76
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Bacterioferritin | Bacterioferritin | Bacterioferritin | 3 |
IPR002026 | 2,026 | Urease, gamma/gamma-beta subunit | Urease_gamma/gamma-beta_su | Family | 13,785 | false | false | Urease (urea amidohydrolase, ) is a nickel-dependent metalloenzyme that catalyses the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. T... | [
"GO:0016151",
"GO:0043419"
] | [
"nickel cation binding",
"urea catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"NCBIFAM",
"CDD"
] | [
"PF00547",
"TIGR00193",
"cd00390"
] | [
"Urease_gamma",
"urease_gam",
"Urease_gamma"
] | [
13784,
13004,
13119
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"3.5.1.5",
"GenProp0051",
"PWY-5704"
] | [
"EC:3.5.1.5",
"GP:GenProp0051",
"METACYC:PWY-5704"
] | 3 | [
"1a5k",
"1a5l",
"1a5m",
"1a5n",
"1a5o",
"1e9y",
"1e9z",
"1ef2",
"1ejr",
"1ejs",
"1ejt",
"1eju",
"1ejv",
"1ejw",
"1ejx",
"1fwa",
"1fwb",
"1fwc",
"1fwd",
"1fwe",
"1fwf",
"1fwg",
"1fwh",
"1fwi",
"1fwj",
"1ie7",
"1kra",
"1krb",
"1krc",
"1s3t",
"1ubp",
"2fvh"... | 86 | [
"PUB00004994",
"PUB00005206",
"PUB00010725"
] | [
"9144792",
"7754395",
"7565414"
] | [
"An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.",
"The crystal structure of urease from Klebsiella aerogenes.",
"Molecular biology of microbial ureases."
] | [
1997,
1995,
1995
] | 3 | [] | [
"IPR012010"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
188,
10838,
2653,
106
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
5,
2,
1,
1,
9
] | 5 | true | Family | Urease, gamma/gamma-beta subunit | Urease, gamma/gamma-beta subunit | Urease_gamma/gamma-beta_su | 9 |
IPR002028 | 2,028 | Tryptophan synthase, alpha chain | Trp_synthase_suA | Family | 29,032 | false | false | Tryptophan synthase ( ) catalyses the last step in the biosynthesis of tryptophan [ , ]: L-serine + 1-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H 2 O It has two functional domains, each found in bacteria and plants on a separate subunit. In Escherichia coli, the two subunits, A and ... | [
"GO:0004834",
"GO:0006568"
] | [
"tryptophan synthase activity",
"L-tryptophan metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00131",
"PF00290",
"PTHR43406",
"TIGR00262",
"cd04724"
] | [
"Trp_synth_alpha",
"Trp_syntA",
"",
"trpA",
"Tryptophan_synthase_alpha"
] | [
27364,
29023,
26856,
28242,
28318
] | 5 | [
"EC",
"GP",
"GP",
"PROSITEDOC"
] | [
"4.2.1.20",
"GenProp0037",
"GenProp1450",
"PDOC00151"
] | [
"EC:4.2.1.20",
"GP:GenProp0037",
"GP:GenProp1450",
"PROSITEDOC:PDOC00151"
] | 4 | [
"1a50",
"1a5a",
"1a5b",
"1a5s",
"1beu",
"1bks",
"1c29",
"1c8v",
"1c9d",
"1cw2",
"1cx9",
"1fuy",
"1geq",
"1k3u",
"1k7e",
"1k7f",
"1k7x",
"1k8x",
"1k8y",
"1k8z",
"1kfb",
"1kfc",
"1kfe",
"1kfj",
"1kfk",
"1qop",
"1qoq",
"1rd5",
"1tjp",
"1tjr",
"1ttp",
"1ttq"... | 176 | [
"PUB00000116",
"PUB00000769",
"PUB00004683",
"PUB00014824"
] | [
"2679363",
"1366510",
"2734310",
"2521855"
] | [
"Evolution of a biosynthetic pathway: the tryptophan paradigm.",
"The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.",
"A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana.",
"Nucleotide sequence of the N... | [
1989,
1990,
1989,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
793,
23622,
4002,
615
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
8,
1,
1,
13,
1,
1,
49
] | 7 | true | Family | Tryptophan synthase, alpha chain | Tryptophan synthase, alpha chain | Trp_synthase_suA | 4 |
IPR002031 | 2,031 | Peptidase A22A, presenilin 1 | Pept_A22A_PS1 | Family | 744 | false | false | This group of aspartic peptidases belong to MEROPS peptidase family A22 (presenilin family, clan AD): subfamily A22A, the type example being presenilin 1 from Homo sapiens (Human). Presenilins are polytopic transmembrane (TM) proteins, mutations in which are associated with the occurrence of early-onset familial Alzhei... | [
"GO:0042500",
"GO:0035556",
"GO:0042987",
"GO:0016020"
] | [
"aspartic endopeptidase activity, intramembrane cleaving",
"intracellular signal transduction",
"amyloid precursor protein catabolic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01073"
] | [
"PRESENILIN1"
] | [
744
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.4.23.-",
"GenProp2017",
"R-BTA-1251985",
"R-BTA-193692",
"R-BTA-205043",
"R-BTA-3928665",
"R-BTA-6798695",
"R-BTA-9839383",
"R-GGA-1251985",
"R-GGA-193692",
"R-GGA-205043",
"R-GGA-3928665",
"R-GGA-6798695",
"R-GGA-9013507",
"R-GGA-9017802",
"R-GGA-9839383",
"R-HSA-1251985",
"R-H... | [
"EC:3.4.23.-",
"GP:GenProp2017",
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-193692",
"REACTOME:R-BTA-205043",
"REACTOME:R-BTA-3928665",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9839383",
"REACTOME:R-GGA-1251985",
"REACTOME:R-GGA-193692",
"REACTOME:R-GGA-205043",
"REACTOME:R-GGA-3928665",
"RE... | 46 | [
"5a63",
"5fn2",
"5fn3",
"5fn4",
"5fn5",
"6idf",
"6iyc",
"6lqg",
"6lr4",
"7c9i",
"7d8x",
"7y5t",
"8im7",
"8k8e",
"8kco",
"8kcp",
"8kcs",
"8kct",
"8kcu",
"8oqy",
"8oqz",
"8x52",
"8x53",
"8x54",
"9k95"
] | 25 | [
"PUB00000974",
"PUB00000975",
"PUB00002010",
"PUB00004220",
"PUB00077847",
"PUB00077848",
"PUB00077849",
"PUB00077850",
"PUB00077851",
"PUB00077852",
"PUB00077853",
"PUB00077854",
"PUB00077855"
] | [
"9791530",
"9791532",
"9521418",
"7566091",
"10864326",
"10801983",
"16046406",
"16135086",
"15734686",
"11851430",
"15173829",
"18239854",
"17082447"
] | [
"Introduction: genetic determinants of mid- and late-life dementias.",
"Monogenic determinants of familial Alzheimer's disease: presenilin-1 mutations.",
"Presenilin mutations in Alzheimer's disease.",
"Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gen... | [
1998,
1998,
1998,
1995,
2000,
2000,
2005,
2005,
2005,
2002,
2004,
2008,
2006
] | 13 | [
"IPR001108"
] | [] | 1 | 0 | 1 | [
"Sarcopterygii"
] | [
744
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
36,
2,
3
] | 3 | true | Family | Peptidase A22A, presenilin 1 | Peptidase A22A, presenilin 1 | Pept_A22A_PS1 | 3 |
IPR002033 | 2,033 | Sec-independent periplasmic protein translocase TatC | TatC | Family | 26,847 | false | false | Proteins encoded by the mttABC operon (formerly yigTUW), mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine" leader motif. This family contains the E. coli mttB gene (TATC) [ ]. A functi... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00902",
"PF00902",
"PR01840",
"PTHR30371",
"TIGR00945"
] | [
"TatC",
"TatC",
"TATCFAMILY",
"",
"tatC"
] | [
24293,
26805,
24676,
26581,
23794
] | 5 | [
"GP",
"GP",
"PROSITEDOC"
] | [
"GenProp0127",
"GenProp1136",
"PDOC00936"
] | [
"GP:GenProp0127",
"GP:GenProp1136",
"PROSITEDOC:PDOC00936"
] | 3 | [
"4b4a",
"4hts",
"4htt",
"9dzz",
"9e01",
"9e02",
"9e03",
"9e04",
"9e06",
"9e07"
] | 10 | [
"PUB00000960",
"PUB00007662",
"PUB00011123"
] | [
"9546395",
"9649434",
"12163163"
] | [
"A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.",
"Overlapping functions of components of a bacterial Sec-independent protein export pathway.",
"Topology determination and functional analysis of the Escherichia coli TatC protein."
] | [
1998,
1998,
2002
] | 3 | [] | [
"IPR011532"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1105,
22098,
3023,
621
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
1,
3,
11
] | 4 | true | Family | Sec-independent periplasmic protein translocase TatC | Sec-independent periplasmic protein translocase TatC | TatC | 5 |
IPR002034 | 2,034 | Alpha-isopropylmalate/homocitrate synthase, conserved site | AIPM/Hcit_synth_CS | Conserved_site | 46,999 | false | false | A number of enzymes have been shown to be functionally as well as evolutionary related [ ]. The nifV and leuA genes encode homocitrate synthase and alpha-isopropylmalate synthase, respectively The N-terminal parts of NifV and LeuA from bacteria are highly similar to each other [ ]. Homocitrate synthase ( ) (gene nifV) ... | [
"GO:0046912",
"GO:0019752"
] | [
"acyltransferase activity, acyl groups converted into alkyl on transfer",
"carboxylic acid metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS00815",
"PS00816"
] | [
"AIPM_HOMOCIT_SYNTH_1",
"AIPM_HOMOCIT_SYNTH_2"
] | [
44282,
37962
] | 2 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC"
] | [
"2.3.3",
"2.3.3.13",
"PWY-6871",
"PDOC00643"
] | [
"EC:2.3.3",
"EC:2.3.3.13",
"METACYC:PWY-6871",
"PROSITEDOC:PDOC00643"
] | 4 | [
"1sr9",
"2ztj",
"2ztk",
"2zyf",
"3a9i",
"3ble",
"3blf",
"3bli",
"3eeg",
"3ewb",
"3fig",
"3hps",
"3hpx",
"3hpz",
"3hq1",
"3ivs",
"3ivt",
"3ivu",
"3mi3",
"3rmj",
"3u6w",
"4ov4",
"4ov9",
"6e1j",
"6ktq"
] | 25 | [
"PUB00002139",
"PUB00006373"
] | [
"2022611",
"9139910"
] | [
"The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum.",
"Identification and characterization of the nifV-nifZ-nifT gene region from the filamentous cyanobacterium Anabaena sp. strain PCC 7120."
] | [
1991,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2051,
37731,
6153,
1064
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"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)",... | [
24,
16,
1,
3,
5,
4,
2,
29
] | 8 | true | Conserved_site | Alpha-isopropylmalate/homocitrate synthase, conserved site | Alpha-isopropylmalate/homocitrate synthase, conserved site | AIPM/Hcit_synth_CS | 9 |
IPR002036 | 2,036 | Endoribonuclease YbeY | YbeY | Family | 28,446 | false | false | YbeY is a single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. It acts together with the RNase R to eliminate defective 70S ribosomes, but not properly matured 70S ribosomes or individual subunits, by a process mediated... | [
"GO:0004222",
"GO:0006364"
] | [
"metalloendopeptidase activity",
"rRNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00009",
"PF02130",
"PTHR46986",
"TIGR00043"
] | [
"Endoribonucl_YbeY",
"YbeY",
"",
""
] | [
27152,
28240,
27363,
27902
] | 4 | [
"PROSITEDOC"
] | [
"PDOC01010"
] | [
"PROSITEDOC:PDOC01010"
] | 1 | [
"1oz9",
"1tvi",
"1xax",
"1xm5",
"7y7o"
] | 5 | [
"PUB00027806",
"PUB00038326",
"PUB00064741",
"PUB00064742",
"PUB00064743",
"PUB00096939"
] | [
"12832766",
"16511207",
"20639334",
"20807199",
"23273979",
"32605982"
] | [
"Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus.",
"The ybeY protein from Escherichia coli is a metalloprotein.",
"The heat shock protein YbeY is required for optimal activity of the 30S ribosomal subunit.",
"Role of Escherichia coli YbeY, a highly conserved protein, in rRNA processing.",... | [
2003,
2005,
2010,
2010,
2013,
2020
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
25315,
2513,
4,
614
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
3,
1,
2,
1,
14,
2,
19
] | 8 | true | Family | Endoribonuclease YbeY | Endoribonuclease YbeY | YbeY | 2 |
IPR002037 | 2,037 | Glycoside hydrolase, family 8 | Glyco_hydro_8 | Family | 7,087 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF01270",
"PR00735"
] | [
"Glyco_hydro_8",
"GLHYDRLASE8"
] | [
7077,
6534
] | 2 | [
"CAZY",
"EC",
"GP",
"METACYC",
"PROSITEDOC"
] | [
"GH8",
"3.2.1.4",
"GenProp0658",
"PWY-6788",
"PDOC00640"
] | [
"CAZY:GH8",
"EC:3.2.1.4",
"GP:GenProp0658",
"METACYC:PWY-6788",
"PROSITEDOC:PDOC00640"
] | 5 | [
"1cem",
"1h12",
"1h13",
"1h14",
"1is9",
"1kwf",
"1v5c",
"1v5d",
"1wu4",
"1wu5",
"1wu6",
"1wzz",
"1xw2",
"1xwq",
"1xwt",
"2a8z",
"2b4f",
"2dro",
"2drq",
"2drr",
"2drs",
"3a3v",
"3qxf",
"3qxq",
"3ren",
"4q2b",
"5cd2",
"5czl",
"5gy3",
"5xd0",
"5yxt",
"6g00"... | 48 | [
"PUB00001778",
"PUB00004870",
"PUB00005266"
] | [
"2806912",
"7624375",
"8535779"
] | [
"Cellulase families revealed by hydrophobic cluster analysis.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases."
] | [
1989,
1995,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Lokiarchaeum ossiferum",
"Eukaryota",
"unclassified sequences"
] | [
6868,
1,
181,
37
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glycoside hydrolase, family 8 | Glycoside hydrolase, family 8 | Glyco_hydro_8 | 4 |
IPR002038 | 2,038 | Osteopontin | Osteopontin | Family | 1,211 | false | false | The major event of endochondrial ossification is the proteolytic degradation of calcified cartilage and the extracellular matrix, and their substitution with bone-specific extracellular matrix produced and organised by osteoblasts [ ]. One of the most abundant products of osteoblasts is osteopontin, a glycosylated phos... | [
"GO:0001503",
"GO:0007155"
] | [
"ossification",
"cell adhesion"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER",
"SMART"
] | [
"PF00865",
"PR00216",
"PTHR10607",
"SM00017"
] | [
"Osteopontin",
"OSTEOPONTIN",
"",
"OSTEO"
] | [
803,
880,
1057,
648
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00689",
"R-HSA-1474228",
"R-HSA-186797",
"R-HSA-216083",
"R-HSA-381426",
"R-HSA-8949275",
"R-HSA-8957275",
"R-HSA-9856532",
"R-MMU-1474228",
"R-MMU-186797",
"R-MMU-216083",
"R-MMU-381426",
"R-MMU-8957275",
"R-RNO-1474228",
"R-RNO-186797",
"R-RNO-216083",
"R-RNO-381426",
"R-RNO... | [
"PROSITEDOC:PDOC00689",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-186797",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8949275",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-9856532",
"REACTOME:R-MMU-1474228",
"REACTOME:R-MMU-186797",
"REACTOME:R-MMU-216083",
"REACTOME:R-MMU... | 23 | [] | 0 | [
"PUB00002704",
"PUB00003048"
] | [
"2033080",
"1414488"
] | [
"cDNA cloning and gene expression of chicken osteopontin. Expression of osteopontin mRNA in chondrocytes is enhanced by trypsin treatment of cells.",
"Isolation and characterization of a cDNA for osteopontin-k: a kidney cell adhesion molecule with high homology to osteopontins."
] | [
1991,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales"
] | [
3,
1204,
4
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
10,
11,
4
] | 4 | true | Family | Osteopontin | Osteopontin | Osteopontin | 8 |
IPR002041 | 2,041 | Ran GTPase | Ran_GTPase | Family | 8,557 | false | false | Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [ , ]. Sequence comparisons of small G proteins from various species ha... | [
"GO:0003924",
"GO:0005525",
"GO:0006913"
] | [
"GTPase activity",
"GTP binding",
"nucleocytoplasmic transport"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"PROFILE",
"PANTHER",
"CDD"
] | [
"PR00627",
"PS51418",
"PTHR24071",
"cd00877"
] | [
"GTPRANTC4",
"RAN",
"",
"Ran"
] | [
7070,
7242,
8380,
6632
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00859",
"R-BTA-1655829",
"R-BTA-5578749",
"R-BTA-9615933",
"R-CEL-1655829",
"R-CEL-9615933",
"R-DDI-9615933",
"R-DME-1655829",
"R-DME-5578749",
"R-DME-9615933",
"R-DRE-9615933",
"R-GGA-1655829",
"R-GGA-5578749",
"R-GGA-9615933",
"R-HSA-165054",
"R-HSA-1655829",
"R-HSA-168333",
... | [
"PROSITEDOC:PDOC00859",
"REACTOME:R-BTA-1655829",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-9615933",
"REACTOME:R-CEL-1655829",
"REACTOME:R-CEL-9615933",
"REACTOME:R-DDI-9615933",
"REACTOME:R-DME-1655829",
"REACTOME:R-DME-5578749",
"REACTOME:R-DME-9615933",
"REACTOME:R-DRE-9615933",
"REACTOME:... | 31 | [
"1byu",
"1i2m",
"1ibr",
"1k5d",
"1k5g",
"1qbk",
"1qg2",
"1qg4",
"1rrp",
"1wa5",
"2bku",
"2mmc",
"2mmg",
"2n1b",
"2x19",
"3a6p",
"3ch5",
"3ea5",
"3gj0",
"3gj3",
"3gj4",
"3gj5",
"3gj6",
"3gj7",
"3gj8",
"3gjx",
"3icq",
"3m1i",
"3nby",
"3nbz",
"3nc0",
"3nc1"... | 158 | [
"PUB00000348",
"PUB00000731",
"PUB00004087",
"PUB00004206",
"PUB00006514",
"PUB00007086",
"PUB00007171",
"PUB00015117",
"PUB00023196",
"PUB00034676",
"PUB00052600"
] | [
"2029511",
"8851043",
"1898771",
"7885480",
"10698256",
"12019565",
"12051861",
"11995995",
"2196171",
"17170104",
"2122258"
] | [
"The ras protein family: evolutionary tree and role of conserved amino acids.",
"The small nuclear GTPase Ran: how much does it run?",
"The GTPase superfamily: conserved structure and molecular mechanism.",
"Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form.",
"Nucleocytoplasmic... | [
1991,
1996,
1991,
1995,
1999,
2002,
2002,
2001,
1990,
2007,
1990
] | 11 | [
"IPR001806"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Odinarchaeota yellowstonii (strain LCB_4)",
"Viruses",
"metagenomes"
] | [
4,
8507,
1,
31,
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... | [
14,
2,
2,
8,
8,
5,
1,
6,
7,
2,
1,
22
] | 12 | true | Family | Ran GTPase | Ran GTPase | Ran_GTPase | 2 |
IPR002042 | 2,042 | Uricase | Uricase | Family | 7,296 | false | false | Uricase ( ) (urate oxidase) [ ] is the peroxisomal enzyme responsible for the degradation of urate into allantoin: Urate + O 2 + H 2 O = 5-hydroxyisourate + H 2 O 2 Some species, like primates and birds, have lost the gene for uricase and are therefore unable to degrade urate [ ]. Uricase is a protein of 300 to 400 ami... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PF01014",
"PIRSF000241",
"PR00093",
"PTHR42874",
"TIGR03383"
] | [
"Uricase",
"Urate_oxidase",
"URICASE",
"",
"urate_oxi"
] | [
7284,
6591,
7066,
7154,
6955
] | 5 | [
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC"
] | [
"1.7.3.3",
"GenProp0688",
"GenProp1652",
"PWY-5691",
"PDOC00315"
] | [
"EC:1.7.3.3",
"GP:GenProp0688",
"GP:GenProp1652",
"METACYC:PWY-5691",
"PROSITEDOC:PDOC00315"
] | 5 | [
"1j2g",
"1r4s",
"1r4u",
"1r51",
"1r56",
"1vax",
"1vay",
"1wrr",
"1ws2",
"1ws3",
"1xt4",
"1xxj",
"1xy3",
"2fub",
"2fxl",
"2iba",
"2ic0",
"2icq",
"2pes",
"2yzb",
"2yzc",
"2yzd",
"2yze",
"2zka",
"2zkb",
"3bjp",
"3bk8",
"3cks",
"3cku",
"3f2m",
"3gko",
"3l8w"... | 121 | [
"PUB00001587",
"PUB00002471",
"PUB00004611",
"PUB00004693"
] | [
"2338140",
"3182808",
"16593585",
"2594778"
] | [
"Organization of rat uricase chromosomal gene differs greatly from that of the corresponding plant gene.",
"Cloning and sequence analysis of cDNA for rat liver uricase.",
"Primary structure of the soybean nodulin-35 gene encoding uricase II localized in the peroxisomes of uninfected cells of nodules.",
"Urate... | [
1990,
1988,
1985,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
3220,
4020,
43,
13
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
5,
1,
2,
6,
1,
4,
9,
1,
8
] | 9 | true | Family | Uricase | Uricase | Uricase | 6 |
IPR002043 | 2,043 | Uracil-DNA glycosylase family 1 | UDG_fam1 | Family | 27,823 | false | false | Uracil-DNA glycosylase (UDG, UNG) [ ] is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. UDGs were classified into 4 families [ , ]. Family 1 enzymes are a... | [
"GO:0004844",
"GO:0006281",
"GO:0006284"
] | [
"uracil DNA N-glycosylase activity",
"DNA repair",
"base-excision repair"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00148",
"PTHR11264",
"TIGR00628",
"cd10027"
] | [
"UDG",
"",
"ung",
"UDG-F1-like"
] | [
25724,
27763,
23581,
26844
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.2.27",
"PDOC00121",
"R-DDI-110329",
"R-DDI-110357",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110357",
"R-HSA-9609690",
"R-HSA-9821002",
"R-MMU-110329",
"R-MMU-110357",
"R-SCE-110329",
"R-SPO-110329"
] | [
"EC:3.2.2.27",
"PROSITEDOC:PDOC00121",
"REACTOME:R-DDI-110329",
"REACTOME:R-DDI-110357",
"REACTOME:R-HSA-110328",
"REACTOME:R-HSA-110329",
"REACTOME:R-HSA-110357",
"REACTOME:R-HSA-9609690",
"REACTOME:R-HSA-9821002",
"REACTOME:R-MMU-110329",
"REACTOME:R-MMU-110357",
"REACTOME:R-SCE-110329",
"... | 13 | [
"1akz",
"1emh",
"1emj",
"1eug",
"1eui",
"1flz",
"1lau",
"1lqg",
"1lqj",
"1lqm",
"1okb",
"1q3f",
"1ssp",
"1udg",
"1udh",
"1udi",
"1ugh",
"1uug",
"1yuo",
"2boo",
"2c53",
"2c56",
"2eug",
"2hxm",
"2j8x",
"2jhq",
"2oxm",
"2oyt",
"2ssp",
"2uug",
"2zhx",
"3a7n"... | 104 | [
"PUB00000054",
"PUB00001176",
"PUB00004423",
"PUB00004816",
"PUB00080616",
"PUB00080617",
"PUB00080625",
"PUB00095219"
] | [
"3052275",
"2555154",
"8332455",
"8389453",
"11223884",
"10946227",
"19008197",
"29596604"
] | [
"DNA repair enzymes.",
"Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme.",
"Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene.",
"Identification of a poxvirus gene encoding a uracil DNA glycosylase.",
"Recent progress in the ... | [
1988,
1989,
1993,
1993,
2001,
2000,
2009,
2018
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
13,
21838,
5038,
560,
374
] | 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 ... | [
4,
1,
14,
1,
15,
5,
1,
4,
3,
1,
1,
10
] | 12 | true | Family | Uracil-DNA glycosylase family 1 | Uracil-DNA glycosylase family 1 | UDG_fam1 | 3 |
IPR002044 | 2,044 | Carbohydrate binding module family 20 | CBM20 | Domain | 17,813 | false | false | This entry represents , which binds starch. The crystal structure of CBM20 has been solved [ ]. It consists of seven β-strands forming an open-sided distorted β-barrel. Several aromatic residues, especially the well-conserved Trp and Tyr residues, participate in granular starch binding. A carbohydrate-binding module (C... | [
"GO:2001070"
] | [
"starch binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00686",
"PS51166",
"SM01065"
] | [
"CBM_20",
"CBM20",
"CBM_2"
] | [
16104,
16990,
16522
] | 3 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1726",
"PDOC51166",
"R-HSA-1483115",
"R-HSA-1483152",
"R-HSA-3322077",
"R-HSA-3785653",
"R-HSA-6798695",
"R-HSA-8980692",
"R-HSA-9013404",
"R-HSA-9013405",
"R-HSA-9013408",
"R-HSA-9013423",
"R-MMU-6798695",
"R-MMU-8980692",
"R-MMU-9013404",
"R-MMU-9013405",
"R-MMU-9013408",
... | [
"GP:GenProp1726",
"PROSITEDOC:PDOC51166",
"REACTOME:R-HSA-1483115",
"REACTOME:R-HSA-1483152",
"REACTOME:R-HSA-3322077",
"REACTOME:R-HSA-3785653",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-90... | 23 | [
"1a47",
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"1dtu",
"1eo5",
"1eo7",
"1gcy",
"1i75",
"1itc",
"1j0y",
"1j0z"... | 90 | [
"PUB00023948",
"PUB00054922",
"PUB00054923",
"PUB00054924"
] | [
"1826034",
"3338453",
"3134347",
"15214846"
] | [
"Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution.",
"Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis.",
"Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulase... | [
1991,
1988,
1988,
2004
] | 4 | [] | [
"IPR034831",
"IPR034835",
"IPR034836",
"IPR034838",
"IPR034839",
"IPR034840",
"IPR034841",
"IPR034848",
"IPR034849"
] | 0 | 9 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
45,
4563,
13149,
56
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
24,
2,
12,
13,
7,
9,
3,
24,
9,
45
] | 10 | true | Domain | Carbohydrate binding module family 20 | Carbohydrate binding module family 20 | CBM20 | 6 |
IPR002045 | 2,045 | Metallothionein, crustacean | Metalthion_crustacean | Family | 57 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF27650",
"PR00858"
] | [
"Metalthion_crustacean",
"MTCRUSTACEAN"
] | [
55,
54
] | 2 | [] | [] | [] | 0 | [
"1dmc",
"1dmd",
"1dme",
"1dmf",
"1j5l",
"1j5m"
] | 6 | [
"PUB00001490",
"PUB00003570",
"PUB00003571",
"PUB00005944",
"PUB00078698"
] | [
"2959513",
"1779825",
"1779826",
"2959504",
"21633816"
] | [
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein.",
"Definitions and nomenclature of metallothioneins.",
"Nomenclature of metallothionein.",
"Metallothionein protein evolution: a miniassay."
