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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000807 | 807 | Imidazoleglycerol-phosphate dehydratase | ImidazoleglycerolP_deHydtase | Family | 25,868 | false | false | Imidazoleglycerol-phosphate dehydratase (IGPD; ) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by... | [
"GO:0004424",
"GO:0000105"
] | [
"imidazoleglycerol-phosphate dehydratase activity",
"L-histidine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"CDD"
] | [
"MF_00076",
"PF00475",
"PTHR23133",
"cd07914"
] | [
"HisB",
"IGPD",
"",
"IGPD"
] | [
24811,
25828,
25762,
24946
] | 4 | [
"EC",
"GP",
"PROSITEDOC"
] | [
"4.2.1.19",
"GenProp0109",
"PDOC00738"
] | [
"EC:4.2.1.19",
"GP:GenProp0109",
"PROSITEDOC:PDOC00738"
] | 3 | [
"1rhy",
"2ae8",
"2f1d",
"4gqu",
"4lom",
"4lpf",
"4mu0",
"4mu1",
"4mu3",
"4mu4",
"4qnj",
"4qnk",
"5dnl",
"5dnx",
"5ekw",
"5el9",
"5elw",
"5xds",
"5zqn",
"6ezj",
"6ezm",
"6fwh",
"6khh",
"6yjh",
"7ddv",
"7dnq",
"7fcy",
"7oj5",
"8qav",
"8qaw",
"8qax",
"8qay"... | 36 | [
"PUB00009674",
"PUB00022600",
"PUB00040491",
"PUB00046135",
"PUB00079788",
"PUB00079789",
"PUB00079790",
"PUB00079791",
"PUB00079792",
"PUB00079793",
"PUB00079794",
"PUB00079795"
] | [
"3007936",
"14724278",
"16338409",
"15042344",
"10885480",
"16511155",
"10450980",
"8066131",
"3001645",
"9767718",
"8511965",
"2664449"
] | [
"Gene structure in the histidine operon of Escherichia coli. Identification and nucleotide sequence of the hisB gene.",
"Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold.",
"Structure and mechanism of imidazoleglycerol-phosphate dehydratase.",
"Molecular evolution ... | [
1986,
2004,
2005,
2004,
2000,
2005,
1999,
1994,
1985,
1998,
1993,
1989
] | 12 | [] | [
"IPR020566"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
800,
21607,
2949,
512
] | 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"
] | [
11,
1,
1,
4,
1,
1,
11
] | 7 | true | Family | Imidazoleglycerol-phosphate dehydratase | Imidazoleglycerol-phosphate dehydratase | ImidazoleglycerolP_deHydtase | 3 |
IPR000808 | 808 | Iron-sulfur cluster carrier protein-like, conserved site | Mrp-like_CS | Conserved_site | 29,214 | false | false | This entry represents a conserved region found in Iron-sulfur cluster carrier protein from Escherichia coli protein (Mrp), a 41kDa ATP-binding protein of unknown function, and other Fe-S cluster protein sequences spread among all cellular organisms. Homologues are present in other bacteria including Bacillus subtilis y... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01215"
] | [
"MRP"
] | [
29214
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00935",
"R-DME-6799198",
"R-HSA-2564830",
"R-HSA-6799198",
"R-MMU-6799198"
] | [
"PROSITEDOC:PDOC00935",
"REACTOME:R-DME-6799198",
"REACTOME:R-HSA-2564830",
"REACTOME:R-HSA-6799198",
"REACTOME:R-MMU-6799198"
] | 5 | [
"3kb1",
"6g2g",
"6oby",
"8zkc"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
918,
17987,
9935,
374
] | 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,
4,
2,
1,
15,
7,
1,
4,
12,
2,
2,
15
] | 13 | true | Conserved_site | Iron-sulfur cluster carrier protein-like, conserved site | Iron-sulfur cluster carrier protein-like, conserved site | Mrp-like_CS | 8 |
IPR000810 | 810 | Cannabinoid receptor type 1 | Canbinoid_rcpt_1 | Family | 1,273 | false | false | Cannabinoid receptors are a class of cell membrane receptors that belong to the rhodopsin-like G-protein coupled receptor (GPCR) family [ , , ]. Typical of G protein-coupled receptors, cannabinoid receptors contain seven transmembrane spanning domains [ ]. Cannabinoid receptors are activated by three major groups of li... | [
"GO:0004949",
"GO:0007186",
"GO:0016020"
] | [