] | [
1987,
1991,
1991,
1987,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
57
] | 1 | [] | [] | 0 | true | Family | Metallothionein, crustacean | Metallothionein, crustacean | Metalthion_crustacean | 7 |
IPR002047 | 2,047 | Adipokinetic hormone, conserved site | Adipokinetic_hormone_CS | Conserved_site | 587 | false | false | Adipokinetic hormones (AKH) [ , ] are small active peptides produced by some insect species. They bring on the release of diglycerides from the fat body and then stimulate the flight muscles to use them as an energy source. There are other types of active peptides structurally related to AKH. These peptides are eight t... | [
"GO:0005179",
"GO:0005576"
] | [
"hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00256"
] | [
"AKH"
] | [
587
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00229"
] | [
"PROSITEDOC:PDOC00229"
] | 1 | [] | 0 | [
"PUB00000487",
"PUB00004502"
] | [
"2117437",
"3226948"
] | [
"The fruitfly Drosophila melanogaster contains a novel charged adipokinetic-hormone-family peptide.",
"Sequence analyses of two neuropeptides of the AKH/RPCH-family from the lubber grasshopper, Romalea microptera."
] | [
1990,
1988
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
34,
552,
1
] | 3 | [
"Drosophila melanogaster"
] | [
2
] | 1 | true | Conserved_site | Adipokinetic hormone, conserved site | Adipokinetic hormone, conserved site | Adipokinetic_hormone_CS | 5 |
IPR002048 | 2,048 | EF-hand domain | EF_hand_dom | Domain | 573,764 | false | false | Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both sides by a twelve residue α-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyra... | [
"GO:0005509"
] | [
"calcium ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00036",
"PF13202",
"PF13405",
"PF13499",
"PF13833",
"PS50222",
"SM00054",
"cd00051"
] | [
"EF-hand_1",
"EF-hand_5",
"EF-hand_6",
"EF-hand_7",
"EF-hand_8",
"EF_HAND_2",
"EFh",
"EFh"
] | [
30688,
68377,
25350,
282821,
44647,
567042,
368362,
257955
] | 8 | [
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1353",
"GenProp1750",
"PDOC00018",
"R-BTA-111447",
"R-BTA-114508",
"R-BTA-114608",
"R-BTA-1474228",
"R-BTA-1483166",
"R-BTA-163560",
"R-BTA-1855204",
"R-BTA-201451",
"R-BTA-2025928",
"R-BTA-2160916",
"R-BTA-2514859",
"R-BTA-2565942",
"R-BTA-2871809",
"R-BTA-3108214",
"R-BTA... | [
"GP:GenProp1353",
"GP:GenProp1750",
"PROSITEDOC:PDOC00018",
"REACTOME:R-BTA-111447",
"REACTOME:R-BTA-114508",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1483166",
"REACTOME:R-BTA-163560",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-2025928",
"RE... | 749 | [
"1a03",
"1a29",
"1a2x",
"1a75",
"1ahr",
"1aj4",
"1aj5",
"1ak8",
"1alv",
"1alw",
"1ap4",
"1aui",
"1avs",
"1b1g",
"1b4c",
"1b7t",
"1b8c",
"1b8l",
"1b8r",
"1b9a",
"1bjf",
"1blq",
"1boc",
"1bod",
"1br1",
"1br4",
"1bu3",
"1c07",
"1c7v",
"1c7w",
"1cb1",
"1cdl"... | 1,709 | [
"PUB00004973",
"PUB00023349",
"PUB00081528",
"PUB00081532",
"PUB00081536"
] | [
"7553064",
"9228939",
"8848832",
"7656053",
"10591109"
] | [
"Calcium-binding proteins 1: EF-hands.",
"EF-hands embrace.",
"Calcium binding and conformational response in EF-hand proteins.",
"Signal transduction versus buffering activity in Ca(2+)-binding proteins.",
"Diversity of conformational states and changes within the EF-hand protein superfamily."
] | [
1995,
1997,
1996,
1994,
1999
] | 5 | [] | [
"IPR029634",
"IPR034325",
"IPR035798",
"IPR035799",
"IPR042736",
"IPR049025"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
420,
24859,
547873,
165,
447
] | 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... | [
716,
166,
998,
314,
892,
668,
23,
418,
950,
16,
20,
1143
] | 12 | true | Domain | EF-hand domain | EF-hand domain | EF_hand_dom | 8 |
IPR002049 | 2,049 | Laminin-type EGF domain | LE_dom | Domain | 73,201 | false | false | This entry represents the laminin-type EGF-like domain (LE) found in Laminin subunit gamma-1 and Netrin-1 from Homo sapiens and Mus musculus. Laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation [ , ]. They are composed of distinct but ... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00053",
"PS01248",
"PS50027",
"SM00180",
"cd00055"
] | [
"EGF_laminin",
"EGF_LAM_1",
"EGF_LAM_2",
"EGF_Lam",
"EGF_Lam"
] | [
54423,
50220,
47687,
58922,
61611
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00961",
"R-BTA-210993",
"R-BTA-5673001",
"R-DDI-114608",
"R-DDI-1474228",
"R-DDI-1566977",
"R-DDI-2129379",
"R-DDI-3000178",
"R-DME-350368",
"R-DME-350376",
"R-DME-350379",
"R-DME-350411",
"R-DME-350480",
"R-DME-373752",
"R-DME-450728",
"R-HSA-1474228",
"R-HSA-163125",
"R-HSA-... | [
"PROSITEDOC:PDOC00961",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-5673001",
"REACTOME:R-DDI-114608",
"REACTOME:R-DDI-1474228",
"REACTOME:R-DDI-1566977",
"REACTOME:R-DDI-2129379",
"REACTOME:R-DDI-3000178",
"REACTOME:R-DME-350368",
"REACTOME:R-DME-350376",
"REACTOME:R-DME-350379",
"REACTOME:R-DME... | 102 | [
"1klo",
"1npe",
"1tle",
"2y38",
"3tbd",
"3zyg",
"3zyi",
"3zyj",
"4aqs",
"4aqt",
"4k0v",
"4ove",
"4plm",
"4pln",
"4plo",
"4urt",
"4wnx",
"4z80",
"4z81",
"5lf2",
"6fkq",
"7ler",
"7lrf",
"7ndg",
"7ne0",
"7ne1",
"8dmk",
"8edk",
"8hn0",
"8hna",
"8s9p",
"8snp"... | 42 | [
"PUB00001500",
"PUB00001576",
"PUB00002795",
"PUB00003361",
"PUB00003362",
"PUB00099094",
"PUB00099095",
"PUB00099096",
"PUB00099097",
"PUB00099098",
"PUB00099099",
"PUB00099100",
"PUB00099101"
] | [
"2404817",
"2666164",
"8349613",
"8648630",
"8648631",
"28483977",
"15343335",
"30923634",
"23263632",
"17174565",
"23263635",
"30108487",
"30224412"
] | [
"Structure and function of laminin: anatomy of a multidomain glycoprotein.",
"EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?",
"Self-assembly and calcium-binding sites in laminin. A three-arm interaction model.",
"Crystal structure of three consecutive lam... | [
1990,
1989,
1993,
1996,
1996,
2017,
2004,
2019,
2013,
2007,
2013,
2018,
2018
] | 13 | [] | [
"IPR056863"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"bird metagenome"
] | [
18,
73150,
32,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
37,
271,
70,
155,
115,
2,
189,
1
] | 8 | true | Domain | Laminin-type EGF domain | Laminin-type EGF domain | LE_dom | 9 |
IPR002051 | 2,051 | Haem oxygenase | Haem_Oase | Family | 9,982 | false | false | Haem oxygenase ( ) (HO) [ ] is the microsomal enzyme that, in animals, carries out the oxidation of haem, it cleaves the haem ring at the alpha-methene bridge to form biliverdin and carbon monoxide [ ]. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. In mammals there are three isozymes of hae... | [
"GO:0004392",
"GO:0006788"
] | [
"heme oxygenase (decyclizing) activity",
"heme oxidation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PRINTS",
"PANTHER",
"CDD"
] | [
"PIRSF000343",
"PR00088",
"PTHR10720",
"cd19165"
] | [
"Haem_Oase",
"HAEMOXYGNASE",
"",
"HemeO"
] | [
4817,
6749,
8202,
9670
] | 4 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.14.14.18",
"PWY-5874",
"PDOC00512",
"R-BTA-189483",
"R-BTA-917937",
"R-BTA-9609523",
"R-BTA-9707564",
"R-BTA-9707587",
"R-HSA-189483",
"R-HSA-6785807",
"R-HSA-6798695",
"R-HSA-844456",
"R-HSA-8980692",
"R-HSA-917937",
"R-HSA-9609523",
"R-HSA-9660826",
"R-HSA-9707564",
"R-HSA-970... | [
"EC:1.14.14.18",
"METACYC:PWY-5874",
"PROSITEDOC:PDOC00512",
"REACTOME:R-BTA-189483",
"REACTOME:R-BTA-917937",
"REACTOME:R-BTA-9609523",
"REACTOME:R-BTA-9707564",
"REACTOME:R-BTA-9707587",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-844456",
"... | 39 | [
"1dve",
"1dvg",
"1irm",
"1ivj",
"1iw0",
"1iw1",
"1ix3",
"1ix4",
"1j02",
"1j2c",
"1n3u",
"1n45",
"1ni6",
"1oyk",
"1oyl",
"1oze",
"1ozl",
"1ozr",
"1ozw",
"1s13",
"1s8c",
"1t5p",
"1twn",
"1twr",
"1ubb",
"1ulx",
"1v8x",
"1vgi",
"1we1",
"1wnv",
"1wnw",
"1wnx"... | 92 | [
"PUB00001493",
"PUB00002314",
"PUB00002451",
"PUB00004905",
"PUB00005160"
] | [
"3290025",
"9006041",
"3032976",
"9326680",
"8093563"
] | [
"Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications.",
"Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin.",
"N... | [
1988,
1997,
1987,
1997,
1993
] | 5 | [
"IPR016053"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Viruses",
"ecological metagenomes"
] | [
3496,
6460,
12,
14
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
19,
15,
1,
24,
10,
1,
5,
8,
1,
31
] | 10 | true | Family | Haem oxygenase | Haem oxygenase | Haem_Oase | 5 |
IPR002052 | 2,052 | DNA methylase, N-6 adenine-specific, conserved site | DNA_methylase_N6_adenine_CS | Conserved_site | 208,574 | false | false | In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. There are 2 major classes of DNA methyltransferase that differ in the nature of the modifications they effect. The members of one class (C-MTases) methylate a ring carbon and form C5-methylcytosine (see ... | [
"GO:0003676",
"GO:0008168",
"GO:0032259"
] | [
"nucleic acid binding",
"methyltransferase activity",
"methylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00092"
] | [
"N6_MTASE"
] | [
208574
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"PDOC00087",
"R-CEL-8876725",
"R-DME-8876725",
"R-DRE-8876725",
"R-GGA-8876725",
"R-HSA-156581",
"R-HSA-6782315",
"R-HSA-72764",
"R-HSA-8876725",
"R-MMU-156581",
"R-MMU-72764",
"R-MMU-8876725",
"R-SCE-156581",
"R-SCE-72764",
"R-SCE-8876725",
"R-SPO-156581",
"R-SPO-72764"
] | [
"EC:2.1.1",
"PROSITEDOC:PDOC00087",
"REACTOME:R-CEL-8876725",
"REACTOME:R-DME-8876725",
"REACTOME:R-DRE-8876725",
"REACTOME:R-GGA-8876725",
"REACTOME:R-HSA-156581",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-72764",
"REACTOME:R-HSA-8876725",
"REACTOME:R-MMU-156581",
"REACTOME:R-MMU-72764",
"R... | 18 | [
"1aqi",
"1aqj",
"1eg2",
"1g38",
"1g60",
"1nv8",
"1nv9",
"1nw5",
"1nw6",
"1nw7",
"1nw8",
"1q0s",
"1q0t",
"1sg9",
"1t43",
"1vq1",
"1wy7",
"1yf3",
"1yfj",
"1yfl",
"2adm",
"2ar0",
"2b3t",
"2dpm",
"2esr",
"2fhp",
"2fpo",
"2g1p",
"2ibs",
"2ibt",
"2ift",
"2ih2"... | 178 | [
"PUB00000092",
"PUB00001770",
"PUB00001857",
"PUB00003225",
"PUB00003245",
"PUB00004831"
] | [
"7663118",
"3248728",
"7607512",
"3323532",
"2541254",
"7971991"
] | [
"Structure and function of DNA methyltransferases.",
"The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases.",
"Sequence motifs characteristic for DNA [cytosine-N4] ... | [
1995,
1988,
1995,
1987,
1989,
1994
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid P6",
"Viruses",
"unclassified sequences"
] | [
3935,
174022,
25075,
1,
1793,
3748
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
41,
6,
13,
20,
12,
20,
15,
3,
29,
38,
3,
2,
57
] | 13 | true | Conserved_site | DNA methylase, N-6 adenine-specific, conserved site | DNA methylase, N-6 adenine-specific, conserved site | DNA_methylase_N6_adenine_CS | 9 |
IPR002054 | 2,054 | DNA-directed DNA polymerase X | DNA-dir_DNA_pol_X | Domain | 14,432 | false | false | DNA carries the biological information that instructs cells how to exist in an ordered fashion: accurate replication is thus one of the most important events in the cell life cycle. This function is mediated by DNA-directed DNA-polymerases, which add nucleotide triphosphate (dNTP) residues to the 5'-end of the growing ... | [
"GO:0003677",
"GO:0003887"
] | [
"DNA binding",
"DNA-directed DNA polymerase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"SMART",
"CDD"
] | [
"SM00483",
"cd00141"
] | [
"POLXc",
"NT_POLXc"
] | [
14422,
12467
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"PDOC00452",
"R-BTA-110362",
"R-BTA-110373",
"R-BTA-110381",
"R-BTA-5649702",
"R-BTA-5651801",
"R-BTA-5689880",
"R-BTA-73930",
"R-DRE-110362",
"R-DRE-110373",
"R-DRE-5649702",
"R-DRE-73930",
"R-HSA-110362",
"R-HSA-110373",
"R-HSA-110381",
"R-HSA-5649702",
"R-HSA-5651801"... | [
"EC:2.7.7.7",
"PROSITEDOC:PDOC00452",
"REACTOME:R-BTA-110362",
"REACTOME:R-BTA-110373",
"REACTOME:R-BTA-110381",
"REACTOME:R-BTA-5649702",
"REACTOME:R-BTA-5651801",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-73930",
"REACTOME:R-DRE-110362",
"REACTOME:R-DRE-110373",
"REACTOME:R-DRE-5649702",
"... | 37 | [
"1bpb",
"1bpd",
"1bpe",
"1bpx",
"1bpy",
"1bpz",
"1huo",
"1huz",
"1jms",
"1jn3",
"1kdh",
"1kej",
"1mq2",
"1mq3",
"1nom",
"1rpl",
"1rzt",
"1tv9",
"1tva",
"1xsl",
"1xsn",
"1xsp",
"1zjm",
"1zjn",
"1zqa",
"1zqb",
"1zqc",
"1zqd",
"1zqe",
"1zqf",
"1zqg",
"1zqh"... | 713 | [
"PUB00004647",
"PUB00004955",
"PUB00041709",
"PUB00080369",
"PUB00080370",
"PUB00080391"
] | [
"3479792",
"2196557",
"17159995",
"16061182",
"15100289",
"18972388"
] | [
"Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.",
"An attempt to unify the structure of polymerases.",
"Structural insight into the substrate specificity of DNA Polymerase mu.",
"A gradient of template dependence defines distinct biological roles for family X polymerases in nonhomologous end... | [
1987,
1990,
2007,
2005,
2004,
2008
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
516,
4750,
8876,
68,
222
] | 5 | [
"Arabidopsis thaliana",
"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",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (st... | [
5,
12,
25,
8,
2,
2,
14,
1,
1,
8
] | 10 | true | Domain | DNA-directed DNA polymerase X | DNA-directed DNA polymerase X | DNA-dir_DNA_pol_X | 3 |
IPR002056 | 2,056 | Protein import receptor MAS20 | MAS20 | Family | 4,164 | false | false | Virtually all mitochondrial precursors are imported via the same mechanism [ ]: precursors first bind to receptors on the mitochondrial surface, then insert into the translocation channel in the outer membrane. Many outer-membrane proteins participate in the early stages of import, four of which (MAS20, MAS22, MAS37 an... | [
"GO:0006886",
"GO:0030150",
"GO:0005742"
] | [
"intracellular protein transport",
"protein import into mitochondrial matrix",
"mitochondrial outer membrane translocase complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PF02064",
"PIRSF037707",
"PR00351",
"PTHR12430",
"TIGR00985"
] | [
"MAS20",
"MAS20_rcpt",
"OM20RECEPTOR",
"",
"3a0801s04tom"
] | [
4159,
2663,
3874,
3975,
613
] | 5 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5205685",
"R-BTA-5689880",
"R-CEL-5205685",
"R-CEL-5689880",
"R-DRE-5205685",
"R-DRE-5689880",
"R-HSA-1268020",
"R-HSA-5205685",
"R-HSA-5689880",
"R-MMU-5205685",
"R-MMU-5689880",
"R-RNO-5205685",
"R-RNO-5689880",
"R-SCE-5205685",
"R-SPO-5205685",
"R-SPO-5689880",
"R-XTR-52056... | [
"REACTOME:R-BTA-5205685",
"REACTOME:R-BTA-5689880",
"REACTOME:R-CEL-5205685",
"REACTOME:R-CEL-5689880",
"REACTOME:R-DRE-5205685",
"REACTOME:R-DRE-5689880",
"REACTOME:R-HSA-1268020",
"REACTOME:R-HSA-5205685",
"REACTOME:R-HSA-5689880",
"REACTOME:R-MMU-5205685",
"REACTOME:R-MMU-5689880",
"REACTOM... | 18 | [
"1om2",
"2v1s",
"2v1t",
"3awr",
"3ax2",
"3ax3",
"3ax5",
"5az6",
"5az7",
"5az8",
"5az9",
"7vby",
"7vc9",
"8uy3",
"8xva",
"9eih",
"9eii",
"9eij",
"9i7s",
"9i7t",
"9j79",
"9j7a",
"9j7b",
"9jce"
] | 24 | [
"PUB00002838",
"PUB00005448"
] | [
"8163528",
"7709435"
] | [
"Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion.",
"The protein import receptor of mitochondria."
] | [
1994,
1995
] | 2 | [] | [
"IPR022422"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
4164
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
2,
3,
4,
3,
5,
1,
6,
1,
1
] | 9 | true | Family | Protein import receptor MAS20 | Protein import receptor MAS20 | MAS20 | 6 |
IPR002057 | 2,057 | Isopenicillin N synthase, conserved site | Isopenicillin-N_synth_CS | Conserved_site | 353 | false | false | Isopenicillin N synthase (IPNS) ( ) is a nonhaem-Fe 2+ -dependent enzyme that belongs to a class of nonhaem Fe 2+ -containing enzymes, which includes 2-oxoglutarate-dependent dioxygenases, 2-oxoglutarate-dependent hydroxylases, and enzymes involved in ethylene formation and anthocyanin biosynthesis. IPNS catalyses the ... | [
"GO:0005506",
"GO:0016491",
"GO:0009058"
] | [
"iron ion binding",
"oxidoreductase activity",
"biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00185",
"PS00186"
] | [
"IPNS_1",
"IPNS_2"
] | [
119,
313
] | 2 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"1.21.3.1",
"PWY-5629",
"PDOC00165"
] | [
"EC:1.21.3.1",
"METACYC:PWY-5629",
"PROSITEDOC:PDOC00165"
] | 3 | [
"1bk0",
"1blz",
"1dcs",
"1e5h",
"1e5i",
"1hb1",
"1hb2",
"1hb3",
"1hb4",
"1hjf",
"1hjg",
"1ips",
"1obn",
"1oc1",
"1odm",
"1odn",
"1qiq",
"1qje",
"1qjf",
"1rxf",
"1rxg",
"1unb",
"1uo9",
"1uob",
"1uof",
"1uog",
"1uzw",
"1w03",
"1w04",
"1w05",
"1w06",
"1w28"... | 101 | [
"PUB00002095"
] | [
"2644235"
] | [
"Cloning, characterization, and expression in Escherichia coli of the Streptomyces clavuligerus gene encoding deacetoxycephalosporin C synthetase."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cordyline virus 4",
"Eukaryota",
"Haloferacaceae"
] | [
87,
1,
263,
2
] | 4 | [] | [] | 0 | true | Conserved_site | Isopenicillin N synthase, conserved site | Isopenicillin N synthase, conserved site | Isopenicillin-N_synth_CS | 1 |
IPR002058 | 2,058 | PAP/25A-associated | PAP_assoc | Domain | 20,077 | false | false | This domain is found in eukaryotic poly(A) polymerases and terminal uridylyltransferases. It has been shown to have polynucleotide adenylyltransferase activity [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03828"
] | [
"PAP_assoc"
] | [
20077
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7",
"2.7.7.19",
"R-HSA-429947",
"R-HSA-6802952",
"R-HSA-9819196",
"R-HSA-9820865",
"R-HSA-9930044",
"R-HSA-9937008"
] | [
"EC:2.7.7",
"EC:2.7.7.19",
"REACTOME:R-HSA-429947",
"REACTOME:R-HSA-6802952",
"REACTOME:R-HSA-9819196",
"REACTOME:R-HSA-9820865",
"REACTOME:R-HSA-9930044",
"REACTOME:R-HSA-9937008"
] | 8 | [
"2b4v",
"2b51",
"2b56",
"2ikf",
"2nom",
"2q0c",
"2q0d",
"2q0e",
"2q0f",
"2q0g",
"3nyb",
"4e7x",
"4e80",
"4e8f",
"4ep7",
"4fh3",
"4fh5",
"4fhp",
"4fhv",
"4fhw",
"4fhx",
"4fhy",
"4nkt",
"4nku",
"4ud4",
"4ud5",
"4zrl",
"5a2v",
"5a2w",
"5a2x",
"5a2y",
"5a2z"... | 64 | [
"PUB00045061"
] | [
"15607976"
] | [
"Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"uncultured marine bacterium HF10_29C11"
] | [
20076,
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... | [
9,
13,
13,
9,
26,
17,
3,
13,
32,
2,
5,
24
] | 12 | true | Domain | PAP/25A-associated | PAP/25A-associated | PAP_assoc | 5 |
IPR002059 | 2,059 | Cold-shock protein Csp, DNA-binding | CSP_DNA-bd | Domain | 100,625 | false | false | When Escherichia coli is exposed to a temperature drop from 37 to 10 degrees centigrade, a 4-5 hour lag phase occurs, after which growth is resumed at a reduced rate [ ]. During the lag phase, the expression of around 13 proteins, which contain specific DNA-binding regions [ ], is increased 2-10 fold. These so-called '... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE",
"CDD"
] | [
"PF00313",
"PR00050",
"PS51857",
"cd04458"
] | [
"CSD",
"COLDSHOCK",
"CSD_2",
"CSP_CDS"
] | [
99367,
85057,
99312,
92747
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00304",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-877300",
"R-DRE-72163",
"R-DRE-877300",
"R-HSA-2173796",
"R-HSA-452723",
"R-HSA-72163",
"R-HSA-72165",
"R-HSA-72203",
"R-HSA-877300",
"R-HSA-9017802",
"R-MMU-72163",
"R-MMU-72165",
"R-MMU-72203",
"R-MMU-877300",
"R-... | [
"PROSITEDOC:PDOC00304",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72165",
"REACTOME:R-BTA-72203",
"REACTOME:R-BTA-877300",
"REACTOME:R-DRE-72163",
"REACTOME:R-DRE-877300",
"REACTOME:R-HSA-2173796",
"REACTOME:R-HSA-452723",
"REACTOME:R-HSA-72163",
"REACTOME:R-HSA-72165",
"REACTOME:R-HSA-72203",
... | 24 | [
"1c9o",
"1csp",
"1csq",
"1g6p",
"1h95",
"1hz9",
"1hza",
"1hzb",
"1hzc",
"1i5f",
"1mjc",
"1nmf",
"1nmg",
"1wfq",
"1x65",
"2bh8",
"2es2",
"2f52",
"2hax",
"2i5l",
"2i5m",
"2k5n",
"2kcm",
"2l15",
"2lss",
"2lxj",
"2lxk",
"2mo0",
"2mo1",
"2mqh",
"2n49",
"2ytv"... | 90 | [
"PUB00003861",
"PUB00004061",
"PUB00004326",
"PUB00004406",
"PUB00004548",
"PUB00004718",
"PUB00025582",
"PUB00036544"
] | [
"8022259",
"2184368",
"1622933",
"1614871",
"1912512",
"2247479",
"11851341",
"8321288"
] | [
"The cold-shock response--a hot topic.",
"Cold shock and DNA binding.",
"The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif.",
"RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock do... | [
1994,
1990,
1992,
1992,
1991,
1990,
2002,
1993
] | 8 | [
"IPR011129"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1597,
79333,
18414,
29,
1252
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
17,
5,
48,
8,
9,
54,
39,
12,
38,
14
] | 10 | true | Domain | Cold-shock protein Csp, DNA-binding | Cold-shock protein Csp, DNA-binding | CSP_DNA-bd | 1 |
IPR002060 | 2,060 | Squalene/phytoene synthase | Squ/phyt_synthse | Family | 35,445 | false | false | Squalene synthase (farnesyl-diphosphate farnesyltransferase)(SQS) and phytoene synthase (PSY) share a number of functional similarities. These similarities are also reflected at the level of their primary structure [ , , ]. In particular three well conserved regions are shared by SQS and PSY; they could be involved in ... | [
"GO:0009058"
] | [
"biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SFLD"
] | [
"PF00494",
"SFLDG01018"
] | [
"SQS_PSY",
"Squalene/Phytoene_Synthase_Lik"
] | [
35443,
24244
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"GenProp0758",
"GenProp1530",
"GenProp1594",
"GenProp1683",
"PDOC00802",
"R-BTA-6799198",
"R-DDI-191273",
"R-DME-6799198",
"R-HSA-191273",
"R-HSA-1989781",
"R-HSA-2426168",
"R-HSA-6799198",
"R-MMU-191273",
"R-MMU-6799198",
"R-RNO-191273",
"R-RNO-6799198",
"R-SCE-191273",
... | [
"EC:2.5.1",
"GP:GenProp0758",
"GP:GenProp1530",
"GP:GenProp1594",
"GP:GenProp1683",
"PROSITEDOC:PDOC00802",
"REACTOME:R-BTA-6799198",
"REACTOME:R-DDI-191273",
"REACTOME:R-DME-6799198",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-6799198",
"R... | 19 | [
"1ezf",
"2zco",
"2zcq",
"2zcr",
"2zcs",
"2zy1",
"3acw",
"3acx",
"3acy",
"3adz",
"3ae0",
"3asx",
"3lee",
"3lgz",
"3npr",
"3nri",
"3q2z",
"3q30",
"3tfn",
"3tfp",
"3tfv",
"3v66",
"3vj8",
"3vj9",
"3vja",
"3vjb",
"3vjc",
"3vjd",
"3vje",
"3w7f",
"3wc9",
"3wca"... | 72 | [
"PUB00000230",
"PUB00001836",
"PUB00003686"
] | [
"8250898",
"8294001",
"8474436"
] | [
"Expression of the genes encoding the early carotenoid biosynthetic enzymes in Capsicum annuum.",
"Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase.",
"Conservation between human and fungal squalene synthetases: similarities... | [
1993,
1993,
1993
] | 3 | [] | [
"IPR044843",
"IPR044844"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
785,
21043,
13227,
2,
388
] | 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... | [
21,
1,
5,
1,
21,
6,
4,
20,
7,
1,
1,
66
] | 12 | true | Family | Squalene/phytoene synthase | Squalene/phytoene synthase | Squ/phyt_synthse | 5 |
IPR002061 | 2,061 | Scorpion long chain toxin/defensin | Scorpion_toxinL/defensin | Family | 1,124 | false | false | This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is a plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids [ ]. The scorpion toxin (a neurotoxin) binds to so... | [
"GO:0008200",
"GO:0019871",
"GO:0005576"
] | [
"ion channel inhibitor activity",
"sodium channel inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00537"
] | [
"Toxin_3"
] | [
1124
] | 1 | [] | [] | [] | 0 | [
"1aho",
"1b3c",
"1b7d",
"1bcg",
"1bmr",
"1chz",
"1cn2",
"1djt",
"1dq7",
"1fh3",
"1i6f",
"1i6g",
"1jxc",
"1jza",
"1jzb",
"1kv0",
"1lqh",
"1lqi",
"1lqq",
"1nh5",
"1npi",
"1nra",
"1nrb",
"1omy",
"1pe4",
"1ptx",
"1seg",
"1sn1",
"1sn4",
"1snb",
"1t0z",
"1t1t"... | 75 | [
"PUB00011377",
"PUB00100742",
"PUB00100743"
] | [
"12581313",
"30733386",
"34379289"
] | [
"Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids.",
"Structural basis of α-scorpion toxin action on Na<sub>v</sub> channels.",
"Expression and purification of recombinant alpha-toxin AnCra1 from the scorpion Androctonus crassicauda and its functional characterization on ma... | [
2003,
2019,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1124
] | 1 | [
"Arabidopsis thaliana"
] | [
18
] | 1 | true | Family | Scorpion long chain toxin/defensin | Scorpion long chain toxin/defensin | Scorpion_toxinL/defensin | 6 |
IPR002062 | 2,062 | Oxytocin receptor | Oxytocn_rcpt | Family | 1,210 | 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:0004990",
"GO:0007186",
"GO:0016020"
] | [
"oxytocin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"CDD"
] | [
"PR00665",
"cd15387"
] | [
"OXYTOCINR",
"7tmA_OT_R"
] | [
1206,
591
] | 2 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"369",
"R-BTA-388479",
"R-BTA-416476",
"R-HSA-388479",
"R-HSA-416476",
"R-MMU-388479",
"R-MMU-416476",
"R-RNO-388479",
"R-RNO-416476"
] | [
"IUPHAR:369",
"REACTOME:R-BTA-388479",
"REACTOME:R-BTA-416476",
"REACTOME:R-HSA-388479",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-388479",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-388479",
"REACTOME:R-RNO-416476"
] | 9 | [
"6tpk",
"7qvm",
"7ryc"
] | 3 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR001817"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1210
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
4,
5
] | 4 | true | Family | Oxytocin receptor | Oxytocin receptor | Oxytocn_rcpt | 5 |
IPR002063 | 2,063 | Haemerythrin | Haemerythrin | Family | 387 | false | false | The hemerythrin family is composed of hemerythrin proteins found in invertebrates, and a broader collection of bacterial and archaeal homologues. Hemerythrin is an oxygen-binding protein found in the vascular system and coelomic fluid, or in muscles (myohemerythrin) in invertebrates [ ]. Many of the homologous proteins... | [
"GO:0005506"
] | [
"iron ion binding"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PRINTS",
"NCBIFAM"
] | [
"PIRSF002033",
"PR00186",
"TIGR00058"
] | [
"Hemerythrin",
"HEMERYTHRIN",
"Hemerythrin"
] | [
317,
387,
359
] | 3 | [] | [] | [] | 0 | [
"1a7d",
"1a7e",
"1hmd",
"1hmo",
"1hrb",
"1i4y",
"1i4z",
"2hmq",
"2hmz",
"2mhr"
] | 10 | [
"PUB00001429",
"PUB00001615",
"PUB00003224",
"PUB00004613",
"PUB00005066"
] | [
"1425663",
"2065779",
"3681996",
"3856224",
"2362933"
] | [
"Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech.",
"Primary structure of myohemerythrin from the annelid Nereis diversicolor.",
"Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution.",
"Active site structures of deoxyhemerythrin and oxyhemerythrin.",
"Th... | [
1992,
1991,
1987,
1985,
1990
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
387
] | 1 | [] | [] | 0 | true | Family | Haemerythrin | Haemerythrin | Haemerythrin | 1 |
IPR002065 | 2,065 | Thiol peroxidase Tpx | TPX | Family | 11,356 | false | false | Escherichia coli protein Tpx [ ] is a bacterial, periplasmic antioxidant protein with a thiol peroxidase activity. It is a small protein of 18kDa whose sequence is well conserved in other bacterial species. Tpx which differs from other peroxidases (PRXs) in that it shows substrate specificity toward alkyl hydroperoxide... | [
"GO:0008379",
"GO:0016209"
] | [
"thioredoxin peroxidase activity",
"antioxidant activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00269",
"NF001808",
"cd03014"
] | [
"Tpx",
"PRK00522.1",
"PRX_Atyp2cys"
] | [
9355,
11075,
11284
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"1.11.1.24",
"PDOC00973",
"R-HSA-1222538",
"R-HSA-1222541"
] | [
"EC:1.11.1.24",
"PROSITEDOC:PDOC00973",
"REACTOME:R-HSA-1222538",
"REACTOME:R-HSA-1222541"
] | 4 | [
"1psq",
"1q98",
"1qxh",
"1xvq",
"1y25",
"2jsy",
"2jsz",
"2xpd",
"2xpe",
"2yjh",
"2yzh",
"3hvs",
"3hvv",
"3hvx",
"3i43",
"3p7x",
"3zrd",
"3zre",
"4af2",
"4je1",
"6udg",
"8xvw",
"8zwt",
"8zxu",
"9f5v",
"9f64",
"9f65"
] | 27 | [
"PUB00002933",
"PUB00010128",
"PUB00030434"
] | [
"7499381",
"12517450",
"14506251"
] | [
"Thioredoxin-linked \"thiol peroxidase\" from periplasmic space of Escherichia coli.",
"Structure, mechanism and regulation of peroxiredoxins.",
"Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys... | [
1995,
2003,
2003
] | 3 | [] | [
"IPR054826"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11236,
20,
100
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Thiol peroxidase Tpx | Thiol peroxidase Tpx | TPX | 3 |
IPR002067 | 2,067 | Mitochondrial carrier protein | MCP | Family | 108,052 | false | false | This family includes mitochondrial carrier proteins that transport a broad variety of substrates and, therefore, they are involved in different metabolic pathways such as the TCA cycle, lipid metabolism, nucleotides metabolism [ , , , ] and energy transfer [ , , , , ]. Some examples of this group are the uncoupling pro... | [
"GO:0055085"
] | [
"transmembrane transport"
] | [
"biological_process"
] | 1 | [
"PRINTS",
"PRINTS"
] | [
"PR00784",
"PR00926"
] | [
"MTUNCOUPLING",
"MITOCARRIER"
] | [
9203,
98849
] | 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-1268020",
"R-BTA-166187",
"R-BTA-167826",
"R-BTA-196819",
"R-BTA-352230",
"R-BTA-425393",
"R-BTA-428643",
"R-BTA-71064",
"R-BTA-83936",
"R-BTA-9837999",
"R-BTA-9856872",
"R-CEL-1614517",
"R-CEL-428643",
"R-CEL-8963693",
"R-CEL-9856872",
"R-DDI-1268020",
"R-DDI-1614517",
"R-D... | [
"REACTOME:R-BTA-1268020",
"REACTOME:R-BTA-166187",
"REACTOME:R-BTA-167826",
"REACTOME:R-BTA-196819",
"REACTOME:R-BTA-352230",
"REACTOME:R-BTA-425393",
"REACTOME:R-BTA-428643",
"REACTOME:R-BTA-71064",
"REACTOME:R-BTA-83936",
"REACTOME:R-BTA-9837999",
"REACTOME:R-BTA-9856872",
"REACTOME:R-CEL-16... | 109 | [
"1okc",
"2c3e",
"2lck",
"4c9g",
"4c9h",
"4c9j",
"4c9q",
"6gci",
"8g8w",
"8hbv",
"8hbw",
"8j1n",
"9fzq"
] | 13 | [
"PUB00001005",
"PUB00001675",
"PUB00003301",
"PUB00005084",
"PUB00005351",
"PUB00005407",
"PUB00029479",
"PUB00057422",
"PUB00097195",
"PUB00101069",
"PUB00101070",
"PUB00101071",
"PUB00152845",
"PUB00152846",
"PUB00152847",
"PUB00152848"
] | [
"8325039",
"8206158",
"8487299",
"8140286",
"2158156",
"8291088",
"14603310",
"11121399",
"30611538",
"21785437",
"9139827",
"20416274",
"19429682",
"31356773",
"35288533",
"35727412"
] | [
"The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.",
"Mitochondrial carrier proteins.",
"Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.",
"Expansion of the mitochondrial carrie... | [
1993,
1994,
1993,
1993,
1990,
1993,
2003,
2001,
2019,
2011,
1997,
2010,
2009,
2019,
2022,
2022
] | 16 | [] | [
"IPR002113",
"IPR002167",
"IPR045315"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
8,
108020,
7,
17
] | 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... | [
165,
21,
104,
58,
110,
64,
16,
108,
113,
22,
12,
214
] | 12 | true | Family | Mitochondrial carrier protein | Mitochondrial carrier protein | MCP | 9 |
IPR002068 | 2,068 | Alpha crystallin/Hsp20 domain | A-crystallin/Hsp20_dom | Domain | 95,949 | false | false | Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by inducing the synthesis of proteins collectively known as heat-shock proteins (hsp) [ ]. Amongst them is a family of proteins with an average molecular weight of 20 Kd, known as the hsp20 proteins [ ]. These seem to act as chaper... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00011",
"PS01031"
] | [
"HSP20",
"SHSP"
] | [
92674,
94113
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00791",
"R-BTA-3371571",
"R-BTA-4420097",
"R-BTA-450408",
"R-BTA-5687128",
"R-BTA-9009391",
"R-CEL-3371571",
"R-CEL-4420097",
"R-DME-3371571",
"R-DME-4420097",
"R-DME-9009391",
"R-GGA-3371571",
"R-HSA-3371571",
"R-HSA-4420097",
"R-HSA-450408",
"R-HSA-5687128",
"R-HSA-9009391",
... | [
"PROSITEDOC:PDOC00791",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-450408",
"REACTOME:R-BTA-5687128",
"REACTOME:R-BTA-9009391",
"REACTOME:R-CEL-3371571",
"REACTOME:R-CEL-4420097",
"REACTOME:R-DME-3371571",
"REACTOME:R-DME-4420097",
"REACTOME:R-DME-9009391",
"REACTOME:R... | 28 | [
"1gme",
"1shs",
"2bol",
"2byu",
"2h50",
"2h53",
"2klr",
"2n0k",
"2n3j",
"2wj5",
"2wj7",
"2y1y",
"2y1z",
"2y22",
"2ygd",
"3aab",
"3aac",
"3gla",
"3gt6",
"3guf",
"3j07",
"3l1e",
"3l1f",
"3l1g",
"3n3e",
"3q9p",
"3q9q",
"3vqk",
"3vql",
"3vqm",
"3w1z",
"4eld"... | 83 | [
"PUB00000102",
"PUB00001454",
"PUB00003438",
"PUB00060735",
"PUB00060736",
"PUB00094298"
] | [
"2853609",
"7925426",
"7723051",
"6285380",
"1370952",
"22120592"
] | [
"The heat-shock proteins.",
"Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology.",
"The expanding small heat-shock protein family, and structure predictions of the conserved \"alpha-crystallin domain\".",
"Four small Drosophila heat shock protei... | [
1988,
1994,
1995,
1982,
1992,
2012
] | 6 | [] | [
"IPR033894",
"IPR037552",
"IPR037876",
"IPR037882",
"IPR037885",
"IPR037913",
"IPR042790"
] | 0 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3017,
40879,
51210,
159,
684
] | 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",... | [
165,
25,
20,
19,
2,
47,
22,
3,
86,
33,
2,
2,
178
] | 13 | true | Domain | Alpha crystallin/Hsp20 domain | Alpha crystallin/Hsp20 domain | A-crystallin/Hsp20_dom | 3 |
IPR002070 | 2,070 | Transcription factor, Brachyury | TF_Brachyury | Family | 5,188 | false | false | The T-box gene family is an ancient group of putative transcription factors that appear to play a critical role in the development of all animal species. These genes were uncovered on the basis of similarity to the DNA binding domain [ ] of murine Brachyury (T) gene product, which similarity is the defining feature of ... | [
"GO:0003700",
"GO:0006355",
"GO:0005634"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00938"
] | [
"BRACHYURY"
] | [
5188
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-9856649",
"R-HSA-9733709",
"R-HSA-9754189",
"R-HSA-9758919",
"R-HSA-9793380",
"R-HSA-9796292",
"R-HSA-9823730",
"R-HSA-9824272",
"R-HSA-9825892",
"R-HSA-9832991"
] | [
"REACTOME:R-CEL-9856649",
"REACTOME:R-HSA-9733709",
"REACTOME:R-HSA-9754189",
"REACTOME:R-HSA-9758919",
"REACTOME:R-HSA-9793380",
"REACTOME:R-HSA-9796292",
"REACTOME:R-HSA-9823730",
"REACTOME:R-HSA-9824272",
"REACTOME:R-HSA-9825892",
"REACTOME:R-HSA-9832991"
] | 10 | [
"1h6f",
"1xbr",
"5qrf",
"5qrg",
"5qrh",
"5qri",
"5qrj",
"5qrk",
"5qrl",
"5qrm",
"5qrn",
"5qro",
"5qrp",
"5qrq",
"5qrr",
"5qrs",
"5qrt",
"5qru",
"5qrv",
"5qrw",
"5qrx",
"5qry",
"5qrz",
"5qs0",
"5qs1",
"5qs2",
"5qs3",
"5qs4",
"5qs5",
"5qs6",
"5qs7",
"5qs8"... | 58 | [
"PUB00000739",
"PUB00001941",
"PUB00001985",
"PUB00003895",
"PUB00005531",
"PUB00006158"
] | [
"9504043",
"8878690",
"9503012",
"7920656",
"9196325",
"9395282"
] | [
"The T-box gene family.",
"Evolution of mouse T-box genes by tandem duplication and cluster dispersion.",
"A combined analysis of genomic and primary protein structure defines the phylogenetic relationship of new members if the T-box family.",
"An ancient family of embryonically expressed mouse genes sharing ... | [
1998,
1996,
1998,
1994,
1997,
1997
] | 6 | [
"IPR001699"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
5188
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
12,
10,
13,
12,
13
] | 6 | true | Family | Transcription factor, Brachyury | Transcription factor, Brachyury | TF_Brachyury | 9 |
IPR002071 | 2,071 | Thermonuclease active site | Thermonucl_AS | Active_site | 6,517 | false | false | Staphylococcus aureus secretes a thermostable nuclease ( ), known as thermonuclease (TNase), which is a calcium-dependent enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond yielding 3'-mononucleotides and dinucleotides [ ]. This signature contains the three residues, ... | [
"GO:0003676",
"GO:0004518"
] | [
"nucleic acid binding",
"nuclease activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE",
"PROSITE"
] | [
"PS01123",
"PS01284"
] | [
"TNASE_1",
"TNASE_2"
] | [
3853,
3760
] | 2 | [
"PROSITEDOC",
"REACTOME"
] | [
"PDOC00865",
"R-HSA-6802952"
] | [
"PROSITEDOC:PDOC00865",
"REACTOME:R-HSA-6802952"
] | 2 | [
"1a2t",
"1a2u",
"1a3t",
"1a3u",
"1a3v",
"1aex",
"1ena",
"1enc",
"1eqv",
"1ey0",
"1ey4",
"1ey5",
"1ey6",
"1ey7",
"1ey8",
"1ey9",
"1eya",
"1eyc",
"1eyd",
"1ez6",
"1ez8",
"1f2m",
"1f2y",
"1f2z",
"1ihz",
"1ii3",
"1jok",
"1joo",
"1joq",
"1jor",
"1kaa",
"1kab"... | 309 | [
"PUB00001847",
"PUB00004982"
] | [
"8045422",
"1896431"
] | [
"Primary structure and biological features of a thermostable nuclease isolated from Staphylococcus hyicus.",
"The crystal structure of staphylococcal nuclease refined at 1.7 A resolution."