"cannabinoid receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS",
"CDD"
] | [
"PIRSF037995",
"PR00522",
"cd15340"
] | [
"Cnoid_rcpt_1",
"CANABINOID1R",
"7tmA_CB1"
] | [
707,
1271,
718
] | 3 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"56",
"R-HSA-373076",
"R-HSA-418594",
"R-MMU-373076",
"R-MMU-418594",
"R-RNO-373076",
"R-RNO-418594"
] | [
"IUPHAR:56",
"REACTOME:R-HSA-373076",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-373076",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-373076",
"REACTOME:R-RNO-418594"
] | 7 | [
"5u09",
"6kpg",
"6kqi",
"6n4b",
"7wv9",
"8gag",
"8ghv",
"8ikg",
"8ikh",
"8k8j",
"8wrz",
"8wu1",
"9b54",
"9b65",
"9dgi",
"9ego",
"9erx"
] | 17 | [
"PUB00068045",
"PUB00068114",
"PUB00068115",
"PUB00068116",
"PUB00068117",
"PUB00068118",
"PUB00068119",
"PUB00068120",
"PUB00068121",
"PUB00068122",
"PUB00068123",
"PUB00068124",
"PUB00068125",
"PUB00068126",
"PUB00068127",
"PUB00068128",
"PUB00068129",
"PUB00068130",
"PUB000681... | [
"21079038",
"12432948",
"18426493",
"19273110",
"6268916",
"5538858",
"7565624",
"2165569",
"7689702",
"2308954",
"1504787",
"12037135",
"9336020",
"8819477",
"9721036",
"1604713",
"3520605",
"12182960",
"11854768",
"23108552",
"10611417",
"16911322",
"19630708",
"12871... | [
"International Union of Basic and Clinical Pharmacology. LXXIX. Cannabinoid receptors and their ligands: beyond CB₁ and CB₂.",
"The cannabinoid receptors.",
"Cannabinoid receptors: where they are and what they do.",
"Cannabinoid receptors: a brief history and \"what's hot\".",
"Behavioral comparisons of the... | [
2010,
2002,
2008,
2009,
1981,
1971,
1995,
1990,
1993,
1990,
1992,
2002,
1997,
1996,
1998,
1992,
1986,
2002,
2001,
2012,
1999,
2006,
2008,
2003,
2002,
2005
] | 26 | [
"IPR002230"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1273
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
6,
3,
3
] | 4 | true | Family | Cannabinoid receptor type 1 | Cannabinoid receptor type 1 | Canbinoid_rcpt_1 | 3 |
IPR000811 | 811 | Glycosyl transferase, family 35 | Glyco_trans_35 | Family | 34,427 | false | false | The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas... | [
"GO:0008184",
"GO:0005975"
] | [
"glycogen phosphorylase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF00343",
"PIRSF000460",
"PTHR11468"
] | [
"Phosphorylase",
"Pprylas_GlgP",
""
] | [
34243,
28363,
26839
] | 3 | [
"CAZY",
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GT35",
"2.4.1.1",
"GenProp1259",
"GenProp1412",
"PWY-5941",
"PWY-6731",
"PWY-6737",
"PWY-7238",
"PDOC00095",
"R-BTA-6798695",
"R-BTA-70221",
"R-DDI-6798695",
"R-DDI-70221",
"R-DME-70221",
"R-HSA-6798695",
"R-HSA-70221",
"R-MMU-6798695",
"R-MMU-70221",
"R-RNO-6798695",
"R-RNO-7... | [
"CAZY:GT35",
"EC:2.4.1.1",
"GP:GenProp1259",
"GP:GenProp1412",
"METACYC:PWY-5941",
"METACYC:PWY-6731",
"METACYC:PWY-6737",
"METACYC:PWY-7238",
"PROSITEDOC:PDOC00095",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70221",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-70221",
"REACTOME:R-DME-70221",... | 22 | [
"1a8i",
"1abb",
"1ahp",
"1axr",
"1b4d",
"1bx3",
"1c50",
"1c8k",
"1c8l",
"1e1y",
"1e4o",
"1em6",
"1exv",
"1fa9",
"1fc0",
"1fs4",
"1ftq",
"1ftw",
"1fty",
"1fu4",
"1fu7",
"1fu8",
"1gfz",
"1gg8",
"1ggn",
"1gpa",
"1gpb",
"1gpy",
"1h5u",
"1hlf",
"1k06",
"1k08"... | 279 | [
"PUB00006243",
"PUB00006246",
"PUB00006354",
"PUB00006436",
"PUB00009409"
] | [
"2667896",
"2182117",
"8798388",
"10077830",
"9334165"
] | [
"The family of glycogen phosphorylases: structure and function.",
"The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis.",
"Role of the active site gate of glycogen phosphorylase in allosteric inhibition and substrate binding.",
"Bacterial alpha-glucan phosphorylases.",