] | [
1994,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
375,
4800,
1194,
13,
2,
133
] | 6 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
2,
2,
6,
6,
1,
5,
3
] | 7 | true | Active_site | Thermonuclease active site | Thermonuclease active site | Thermonucl_AS | 7 |
IPR002072 | 2,072 | Nerve growth factor-related | Nerve_growth_factor-rel | Domain | 14,828 | false | false | During the development of the vertebrate nervous system, many neurons become redundant (because they have died, failed to connect to target cells, etc.) and are eliminated. At the same time, developing neurons send out axon outgrowths that contact their target cells [ ]. Such cells control their degree of innervation (... | [
"GO:0005102"
] | [
"signaling receptor binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"SMART"
] | [
"PF00243",
"PR00268",
"SM00140"
] | [
"NGF",
"NGF",
"NGF"
] | [
14819,
12579,
14613
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00221",
"R-BTA-1257604",
"R-BTA-6811558",
"R-BTA-9026527",
"R-BTA-9028731",
"R-BTA-9032759",
"R-BTA-9034013",
"R-BTA-9034793",
"R-BTA-9603381",
"R-DRE-167060",
"R-DRE-170984",
"R-DRE-205017",
"R-DRE-209543",
"R-DRE-209563",
"R-GGA-1257604",
"R-GGA-6811558",
"R-GGA-9026527",
"R... | [
"PROSITEDOC:PDOC00221",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-6811558",
"REACTOME:R-BTA-9026527",
"REACTOME:R-BTA-9028731",
"REACTOME:R-BTA-9032759",
"REACTOME:R-BTA-9034013",
"REACTOME:R-BTA-9034793",
"REACTOME:R-BTA-9603381",
"REACTOME:R-DRE-167060",
"REACTOME:R-DRE-170984",
"REACTOME:R-... | 103 | [
"1b8k",
"1b8m",
"1b98",
"1bet",
"1bnd",
"1btg",
"1hcf",
"1nt3",
"1sg1",
"1sgf",
"1www",
"2ifg",
"3buk",
"3ij2",
"4eax",
"4ec7",
"4edw",
"4edx",
"4efv",
"4xpj",
"4zbn",
"5jz7",
"5lsd",
"6ffy",
"6xuo",
"6yw8",
"9fik"
] | 27 | [
"PUB00000638",
"PUB00001187",
"PUB00001600",
"PUB00005102",
"PUB00005408",
"PUB00043579",
"PUB00043580"
] | [
"1477101",
"2369898",
"1995338",
"3589669",
"8488558",
"2236018",
"8527932"
] | [
"Purification and amino-acid sequence of a nerve growth factor from the venom of Vipera russelli russelli.",
"Regional distribution of brain-derived neurotrophic factor mRNA in the adult mouse brain.",
"Amino acid sequences of nerve growth factors derived from cobra venoms.",
"Recruitment of enzymes as lens s... | [
1992,
1990,
1991,
1987,
1993,
1990,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Avipoxvirus",
"Bilateria"
] | [
20,
14808
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
14,
14,
24
] | 4 | true | Domain | Nerve growth factor-related | Nerve growth factor-related | Nerve_growth_factor-rel | 5 |
IPR002074 | 2,074 | Somatostatin receptor 2 | Somatstn_rcpt_2 | Family | 955 | 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"
] | [
"PR00588"
] | [
"SOMATOSTTN2R"
] | [
955
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"356",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594",
"R-SSC-375276",
"R-SSC-418594"
] | [
"IUPHAR:356",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594",
"REACTOME:R-SSC-375276",
"REACTOME:R-SSC-418594"
] | 9 | [
"7t10",
"7t11",
"7ul5",
"7wic",
"7wig",
"7wj5",
"7xat",
"7xau",
"7xav",
"7xmr",
"7xn9",
"7xna",
"7y24",
"7y26",
"7y27",
"7yac",
"7yae"
] | 17 | [
"PUB00013316",
"PUB00063572",
"PUB00063590",
"PUB00063595",
"PUB00063596",
"PUB00063597",
"PUB00063598",
"PUB00063599",
"PUB00063600",
"PUB00063601",
"PUB00063602",
"PUB00063603",
"PUB00063604",
"PUB00063605",
"PUB00063619"
] | [
"14507421",
"10433861",
"7792934",
"8243278",
"8078491",
"7907795",
"1346068",
"8483934",
"15361490",
"10598790",
"1328199",
"7538774",
"9426226",
"8684611",
"8034040"
] | [
"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,
1994
] | 15 | [
"IPR000586"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
955
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
1,
3
] | 4 | true | Family | Somatostatin receptor 2 | Somatostatin receptor 2 | Somatstn_rcpt_2 | 1 |
IPR002075 | 2,075 | Nuclear transport factor 2 domain | NTF2_dom | Domain | 25,906 | false | false | This entry represent the main structural domain of NTF2, Nuclear RNA export factors and related proteins [ , ]. Nuclear transport factor 2 (NTF2) is a homodimer which stimulates efficient nuclear import of a cargo protein. NTF2 binds to both RanGDP and FxFG repeat-containing nucleoporins. NTF2 folds into a cone with a ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF02136",
"PF22602"
] | [
"NTF2",
"NXF_NTF2"
] | [
20744,
5162
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50177",
"R-BTA-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-CEL-159236",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-GGA-159236",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-HSA-9705671",
"R-MMU-159227",
"R-MMU-15923... | [
"PROSITEDOC:PDOC50177",
"REACTOME:R-BTA-159227",
"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-CEL-159236",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-GGA-159236",
"REACTOME:R-HSA-1592... | 28 | [
"1ar0",
"1ask",
"1gy5",
"1gy6",
"1gy7",
"1gyb",
"1jb2",
"1jb4",
"1jb5",
"1jkg",
"1jn5",
"1of5",
"1oun",
"1q40",
"1qma",
"1u5o",
"1zo2",
"1zx2",
"2a15",
"2qiy",
"2z76",
"2z77",
"2z7a",
"3mg1",
"3mg2",
"3mg3",
"3nv0",
"3q90",
"3ujm",
"4fcj",
"4fcm",
"4iia"... | 98 | [
"PUB00018169",
"PUB00021156",
"PUB00025422",
"PUB00026326",
"PUB00026433"
] | [
"9533885",
"9368653",
"12065398",
"11846560",
"11583626"
] | [
"Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran.",
"Nuclear protein import is decreased by engineered mutants of nuclear transport factor 2 (NTF2) that do not bind GDP-Ran.",
"Structural basis for the interaction between N... | [
1998,
1997,
2002,
2001,
2001
] | 5 | [] | [
"IPR018222"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"metagenomes"
] | [
1191,
24703,
8,
4
] | 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... | [
74,
7,
24,
18,
54,
28,
3,
21,
35,
3,
4,
70
] | 12 | true | Domain | Nuclear transport factor 2 domain | Nuclear transport factor 2 domain | NTF2_dom | 3 |
IPR002076 | 2,076 | ELO family | ELO_fam | Family | 26,939 | false | false | The ELO family consist of eukaryotic integral membrane proteins involved in fatty acid elongation. This family consist of: Mammalian proteins ELOVL1 to ELOVL7 [ , ]. These proteins catalyse the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle, each of th... | [
"GO:0009922",
"GO:0016020"
] | [
"fatty acid elongase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF01151",
"PTHR11157"
] | [
"ELO",
""
] | [
26935,
26026
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"2.3.1.199",
"GenProp1376",
"PWY-5080",
"PWY-5972",
"PWY-6433",
"PWY-6598",
"PWY-7035",
"PWY-7036",
"PWY-7601",
"PWY-7602",
"PWY-7619",
"PWY-7724",
"PWY-7725",
"PWY-8041",
"PDOC00914",
"R-BTA-2046105",
"R-BTA-2046106",
"R-BTA-75876",
"R-CEL-2046105",
"R-CEL-2046106",
"R-CEL-7... | [
"EC:2.3.1.199",
"GP:GenProp1376",
"METACYC:PWY-5080",
"METACYC:PWY-5972",
"METACYC:PWY-6433",
"METACYC:PWY-6598",
"METACYC:PWY-7035",
"METACYC:PWY-7036",
"METACYC:PWY-7601",
"METACYC:PWY-7602",
"METACYC:PWY-7619",
"METACYC:PWY-7724",
"METACYC:PWY-7725",
"METACYC:PWY-8041",
"PROSITEDOC:PD... | 51 | [
"6y7f"
] | 1 | [
"PUB00002271",
"PUB00002856",
"PUB00018033",
"PUB00018034",
"PUB00097860",
"PUB00097862",
"PUB00097863"
] | [
"7768822",
"8027068",
"10791983",
"9211877",
"29458843",
"21959040",
"30487246"
] | [
"Cloning and characterization of GNS1: a Saccharomyces cerevisiae gene involved in synthesis of 1,3-beta-glucan in vitro.",
"Transcriptional control of yeast plasma membrane H(+)-ATPase by glucose. Cloning and characterization of a new gene involved in this regulation.",
"Role of a new mammalian gene family in ... | [
1995,
1994,
2000,
1997,
2018,
2011,
2019
] | 7 | [] | [
"IPR033670",
"IPR033675",
"IPR033677",
"IPR033678",
"IPR033679",
"IPR033680",
"IPR033681"
] | 0 | 7 | 0 | [
"Eukaryota",
"Nocardioides malaquae",
"Viruses",
"metagenomes"
] | [
26874,
1,
25,
39
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
16,
9,
20,
37,
18,
20,
2,
5,
23,
3,
2,
7
] | 12 | true | Family | ELO family | ELO family | ELO_fam | 7 |
IPR002077 | 2,077 | Voltage-dependent calcium channel, alpha-1 subunit | VDCCAlpha1 | Family | 23,176 | false | false | Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d... | [
"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"
] | [
"PR00167"
] | [
"CACHANNEL"
] | [
23176
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-112308",
"R-DME-422356",
"R-DME-5576892",
"R-DME-5576893",
"R-GGA-422356",
"R-HSA-112308",
"R-HSA-400042",
"R-HSA-419037",
"R-HSA-422356",
"R-HSA-445355",
"R-HSA-5576892",
"R-HSA-5576893",
"R-HSA-9662360",
"R-MMU-112308",
"R-MMU-422356",
"R-MMU-5576892",
"R-MMU-5576893",
"R-... | [
"REACTOME:R-DME-112308",
"REACTOME:R-DME-422356",
"REACTOME:R-DME-5576892",
"REACTOME:R-DME-5576893",
"REACTOME:R-GGA-422356",
"REACTOME:R-HSA-112308",
"REACTOME:R-HSA-400042",
"REACTOME:R-HSA-419037",
"REACTOME:R-HSA-422356",
"REACTOME:R-HSA-445355",
"REACTOME:R-HSA-5576892",
"REACTOME:R-HSA-... | 22 | [
"3jbr",
"5gjv",
"5gjw",
"6byo",
"6jp5",
"6jp8",
"6jpa",
"6jpb",
"7jpk",
"7jpl",
"7jpv",
"7jpw",
"7jpx",
"7mix",
"7miy",
"7uhf",
"7uhg",
"7vfs",
"7vfu",
"7vfv",
"7vfw",
"7wli",
"7wlj",
"7wlk",
"7wll",
"7xlq",
"7yg5",
"8e56",
"8e57",
"8e58",
"8e59",
"8e5a"... | 50 | [
"PUB00036034",
"PUB00036040",
"PUB00036041"
] | [
"14657414",
"11031246",
"10774722"
] | [
"International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels.",
"Structure and regulation of voltage-gated Ca2+ channels.",
"Nomenclature of voltage-gated calcium channels."
] | [
2003,
2000,
2000
] | 3 | [] | [
"IPR005446",
"IPR005447",
"IPR005448",
"IPR005449"
] | 0 | 4 | 0 | [
"Eukaryota"
] | [
23176
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
23,
205,
21,
78,
75,
86,
1
] | 7 | true | Family | Voltage-dependent calcium channel, alpha-1 subunit | Voltage-dependent calcium channel, alpha-1 subunit | VDCCAlpha1 | 8 |
IPR002078 | 2,078 | RNA polymerase sigma factor 54 interaction domain | Sigma_54_int | Domain | 162,390 | false | false | This entry represents the whole ATP-binding domain, including the ATP-binding motif A and the motif B. This domain has been termed RNA polymerase sigma factor 54 interaction domain. Some bacterial regulatory proteins activate the expression of genes from promoters recognised by core RNA polymerase associated with the a... | [
"GO:0005524",
"GO:0008134",
"GO:0006355"
] | [
"ATP binding",
"transcription factor binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00158",
"PF14532",
"PS50045"
] | [
"Sigma54_activat",
"Sigma54_activ_2",
"SIGMA54_INTERACT_4"
] | [
152634,
3937,
159040
] | 3 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0634",
"PDOC00579"
] | [
"GP:GenProp0634",
"PROSITEDOC:PDOC00579"
] | 2 | [
"1ny5",
"1ny6",
"1ojl",
"2bjv",
"2bjw",
"2c96",
"2c98",
"2c99",
"2c9c",
"2vii",
"3co5",
"3dzd",
"3k1j",
"3m0e",
"3n70",
"4bs1",
"4bt0",
"4bt1",
"4l4u",
"4ly6",
"4lzz",
"4qhs",
"4qht",
"4qnm",
"4qnr",
"4qos",
"4zpx",
"5ep0",
"5ep1",
"5ep2",
"5ep3",
"5ep4"... | 68 | [
"PUB00000103",
"PUB00001221",
"PUB00002228",
"PUB00004389"
] | [
"2694934",
"1534752",
"8407777",
"2041769"
] | [
"Prokaryotic signal transduction mediated by sensor and regulator protein pairs.",
"The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent.",
"The sigma 54 bacterial enhancer-binding protein family: mechanism of action and phylogenetic relationship of the... | [
1989,
1992,
1993,
1991
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
781,
158786,
601,
4,
2218
] | 5 | [
"Escherichia coli (strain K12)"
] | [
13
] | 1 | true | Domain | RNA polymerase sigma factor 54 interaction domain | RNA polymerase sigma factor 54 interaction domain | Sigma_54_int | 2 |
IPR002079 | 2,079 | Gag polyprotein, inner coat protein p12 | Gag_p12 | Domain | 351 | false | false | The retroviral p12 protein is a proline rich virion structural protein found in the inner coat. p12 is associated with pathogenicity of the virus [ ]. It is a constituent of the pre-integration complex (PIC) and mediates its integration [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01141"
] | [
"Gag_p12"
] | [
351
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00003504",
"PUB00096937"
] | [
"7690416",
"23300449"
] | [
"The MA (p15) and p12 regions of the gag gene are sufficient for the pathogenicity of the murine AIDS virus.",
"p12 tethers the murine leukemia virus pre-integration complex to mitotic chromosomes."
] | [
1993,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Boreoeutheria",
"Geopseudomonas aromaticivorans",
"Retroviridae"
] | [
80,
1,
270
] | 3 | [
"Mus musculus",
"Rattus norvegicus"
] | [
21,
2
] | 2 | true | Domain | Gag polyprotein, inner coat protein p12 | Gag polyprotein, inner coat protein p12 | Gag_p12 | 6 |
IPR002080 | 2,080 | Seminal vesicle protein II, conserved site | SVP_II_CS | Conserved_site | 18 | false | false | Seminal vesicle protein II (SVP-II) [ ] is one of the six major secretory proteins secreted by rat seminal vesicle. It is a clotting protein that serves as the substrate in the formation of the copulatory plug. Covalent clotting of this protein is catalyzed by a transglutaminase and involves the formation of gamma-glut... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00515"
] | [
"SVP_II"
] | [
18
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00446"
] | [
"PROSITEDOC:PDOC00446"
] | 1 | [] | 0 | [
"PUB00002629"
] | [
"2351680"
] | [
"Structural characterization of the rat seminal vesicle secretion II protein and gene."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Muroidea"
] | [
18
] | 1 | [
"Mus musculus",
"Rattus norvegicus"
] | [
6,
4
] | 2 | true | Conserved_site | Seminal vesicle protein II, conserved site | Seminal vesicle protein II, conserved site | SVP_II_CS | 3 |
IPR002081 | 2,081 | Cryptochrome/DNA photolyase class 1 | Cryptochrome/DNA_photolyase_1 | Family | 38,705 | false | false | This entry represents the class1 cryptochrome/DNA photolyase family. Its members include cryptochromes, DNA photolyases and cryptochrome-DASH (Cry-DASH). The Cry-DASH family members have been shown to act as photolyases with high degree of specificity for cyclobutane pyrimidine dimers in ssDNA [ ]. This protein family ... | [] | [] | [] | 0 | [
"PRINTS",
"PANTHER"
] | [
"PR00147",
"PTHR11455"
] | [
"DNAPHOTLYASE",
""
] | [
25923,
38628
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00331",
"R-DME-432395",
"R-DME-432553",
"R-DME-538864",
"R-HSA-9931510",
"R-HSA-9931521",
"R-HSA-9931530",
"R-HSA-9932298"
] | [
"PROSITEDOC:PDOC00331",
"REACTOME:R-DME-432395",
"REACTOME:R-DME-432553",
"REACTOME:R-DME-538864",
"REACTOME:R-HSA-9931510",
"REACTOME:R-HSA-9931521",
"REACTOME:R-HSA-9931530",
"REACTOME:R-HSA-9932298"
] | 8 | [
"1dnp",
"1iqr",
"1iqu",
"1np7",
"1owl",
"1owm",
"1own",
"1owo",
"1owp",
"1qnf",
"1tez",
"1u3c",
"1u3d",
"2e0i",
"2ijg",
"2j07",
"2j08",
"2j09",
"2j4d",
"2vtb",
"2wb2",
"2wq6",
"2wq7",
"3cvu",
"3cvv",
"3cvw",
"3cvx",
"3cvy",
"3fy4",
"4ct0",
"4gu5",
"4i6e"... | 112 | [
"PUB00001269",
"PUB00076728",
"PUB00076729",
"PUB00076730",
"PUB00163231"
] | [
"7813451",
"17062752",
"25910181",
"26352435",
"22066008"
] | [
"A new class of DNA photolyases present in various organisms including aplacental mammals.",
"A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity.",
"Binding of Substrate Locks the Electrochemistry of CRY-DASH into DNA Repair.",
"Evolutionary History of the Photoly... | [
1994,
2006,
2015,
2015,
2011
] | 5 | [] | [
"IPR014133",
"IPR014134",
"IPR019947"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Nucleocytoviricota",
"unclassified sequences"
] | [
757,
20622,
16861,
28,
437
] | 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... | [
41,
22,
4,
1,
8,
3,
2,
24,
6,
1,
56
] | 11 | true | Family | Cryptochrome/DNA photolyase class 1 | Cryptochrome/DNA photolyase class 1 | Cryptochrome/DNA_photolyase_1 | 4 |
IPR002082 | 2,082 | Aspartate carbamoyltransferase | Asp_carbamoyltransf | Family | 29,424 | false | false | Aspartate carbamoyltransferase (ATCase) catalyses the formation of carbamoyl-aspartate in the pyrimidine biosynthesis pathway, by the association of aspartate and carbamoyl-phosphate. This is the commitment step in the Escherichia coli pathway and is regulated by feedback inhibition by CTP, the final product of the pat... | [
"GO:0004070",
"GO:0006207"
] | [
"aspartate carbamoyltransferase activity",
"'de novo' pyrimidine nucleobase biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00001",
"TIGR00670"
] | [
"Asp_carb_tr",
"asp_carb_tr"
] | [
26826,
29383
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.3.2",
"GenProp0187",
"GenProp1172",
"GenProp1418",
"GenProp1427",
"GenProp1614",
"PWY-5686",
"PWY-7790",
"PWY-7791",
"R-CEL-500753",
"R-DDI-500753",
"R-DME-500753",
"R-HSA-500753",
"R-MMU-500753",
"R-SCE-500753",
"R-SPO-500753"
] | [
"EC:2.1.3.2",
"GP:GenProp0187",
"GP:GenProp1172",
"GP:GenProp1418",
"GP:GenProp1427",
"GP:GenProp1614",
"METACYC:PWY-5686",
"METACYC:PWY-7790",
"METACYC:PWY-7791",
"REACTOME:R-CEL-500753",
"REACTOME:R-DDI-500753",
"REACTOME:R-DME-500753",
"REACTOME:R-HSA-500753",
"REACTOME:R-MMU-500753",
... | 16 | [
"1acm",
"1at1",
"1d09",
"1ekx",
"1ezz",
"1f1b",
"1i5o",
"1ml4",
"1nbe",
"1pg5",
"1q95",
"1r0b",
"1r0c",
"1raa",
"1rab",
"1rac",
"1rad",
"1rae",
"1raf",
"1rag",
"1rah",
"1rai",
"1sku",
"1tth",
"1tu0",
"1tug",
"1xjw",
"1za1",
"1za2",
"2a0f",
"2air",
"2at1"... | 117 | [
"PUB00000720",
"PUB00002421",
"PUB00070200"
] | [
"8098212",
"3015959",
"3722124"
] | [
"The evolutionary history of the first three enzymes in pyrimidine biosynthesis.",
"Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).",
"In vivo formation of hybrid aspartate transcarbamoylases from native subunits of divergent members of the family Enterobacteriaceae."
] | [
1993,
1986,
1986
] | 3 | [
"IPR006130"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
883,
23629,
4373,
5,
534
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
4,
3,
1,
3,
4,
1,
1,
5,
1,
1,
7
] | 13 | true | Family | Aspartate carbamoyltransferase | Aspartate carbamoyltransferase | Asp_carbamoyltransf | 2 |
IPR002083 | 2,083 | MATH/TRAF domain | MATH/TRAF_dom | Domain | 59,204 | false | false | Although apparently functionally unrelated, intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the meprin and TRAF homology (MATH) domain [ ]. Meprins are mammalian tissue-specific metalloendopeptidases of the astacin family implicated in developmental, normal and pathological... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00917",
"PF22486",
"PS50144",
"SM00061",
"cd00121"
] | [
"MATH",
"MATH_2",
"MATH",
"MATH",
"MATH"
] | [
2197,
41508,
53917,
37133,
30416
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50144",
"R-BTA-1257604",
"R-BTA-166058",
"R-BTA-193692",
"R-BTA-202424",
"R-BTA-205043",
"R-BTA-209543",
"R-BTA-209560",
"R-BTA-2871837",
"R-BTA-450302",
"R-BTA-450321",
"R-BTA-5607764",
"R-BTA-5632684",
"R-BTA-5689880",
"R-BTA-5689896",
"R-BTA-6811558",
"R-BTA-9020702",
"R-BT... | [
"PROSITEDOC:PDOC50144",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-166058",
"REACTOME:R-BTA-193692",
"REACTOME:R-BTA-202424",
"REACTOME:R-BTA-205043",
"REACTOME:R-BTA-209543",
"REACTOME:R-BTA-209560",
"REACTOME:R-BTA-2871837",
"REACTOME:R-BTA-450302",
"REACTOME:R-BTA-450321",
"REACTOME:R-BTA-56... | 243 | [
"1ca4",
"1ca9",
"1czy",
"1czz",
"1d00",
"1d01",
"1d0a",
"1d0j",
"1f3v",
"1flk",
"1fll",
"1kzz",
"1l0a",
"1lb4",
"1lb5",
"1lb6",
"1qsc",
"1rf3",
"1yy6",
"1yze",
"1zms",
"2cr2",
"2f1w",
"2f1x",
"2f1y",
"2f1z",
"2foj",
"2foo",
"2fop",
"2gkw",
"2xxn",
"3hqh"... | 102 | [
"PUB00011812",
"PUB00011813",
"PUB00011814",
"PUB00011815",
"PUB00011816",
"PUB00024776",
"PUB00024974",
"PUB00026885"
] | [
"12387856",
"7890660",
"8069916",
"10518213",
"10206649",
"10892748",
"10984535",
"12005438"
] | [
"The new MATH: homology suggests shared binding surfaces in meprin tetramers and TRAF trimers.",
"COOH-terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum.",
"A novel family o... | [
2002,
1995,
1994,
1999,
1999,
2000,
2000,
2002
] | 8 | [] | [
"IPR037299",
"IPR049342"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Megaviricetes",
"Methanobacteriota",
"metagenomes"
] | [
40,
59133,
22,
5,
4
] | 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... | [
449,
109,
47,
14,
46,
46,
1,
322,
68,
1,
2,
285
] | 12 | true | Domain | MATH/TRAF domain | MATH/TRAF domain | MATH/TRAF_dom | 4 |
IPR002084 | 2,084 | Methionine repressor MetJ | Met_repressor_MetJ | Family | 1,992 | false | false | Binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the Escherichia coli methionine repressor (MetJ) leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformatio... | [
"GO:0003700",
"GO:0006355",
"GO:0006555"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"methionine metabolic process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"CDD"
] | [
"MF_00744",
"PF01340",
"cd00490"
] | [
"MetJ",
"MetJ",
"Met_repressor_MetJ"
] | [
1387,
1992,
1316
] | 3 | [] | [] | [] | 0 | [
"1cma",
"1cmb",
"1cmc",
"1mj2",
"1mjk",
"1mjl",
"1mjm",
"1mjo",
"1mjp",
"1mjq"
] | 10 | [
"PUB00000028",
"PUB00006686",
"PUB00008039",
"PUB00013999",
"PUB00037197"
] | [
"8092669",
"8026581",
"1406951",
"1943695",
"10986458"
] | [
"The Met repressor-operator complex: DNA recognition by beta-strands.",
"Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system.",
"Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands.",... | [
1994,
1994,
1992,
1991,
2000
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
1984,
3,
5
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Methionine repressor MetJ | Methionine repressor MetJ | Met_repressor_MetJ | 4 |
IPR002087 | 2,087 | Anti-proliferative protein | Anti_prolifrtn | Domain | 7,301 | false | false | This entry represents a conserved domain found in the N-terminal of the BTG family members (also known as anti-proliferative proteins). In mammals, BTG family comprises six proteins: BTG1, BTG2/PC3/Tis21, BTG3/ANA, BTG4/PC3B, Tob1/Tob and Tob2. They regulate cell cycle progression in a variety of cell types [ ]. These ... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROSITE",
"SMART"
] | [
"PF07742",
"PR00310",
"PS00960",
"PS01203",
"SM00099"
] | [
"BTG",
"ANTIPRLFBTG1",
"BTG_1",
"BTG_2",
"btg1"
] | [
7300,
6518,
3497,
4959,
6865
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00742",
"R-DDI-6804115",
"R-HSA-6804115",
"R-HSA-9617828",
"R-HSA-9820841",
"R-MMU-6804115",
"R-RNO-6804115"
] | [
"PROSITEDOC:PDOC00742",
"REACTOME:R-DDI-6804115",
"REACTOME:R-HSA-6804115",
"REACTOME:R-HSA-9617828",
"REACTOME:R-HSA-9820841",
"REACTOME:R-MMU-6804115",
"REACTOME:R-RNO-6804115"
] | 7 | [
"2d5r",
"2z15",
"3djn",
"3dju",
"3e9v",
"5ci8",
"5ci9",
"5td6"
] | 8 | [
"PUB00078467"
] | [
"19746446"
] | [
"The mammalian anti-proliferative BTG/Tob protein family."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
7,
7294
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
15,
4,
16,
25,
23
] | 6 | true | Domain | Anti-proliferative protein | Anti-proliferative protein | Anti_prolifrtn | 5 |
IPR002088 | 2,088 | Protein prenyltransferase, alpha subunit | Prenyl_trans_a | Repeat | 13,091 | false | false | Protein prenylation is the posttranslational attachment of either a farnesyl group or a geranylgeranyl group via a thioether linkage (-C-S-C-) to a cysteine at or near the carboxyl terminus of the protein. Farnesyl and geranylgeranyl groups are polyisoprenes, unsaturated hydrocarbons with a multiple of five carbons; th... | [
"GO:0008318",
"GO:0018342"
] | [
"protein prenyltransferase activity",
"protein prenylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF01239",
"PS51147"
] | [
"PPTA",
"PFTA"
] | [
12856,
11847
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.5.1",
"PDOC00703",
"R-BTA-6803205",
"R-BTA-8873719",
"R-DDI-6803205",
"R-DDI-8873719",
"R-DDI-9648002",
"R-HSA-111465",
"R-HSA-2514859",
"R-HSA-6803205",
"R-HSA-8873719",
"R-HSA-9648002",
"R-HSA-9679191",
"R-MMU-111465",
"R-MMU-2514859",
"R-MMU-6803205",
"R-MMU-8873719",
"R-MMU-... | [
"EC:2.5.1",
"PROSITEDOC:PDOC00703",
"REACTOME:R-BTA-6803205",
"REACTOME:R-BTA-8873719",
"REACTOME:R-DDI-6803205",
"REACTOME:R-DDI-8873719",
"REACTOME:R-DDI-9648002",
"REACTOME:R-HSA-111465",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-6803205",
"REACTOME:R-HSA-8873719",
"REACTOME:R-HSA-9648002",... | 29 | [
"1d8d",
"1d8e",
"1dce",
"1fpp",
"1ft1",
"1ft2",
"1jcq",
"1jcr",
"1jcs",
"1kzo",
"1kzp",
"1ld7",
"1ld8",
"1ltx",
"1mzc",
"1n4p",
"1n4q",
"1n4r",
"1n4s",
"1n94",
"1n95",
"1n9a",
"1ni1",
"1nl4",
"1o1r",
"1o1s",
"1o1t",
"1o5m",
"1qbq",
"1s63",
"1s64",
"1sa4"... | 119 | [
"PUB00004327"
] | [
"1622936"
] | [
"Novel repetitive sequence motifs in the alpha and beta subunits of prenyl-protein transferases and homology of the alpha subunit to the MAD2 gene product of yeast."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
37,
139,
12906,
9
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
26,
2,
5,
3,
15,
8,
3,
11,
13,
2,
2,
32
] | 12 | true | Repeat | Protein prenyltransferase, alpha subunit | Protein prenyltransferase, alpha subunit | Prenyl_trans_a | 9 |
IPR002089 | 2,089 | Influenza virus matrix protein 2 | Flu_M2 | Family | 64,325 | false | false | This entry contains Influenza virus matrix protein 2. It is an integral membrane protein that is expressed on the infected cell surface and incorporated into virions where it is a minor component. The protein spans the viral membrane with an extracellular amino-terminus and a cytoplasmic carboxy-terminus. The transmemb... | [
"GO:0015078",
"GO:1902600",
"GO:0033644",
"GO:0055036"
] | [
"proton transmembrane transporter activity",
"proton transmembrane transport",
"host cell membrane",
"virion membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"PFAM"
] | [
"MF_04069",
"PF00599"
] | [
"INFV_M2",
"Flu_M2"
] | [
58738,
64325
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1012",
"R-HSA-168255",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168336",
"R-HSA-168874",
"R-HSA-192823"
] | [
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-168874",
"REACTOME:R-HSA-192823"
] | 11 | [
"1mp6",
"1nyj",
"2kad",
"2kih",
"2kqt",
"2kwx",
"2l0j",
"2ljb",
"2ljc",
"2ly0",
"2muv",
"2muw",
"2n70",
"2rlf",
"3bkd",
"3c9j",
"3lbw",
"4n8c",
"4qk7",
"4qkc",
"4qkl",
"4qkm",
"4rwb",
"4rwc",
"5c02",
"5dlm",
"5joo",
"5ttc",
"5um1",
"6bkk",
"6bkl",
"6bmz"... | 45 | [
"PUB00006276",
"PUB00006389"
] | [
"1374685",
"9360376"
] | [
"Influenza virus M2 protein has ion channel activity.",
"[Structure and function of the influenza virus M2 ion channel protein]"
] | [
1992,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Orthomyxoviridae"
] | [
5,
64320
] | 2 | [] | [] | 0 | true | Family | Influenza virus matrix protein 2 | Influenza virus matrix protein 2 | Flu_M2 | 9 |
IPR002090 | 2,090 | Sodium/hydrogen exchanger 6/7/9 | NHE-6/7/9 | Family | 5,210 | false | false | Sodium proton exchangers (NHEs) constitute a large family of integral membrane protein transporters that are responsible for the counter-transport of protons and sodium ions across lipid bilayers [ , ]. These proteins are found in organisms across all domains of life. In archaea, bacteria, yeast and plants, these excha... | [
"GO:0015385",
"GO:0006814",
"GO:0006885",
"GO:0016020"
] | [
"sodium:proton antiporter activity",
"sodium ion transport",
"regulation of pH",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01088"
] | [
"NAHEXCHNGR6"
] | [
5210
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-425986",
"R-HSA-5619052",
"R-HSA-5619092",
"R-MMU-425986",
"R-RNO-425986"
] | [
"REACTOME:R-HSA-425986",
"REACTOME:R-HSA-5619052",
"REACTOME:R-HSA-5619092",
"REACTOME:R-MMU-425986",
"REACTOME:R-RNO-425986"
] | 5 | [
"6z3y",
"6z3z",
"8pvr",
"8pxb"
] | 4 | [
"PUB00001715",
"PUB00002996",
"PUB00003039",
"PUB00044828",
"PUB00044829",
"PUB00044830",
"PUB00044831",
"PUB00044832",
"PUB00044833",
"PUB00044834",
"PUB00070284",
"PUB00093743",
"PUB00100486",
"PUB00100487"
] | [
"9537504",
"9278382",
"9507001",
"12027219",
"12502567",
"16734752",
"17071327",
"16513813",
"11187762",
"17218973",
"15522866",
"11279194",
"32277048",
"30335141"
] | [
"Comparative molecular analysis of Na+/H+ exchangers: a unified model for Na+/H+ antiport?",
"Na+/H+ exchangers of mammalian cells.",
"Identification of a mitochondrial Na+/H+ exchanger.",
"The Na+/H+ exchanger gene family.",
"Multiple modes of regulation of Na+/H+ exchangers.",
"Na+/H+ exchangers and the... | [
1998,
1997,
1998,
2002,
2002,
2006,
2006,
2006,
2000,
2006,
2005,
2001,
2020,
2019
] | 14 | [
"IPR004709"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
5210
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
8,
7,
16,
9,
9
] | 6 | true | Family | Sodium/hydrogen exchanger 6/7/9 | Sodium/hydrogen exchanger 6/7/9 | NHE-6/7/9 | 3 |
IPR002093 | 2,093 | BRCA2 repeat | BRCA2_repeat | Repeat | 3,549 | false | false | The breast cancer type 2 susceptibility protein has a number of 39 amino acid repeats [ ] that are critical for binding to RAD51 (a key protein in DNA recombinational repair) and resistance to methyl methanesulphonate treatment [ , , ]. BRCA2 is a breast tumour suppressor with a potential function in the cellular respo... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00634",
"PS50138"
] | [
"BRCA2",
"BRCA2_REPEAT"
] | [
3244,
3439
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50138",
"R-HSA-5685939",
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"R-HSA-5693579",
"R-HSA-5693616",
"R-HSA-912446",
"R-HSA-9701192",
"R-HSA-9704331",
"R-HSA-9704646",
"R-HSA-9709275",
"R-HSA-9709570",
"R-HSA-9709603",
"R-HSA-9763198",
"R-MMU-5685939",
"R-MMU-5685942",
... | [
"PROSITEDOC:PDOC50138",
"REACTOME:R-HSA-5685939",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693579",
"REACTOME:R-HSA-5693616",
"REACTOME:R-HSA-912446",
"REACTOME:R-HSA-9701192",
"REACTOME:R-HSA-9704331",
"REACTOME:R-HSA-9704646",
"REACTOME:R... | 25 | [
"1n0w",
"6hqu",
"7qv8",
"8br9",
"8c3j",
"8c3n",
"8uvw"
] | 7 | [
"PUB00003901",
"PUB00005803",
"PUB00005815",
"PUB00005834",
"PUB00007172"
] | [
"8673099",
"9405383",
"9560268",
"9811893",
"10551859"
] | [
"Internal repeats in the BRCA2 protein sequence.",
"RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2.",
"The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment.",
"The BRCA2 gene product funct... | [
1996,
1997,
1998,
1998,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"bioreactor metagenome"
] | [
35,
3510,
3,
1
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
14,
3,
1,
102,
2,
5,
6,
30
] | 8 | true | Repeat | BRCA2 repeat | BRCA2 repeat | BRCA2_repeat | 8 |
IPR002095 | 2,095 | Monellin, B chain | Monellin_B | Family | 1 | false | false | Monellin is an intensely sweet-tasting protein derived from Dioscoreophyllum cumminsii (Serendipity berry). The protein has a very high specificity for the sweet receptors, making it ~100,000 times sweeter than sugar on a molar basis and several thousand times sweeter on a weight basis [ ]. Like the sweet-tasting prote... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00631"
] | [
"MONELLINB"
] | [
1
] | 1 | [] | [] | [] | 0 | [
"1fa3",
"1fuw",
"1iv7",
"1iv9",
"1krl",
"1m9g",
"1mnl",
"1mol",
"2o9u",
"2q33",
"3mon",
"3pxm",
"3pyj",
"3q2p",
"4mon",
"5lc6",
"5lc7",
"5o7k",
"5o7l",
"5o7q",
"5o7r",
"5o7s",
"5xfu",
"5yct",
"5ycu",
"5ycw",
"5z1p",
"6l44",
"6l4i",
"6l4j",
"6l4n",
"6lay"... | 49 | [
"PUB00000017",
"PUB00000577",
"PUB00004005"
] | [
"1368575",
"4107",
"3614382"
] | [
"Complete amino acid sequence of the sweet protein monellin.",
"The structure of monellin and its relation to the sweetness of the protein.",
"Crystal structure of the intensely sweet protein monellin."
] | [
1990,
1976,
1987
] | 3 | [
"IPR015283"
] | [] | 1 | 0 | 1 | [
"Dioscoreophyllum cumminsii"
] | [
1
] | 1 | [] | [] | 0 | true | Family | Monellin, B chain | Monellin, B chain | Monellin_B | 3 |
IPR002098 | 2,098 | Seminal vesicle protein I | SVP_I | Repeat | 99 | false | false | Seminal vesicle protein I (SVP-1) is one of the four major secretory proteins secreted by Cavia porcellus (Guinea pig) seminal vesicle epithelium. It is a clotting protein that serves as the substrate in the formation of the copulatory plug. Covalent clotting of this protein is catalyzed by a transglutaminase and invol... | [
"GO:0007620",
"GO:0005576"
] | [
"copulation",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PROSITE"
] | [
"PS00313"
] | [
"SVP_I"
] | [
99
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC00282",
"R-HSA-6803157",
"R-HSA-6809371"
] | [
"PROSITEDOC:PDOC00282",
"REACTOME:R-HSA-6803157",
"REACTOME:R-HSA-6809371"
] | 3 | [] | 0 | [
"PUB00004644"
] | [
"3477802"
] | [
"The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain."
] | [
1987
] | 1 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
99
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Repeat | Seminal vesicle protein I | Seminal vesicle protein I | SVP_I | 8 |
IPR002101 | 2,101 | Myristoylated alanine-rich C-kinase substrate MARCKS | MARCKS | Family | 1,496 | false | false | Myristoylated alanine-rich C-kinase substrate (MARCKS) is a predominent cellular substrate for protein kinase C (PKC) that has been implicated in the regulation of brain development, macrophage activation, neuro-secretion and growth factor-dependent mitogenesis [ , ]. The N-terminal glycine is the site of myristoylatio... | [
"GO:0005516"
] | [
"calmodulin binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PF02063",
"PR00963",
"PS00826",
"PS00827",
"PTHR14353"
] | [
"MARCKS",
"MARCKS",
"MARCKS_1",
"MARCKS_2",
""
] | [
1449,
1421,
980,
524,
1473
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00649",
"R-HSA-399997",
"R-MMU-399997",
"R-RNO-399997"
] | [
"PROSITEDOC:PDOC00649",
"REACTOME:R-HSA-399997",
"REACTOME:R-MMU-399997",
"REACTOME:R-RNO-399997"
] | 4 | [
"1iwq",
"9ndp"
] | 2 | [
"PUB00001618",
"PUB00002789",
"PUB00004094",
"PUB00004119",
"PUB00007173"
] | [
"1864362",
"8420923",
"2034276",
"1560845",
"11829734"
] | [
"A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS.",
"The MARCKS family of cellular protein kinase C substrates.",
"Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.",
... | [
1991,
1993,
1991,
1992,
2002
] | 5 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Pseudomonadota"
] | [
1494,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
4,
6
] | 4 | true | Family | Myristoylated alanine-rich C-kinase substrate MARCKS | Myristoylated alanine-rich C-kinase substrate MARCKS | MARCKS | 8 |
IPR002102 | 2,102 | Cellulosome anchoring protein, cohesin domain | Cohesin_dom | Domain | 4,274 | false | false | Cohesin domains interact with a complementary domain, termed the dockerin domain (see ). The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome [ ]. The scaffoldin component of the cellulolytic bacterium Clostridium thermocellum is a non-hydrolytic protein which organises t... | [
"GO:0030246",
"GO:0000272"
] | [
"carbohydrate binding",
"polysaccharide catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00963"
] | [
"Cohesin"
] | [
4274
] | 1 | [
"GP"
] | [
"GenProp0944"
] | [
"GP:GenProp0944"
] | 1 | [
"1anu",
"1aoh",
"1g1k",
"1ohz",
"1qzn",
"1tyj",
"1zv9",
"2b59",
"2bm3",
"2ccl",
"2jh2",
"2o4e",
"2ozn",
"2vn5",
"2vn6",
"2vo8",
"2w1n",
"2xdh",
"2y3n",
"3bwz",
"3f2l",
"3fnk",
"3ghp",
"3kcp",
"3l8q",
"3ul4",
"4dh2",
"4fl4",
"4u3s",
"4ums",
"4uyp",
"4uyq"... | 47 | [
"PUB00005288"
] | [
"9083107"
] | [
"A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
362,
3787,
2,
22,
101
] | 5 | [] | [] | 0 | true | Domain | Cellulosome anchoring protein, cohesin domain | Cellulosome anchoring protein, cohesin domain | Cohesin_dom | 8 |
IPR002104 | 2,104 | Integrase, catalytic domain | Integrase_catalytic | Domain | 279,825 | false | false | Phage integrase proteins cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment [ , ]. The catalytic site residues in CRE recombinase ( ) are Arg-173, His-289, Arg-292 and Tyr-324. | [
"GO:0003677",
"GO:0006310",
"GO:0015074"
] | [
"DNA binding",
"DNA recombination",
"DNA integration"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF00589",
"PS51898"
] | [
"Phage_integrase",
"TYR_RECOMBINASE"
] | [
265496,
270475
] | 2 | [] | [] | [] | 0 | [
"1a0p",
"1ae9",
"1aih",
"1crx",
"1drg",
"1f44",
"1kbu",
"1ma7",
"1nzb",
"1ouq",
"1p7d",
"1pvp",
"1pvq",
"1pvr",
"1q3u",
"1q3v",
"1xns",
"1xo0",
"1z19",
"1z1b",
"1z1g",
"2a3v",
"2crx",
"2hof",
"2hoi",
"3c28",
"3c29",
"3crx",
"3mgv",
"3nkh",
"3uxu",
"3vcf"... | 54 | [
"PUB00004261",
"PUB00005224"
] | [
"9288963",
"9082984"
] | [
"Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse.",
"Flexibility in DNA recombination: structure of the lambda integrase catalytic core."
] | [
1997,
1997
] | 2 | [] | [
"IPR042721"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"other sequences",
"unclassified sequences"
] | [
4846,
261019,
5737,
2894,
8,
5321
] | 6 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
7,
15,
1
] | 3 | true | Domain | Integrase, catalytic domain | Integrase, catalytic domain | Integrase_catalytic | 3 |
IPR002105 | 2,105 | Dockerin type I repeat | Dockerin_1_rpt | Repeat | 9,178 | false | false | Gram-positive, thermophilic anaerobes such as Clostridium thermocellum or Clostridium cellulolyticum secretes a highly active and thermostable cellulase complex (cellulosome) responsible for the degradation of crystalline cellulose [ , ]. The cellulosome contains at least 30 polypeptides, the majority of the enzymes ar... | [
"GO:0004553",
"GO:0000272"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"polysaccharide catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE"
] | [
"PF00404",
"PS00448"
] | [
"Dockerin_1",
"CLOS_CELLULOSOME_RPT"
] | [
8913,
1283
] | 2 | [
"EC",
"GP",
"PROSITEDOC"
] | [
"3.2.1",
"GenProp0944",
"PDOC00416"
] | [
"EC:3.2.1",
"GP:GenProp0944",
"PROSITEDOC:PDOC00416"
] | 3 | [
"1clc",
"1daq",
"1dav",
"1ohz",
"2b59",
"2ccl",
"2jnk",
"2mte",
"2ozn",
"2vn5",
"2vn6",
"2y3n",
"2yik",
"3kcp",
"3ul4",
"4cj0",
"4cj1",
"4dh2",
"4fl4",
"4u3s",
"4uyp",
"4uyq",
"4wi0",
"5g5d",
"5k39",
"5lxv",
"5m0y",
"5m2o",
"5m2s",
"5nrk",
"5nrm",
"6kg9"... | 42 | [
"PUB00000117",
"PUB00001731",
"PUB00005535"
] | [
"2252383",
"1478480",
"10390637"
] | [
"Molecular biology of cellulose degradation.",
"Cellulose degradation by Clostridium thermocellum: from manure to molecular biology.",
"The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides."
] | [
1990,
1992,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
596,
8134,
6,
87,
355
] | 5 | [] | [] | 0 | true | Repeat | Dockerin type I repeat | Dockerin type I repeat | Dockerin_1_rpt | 2 |
IPR002107 | 2,107 | Rotavirus non-structural protein 4 | Rotavirus_NSP4 | Family | 4,075 | false | false | This entry contains rotaviral non-structural protein 4 (NSP4) as well as related proteins: NSP5, NS28, and NCVP5. The final steps in the assembly of rotavirus occur in the lumen of the endoplasmic reticulum (ER). Targeting of the immature inner capsid particle (ICP) to this compartment is mediated by the cytoplasmic ta... | [] | [] | [] | 0 | [
"HAMAP",
"PFAM"
] | [
"MF_04091",
"PF01452"
] | [
"ROTA_NSP4",
"Rota_NSP4"
] | [
3836,
3996
] | 2 | [] | [] | [] | 0 | [
"1g1i",
"1g1j",
"2o1j",
"2o1k",
"3miw",
"4wb4",
"4wba",
"5y2e",
"5y2h",
"5y2j",
"5y9r"
] | 11 | [
"PUB00001166",
"PUB00001292"
] | [
"2548854",
"8887538"
] | [
"Topology of the non-structural rotavirus receptor glycoprotein NS28 in the rough endoplasmic reticulum.",
"The cytoplasmic tail of NSP4, the endoplasmic reticulum-localized non-structural glycoprotein of rotavirus, contains distinct virus binding and coiled coil domains."