"A classification o... | [
1989,
1990,
1996,
1999,
1997
] | 5 | [] | [
"IPR011833",
"IPR011834"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
306,
22031,
11752,
4,
334
] | 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",... | [
11,
4,
9,
2,
2,
14,
14,
1,
9,
22,
1,
23
] | 12 | true | Family | Glycosyl transferase, family 35 | Glycosyl transferase, family 35 | Glyco_trans_35 | 4 |
IPR000812 | 812 | Transcription factor TFIIB | TFIIB | Family | 19,464 | false | false | In eukaryotes, transcription initiation by polymerase II is modulated by both general and specific transcription factors. The general factors (which include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIG and TFIIH) operate through common promoter elements, such as the TATA box. Transcription factor IIB (TFIIB) is of central ... | [
"GO:0006352",
"GO:0070897"
] | [
"DNA-templated transcription initiation",
"transcription preinitiation complex assembly"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PRINTS",
"PANTHER"
] | [
"PR00685",
"PTHR11618"
] | [
"TIFACTORIIB",
""
] | [
16049,
18825
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00624",
"R-BTA-76071",
"R-CEL-674695",
"R-CEL-6807505",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-DME-674695",
"R-DME-6807505",
"R-DME-73776",
"R-DME-73779",
"R-... | [
"PROSITEDOC:PDOC00624",
"REACTOME:R-BTA-76071",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6807505",
"REACTOME:R-CEL-73776",
"REACTOME:R-CEL-73779",
"REACTOME:R-CEL-75953",
"REACTOME:R-CEL-76042",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-73776",
"REACTOME:R-DDI-73779",
... | 64 | [
"1ais",
"1c9b",
"1d3u",
"1dl6",
"1pft",
"1rly",
"1ro4",
"1tfb",
"1vol",
"2phg",
"3k1f",
"3k7a",
"4bbr",
"4bbs",
"4roc",
"4rod",
"4roe",
"4v1n",
"4v1o",
"5fmf",
"5fyw",
"5fz5",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5n9g",
"5oqj"... | 122 | [
"PUB00004101",
"PUB00005378",
"PUB00056255"
] | [
"1876184",
"1949150",
"11433012"
] | [
"Cloning of a human gene encoding the general transcription initiation factor IIB.",
"Transcriptional activation: enter TFIIB.",
"Comparison of the RNA polymerase III transcription machinery in Schizosaccharomyces pombe, Saccharomyces cerevisiae and human."
] | [
1991,
1991,
2001
] | 3 | [] | [
"IPR023484"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4417,
11,
14506,
77,
453
] | 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... | [
52,
3,
10,
5,
15,
8,
2,
21,
12,
2,
2,
63
] | 12 | true | Family | Transcription factor TFIIB | Transcription factor TFIIB | TFIIB | 8 |
IPR000813 | 813 | 7Fe ferredoxin | 7Fe_ferredoxin | Family | 19,042 | false | false | Ferredoxins [ ] are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions. The proteins fall into several subgroups according to the nature of their iron-sulphur cluster(s). The 7Fe ferredoxins [ , ] contain both 4Fe-4S and 3Fe-4S centres. The 4Fe-4S domain is similar to those found in ... | [
"GO:0009055"
] | [
"electron transfer activity"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00354"
] | [
"7FE8SFRDOXIN"
] | [
19042
] | 1 | [
"REACTOME"
] | [
"R-MTU-936721"
] | [
"REACTOME:R-MTU-936721"
] | 1 | [
"1a6l",
"1axq",
"1b0t",
"1b0v",
"1bc6",
"1bd6",
"1bqx",
"1bwe",
"1clf",
"1d3w",
"1dur",
"1f5b",
"1f5c",
"1fca",
"1fd2",
"1fda",
"1fdb",
"1fdd",
"1fdn",
"1fer",
"1ff2",
"1frh",
"1fri",
"1frj",
"1frk",
"1frl",
"1frm",
"1frx",
"1ftc",
"1g3o",
"1g6b",
"1gao"... | 48 | [
"PUB00000597",
"PUB00003240",
"PUB00003397"
] | [
"2106913",
"2926817",
"3932661"
] | [
"Primary structure of a 7Fe ferredoxin from Streptomyces griseus.",
"Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 A resolution.",
"New perspectives on bacterial ferredoxin evolution."