] | [
1989,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Rotavirus"
] | [
4075
] | 1 | [] | [] | 0 | true | Family | Rotavirus non-structural protein 4 | Rotavirus non-structural protein 4 | Rotavirus_NSP4 | 1 |
IPR002108 | 2,108 | Actin-depolymerising factor homology domain | ADF-H | Domain | 30,910 | false | false | The actin-depolymerising factor homology (ADF-H) domain is an ~150-amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins [ , , ]: ADF/cofilins, which include ADF, cofilin, destrin, actophorin, coactosin, depactin and glia maturation factors (GMFs) beta and gamm... | [
"GO:0003779"
] | [
"actin binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00241",
"PS51263",
"SM00102"
] | [
"Cofilin_ADF",
"ADF_H",
"ADF"
] | [
30661,
30193,
28052
] | 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-6798695",
"R-DDI-6798695",
"R-DDI-9013418",
"R-DME-6798695",
"R-DME-9013418",
"R-HSA-114608",
"R-HSA-2029482",
"R-HSA-264870",
"R-HSA-3928662",
"R-HSA-399954",
"R-HSA-5627117",
"R-HSA-6794361",
"R-HSA-6798695",
"R-HSA-8950505",
"R-HSA-9013405",
"R-HSA-9013407",
"R-HSA-9013418"... | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-9013418",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-9013418",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-264870",
"REACTOME:R-HSA-3928662",
"REACTOME:R-HSA-399954",
"REACTOME:R-HSA-5627117",
"REACTOME:R... | 27 | [
"1ahq",
"1ak6",
"1ak7",
"1cfy",
"1cnu",
"1cof",
"1f7s",
"1hqz",
"1m4j",
"1q8g",
"1q8x",
"1qpv",
"1t2l",
"1t3x",
"1t3y",
"1tmw",
"1tvj",
"1udm",
"1v6f",
"1vfq",
"1vkk",
"1wfs",
"1wm4",
"1wnj",
"1x67",
"2d8b",
"2hd7",
"2i2q",
"2kvk",
"2l72",
"2lj8",
"2lxx"... | 79 | [
"PUB00022142",
"PUB00031293",
"PUB00043718",
"PUB00043719"
] | [
"12207032",
"15522287",
"9693358",
"9047337"
] | [
"Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin.",
"Crystal structure of human coactosin-like protein.",
"The ADF homology (ADF-H) domain: a highly exploited actin-binding module.",
"Structure and expression of a novel filarial gene f... | [
2002,
2004,
1998,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2,
80,
30826,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
44,
4,
26,
11,
50,
31,
5,
21,
47,
4,
4,
69
] | 12 | true | Domain | Actin-depolymerising factor homology domain | Actin-depolymerising factor homology domain | ADF-H | 8 |
IPR002109 | 2,109 | Glutaredoxin | Glutaredoxin | Domain | 89,899 | false | false | This entry represents Glutaredoxin. Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these component... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00462"
] | [
"Glutaredoxin"
] | [
89899
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-1362409",
"R-HSA-1362409",
"R-HSA-1989781",
"R-HSA-2408550",
"R-HSA-3299685",
"R-HSA-499943",
"R-HSA-5263617",
"R-HSA-5336415",
"R-HSA-5628897",
"R-HSA-917937",
"R-HSA-9662360",
"R-HSA-9662361",
"R-HSA-9818027",
"R-MMU-1362409",
"R-MMU-499943",
"R-RNO-499943",
"R-SCE-1362409",... | [
"REACTOME:R-DDI-1362409",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-2408550",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-499943",
"REACTOME:R-HSA-5263617",
"REACTOME:R-HSA-5336415",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-917937",
"REACTOME:R-HSA-9662360",
"REACTOME:... | 19 | [
"1aaz",
"1aba",
"1b4q",
"1de1",
"1de2",
"1ego",
"1egr",
"1fov",
"1grx",
"1h75",
"1jhb",
"1kte",
"1nm3",
"1qfn",
"1r7h",
"1wik",
"1yka",
"1z7p",
"1z7r",
"2cq9",
"2e7p",
"2fls",
"2ht9",
"2hze",
"2hzf",
"2jac",
"2jad",
"2khp",
"2klx",
"2lku",
"2lqo",
"2lqq"... | 173 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005
] | 10 | [] | [
"IPR014025",
"IPR033658"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
900,
44315,
42216,
1537,
931
] | 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",... | [
153,
13,
13,
9,
4,
13,
21,
4,
76,
20,
8,
5,
180
] | 13 | true | Domain | Glutaredoxin | Glutaredoxin | Glutaredoxin | 9 |
IPR002110 | 2,110 | Ankyrin repeat | Ankyrin_rpt | Repeat | 716,687 | false | false | The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00023",
"PF12796",
"PF13606",
"PF13637",
"PF13857",
"PR01415",
"PS50088",
"SM00248"
] | [
"Ank",
"Ank_2",
"Ank_3",
"Ank_4",
"Ank_5",
"ANKYRIN",
"ANK_REPEAT",
"ANK"
] | [
242961,
630699,
9518,
96256,
26537,
212697,
653130,
663672
] | 8 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50088",
"R-BTA-114508",
"R-BTA-139853",
"R-BTA-2151201",
"R-BTA-2559580",
"R-BTA-2559582",
"R-BTA-2559585",
"R-BTA-3295583",
"R-BTA-446343",
"R-BTA-446353",
"R-BTA-6798695",
"R-BTA-69231",
"R-BTA-8951664",
"R-BTA-983168",
"R-CEL-114508",
"R-CEL-139853",
"R-CEL-1912420",
"R-CEL... | [
"PROSITEDOC:PDOC50088",
"REACTOME:R-BTA-114508",
"REACTOME:R-BTA-139853",
"REACTOME:R-BTA-2151201",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559582",
"REACTOME:R-BTA-2559585",
"REACTOME:R-BTA-3295583",
"REACTOME:R-BTA-446343",
"REACTOME:R-BTA-446353",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BT... | 513 | [
"1ap7",
"1awc",
"1bd8",
"1bi7",
"1bi8",
"1blx",
"1bu9",
"1d9s",
"1dcq",
"1g3n",
"1ihb",
"1ikn",
"1ixv",
"1k1a",
"1k1b",
"1k3z",
"1mj0",
"1mx2",
"1mx4",
"1mx6",
"1myo",
"1n0q",
"1n0r",
"1n11",
"1nfi",
"1ot8",
"1oy3",
"1qym",
"1s70",
"1svx",
"1sw6",
"1tr4"... | 1,068 | [
"PUB00006219",
"PUB00006220",
"PUB00006221",
"PUB00006222",
"PUB00006223",
"PUB00009776",
"PUB00094371",
"PUB00094372"
] | [
"8108379",
"8875926",
"9353127",
"9461436",
"9865693",
"12461176",
"31000436",
"29769718"
] | [
"Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?",
"Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.",
"Structure of the cyclin-dependent kinase inhibitor p19Ink4d.",
"The structure of GABPalpha/beta: an ETS d... | [
1993,
1996,
1997,
1998,
1998,
2002,
2019,
2018
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
169,
43716,
665428,
5839,
1535
] | 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",... | [
684,
146,
1601,
301,
3,
1079,
771,
54,
580,
969,
18,
14,
694
] | 13 | true | Repeat | Ankyrin repeat | Ankyrin repeat | Ankyrin_rpt | 9 |
IPR002112 | 2,112 | Transcription factor Jun | Leuzip_Jun | Family | 5,900 | false | false | The transcription factor activator protein (AP)-1 consists of Jun (c-Jun, JunB, and JunD), Fos (c-Fos, FosB, Fra1, and Fra2), ATF (ATFa, ATF-2 and ATF-3) and JDP (JDP-1 and JDP-2) family members [ ]. They are basic leucine zipper transcription factors that play a central role in regulating gene transcription in various... | [
"GO:0003677",
"GO:0003700",
"GO:0006355"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS"
] | [
"PR00043"
] | [
"LEUZIPPRJUN"
] | [
5900
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CEL-2559580",
"R-CEL-2871796",
"R-CEL-450341",
"R-DME-209394",
"R-DME-209409",
"R-DME-209425",
"R-DME-2559580",
"R-DME-2871796",
"R-DME-450341",
"R-DME-9018519",
"R-GGA-437986",
"R-HSA-1912408",
"R-HSA-2173796",
"R-HSA-2559580",
"R-HSA-2559582",
"R-HSA-2871796",
"R-HSA-450341",
... | [
"REACTOME:R-CEL-2559580",
"REACTOME:R-CEL-2871796",
"REACTOME:R-CEL-450341",
"REACTOME:R-DME-209394",
"REACTOME:R-DME-209409",
"REACTOME:R-DME-209425",
"REACTOME:R-DME-2559580",
"REACTOME:R-DME-2871796",
"REACTOME:R-DME-450341",
"REACTOME:R-DME-9018519",
"REACTOME:R-GGA-437986",
"REACTOME:R-HS... | 37 | [
"1a02",
"1fos",
"1jnm",
"1jun",
"1s9k",
"1t2k",
"2h7h",
"5fv8",
"5t01",
"5vpa",
"5vpb",
"5vpc",
"5vpd",
"5vpe",
"5vpf",
"6v7y",
"6v7z",
"6v80",
"7ucc",
"7ucd",
"8sgb",
"8sos"
] | 22 | [
"PUB00071041",
"PUB00071073",
"PUB00071074"
] | [
"12424143",
"23787991",
"15564374"
] | [
"Role and regulation of activator protein-1 in toxicant-induced responses of the lung.",
"Specificity through cooperation: BATF-IRF interactions control immune-regulatory networks.",
"AP-1 subunits: quarrel and harmony among siblings."
] | [
2002,
2013,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Kangiella spongicola",
"Viruses",
"bird metagenome"
] | [
5892,
3,
4,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
5,
9,
2,
8,
11,
7,
2
] | 7 | true | Family | Transcription factor Jun | Transcription factor Jun | Leuzip_Jun | 8 |
IPR002113 | 2,113 | ADP/ATP carrier protein, eukaryotic type | ADT_euk_type | Family | 14,859 | false | false | This family contains proteins found in eukaryotes. A variety of substrate carrier proteins that are involved in energy transfer are found in the inner mitochondrial membrane [ , , , , ]. Such proteins include: ADP,ATP carrier protein (ADP/ATP translocase); 2-oxoglutarate/malate carrier protein; phosphate carrier protei... | [
"GO:0005471",
"GO:0140021",
"GO:1990544",
"GO:0005743"
] | [
"ATP:ADP antiporter activity",
"mitochondrial ADP transmembrane transport",
"mitochondrial ATP transmembrane transport",
"mitochondrial inner membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"PANTHER"
] | [
"PR00927",
"PTHR45635"
] | [
"ADPTRNSLCASE",
""
] | [
13289,
14067
] | 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-1268020",
"R-BTA-166187",
"R-BTA-83936",
"R-BTA-9837999",
"R-CEL-200425",
"R-DDI-1268020",
"R-DDI-166187",
"R-DDI-83936",
"R-DDI-9837999",
"R-DME-1268020",
"R-DME-166187",
"R-DME-83936",
"R-DME-9837999",
"R-HSA-1268020",
"R-HSA-166187",
"R-HSA-168277",
"R-HSA-180897",
"R-HSA... | [
"REACTOME:R-BTA-1268020",
"REACTOME:R-BTA-166187",
"REACTOME:R-BTA-83936",
"REACTOME:R-BTA-9837999",
"REACTOME:R-CEL-200425",
"REACTOME:R-DDI-1268020",
"REACTOME:R-DDI-166187",
"REACTOME:R-DDI-83936",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-1268020",
"REACTOME:R-DME-166187",
"REACTOME:R-DME-... | 36 | [
"1okc",
"2c3e",
"4c9g",
"4c9h",
"4c9j",
"4c9q",
"6gci"
] | 7 | [
"PUB00001005",
"PUB00003243",
"PUB00003301",
"PUB00005084",
"PUB00005351",
"PUB00094737",
"PUB00097195"
] | [
"8325039",
"2541251",
"8487299",
"8140286",
"2158156",
"27693233",
"30611538"
] | [
"The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.",
"DNA sequences of two expressed nuclear genes for human mitochondrial ADP/ATP translocase.",
"Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine... | [
1993,
1989,
1993,
1993,
1990,
2016,
2019
] | 7 | [
"IPR002067"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
7,
14852
] | 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... | [
20,
10,
7,
4,
14,
6,
2,
10,
13,
5,
1,
26
] | 12 | true | Family | ADP/ATP carrier protein, eukaryotic type | ADP/ATP carrier protein, eukaryotic type | ADT_euk_type | 2 |
IPR002114 | 2,114 | Phosphotransferase system, HPr serine phosphorylation site | PTS_HPr_Ser_P_site | PTM | 14,599 | false | false | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl gro... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00589"
] | [
"PTS_HPR_SER"
] | [
14599
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00318"
] | [
"PROSITEDOC:PDOC00318"
] | 1 | [
"1cm2",
"1cm3",
"1fu0",
"1ggr",
"1hdn",
"1j6t",
"1jem",
"1k1c",
"1ka5",
"1kkl",
"1kkm",
"1mo1",
"1mu4",
"1pch",
"1pfh",
"1poh",
"1ptf",
"1qfr",
"1qr5",
"1rzr",
"1txe",
"1vrc",
"1y4y",
"1y50",
"1y51",
"1zvv",
"2ak7",
"2fep",
"2hid",
"2hpr",
"2jel",
"2lrk"... | 56 | [
"PUB00000073",
"PUB00003612"
] | [
"2197982",
"8246840"
] | [
"The bacterial phosphoenolpyruvate: glycose phosphotransferase system.",
"Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria."
] | [
1990,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
14457,
46,
9,
87
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | PTM | Phosphotransferase system, HPr serine phosphorylation site | Phosphotransferase system, HPr serine phosphorylation site | PTS_HPr_Ser_P_site | 2 |
IPR002116 | 2,116 | Melittin/ Api allergen | Melittin/Api_allergen | Family | 25 | false | false | Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS All... | [
"GO:0004860",
"GO:0005576"
] | [
"protein kinase inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF01372"
] | [
"Melittin"
] | [
25
] | 1 | [] | [] | [] | 0 | [
"1bh1",
"2k98",
"2l36",
"2mlt",
"2mw6",
"3qrx",
"6dst",
"6o4m",
"8ahs",
"8aht"
] | 10 | [
"PUB00006248",
"PUB00006570",
"PUB00006574"
] | [
"2187536",
"10072885",
"10692322"
] | [
"The actions of melittin on membranes.",
"Effect of melittin on ion transport across cell membranes.",
"Protein-induced membrane disorder: a molecular dynamics study of melittin in a dipalmitoylphosphatidylcholine bilayer."
] | [
1990,
1997,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Pseudomonadota"
] | [
22,
3
] | 2 | [] | [] | 0 | true | Family | Melittin/ Api allergen | Melittin/ Api allergen | Melittin/Api_allergen | 4 |
IPR002117 | 2,117 | p53 tumour suppressor family | p53_tumour_suppressor | Family | 6,348 | false | false | This entry also includes the p53 family members p63 [ ], p73 [ ] and transcription factor cep-1 [ ]. The p53 tumour suppressor [ , , , , ] is a protein found in increased amounts in a wide variety of transformed cells. It is also detectable in many proliferating non-transformed cells, but it is undetectable or present ... | [
"GO:0003677",
"GO:0003700",
"GO:0006355",
"GO:0006915",
"GO:0005634"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription",
"apoptotic process",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS",
"PANTHER"
] | [
"PR00386",
"PTHR11447"
] | [
"P53SUPPRESSR",
""
] | [
5870,
6338
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00301",
"R-BTA-2559580",
"R-BTA-2559586",
"R-BTA-349425",
"R-BTA-5689880",
"R-BTA-5689896",
"R-BTA-5693565",
"R-BTA-6804754",
"R-BTA-6804756",
"R-BTA-6804757",
"R-BTA-6804758",
"R-BTA-6804759",
"R-BTA-6804760",
"R-BTA-6811555",
"R-BTA-69473",
"R-BTA-69481",
"R-BTA-69541",
"R-B... | [
"PROSITEDOC:PDOC00301",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-349425",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-5689896",
"REACTOME:R-BTA-5693565",
"REACTOME:R-BTA-6804754",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6804757",
"REACTOME:R-BTA-6804758",
"REACTOME:R... | 151 | [
"1cok",
"1dxs",
"1gzh",
"1hu8",
"1kzy",
"1rg6",
"1tsr",
"1tup",
"1uol",
"1ycs",
"2ac0",
"2ady",
"2ahi",
"2ata",
"2bim",
"2bin",
"2bio",
"2bip",
"2biq",
"2fej",
"2geq",
"2h1l",
"2ioi",
"2iom",
"2ioo",
"2j1w",
"2j1x",
"2j1y",
"2j1z",
"2j20",
"2j21",
"2kby"... | 239 | [
"PUB00000596",
"PUB00001893",
"PUB00002729",
"PUB00003921",
"PUB00004096",
"PUB00004490",
"PUB00005186",
"PUB00059264",
"PUB00059265",
"PUB00059266"
] | [
"2142001",
"2137806",
"1639769",
"7796267",
"2046748",
"2142762",
"8023159",
"9315105",
"11932750",
"11696333"
] | [
"Tumor suppressor genes: the p53 and retinoblastoma sensitivity genes and gene products.",
"p53: oncogene or anti-oncogene?",
"The p53 tumor suppressor protein, a modulator of cell proliferation.",
"Refined solution structure of the oligomerization domain of the tumour suppressor p53.",
"The p53 tumour supp... | [
1990,
1990,
1992,
1995,
1991,
1990,
1994,
1997,
2002,
2001
] | 10 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
6347,
1
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
69,
6,
168,
29,
20
] | 5 | true | Family | p53 tumour suppressor family | p53 tumour suppressor family | p53_tumour_suppressor | 5 |
IPR002119 | 2,119 | Histone H2A | Histone_H2A | Family | 34,209 | false | false | Histone H2A is a small, highly conserved nuclear protein that, together with two molecules each of histones H2B, H3 and H4, forms the eukaryotic nucleosome core [ ]; the nucleosome octamer winds ~146 DNA base-pairs. In the mouse, histone H2A can be replaced by histone H2A-like 1 [ ]. | [
"GO:0003677",
"GO:0030527",
"GO:0000786"
] | [
"DNA binding",
"structural constituent of chromatin",
"nucleosome"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PRINTS",
"PANTHER",
"SMART"
] | [
"PR00620",
"PTHR23430",
"SM00414"
] | [
"HISTONEH2A",
"",
"H2A"
] | [
32839,
32113,
33125
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00045",
"R-BTA-110330",
"R-BTA-110331",
"R-BTA-171306",
"R-BTA-201722",
"R-BTA-212300",
"R-BTA-2299718",
"R-BTA-2559580",
"R-BTA-2559582",
"R-BTA-2559586",
"R-BTA-3214815",
"R-BTA-3214847",
"R-BTA-3214858",
"R-BTA-427359",
"R-BTA-427413",
"R-BTA-5250924",
"R-BTA-5578749",
"R-B... | [
"PROSITEDOC:PDOC00045",
"REACTOME:R-BTA-110330",
"REACTOME:R-BTA-110331",
"REACTOME:R-BTA-171306",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-2299718",
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2559582",
"REACTOME:R-BTA-2559586",
"REACTOME:R-BTA-3214815",
"REACTOME:R-BTA... | 255 | [
"1aoi",
"1eqz",
"1f66",
"1hio",
"1hq3",
"1id3",
"1kx3",
"1kx4",
"1kx5",
"1m18",
"1m19",
"1m1a",
"1p34",
"1p3a",
"1p3b",
"1p3f",
"1p3g",
"1p3i",
"1p3k",
"1p3l",
"1p3m",
"1p3o",
"1p3p",
"1q9c",
"1s32",
"1tzy",
"1u35",
"1zbb",
"1zla",
"2aro",
"2cv5",
"2f8n"... | 967 | [
"PUB00004448",
"PUB00085658"
] | [
"8121801",
"17261847"
] | [
"Phylogenetic analysis of the core histones H2A, H2B, H3, and H4.",
"Pericentric heterochromatin reprogramming by new histone variants during mouse spermiogenesis."