] | [
1990,
1989,
1985
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
128,
18495,
26,
392,
1
] | 5 | [] | [] | 0 | true | Family | 7Fe ferredoxin | 7Fe ferredoxin | 7Fe_ferredoxin | 1 |
IPR000814 | 814 | TATA-box binding protein | TBP | Family | 13,868 | false | false | The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [ , ]. TBP associates with a host of factors, including the general transcription factors SL1, TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiati... | [
"GO:0003677",
"GO:0006352"
] | [
"DNA binding",
"DNA-templated transcription initiation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER"
] | [
"MF_00408",
"PF00352",
"PR00686",
"PTHR10126"
] | [
"TATA_bind_prot_arch",
"TBP",
"TIFACTORIID",
""
] | [
6997,
13839,
12661,
13315
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00303",
"R-BTA-5250924",
"R-BTA-674695",
"R-BTA-6804756",
"R-BTA-6807505",
"R-BTA-73762",
"R-BTA-73772",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-73863",
"R-BTA-75953",
"R-BTA-76042",
"R-BTA-76061",
"R-BTA-76066",
"R-BTA-76071",
"R-BTA-9018519",
"R-CEL-5250924",
"R-CEL-674695",
... | [
"PROSITEDOC:PDOC00303",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-73762",
"REACTOME:R-BTA-73772",
"REACTOME:R-BTA-73776",
"REACTOME:R-BTA-73779",
"REACTOME:R-BTA-73863",
"REACTOME:R-BTA-75953",
"REACTOME:R-BTA-76042",... | 116 | [
"1ais",
"1c9b",
"1cdw",
"1d3u",
"1jfi",
"1mp9",
"1ngm",
"1nh2",
"1nvp",
"1pcz",
"1qn3",
"1qn4",
"1qn5",
"1qn6",
"1qn7",
"1qn8",
"1qn9",
"1qna",
"1qnb",
"1qnc",
"1qne",
"1rm1",
"1tba",
"1tbp",
"1tgh",
"1vok",
"1vol",
"1vtl",
"1vto",
"1ytb",
"1ytf",
"2z8u"... | 167 | [
"PUB00004136",
"PUB00017041",
"PUB00017042",
"PUB00017043"
] | [
"1436073",
"12878007",
"10974559",
"12782648"
] | [
"Crystal structure of TFIID TATA-box binding protein.",
"The genetics of TBP and TBP-related factors.",
"Control of gene expression through regulation of the TATA-binding protein.",
"Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression."
] | [
1992,
2003,
2000,
2003
] | 4 | [] | [
"IPR015445",
"IPR033710",
"IPR033711"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1725,
6,
11882,
46,
209
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
8,
2,
8,
16,
14,
11,
1,
8,
19,
1,
1,
19
] | 12 | true | Family | TATA-box binding protein | TATA-box binding protein | TBP | 7 |
IPR000816 | 816 | Peptidase C15, pyroglutamyl peptidase I | Peptidase_C15 | Family | 10,268 | false | false | This group of cysteine peptidases belong to MEROPS peptidase family C15 (pyroglutamyl peptidase I, clan CF). The type example being pyroglutamyl peptidase I of Bacillus amyloliquefaciens. There are similarities in structure between members of clan CF and members of three clans of metallopeptidases (MC, MF and MH) and a... | [
"GO:0016920",
"GO:0006508",
"GO:0005829"
] | [
"pyroglutamyl-peptidase activity",
"proteolysis",
"cytosol"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS",
"CDD"
] | [
"PIRSF015592",
"PR00706",
"cd00501"
] | [
"Prld-crbxl_pptds",
"PYROGLUPTASE",
"Peptidase_C15"
] | [
8498,
8185,
9313
] | 3 | [
"EC",
"METACYC",
"PROSITEDOC"
] | [
"3.4.19.3",
"PWY-7942",
"PDOC01036"
] | [
"EC:3.4.19.3",
"METACYC:PWY-7942",
"PROSITEDOC:PDOC01036"
] | 3 | [
"1a2z",
"1aug",
"1iof",
"1ioi",
"1iu8",
"1x10",
"1x12",
"1z8t",
"1z8w",
"1z8x",
"2df5",
"2ebj",
"2eo8",
"3giu",
"3lac",
"3rnz",
"3ro0",
"4gxh",
"4hps",
"5z40",
"5z47",
"5z48",
"6ltq"
] | 23 | [
"PUB00001639",
"PUB00002244",
"PUB00004992",
"PUB00076955"
] | [
"1353026",
"7909543",
"7824521",
"1999"
] | [
"Characterization of the pcp gene encoding the pyrrolidone carboxyl peptidase of Bacillus subtilis.",
"Characterization of the pcp gene of Pseudomonas fluorescens and of its product, pyrrolidone carboxyl peptidase (Pcp).",
"Pyrrolidone carboxyl peptidase (Pcp): an enzyme that removes pyroglutamic acid (pGlu) fr... | [
1992,
1994,
1994,
1975
] | 4 | [
"IPR016125"
] | [
"IPR029762"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
169,
6197,
3864,
38
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
2,
3,
1,
4,
2,
7,
3,
7
] | 9 | true | Family | Peptidase C15, pyroglutamyl peptidase I | Peptidase C15, pyroglutamyl peptidase I | Peptidase_C15 | 3 |
IPR000817 | 817 | Prion protein | Prion | Family | 1,446 | false | false | Prion protein (PrP-c) [ , , ] is a small glycoprotein found in high quantity in the brain of animals infected with certain degenerative neurological diseases, such as sheep scrapie and bovine spongiform encephalopathy (BSE), and the human dementias Creutzfeldt-Jacob disease (CJD) and Gerstmann-Straussler syndrome (GSS)... | [
"GO:0051260",
"GO:0016020"
] | [
"protein homooligomerization",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS",
"SMART"
] | [
"PR00341",
"SM00157"
] | [
"PRION",
"PRP"
] | [
822,
1446
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00263",
"R-GGA-163125",
"R-GGA-9609523",
"R-HSA-419037",
"R-HSA-9609523",
"R-MMU-9609523",
"R-RNO-9609523",
"R-SSC-9609523"
] | [
"PROSITEDOC:PDOC00263",
"REACTOME:R-GGA-163125",
"REACTOME:R-GGA-9609523",
"REACTOME:R-HSA-419037",
"REACTOME:R-HSA-9609523",
"REACTOME:R-MMU-9609523",
"REACTOME:R-RNO-9609523",
"REACTOME:R-SSC-9609523"
] | 8 | [
"1ag2",
"1b10",
"1dwy",
"1dwz",
"1dx0",
"1dx1",
"1e1g",
"1e1j",
"1e1p",
"1e1s",
"1e1u",
"1e1w",
"1fkc",
"1fo7",
"1h0l",
"1hjm",
"1hjn",
"1i4m",
"1qlx",
"1qlz",
"1qm0",
"1qm1",
"1qm2",
"1qm3",
"1tpx",
"1tqb",
"1tqc",
"1uw3",
"1xyj",
"1xyk",
"1xyq",
"1xyu"... | 113 | [
"PUB00000114",
"PUB00001512",
"PUB00005333",
"PUB00009996"
] | [
"2572197",
"1916104",
"2908696",
"12354606"
] | [
"Scrapie prions.",
"Prions and prion proteins.",
"The scrapie agent and the prion hypothesis.",
"Prion diseases: pathogenesis and public health concerns."
] | [
1989,
1991,
1988,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Euteleostomi"
] | [
1446
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
7,
2
] | 3 | true | Family | Prion protein | Prion protein | Prion | 9 |
IPR000818 | 818 | TEA/ATTS domain | TEA/ATTS_dom | Domain | 9,601 | false | false | The TEA domain is a DNA-binding region of about 66 to 68 amino acids that has been named after the two proteins that originally defined the domain: TEF-1 and AbaA. The TEA domain is located toward the N-terminal of eukaryotic transcription factors of the TEA/ATTS family. It shows a three-helix bundle with a homeodomain... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF01285",
"PR00065",
"PS00554",
"PS51088",
"SM00426"
] | [
"TEA",
"TEADOMAIN",
"TEA_1",
"TEA_2",
"TEA"
] | [
9584,
7889,
6609,
9367,
9250
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00479",
"R-CEL-2032785",
"R-CEL-8951671",
"R-DME-390193",
"R-GGA-2032785",
"R-GGA-8951671",
"R-HSA-2032785",
"R-HSA-8951671",
"R-HSA-9619665",
"R-HSA-9796292",
"R-HSA-9819196",
"R-MMU-2032785",
"R-MMU-8951671"
] | [
"PROSITEDOC:PDOC00479",
"REACTOME:R-CEL-2032785",
"REACTOME:R-CEL-8951671",
"REACTOME:R-DME-390193",
"REACTOME:R-GGA-2032785",