] | [
1994,
2007
] | 2 | [] | [
"IPR021171"
] | 0 | 1 | 0 | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"metagenomes"
] | [
34170,
3,
23,
13
] | 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... | [
44,
6,
36,
3,
54,
55,
2,
23,
62,
3,
3,
125
] | 12 | true | Family | Histone H2A | Histone H2A | Histone_H2A | 8 |
IPR002120 | 2,120 | Thyrotropin-releasing hormone receptor | TRH_rcpt_1 | Family | 2,950 | false | false | Thyrotropin-releasing hormone, also known as thyroliberin (TRH) stimulates the synthesis and release of thyroid-stimulating hormone in the anterior pituitary [ , ]. TRH is produced in many other tissues, especially within the nervous system, where it appears to act as a neurotransmitter/neuromodulator. It also stimulat... | [
"GO:0004997",
"GO:0007186",
"GO:0016020"
] | [
"thyrotropin-releasing hormone receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PRINTS",
"PRINTS",
"PANTHER"
] | [
"PR00751",
"PR01654",
"PR01846",
"PTHR46061"
] | [
"THYROLIBRINR",
"TRHRECEPTOR2",
"TRHRFAMILY",
""
] | [
2266,
31,
2553,
2810
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-375276",
"R-BTA-416476",
"R-HSA-375276",
"R-HSA-416476",
"R-MMU-375276",
"R-MMU-416476",
"R-RNO-375276",
"R-RNO-416476"
] | [
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476"
] | 8 | [
"7wkd",
"7x1t",
"7x1u",
"7xw9"
] | 4 | [
"PUB00007864",
"PUB00067382",
"PUB00067383",
"PUB00067384",
"PUB00067385",
"PUB00067386",
"PUB00067387",
"PUB00067388",
"PUB00067389",
"PUB00067390",
"PUB00067391",
"PUB00067392",
"PUB00067393",
"PUB00067394",
"PUB00067395"
] | [
"9822707",
"4982117",
"4985794",
"8147889",
"2423357",
"12683933",
"2175902",
"1377915",
"8395824",
"11181534",
"18984166",
"8387653",
"10628757",
"1333052",
"1334076"
] | [
"Cloning and characterization of a cDNA encoding a novel subtype of rat thyrotropin-releasing hormone receptor.",
"The identity of chemical and hormonal properties of the thyrotropin releasing hormone and pyroglutamyl-histidyl-proline amide.",
"Characterization of ovine hypothalamic hypophysiotropic TSH-releasi... | [
1998,
1969,
1970,
1994,
1986,
2003,
1990,
1992,
1993,
2001,
2008,
1993,
2000,
1992,
1992
] | 15 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
2950
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
21,
4,
1,
6,
8
] | 6 | true | Family | Thyrotropin-releasing hormone receptor | Thyrotropin-releasing hormone receptor | TRH_rcpt_1 | 8 |
IPR002121 | 2,121 | HRDC domain | HRDC_dom | Domain | 52,585 | false | false | The HRDC (helicase and RNaseD C-terminal) domain is comprised of two orthogonally packed α-hairpin subdomains, and is involved in interactions with DNA and protein. It has been suggested that this domain plays a role dissolving double Holliday junctions efficiently [ ]. HRDC domains are found at the C terminus of many ... | [
"GO:0003676"
] | [
"nucleic acid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00570",
"PS50967",
"SM00341"
] | [
"HRDC",
"HRDC",
"HRDC"
] | [
51562,
51939,
44954
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50967",
"R-CEL-5693607",
"R-CEL-6791226",
"R-CEL-9930044",
"R-DME-3108214",
"R-DME-5693607",
"R-DME-6791226",
"R-DME-6804756",
"R-DME-69473",
"R-DME-9930044",
"R-HSA-174414",
"R-HSA-174437",
"R-HSA-3108214",
"R-HSA-5685938",
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"... | [
"PROSITEDOC:PDOC50967",
"REACTOME:R-CEL-5693607",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-9930044",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-5693607",
"REACTOME:R-DME-6791226",
"REACTOME:R-DME-6804756",
"REACTOME:R-DME-69473",
"REACTOME:R-DME-9930044",
"REACTOME:R-HSA-174414",
"REACTOME:R-H... | 47 | [
"1d8b",
"1wud",
"1yt3",
"2cpr",
"2dgz",
"2e1e",
"2e1f",
"2hbj",
"2hbk",
"2hbl",
"2hbm",
"2kv2",
"2ma1",
"2rhf",
"2rrd",
"3cym",
"3saf",
"3sag",
"3sah",
"4cdg",
"4cgz",
"4nlb",
"4nlc",
"4o3m",
"4oo1",
"5c0w",
"5c0x",
"5c0y",
"5k36",
"5vzj",
"6d6q",
"6d6r"... | 49 | [
"PUB00005473",
"PUB00007873",
"PUB00014060",
"PUB00032236",
"PUB00101132"
] | [
"9397680",
"11741548",
"10647186",
"15591044",
"25901030"
] | [
"A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases.",
"Structure of an archaeal homolog of the eukaryotic RNA polymerase II RPB4/RPB7 complex.",
"The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins.",
"Structures of com... | [
1997,
2001,
1999,
2005,
2015
] | 5 | [] | [
"IPR022758"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
141,
39037,
12690,
717
] | 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",... | [
37,
3,
8,
3,
2,
12,
12,
2,
21,
11,
2,
2,
50
] | 13 | true | Domain | HRDC domain | HRDC domain | HRDC_dom | 9 |
IPR002122 | 2,122 | Melanocortin 3 receptor | Mcort_3_rcpt | Family | 558 | 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"
] | [
"PR01061"
] | [
"MELNOCORTN3R"
] | [
558
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"284",
"R-HSA-375276",
"R-HSA-418555",
"R-HSA-9856649",
"R-MMU-375276",
"R-MMU-418555",
"R-RNO-375276"
] | [
"IUPHAR:284",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-375276"
] | 7 | [
"8ioc",
"8kig",
"8w8w",
"8w8x",
"8w8y",
"9k3f"
] | 6 | [
"PUB00000131",
"PUB00000530",
"PUB00002477",
"PUB00002830",
"PUB00004827",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"8172596",
"2830256",
"8463333",
"8415620",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"Molecular cloning, functional expression and pharmacological characterization of a mouse melanocortin receptor gene.",
"G protein involvement in receptor-effector coupling.",
"Molecular cloning of a novel melanocortin receptor.",
"Identification of a receptor for gamma... | [
1990,
1994,
1988,
1993,
1993,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 13 | [
"IPR001908"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
558
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3,
1
] | 4 | true | Family | Melanocortin 3 receptor | Melanocortin 3 receptor | Mcort_3_rcpt | 4 |
IPR002123 | 2,123 | Phospholipid/glycerol acyltransferase | Plipid/glycerol_acylTrfase | Domain | 165,943 | false | false | This family is found in diverse acyltransferases involved in phospholipid biosynthesis [ ]. This domain is found in tafazzins, phospholipid transacylases involved in the remodeling of cardiolipin, a mitochondrial phospholipid required for oxidative phosphorylation and whose defects cause of Barth syndrome; a severe inh... | [
"GO:0016746"
] | [
"acyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01553",
"SM00563"
] | [
"Acyltransferase",
"PlsC"
] | [
158706,
156809
] | 2 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1",
"GenProp1316",
"GenProp1718",
"R-BTA-1483166",
"R-CEL-1483166",
"R-CEL-6798695",
"R-CEL-75109",
"R-DDI-1268020",
"R-DDI-1482798",
"R-DME-1268020",
"R-DME-1482788",
"R-DME-1482798",
"R-DME-1482801",
"R-DME-1482839",
"R-DME-1482925",
"R-DME-1483166",
"R-DME-6798695",
"R-DRE-... | [
"EC:2.3.1",
"GP:GenProp1316",
"GP:GenProp1718",
"REACTOME:R-BTA-1483166",
"REACTOME:R-CEL-1483166",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-75109",
"REACTOME:R-DDI-1268020",
"REACTOME:R-DDI-1482798",
"REACTOME:R-DME-1268020",
"REACTOME:R-DME-1482788",
"REACTOME:R-DME-1482798",
"REACTOME:R-... | 79 | [
"1iuq",
"1k30",
"5kym",
"7zkq",
"8e4y",
"8e50",
"8ia1"
] | 7 | [
"PUB00006582",
"PUB00043329",
"PUB00097282"
] | [
"9259571",
"18369234",
"33096711"
] | [
"Barth syndrome may be due to an acyltransferase deficiency.",
"Thematic review series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis.",
"Tafazzin Mutation Affecting Cardiolipin Leads to Increased Mitochondrial Superoxide Anions and Mitophagy Inhibition in Barth Syndrome."
] | [
1997,
2008,
2020
] | 3 | [] | [
"IPR004552",
"IPR041728",
"IPR045252",
"IPR045746"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
66,
105927,
58121,
33,
1796
] | 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",... | [
82,
25,
32,
33,
4,
80,
62,
5,
84,
74,
6,
4,
136
] | 13 | true | Domain | Phospholipid/glycerol acyltransferase | Phospholipid/glycerol acyltransferase | Plipid/glycerol_acylTrfase | 7 |
IPR002124 | 2,124 | Cytochrome c oxidase, subunit Vb | Cyt_c_oxidase_su5b | Family | 5,230 | false | false | Cytochrome c oxidase ( ) is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen [ ]. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plas... | [
"GO:0006123",
"GO:0005740"
] | [
"mitochondrial electron transport, cytochrome c to oxygen",
"mitochondrial envelope"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE",
"PANTHER",
"CDD"
] | [
"PF01215",
"PS51359",
"PTHR10122",
"cd00924"
] | [
"COX5B",
"COX5B_2",
"",
"Cyt_c_Oxidase_Vb"
] | [
4996,
5025,
5025,
4054
] | 4 | [
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1426",
"GenProp1637",
"PDOC00663",
"R-DDI-9837999",
"R-HSA-5628897",
"R-HSA-611105",
"R-HSA-9707564",
"R-HSA-9837999",
"R-HSA-9864848",
"R-MMU-5628897",
"R-MMU-611105",
"R-MMU-9707564",
"R-MMU-9837999",
"R-MMU-9864848",
"R-RNO-5628897",
"R-RNO-611105",
"R-RNO-9707564",
"R-R... | [
"GP:GenProp1426",
"GP:GenProp1637",
"PROSITEDOC:PDOC00663",
"REACTOME:R-DDI-9837999",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-9707564",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9864848",
"REACTOME:R-MMU-5628897",
"REACTOME:R-MMU-611105",
"REACTOME:R-MMU-9707564",
... | 25 | [
"1occ",
"1oco",
"1ocr",
"1ocz",
"1v54",
"1v55",
"2dyr",
"2dys",
"2eij",
"2eik",
"2eil",
"2eim",
"2ein",
"2occ",
"2odx",
"2y69",
"2ybb",
"2zxw",
"3abk",
"3abl",
"3abm",
"3ag1",
"3ag2",
"3ag3",
"3ag4",
"3asn",
"3aso",
"3wg7",
"3x2q",
"5b1a",
"5b1b",
"5b3s"... | 141 | [
"PUB00000581",
"PUB00000625",
"PUB00005218"
] | [
"6307356",
"1661610",
"8638158"
] | [
"Structure of cytochrome c oxidase.",
"The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideum.",
"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."
] | [
1983,
1991,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
5229,
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... | [
11,
1,
3,
3,
4,
4,
1,
5,
6,
1,
1,
26
] | 12 | true | Family | Cytochrome c oxidase, subunit Vb | Cytochrome c oxidase, subunit Vb | Cyt_c_oxidase_su5b | 9 |
IPR002125 | 2,125 | Cytidine and deoxycytidylate deaminase domain | CMP_dCMP_dom | Domain | 129,526 | false | false | Cytidine deaminase ( ) (cytidine aminohydrolase) catalyses the hydrolysis of cytidine into uridine and ammonia while deoxycytidylate deaminase ( ) (dCMP deaminase) hydrolyses dCMP into dUMP. Both enzymes are known to bind zinc and to require it for their catalytic activity [ , ]. The deaminases possess either one or tw... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00383",
"PF14437",
"PS51747"
] | [
"dCMP_cyt_deam_1",
"MafB19-deam",
"CYT_DCMP_DEAMINASES_2"
] | [
114137,
9048,
127558
] | 3 | [
"EC",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.5.4",
"GenProp1361",
"GenProp1540",
"R-DDI-6798695",
"R-DDI-73614",
"R-HSA-180585",
"R-HSA-180689",
"R-HSA-499943",
"R-HSA-6782315",
"R-HSA-6798695",
"R-HSA-72200",
"R-HSA-73614",
"R-HSA-75094",
"R-HSA-9821002",
"R-MMU-499943",
"R-MMU-6798695",
"R-MMU-72200",
"R-MMU-73614",
"R... | [
"EC:3.5.4",
"GP:GenProp1361",
"GP:GenProp1540",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-73614",
"REACTOME:R-HSA-180585",
"REACTOME:R-HSA-180689",
"REACTOME:R-HSA-499943",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-72200",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-750... | 26 | [
"1af2",
"1aln",
"1ctt",
"1ctu",
"1jtk",
"1mq0",
"1ox7",
"1p6o",
"1r5t",
"1rb7",
"1tiy",
"1uaq",
"1uwz",
"1ux0",
"1ux1",
"1vq2",
"1wkq",
"1wn5",
"1wn6",
"1wwr",
"1ysb",
"1ysd",
"1z3a",
"1zab",
"2a8n",
"2b3j",
"2b3z",
"2d30",
"2d5n",
"2fr5",
"2fr6",
"2g6v"... | 232 | [
"PUB00000364",
"PUB00002807",
"PUB00021931",
"PUB00054844",
"PUB00057473",
"PUB00075557"
] | [
"1567863",
"8428902",
"11851403",
"20152150",
"21890906",
"23150645"
] | [
"Cloning and nucleotide sequence of the Escherichia coli cytidine deaminase (ccd) gene.",
"T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit.",
"Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution.",
"Crystal structure of... | [
1992,
1993,
2002,
2010,
2011,
2013
] | 6 | [] | [
"IPR013158",
"IPR035105",
"IPR059135",
"IPR059136",
"IPR059203"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1275,
93157,
31833,
1301,
1960
] | 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",... | [
78,
8,
17,
8,
3,
75,
48,
9,
36,
48,
6,
6,
78
] | 13 | true | Domain | Cytidine and deoxycytidylate deaminase domain | Cytidine and deoxycytidylate deaminase domain | CMP_dCMP_dom | 9 |
IPR002126 | 2,126 | Cadherin-like | Cadherin-like_dom | Domain | 143,534 | false | false | This entry represents the extracellular repeated domains found in cadherins and related proteins. Cadherins are a group of transmembrane proteins that serve as the major adhesion molecules located within adherens junctions. They can regulate cell-cell adhesion through their extracellular domain and their cytosolic doma... | [
"GO:0005509",
"GO:0007156",
"GO:0016020"
] | [
"calcium ion binding",
"homophilic cell-cell adhesion",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00028",
"PR00205",
"PS50268",
"SM00112"
] | [
"Cadherin",
"CADHERIN",
"CADHERIN_2",
"CA"
] | [
126024,
125163,
143087,
130597
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00205",
"R-BTA-418990",
"R-CEL-351906",
"R-CEL-6798695",
"R-CEL-6809371",
"R-CEL-9013404",
"R-CEL-9013408",
"R-CEL-9013423",
"R-CFA-1474228",
"R-CFA-216083",
"R-CFA-351906",
"R-CFA-418990",
"R-CFA-6805567",
"R-CFA-6809371",
"R-CFA-9764561",
"R-CFA-9766229",
"R-CFA-9768727",
"R... | [
"PROSITEDOC:PDOC00205",
"REACTOME:R-BTA-418990",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6809371",
"REACTOME:R-CEL-9013404",
"REACTOME:R-CEL-9013408",
"REACTOME:R-CEL-9013423",
"REACTOME:R-CFA-1474228",
"REACTOME:R-CFA-216083",
"REACTOME:R-CFA-351906",
"REACTOME:R-CF... | 144 | [
"1edh",
"1ff5",
"1l3w",
"1ncg",
"1nch",
"1nci",
"1ncj",
"1o6s",
"1q1p",
"1q55",
"1q5a",
"1q5b",
"1q5c",
"1suh",
"1wuz",
"1wyj",
"1zvn",
"1zxk",
"2a4c",
"2a4e",
"2a62",
"2ee0",
"2kpn",
"2o72",
"2omt",
"2omu",
"2omv",
"2omw",
"2omx",
"2omy",
"2omz",
"2qvf"... | 238 | [
"PUB00007174",
"PUB00071518"
] | [
"11736639",
"25014356"
] | [
"Structure and functions of classical cadherins.",
"E-Cadherin Can Replace N-Cadherin during Secretory-Stage Enamel Development."
] | [
2001,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
132,
9247,
133860,
31,
264
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
25,
452,
43,
420,
363,
382
] | 6 | true | Domain | Cadherin-like | Cadherin-like | Cadherin-like_dom | 4 |
IPR002128 | 2,128 | NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal | NADH_UbQ_OxRdtase_chlpt_su5_C | Domain | 41,758 | false | false | This domain represents a C-terminal extension of NADH-Ubiquinone/plastoquinone (complex I) chains (see ). Chain 5 is a component of complex I which catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01010"
] | [
"Proton_antipo_C"
] | [
41758
] | 1 | [
"EC"
] | [
"7.1.1.-"
] | [
"EC:7.1.1.-"
] | 1 | [
"6hum",
"6khi",
"6khj",
"6l7o",
"6l7p",
"6nbq",
"6nbx",
"6nby",
"7eu3",
"7f9o",
"7wff",
"7wg5",
"9grx"
] | 13 | [
"PUB00005074",
"PUB00043561",
"PUB00045437"
] | [
"1470679",
"10940377",
"18394423"
] | [
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.",
"Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)."
] | [
1992,
2000,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
530,
41176,
52
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
3,
2
] | 3 | true | Domain | NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal | NADH:ubiquinone/plastoquinone oxidoreductase, chloroplast chain 5, C-terminal | NADH_UbQ_OxRdtase_chlpt_su5_C | 1 |
IPR002129 | 2,129 | Pyridoxal phosphate-dependent decarboxylase, major domain | PyrdxlP-dep_de-COase | Domain | 68,083 | false | false | A number of pyridoxal-dependent decarboxylases share regions of sequence similarity, particularly in the vicinity of a conserved lysine residue, which provides the attachment site for the pyridoxal-phosphate (PLP) group [ , ]. Among these enzymes are aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptoph... | [
"GO:0016830",
"GO:0030170",
"GO:0019752"
] | [
"carbon-carbon lyase activity",
"pyridoxal phosphate binding",
"carboxylic acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00282"
] | [
"Pyridoxal_deC"
] | [
68083
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"4.1.1",
"GenProp1277",
"GenProp1288",
"GenProp1335",
"GenProp1363",
"GenProp1551",
"GenProp1606",
"GenProp1695",
"PDOC00329",
"R-BTA-1614558",
"R-BTA-70921",
"R-BTA-888568",
"R-BTA-888590",
"R-BTA-8963693",
"R-CEL-9845614",
"R-CFA-888568",
"R-CFA-888590",
"R-DDI-9845614",
"R-DME... | [
"EC:4.1.1",
"GP:GenProp1277",
"GP:GenProp1288",
"GP:GenProp1335",
"GP:GenProp1363",
"GP:GenProp1551",
"GP:GenProp1606",
"GP:GenProp1695",
"PROSITEDOC:PDOC00329",
"REACTOME:R-BTA-1614558",
"REACTOME:R-BTA-70921",
"REACTOME:R-BTA-888568",
"REACTOME:R-BTA-888590",
"REACTOME:R-BTA-8963693",
... | 52 | [
"1js3",
"1js6",
"1pmm",
"1pmo",
"1xey",
"2dgk",
"2dgl",
"2dgm",
"2jis",
"2okj",
"2okk",
"2qma",
"3f9t",
"3fz6",
"3fz7",
"3fz8",
"3hbx",
"3k40",
"3mad",
"3maf",
"3mau",
"3mbb",
"3mc6",
"3rbf",
"3rbl",
"3rch",
"3vp6",
"4e1o",
"4obu",
"4obv",
"4q6r",
"4rit"... | 96 | [
"PUB00001452",
"PUB00002358",
"PUB00003414",
"PUB00004715",
"PUB00006322",
"PUB00035504",
"PUB00035505",
"PUB00035506",
"PUB00035507",
"PUB00035508",
"PUB00076906",
"PUB00094543"
] | [
"8181483",
"8889823",
"2124279",
"2300558",
"7748903",
"15581583",
"8690703",
"15189147",
"17109392",
"16763894",
"24415726",
"16766535"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.",
"Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous.",
... | [
1994,
1996,
1990,
1990,
1995,
2005,
1995,
2004,
2006,
2006,
2014,
2006
] | 12 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
883,
23567,
43119,
15,
499
] | 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",... | [
53,
17,
27,
23,
2,
95,
36,
6,
48,
53,
2,
56
] | 12 | true | Domain | Pyridoxal phosphate-dependent decarboxylase, major domain | Pyridoxal phosphate-dependent decarboxylase, major domain | PyrdxlP-dep_de-COase | 4 |
IPR002130 | 2,130 | Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain | Cyclophilin-type_PPIase_dom | Domain | 132,603 | false | false | Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity ( ), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ , ]. They also have protein chaperone-like functions [ ] and are the major high-affinity binding proteins for the immu... | [
"GO:0003755",
"GO:0000413"
] | [
"peptidyl-prolyl cis-trans isomerase activity",
"protein peptidyl-prolyl isomerization"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00160",
"PR00153",
"PS50072"
] | [
"Pro_isomerase",
"CSAPPISMRASE",
"CSA_PPIASE_2"
] | [
132262,
115059,
129886
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.2.1.8",
"PDOC00154",
"R-BTA-210991",
"R-BTA-6798695",
"R-BTA-72163",
"R-CEL-210991",
"R-CEL-72163",
"R-DDI-72163",
"R-DME-210991",
"R-DME-6798695",
"R-GGA-72163",
"R-HSA-114608",
"R-HSA-1169408",
"R-HSA-141444",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"... | [
"EC:5.2.1.8",
"PROSITEDOC:PDOC00154",
"REACTOME:R-BTA-210991",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-72163",
"REACTOME:R-CEL-210991",
"REACTOME:R-CEL-72163",
"REACTOME:R-DDI-72163",
"REACTOME:R-DME-210991",
"REACTOME:R-DME-6798695",
"REACTOME:R-GGA-72163",
"REACTOME:R-HSA-114608",
"REACT... | 98 | [
"1a33",
"1a58",
"1ak4",
"1awq",
"1awr",
"1aws",
"1awt",
"1awu",
"1awv",
"1bck",
"1c5f",
"1clh",
"1cwa",
"1cwb",
"1cwc",
"1cwf",
"1cwh",
"1cwi",
"1cwj",
"1cwk",
"1cwl",
"1cwm",
"1cwo",
"1cyn",
"1dyw",
"1e3b",
"1e8k",
"1fgl",
"1h0p",
"1ihg",
"1iip",
"1ist"... | 484 | [
"PUB00000320",
"PUB00017852",
"PUB00021063",
"PUB00056846",
"PUB00056847"
] | [
"2186809",
"14731520",
"15998457",
"21309470",
"21295323"
] | [
"The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.",
"Cyclophilins: a new family of proteins involved in intracellular folding.",
"The cyclophilins.",
"An overview of cyclophilins in human cancers.",
"Emerging picture of ho... | [
1990,
1992,
2005,
2010,
2011
] | 5 | [] | [
"IPR035538"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Imitervirales",
"unclassified sequences"
] | [
817,
49082,
81550,
31,
1123
] | 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",... | [
116,
21,
32,
30,
2,
128,
56,
10,
83,
97,
9,
9,
234
] | 13 | true | Domain | Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain | Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain | Cyclophilin-type_PPIase_dom | 9 |
IPR002131 | 2,131 | Glycoprotein hormone receptor family | Gphrmn_rcpt_fam | Family | 9,196 | false | false | Glycoprotein hormones (or gonadotropins) are protein hormones, that includes the mammalian hormones follicle-stimulating hormone (FSH, also known as follitropin), luteinizing hormone (LH, also known as lutropin), thyroid-stimulating hormone (TSH, also known as thyrotropin) and human chorionic gonadotropin (hCG). These ... | [
"GO:0016500",
"GO:0007186",
"GO:0016020"
] | [
"protein-hormone receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00373"
] | [
"GLYCHORMONER"
] | [
9196
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-375281",
"R-HSA-375281",
"R-HSA-418555",
"R-HSA-4641263",
"R-MMU-375281",
"R-MMU-418555",
"R-MMU-4641263",
"R-RNO-375281",
"R-RNO-4641263",
"R-SSC-375281",
"R-SSC-418555",
"R-XTR-4641263"
] | [
"REACTOME:R-CFA-375281",
"REACTOME:R-HSA-375281",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-4641263",
"REACTOME:R-MMU-375281",
"REACTOME:R-MMU-418555",
"REACTOME:R-MMU-4641263",
"REACTOME:R-RNO-375281",
"REACTOME:R-RNO-4641263",
"REACTOME:R-SSC-375281",
"REACTOME:R-SSC-418555",
"REACTOME:R-XTR-... | 12 | [
"7fig",
"7fih",
"7fii",
"7fij",
"7t9i",
"7t9m",
"7t9n",
"7utz",
"7xw5",
"7xw6",
"7xw7",
"8i2g",
"8i2h",
"8wvu",
"8wvv",
"8wvw",
"8wvx",
"8wvy",
"8xfp",
"8xfs",
"8xft",
"8xt9",
"8xum",
"8y69",
"9kb6",
"9kb7",
"9kb8",
"9kb9",
"9kgk",
"9khh",
"9s37",
"9s38"... | 33 | [
"PUB00000033",
"PUB00000517",
"PUB00002390",
"PUB00005254",
"PUB00067495"
] | [
"6267989",
"1445230",
"6177696",
"8747461",
"19171054"
] | [
"Glycoprotein hormones: structure and function.",
"Molecular structures of glycoprotein hormones and functions of their carbohydrate components.",
"alpha Subunit of rat pituitary glycoprotein hormones. Primary structure of the precursor determined from the nucleotide sequence of cloned cDNAs.",
"Structural pr... | [
1981,
1992,
1982,
1995,
2009
] | 5 | [
"IPR000276"
] | [
"IPR002272",
"IPR002273",
"IPR002274"
] | 1 | 3 | 0 | [
"Eukaryota"
] | [
9196
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
26,
7,
25,
11,
28
] | 6 | true | Family | Glycoprotein hormone receptor family | Glycoprotein hormone receptor family | Gphrmn_rcpt_fam | 7 |
IPR002132 | 2,132 | Large ribosomal subunit protein uL5 | Ribosomal_uL5 | Family | 36,094 | false | false | Large ribosomal subunit protein uL5, previously known as Ribosomal protein L5, is ~180 amino acids in length. In Escherichia coli, uL5 is known to be involved in binding 5S RNA to the large ribosomal subunit [ ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of t... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF002161",
"PTHR11994"
] | [
"Ribosomal_L5",
""
] | [
31779,
35987
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00309",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
... | [
"PROSITEDOC:PDOC00309",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956... | 58 | [
"1ffk",
"1iq4",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1mji",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9"... | 1,748 | [
"PUB00000599",
"PUB00000693",
"PUB00001802",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00104042"
] | [
"2198942",
"1840500",
"2016059",
"11297922",
"11290319",
"11114498",
"11866091"
] | [
"Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.",
"The structure of the gene for ribosomal protein L5 in the archaebacterium Sulfolobus acidocaldarius.",
"Structure and evolution of the Tetrahymena thermophila gene encoding ribosomal protein L21... | [
1990,
1991,
1991,
2001,
2001,
2000,
2002
] | 7 | [] | [
"IPR020930",
"IPR057266"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
942,
23764,
10903,
485
] | 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,
3,
1,
3,
1,
4,
3,
2,
15,
5,
3,
3,
49
] | 13 | true | Family | Large ribosomal subunit protein uL5 | Large ribosomal subunit protein uL5 | Ribosomal_uL5 | 1 |
IPR002134 | 2,134 | Histidine-rich calcium-binding repeat | His-rich_Ca-bd_rpt | Repeat | 32 | false | false | The histidine-rich calcium-binding protein (HCP) of sarcoplasmic reticulum [ ] may play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle. This protein is very acidic (31% of Asp and Glu) and rich in histidine (13%). The sequence of HCP contains 10 tandem repeats of a... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00328"
] | [
"HCP"
] | [
32
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00292"
] | [
"PROSITEDOC:PDOC00292"
] | 1 | [] | 0 | [
"PUB00002520"
] | [
"2808365"
] | [
"Molecular cloning of a histidine-rich Ca2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Boreoeutheria"
] | [
32
] | 1 | [
"Homo sapiens"
] | [
1
] | 1 | true | Repeat | Histidine-rich calcium-binding repeat | Histidine-rich calcium-binding repeat | His-rich_Ca-bd_rpt | 1 |
IPR002136 | 2,136 | Large ribosomal subunit protein uL4 | Ribosomal_uL4 | Family | 37,685 | false | false | This family includes large ribosomal subunit protein uL4 from eukaryotes, archaea and bacteria. This protein is well characterised [ , , , , ]. Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00573"
] | [
"Ribosomal_L4"
] | [
37685
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-... | 76 | [
"1dmg",
"1ffk",
"1j5a",
"1jj2",
"1jzx",
"1jzy",
"1jzz",
"1k01",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1ml5",
"1n8r",
"1nji",
"1nkw",
"1nwx",
"1nwy",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1sm1",
"1vq4",
"1vq5"... | 1,994 | [
"PUB00000678",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00028961",
"PUB00034484",
"PUB00114401",
"PUB00151129",
"PUB00151130"
] | [
"9838082",
"11297922",
"11290319",
"11114498",
"12511961",
"16285925",
"24499919",
"33357414",
"27373148"
] | [
"Yeast ribosomal proteins L4, L17, L20, and L25 exhibit different binding characteristics for the yeast 35S precursor rRNA.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Structure of the Escherichia col... | [
1998,
2001,
2001,
2000,
2003,
2005,
2014,
2021,
2016
] | 9 | [] | [
"IPR013005",
"IPR045240"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
951,
24215,
11985,
534
] | 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",... | [
25,
2,
3,
3,
1,
16,
8,
2,
15,
10,
3,
3,
26
] | 13 | true | Family | Large ribosomal subunit protein uL4 | Large ribosomal subunit protein uL4 | Ribosomal_uL4 | 1 |
IPR002137 | 2,137 | Beta-lactamase, class-D active site | Beta-lactam_class-D_AS | Active_site | 3,805 | false | false | Beta-lactamases ( ) [ , ] are enzymes which catalyse the hydrolysis of an amide bond in the beta-lactam ring of antibiotics belonging to the penicillin/cephalosporin family. Four kinds of beta-lactamase have been identified [ ]. Class-B enzymes are zinc containing proteins whilst class -A, C and D enzymes are serine hy... | [
"GO:0008800",
"GO:0017001"
] | [
"beta-lactamase activity",
"antibiotic catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00337"
] | [
"BETA_LACTAMASE_D"
] | [
3805
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"3.5.2.6",
"PDOC00134",
"R-HSA-9913143"
] | [
"EC:3.5.2.6",
"PROSITEDOC:PDOC00134",
"REACTOME:R-HSA-9913143"
] | 3 | [
"1e3u",
"1e4d",
"1ewz",
"1fof",
"1h5x",
"1h8y",
"1h8z",
"1k38",
"1k4e",
"1k4f",
"1k54",
"1k55",
"1k56",
"1k57",
"1k6r",
"1k6s",
"1m6k",
"2hp5",
"2hp6",
"2hp9",
"2hpb",
"2rl3",
"2wgi",
"2wgv",
"2wgw",
"2x02",
"3hbr",
"3if6",
"3isg",
"3lce",
"3qnb",
"3qnc"... | 229 | [
"PUB00000133",
"PUB00000464",
"PUB00003800",
"PUB00004510"
] | [
"2658779",
"3128280",
"2082152",
"6109327"
] | [
"Characterization of beta-lactamases.",
"The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.",
"Molecular evolution of class A beta-lactamases: phylogeny and patterns of sequence conservation.",
"The structure of beta-lactamases."