"REACTOME:R-GGA-8951671",
"REACTOME:R-HSA-2032785",
"REACTOME:R-HSA-8951671",
"REACTOME:R-HSA-9619665",
"REACTOME:R-HSA-9796292",
"REACTOME:R-HSA-9819196",
"REACTOME:R... | 13 | [
"2hzd",
"4z8e",
"5gzb",
"5nnx",
"5no6"
] | 5 | [
"PUB00017959",
"PUB00041557",
"PUB00103734"
] | [
"8389695",
"17085591",
"27421669"
] | [
"Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1.",
"Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain.",
"An evolutionary, structural and functional overview of the mammalian TEA... | [
1993,
2006,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9601
] | 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)"
] | [
6,
17,
12,
21,
34,
1,
35,
1
] | 8 | true | Domain | TEA/ATTS domain | TEA/ATTS domain | TEA/ATTS_dom | 6 |
IPR000819 | 819 | Peptidase M17, leucyl aminopeptidase, C-terminal | Peptidase_M17_C | Domain | 38,921 | false | false | This domain is found in a group of metallopeptidases that belong to the MEROPS peptidase family M17 (leucyl aminopeptidase family, clan MF), including leucyl aminopeptidase from Bos taurus (Bovine). Aminopeptidases are exopeptidases involved in the processing and regular turnover of intracellular proteins, although the... | [
"GO:0046872",
"GO:0070006",
"GO:0006508"
] | [
"metal ion binding",
"metalloaminopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PROSITE"
] | [
"PF00883",
"PS00631"
] | [
"Peptidase_M17",
"CYTOSOL_AP"
] | [
38877,
34801
] | 2 | [
"EC",
"EC",
"EC",
"GP",
"PROSITEDOC"
] | [
"3.4.11",
"3.4.11.1",
"3.4.11.10",
"GenProp1664",
"PDOC00548"
] | [
"EC:3.4.11",
"EC:3.4.11.1",
"EC:3.4.11.10",
"GP:GenProp1664",
"PROSITEDOC:PDOC00548"
] | 5 | [
"1bll",
"1bpm",
"1bpn",
"1gyt",
"1lam",
"1lan",
"1lap",
"1lcp",
"2ewb",
"2hb6",
"2hc9",
"2j9a",
"3h8e",
"3h8f",
"3h8g",
"3ij3",
"3jru",
"3kqx",
"3kqz",
"3kr4",
"3kr5",
"3kzw",
"3pei",
"3t8w",
"4efd",
"4k3n",
"4ksi",
"4r6t",
"4r76",
"4r7m",
"4x2t",
"4zi6"... | 69 | [
"PUB00001416",
"PUB00003579",
"PUB00004713"
] | [
"1555602",
"7674922",
"2395881"
] | [
"Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.",
"Evolutionary families of metallopeptidases.",
"Molecular structure of leucine aminopeptidase at 2.7-A resolution."
] | [
1992,
1995,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
85,
28816,
9265,
3,
752
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
16,
2,
5,
14,
2,
7,
8,
3,
7,
1,
25
] | 11 | true | Domain | Peptidase M17, leucyl aminopeptidase, C-terminal | Peptidase M17, leucyl aminopeptidase, C-terminal | Peptidase_M17_C | 9 |
IPR000820 | 820 | Proto-oncogene Mas | Proto-oncogene_Mas | Family | 204 | false | false | The mas proto-oncogene was intially discovered following co-transfection with DNA isolated from a human epidermal carcinoma. It efficiently induces tumorigenicity and has weak focus-inducing activity in NIH 3T3 cells. To date, it is the only oncogene to have been sequenced that encodes a 7TM protein. The oncogene is a ... | [
"GO:0004930",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00533"
] | [
"MASONCOGENE"
] | [
204
] | 1 | [
"GP",
"REACTOME"
] | [
"GenProp2085",
"R-HSA-375276"
] | [
"GP:GenProp2085",
"REACTOME:R-HSA-375276"
] | 2 | [
"9jlc"
] | 1 | [
"PUB00063841",
"PUB00063842",
"PUB00063843"
] | [
"12829792",
"17293687",
"17214600"
] | [
"Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled receptor Mas.",
"Angiotensin-(1-7) and the renin-angiotensin system.",
"Pharmacological effects of AVE 0991, a nonpeptide angiotensin-(1-7) receptor agonist."
] | [
2003,
2007,
2006
] | 3 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Mammalia"
] | [
204
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
2
] | 3 | true | Family | Proto-oncogene Mas | Proto-oncogene Mas | Proto-oncogene_Mas | 1 |
IPR000821 | 821 | Alanine racemase | Ala_racemase | Family | 35,935 | false | false | Alanine racemase catalyses the pyridoxal-dependent conversion of L-alanine into D-alanine, a key component of bacterial peptidoglycan [ ]. In bacteria such as Escherichia coli and Salmonella typhimurium, there are two alanine racemase isoforms synthesised by the genes alr and dadX, where the first is a biosynthetic for... | [
"GO:0008784",
"GO:0006522"
] | [
"alanine racemase activity",
"alanine metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_01201",
"PR00992",
"PTHR30511",
"TIGR00492"
] | [
"Ala_racemase",
"ALARACEMASE",
"",
"alr"
] | [
29411,
32762,
35004,
31291
] | 4 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"5.1.1",
"5.1.1.1",
"GenProp1333",
"GenProp1626",
"GenProp1667",
"PWY-7383",
"PWY-8040",
"PWY-8072",
"PWY-8443",
"PDOC00332"
] | [
"EC:5.1.1",
"EC:5.1.1.1",
"GP:GenProp1333",
"GP:GenProp1626",
"GP:GenProp1667",
"METACYC:PWY-7383",
"METACYC:PWY-8040",
"METACYC:PWY-8072",
"METACYC:PWY-8443",
"PROSITEDOC:PDOC00332"
] | 10 | [
"1bd0",
"1epv",
"1ftx",
"1l6f",
"1l6g",
"1niu",
"1rcq",
"1sft",
"1vfh",
"1vfs",
"1vft",
"1xfc",
"1xqk",
"1xql",
"2dy3",
"2odo",
"2rjg",
"2rjh",
"2sfp",
"2vd8",
"2vd9",
"3b8t",
"3b8u",
"3b8v",
"3b8w",
"3co8",
"3e5p",
"3e6e",
"3ha1",
"3hur",
"3kw3",
"3oo2"... | 74 | [
"PUB00000074",
"PUB00000440",
"PUB00014409",
"PUB00014498",
"PUB00163391",
"PUB00163392",
"PUB00163393"
] | [
"2197992",
"9063881",
"10878136",
"10209740",
"20971724",
"28042035",
"37129190"
] | [
"Recent topics in pyridoxal 5'-phosphate enzyme studies.",
"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.",
"Serine and alanine racemase activities of VanT: a protein necessary for vancomycin resistance in Enterococcus gallinarum BM4174.",
"Characteri... | [
1990,
1997,
2000,
1999,
2011,
2017,
2023
] | 7 | [] | [
"IPR011248"
] | 0 | 1 | 0 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
34813,
6,
327,
31,
758
] | 5 | [
"Escherichia coli (strain K12)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2
] | 2 | true | Family | Alanine racemase | Alanine racemase | Ala_racemase | 6 |
IPR000823 | 823 | Plant peroxidase | Peroxidase_pln | Family | 49,054 | false | false | Peroxidases are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme: Fe 3+ + H 2 O 2 -->[Fe 4+ =O]R' (Compound I) + H 2 O [Fe 4+ =O]R' + substrate -->[Fe 4+ =O]R (Compound II) + oxidised substrate [Fe 4... | [
"GO:0004601",
"GO:0020037",
"GO:0006979"
] | [
"peroxidase activity",
"heme binding",
"response to oxidative stress"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"PANTHER",
"PANTHER",
"PANTHER"
] | [
"PR00461",
"PTHR31235",
"PTHR31388",
"PTHR31517"
] | [
"PLPEROXIDASE",
"",
"",
""
] | [
46753,
13273,
18325,
16983
] | 4 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.11.1.7",
"PWY-5461",
"PWY-5466",
"PWY-5469",
"PWY-6824",
"PWY-7214",
"PWY-7445",
"PWY-8249"
] | [
"EC:1.11.1.7",
"METACYC:PWY-5461",
"METACYC:PWY-5466",
"METACYC:PWY-5469",
"METACYC:PWY-6824",
"METACYC:PWY-7214",
"METACYC:PWY-7445",
"METACYC:PWY-8249"
] | 8 | [
"1atj",
"1bgp",
"1fhf",
"1gw2",
"1gwo",
"1gwt",
"1gwu",
"1gx2",
"1h55",
"1h57",
"1h58",
"1h5a",
"1h5c",
"1h5d",
"1h5e",
"1h5f",
"1h5g",
"1h5h",
"1h5i",
"1h5j",
"1h5k",
"1h5l",
"1h5m",
"1hch",
"1kzm",
"1pa2",
"1qgj",
"1qo4",
"1sch",
"1w4w",
"1w4y",
"2atj"... | 45 | [
"PUB00001259",
"PUB00005246",
"PUB00005278"
] | [
"8062820",
"7922023",
"8805539"
] | [
"Peroxidasin: a novel enzyme-matrix protein of Drosophila development.",
"Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures.",
"The crystal structure of peanut peroxidase."