] | [
1989,
1988,
1990,
1980
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes",
"plasmids"
] | [
3730,
51,
21,
3
] | 4 | [] | [] | 0 | true | Active_site | Beta-lactamase, class-D active site | Beta-lactamase, class-D active site | Beta-lactam_class-D_AS | 9 |
IPR002138 | 2,138 | Peptidase C14, caspase non-catalytic subunit p10 | Pept_C14_p10 | Domain | 18,320 | false | false | This group of sequences represent the p10 subunit found in caspases. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family, clan CD) based on the architecture of their catalytic dyad or triad [ ]. Caspases are tightly regulated pr... | [
"GO:0004197",
"GO:0006508"
] | [
"cysteine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROFILE"
] | [
"PS50207"
] | [
"CASPASE_P10"
] | [
18320
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.22",
"PDOC00864",
"R-BTA-5620971",
"R-CEL-111465",
"R-CEL-140342",
"R-CEL-198323",
"R-CEL-2028269",
"R-CEL-264870",
"R-CEL-351906",
"R-CEL-418889",
"R-CEL-5357905",
"R-DME-111458",
"R-DME-111459",
"R-DME-111465",
"R-DME-111469",
"R-DME-140342",
"R-DME-198323",
"R-DME-2028269",... | [
"EC:3.4.22",
"PROSITEDOC:PDOC00864",
"REACTOME:R-BTA-5620971",
"REACTOME:R-CEL-111465",
"REACTOME:R-CEL-140342",
"REACTOME:R-CEL-198323",
"REACTOME:R-CEL-2028269",
"REACTOME:R-CEL-264870",
"REACTOME:R-CEL-351906",
"REACTOME:R-CEL-418889",
"REACTOME:R-CEL-5357905",
"REACTOME:R-DME-111458",
"R... | 146 | [
"1bmq",
"1cp3",
"1f1j",
"1f9e",
"1gfw",
"1gqf",
"1i3o",
"1i4e",
"1i4o",
"1i51",
"1ibc",
"1ice",
"1jxq",
"1k86",
"1k88",
"1kmc",
"1m72",
"1nme",
"1nmq",
"1nms",
"1nw9",
"1pau",
"1pyo",
"1qdu",
"1qtn",
"1qx3",
"1re1",
"1rhj",
"1rhk",
"1rhm",
"1rhq",
"1rhr"... | 321 | [
"PUB00011704",
"PUB00014747",
"PUB00014748",
"PUB00015006",
"PUB00015008"
] | [
"11517925",
"15077141",
"15066636",
"10578171",
"10872455"
] | [
"Evolutionary lines of cysteine peptidases.",
"Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies.",
"Death without caspases, caspases without death.",
"Caspase structure, proteolytic substrates, and function during apoptotic cell death.",
"Mammalian caspases: st... | [
2001,
2004,
2004,
1999,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Enterovirus C",
"Eukaryota",
"Halapricum desulfuricans",
"ecological metagenomes"
] | [
152,
1,
18163,
1,
3
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
56,
12,
45,
28,
37
] | 6 | true | Domain | Peptidase C14, caspase non-catalytic subunit p10 | Peptidase C14, caspase non-catalytic subunit p10 | Pept_C14_p10 | 4 |
IPR002139 | 2,139 | Ribokinase/fructokinase | Ribo/fructo_kinase | Family | 47,331 | false | false | Ribokinases participate in the first step of ribose metabolism, and are members of the superfamily of carbohydrate kinases. Ribokinases phosphorylate ribose to ribose-5-phosphate in the presence of ATP and magnesium [ ]: ATP + D-Ribose = ADP + D-Ribose-5-Phosphate The phosphorylated sugar may then enter the pentose pho... | [
"GO:0016301"
] | [
"kinase activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00990"
] | [
"RIBOKINASE"
] | [
47331
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1",
"R-DDI-71336",
"R-HSA-71336",
"R-MMU-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:2.7.1",
"REACTOME:R-DDI-71336",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 6 | [
"1gqt",
"1rk2",
"1rka",
"1rkd",
"1rks",
"1tyy",
"1tz3",
"1tz6",
"1v19",
"1v1a",
"1v1b",
"1v1s",
"1vm7",
"2c49",
"2c4e",
"2fv7",
"3ewm",
"3gbu",
"3go6",
"3go7",
"3h49",
"3hj6",
"3i3y",
"3ih0",
"3ikh",
"3in1",
"3ry7",
"4u7x",
"4wjm",
"4x8f",
"4xck",
"4xda"... | 68 | [
"PUB00001470",
"PUB00004876",
"PUB00005046",
"PUB00015675",
"PUB00074171",
"PUB00079958",
"PUB00079959",
"PUB00085020",
"PUB00097196",
"PUB00100236",
"PUB00153414"
] | [
"8917457",
"8577746",
"9385653",
"8382990",
"24463506",
"12475618",
"11120475",
"17021658",
"25822915",
"31907295",
"10648508"
] | [
"Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene.",
"Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and f... | [
1996,
1996,
1997,
1993,
2014,
2003,
2000,
2007,
2015,
2020,
2000
] | 11 | [] | [
"IPR011877",
"IPR030877"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1241,
36761,
8883,
446
] | 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",... | [
49,
1,
1,
3,
4,
1,
1,
1,
17,
4,
1,
1,
24
] | 13 | true | Family | Ribokinase/fructokinase | Ribokinase/fructokinase | Ribo/fructo_kinase | 7 |
IPR002140 | 2,140 | Ribosome maturation protein Sdo1/SBDS | Sdo1/SBDS | Family | 5,012 | false | false | The proteins in this entry are highly conserved in species ranging from archaea to vertebrates and plants [ ]. The family contains several Shwachman-Bodian-Diamond syndrome (SBDS, OMIM 260400) proteins from both mouse and humans. Shwachman-Diamond syndrome is an autosomal recessive disorder with clinical features that ... | [
"GO:0042256"
] | [
"cytosolic ribosome assembly"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR00291"
] | [
"RNA_SBDS"
] | [
5012
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00974"
] | [
"PROSITEDOC:PDOC00974"
] | 1 | [
"1p9q",
"1t95",
"2kdo",
"2l9n",
"2wbm",
"5an9",
"5anb",
"5anc",
"6fsw",
"6qkl",
"6skg"
] | 11 | [
"PUB00020303",
"PUB00045126",
"PUB00076339",
"PUB00076340"
] | [
"12496757",
"17353896",
"23831625",
"21536732"
] | [
"Mutations in SBDS are associated with Shwachman-Diamond syndrome.",
"The Shwachman-Bodian-Diamond syndrome protein mediates translational activation of ribosomes in yeast.",
"Guanine nucleotide exchange in the ribosomal GTPase EFL1 is modulated by the protein mutated in the Shwachman-Diamond syndrome.",
"Unc... | [
2003,
2007,
2013,
2011
] | 4 | [
"IPR039100"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
905,
2,
4064,
41
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
2,
3,
4,
2,
1,
2,
4,
1,
1,
3
] | 12 | true | Family | Ribosome maturation protein Sdo1/SBDS | Ribosome maturation protein Sdo1/SBDS | Sdo1/SBDS | 4 |
IPR002141 | 2,141 | Influenza virus nucleoprotein (NP) | Flu_NP | Family | 63,572 | false | false | Influenza virus nucleoprotein (NP) is a structural protein which encapsidates the negative strand viral RNA. NP is one of the main determinants of species specificity. The question of how far the NP gene can cross the species barrier by reassortment and become adapted by mutation to the new host has been discussed [ ]. | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM"
] | [
"MF_04070",
"PF00506"
] | [
"INFV_NCAP",
"Flu_NP"
] | [
60251,
63572
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1012",
"R-HSA-168255",
"R-HSA-168271",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168325",
"R-HSA-168330",
"R-HSA-168333",
"R-HSA-168336",
"R-HSA-192814",
"R-HSA-192823",
"R-HSA-192869",
"R-HSA-192905"
] | [
"GP:GenProp1012",
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168271",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168325",
"REACTOME:R-HSA-168330",
"REACTOME:R-HSA-168333",
... | 17 | [
"2iqh",
"2q06",
"2wfs",
"2ymn",
"3ro5",
"3tg6",
"3tj0",
"3zdp",
"4bbl",
"4dya",
"4dyb",
"4dyn",
"4dyp",
"4dys",
"4dyt",
"4iry",
"5b7b",
"5n2u",
"5tjw",
"6h9g",
"6i54",
"6i7b",
"6i7m",
"6i85",
"6j1u",
"7dkg",
"7dxp",
"7nt8",
"8pzp",
"8pzq",
"8twp",
"8twr"... | 51 | [
"PUB00006231"
] | [
"4024728"
] | [
"Sequence of the nucleoprotein gene of influenza A/parrot/Ulster/73."
] | [
1985
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Orthomyxoviridae"
] | [
8,
63564
] | 2 | [] | [] | 0 | true | Family | Influenza virus nucleoprotein (NP) | Influenza virus nucleoprotein (NP) | Flu_NP | 2 |
IPR002142 | 2,142 | Peptidase S49 | Peptidase_S49 | Domain | 31,228 | false | false | This group of serine peptidases belong to MEROPS peptidase family S49 (protease IV family, clan S-). The predicted active site serine for members of this family occurs in a transmembrane domain. Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and euka... | [
"GO:0008233",
"GO:0006508"
] | [
"peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01343"
] | [
"Peptidase_S49"
] | [
31228
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.21.-",
"PWY-7884"
] | [
"EC:3.4.21.-",
"METACYC:PWY-7884"
] | 2 | [
"3bez",
"3bf0",
"3rst",
"4kwb"
] | 4 | [
"PUB00000522",
"PUB00003576"
] | [
"8439290",
"7845208"
] | [
"Evolutionary families of peptidases.",
"Families of serine peptidases."
] | [
1993,
1994
] | 2 | [] | [
"IPR004635",
"IPR033855",
"IPR047217",
"IPR047272"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
853,
27746,
1759,
431,
439
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
2,
4,
8
] | 4 | true | Domain | Peptidase S49 | Peptidase S49 | Peptidase_S49 | 2 |
IPR002143 | 2,143 | Large ribosomal subunit protein uL1 | Ribosomal_uL1 | Family | 30,324 | false | false | Ribosomal protein uL1 (also known as L1) is the largest protein from the large ribosomal subunit. The uL1 protein contains two domains: 2-layer α/β domain and a 3-layer α/β domain (interrupts the first domain). In Escherichia coli , uL1 is known to bind to the 23S rRNA [ , , ]. Ribosomes are the particles that catalyse... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0015934"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"large ribosomal subunit"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF002155"
] | [
"Ribosomal_L1"
] | [
30324
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00922",
"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:PDOC00922",
"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 | [
"1ad2",
"1cjs",
"1dwu",
"1eg0",
"1i2a",
"1ml5",
"1mzp",
"1u63",
"1zho",
"2ftc",
"2hw8",
"2noq",
"2om7",
"2rdo",
"3j0l",
"3j0o",
"3j0p",
"3j0q",
"3j3v",
"3j3w",
"3j46",
"3j5s",
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7r",
"3j8g",
"3j9z",
"3ja1",
"3jcd",
"3jce"... | 492 | [
"PUB00000254",
"PUB00001280",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00029919",
"PUB00039425"
] | [
"8607874",
"8635468",
"11297922",
"11290319",
"11114498",
"12859903",
"16272117"
] | [
"The primary structure of rat ribosomal protein L10a.",
"Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Locking and ... | [
1996,
1996,
2001,
2001,
2000,
2003,
2005
] | 7 | [
"IPR028364"
] | [
"IPR005878",
"IPR005879",
"IPR023669"
] | 1 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
901,
23021,
5977,
425
] | 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,
2,
1,
2,
2,
2,
5,
1,
9,
6,
3,
3,
16
] | 13 | true | Family | Large ribosomal subunit protein uL1 | Large ribosomal subunit protein uL1 | Ribosomal_uL1 | 2 |
IPR002144 | 2,144 | GPCR, family 2, secretin receptor | GPCR_2_secretin_rcpt | Family | 348 | 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:0004930",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00490"
] | [
"SECRETINR"
] | [
348
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"252",
"R-HSA-418555",
"R-HSA-420092",
"R-MMU-418555",
"R-MMU-420092",
"R-RNO-420092"
] | [
"IUPHAR:252",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-420092",
"REACTOME:R-MMU-418555",
"REACTOME:R-MMU-420092",
"REACTOME:R-RNO-420092"
] | 6 | [
"6wi9",
"6wzg",
"7d3s"
] | 3 | [
"PUB00001208",
"PUB00004310",
"PUB00004961",
"PUB00005147",
"PUB00005148",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816",
"PUB00095382",
"PUB00101676",
"PUB00101679",
"PUB00101680",
"PUB00101681"
] | [
"1646711",
"1314625",
"8170923",
"1658940",
"1658941",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293",
"30449620",
"23316183",
"21777182",
"23903216",
"24359917"
] | [
"Molecular cloning and expression of a cDNA encoding the secretin receptor.",
"Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.",
"Fingerprinting G-protein-coupled receptors.",
"Expression cloning of an adenylate cyclase-coupled calcitonin receptor.",
... | [
1991,
1992,
1994,
1991,
1991,
2003,
1994,
2005,
2009,
2006,
2013,
2018,
2012,
2012,
2013,
2014
] | 16 | [
"IPR000832"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
348
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
2,
6
] | 3 | true | Family | GPCR, family 2, secretin receptor | GPCR, family 2, secretin receptor | GPCR_2_secretin_rcpt | 6 |
IPR002145 | 2,145 | Ribbon-helix-helix protein, CopG | CopG | Domain | 17,152 | false | false | The structure of this protein repressor, which is the shortest reported to date and the first isolated from a plasmid, has a homodimeric ribbon-helix-helix arrangement [ ]. The helix-turn-helix-like structure is involved in dimerisation and not DNA binding as might have been expected [ ]. | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01402"
] | [
"RHH_1"
] | [
17152
] | 1 | [] | [] | [] | 0 | [
"1b01",
"1ea4",
"1q5v",
"2bj1",
"2bj3",
"2bj7",
"2bj8",
"2bj9",
"2ca9",
"2cad",
"2caj",
"2cpg",
"2hza",
"2hzv",
"2mdv",
"2wvb",
"2wvc",
"2wvd",
"2wve",
"2wvf",
"3h87",
"3lgh",
"3od2",
"3pht",
"4me7",
"5x3t",
"6iya",
"6mrj",
"6xrw",
"7by2",
"7by3",
"7etr"... | 37 | [
"PUB00001322"
] | [
"9857196"
] | [
"The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3328,
13200,
12,
141,
471
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Ribbon-helix-helix protein, CopG | Ribbon-helix-helix protein, CopG | CopG | 4 |
IPR002146 | 2,146 | ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast | ATP_synth_b/b'su_bac/chlpt | Family | 45,443 | 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"
] | [
"MF_01398",
"PF00430"
] | [
"ATP_synth_b_bprime",
"ATP-synt_B"
] | [
43228,
45416
] | 2 | [
"GP"
] | [
"GenProp0128"
] | [
"GP:GenProp0128"
] | 1 | [
"1l2p",
"2khk",
"5t4o",
"5t4p",
"5t4q",
"6fkf",
"6fkh",
"6fki",
"6n2d",
"6n2y",
"6n2z",
"6n30",
"6oqr",
"6oqs",
"6oqt",
"6oqu",
"6oqv",
"6oqw",
"6pqv",
"6vm1",
"6vm4",
"6vmb",
"6vmg",
"6vof",
"6voh",
"6voj",
"6vol",
"6von",
"6vwk",
"6wnq",
"6wnr",
"7jg5"... | 105 | [
"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 | [] | [
"IPR005864",
"IPR017707",
"IPR034679"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
29254,
15546,
29,
614
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
1,
8,
9
] | 4 | true | Family | ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast | ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast | ATP_synth_b/b'su_bac/chlpt | 1 |
IPR002147 | 2,147 | 5-Hydroxytryptamine 1B receptor | 5HT1B_rcpt | Family | 838 | 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:0007268",
"GO:0042310",
"GO:0046849",
"GO:0050795",
"GO:0005886"
] | [
"G protein-coupled serotonin receptor activity",
"G protein-coupled receptor signaling pathway",
"chemical synaptic transmission",
"vasoconstriction",
"bone remodeling",
"regulation of behavior",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 7 | [
"PRINTS"
] | [
"PR00513"
] | [
"5HT1BRECEPTR"
] | [
838
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2",
"R-CFA-390666",
"R-CFA-418594",
"R-HSA-390666",
"R-HSA-418594",
"R-MMU-390666",
"R-MMU-418594",
"R-RNO-390666",
"R-RNO-418594"
] | [
"IUPHAR:2",
"REACTOME:R-CFA-390666",
"REACTOME:R-CFA-418594",
"REACTOME:R-HSA-390666",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-390666",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-390666",
"REACTOME:R-RNO-418594"
] | 9 | [
"6g79"
] | 1 | [
"PUB00064376",
"PUB00064405",
"PUB00064406",
"PUB00064407",
"PUB00064408",
"PUB00064409",
"PUB00064410",
"PUB00064412",
"PUB00064413",
"PUB00064414",
"PUB00066696",
"PUB00066697",
"PUB00066704"
] | [
"18476671",
"20945968",
"1578282",
"10234032",
"11080193",
"8091214",
"15380839",
"10193663",
"12052194",
"19041748",
"9559931",
"9453271",
"11989819"
] | [
"Serotonin receptors.",
"Serotonin receptors - from molecular biology to clinical applications.",
"5-hydroxytryptamine1B receptors block the GABAB synaptic potential in rat dopamine neurons.",
"5-HT1B receptor-mediated presynaptic inhibition of retinal input to the suprachiasmatic nucleus.",
"Altered seroto... | [
2008,
2011,
1992,
1999,
2000,
1994,
2004,
1999,
2002,
2008,
1998,
1997,
2002
] | 13 | [
"IPR002231"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
838
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
2
] | 4 | true | Family | 5-Hydroxytryptamine 1B receptor | 5-Hydroxytryptamine 1B receptor | 5HT1B_rcpt | 7 |
IPR002148 | 2,148 | Rotavirus non-structural protein 1 | Rotavirus_NSP1 | Family | 3,603 | false | false | The proteins in this family are non-structural protein 1 (NSP1), also known as non-structural RNA-binding protein 53(NS53). They are RNA binding proteins that contain a characteristic cysteine rich region [ , ]. They are made at low levels in infected cells and are a component of early replication and are known to accu... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM"
] | [
"MF_04088",
"PF00981"
] | [
"ROTA_NSP1",
"Rota_NS53"
] | [
3471,
3578
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000172",
"PUB00005593"
] | [
"9015101",
"8395125"
] | [
"Structure and function of rotavirus NSP1.",
"Comparative analysis of the rotavirus NS53 gene: conservation of basic and cysteine-rich regions in the protein and possible stem-loop structures in the RNA."
] | [
1996,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Rotavirus"
] | [
3603
] | 1 | [] | [] | 0 | true | Family | Rotavirus non-structural protein 1 | Rotavirus non-structural protein 1 | Rotavirus_NSP1 | 9 |
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