] | [
1994,
1994,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
17,
49037
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
321,
494,
513
] | 3 | true | Family | Plant peroxidase | Plant peroxidase | Peroxidase_pln | 5 |
IPR000824 | 824 | Transcription attenuation protein MtrB | MtrB | Family | 1,370 | false | false | This entry represents transcription attenuation protein MtrB. MtrB is required for transcription attenuation control in the Trp operon. This trans-acting factor seems to recognise a 10 bases nucleotide sequence in the Trp leader transcript causing transcription termination. It binds the leader RNA only in presence of L... | [
"GO:0003723",
"GO:0006353",
"GO:0006355"
] | [
"RNA binding",
"DNA-templated transcription termination",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"PRINTS"
] | [
"MF_00798",
"PR00687"
] | [
"Trp_attenuator",
"TRPRNAAP"
] | [
517,
1370
] | 2 | [] | [] | [] | 0 | [
"1c9s",
"1gtf",
"1gtn",
"1qaw",
"1utd",
"1wap",
"2exs",
"2ext",
"2zcz",
"2zd0",
"2zp8",
"2zp9",
"3aqd",
"3zte",
"3zzl",
"3zzq",
"3zzs",
"4b27",
"4v4f",
"5eeu",
"5eev",
"5eew",
"5eex",
"5eey",
"5eez",
"5ef0",
"5ef1",
"5ef2",
"5ef3",
"6rvv",
"6rvw",
"8r59"... | 36 | [
"PUB00002166"
] | [
"1551827"
] | [
"The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Phytophthora kernoviae 00238/432",
"Thermococcus litoralis",
"ecological metagenomes"
] | [
1362,
1,
1,
6
] | 4 | [] | [] | 0 | true | Family | Transcription attenuation protein MtrB | Transcription attenuation protein MtrB | MtrB | 4 |
IPR000825 | 825 | SUF system FeS cluster assembly, SufBD core domain | SUF_FeS_clus_asmbl_SufBD_core | Domain | 43,190 | false | false | This entry represents the core domain of SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system [ ]. SufB accepts sulfur transferred from SufE [ ], whereas SufD may play a role in iron acquisition [ ]. This domain adopts a right-handed β-helix fold [ ]. Iron-sulphur (FeS) cl... | [
"GO:0016226"
] | [
"iron-sulfur cluster assembly"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01458"
] | [
"SUFBD_core"
] | [
43190
] | 1 | [] | [] | [] | 0 | [
"1vh4",
"2zu0",
"4dn7",
"5awf",
"5awg",
"9h78",
"9h7y",
"9hbl"
] | 8 | [
"PUB00035635",
"PUB00035639",
"PUB00035640",
"PUB00089442",
"PUB00089443",
"PUB00089444"
] | [
"16221578",
"17350000",
"15278785",
"17350958",
"20857974",
"26472926"
] | [
"How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.",
"The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA.",
"SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly.",
"SufE transfers sulfur from... | [
2005,
2007,
2004,
2007,
2010,
2015
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
1652,
38031,
2,
2538,
967
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
2,
5,
10
] | 4 | true | Domain | SUF system FeS cluster assembly, SufBD core domain | SUF system FeS cluster assembly, SufBD core domain | SUF_FeS_clus_asmbl_SufBD_core | 3 |
IPR000827 | 827 | CC chemokine, conserved site | Chemokine_CC_CS | Conserved_site | 6,442 | false | false | Many low-molecular weight factors secreted by cells including fibroblasts, macrophages and endothelial cells, in response to a variety of stimuli such as growth factors, interferons, viral transformation and bacterial products, are structurally related [ , , ]. Most members of this family of proteins seem to have mitog... | [
"GO:0008009",
"GO:0006955",
"GO:0005576"
] | [
"chemokine activity",
"immune response",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00472"
] | [
"SMALL_CYTOKINES_CC"
] | [
6442
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00434",
"R-BTA-380108",
"R-BTA-418594",
"R-CFA-380108",
"R-CFA-418594",
"R-GGA-380108",
"R-GGA-416476",
"R-GGA-418594",
"R-HSA-380108",
"R-HSA-380994",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-444473",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-9818026",
"R-MMU-380108",
"R-MMU-416... | [
"PROSITEDOC:PDOC00434",
"REACTOME:R-BTA-380108",
"REACTOME:R-BTA-418594",
"REACTOME:R-CFA-380108",
"REACTOME:R-CFA-418594",
"REACTOME:R-GGA-380108",
"REACTOME:R-GGA-416476",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-380994",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-4185... | 26 | [
"1b3a",
"1b50",
"1b53",
"1bo0",
"1cm9",
"1dok",
"1dol",
"1dom",
"1don",
"1el0",
"1eot",
"1esr",
"1g2s",
"1g2t",
"1g91",
"1ha6",
"1hfg",
"1hfn",
"1hhv",
"1hrj",
"1hum",
"1hun",
"1m8a",
"1ml0",
"1ncv",
"1nr2",
"1nr4",
"1rtn",
"1rto",
"1u4l",
"1u4m",
"1u4p"... | 115 | [
"PUB00000108",
"PUB00001499",
"PUB00004320"
] | [
"1910690",
"2687068",
"2149646"
] | [
"Properties of the novel proinflammatory supergene \"intercrine\" cytokine family.",
"Macrophage inflammatory proteins 1 and 2: members of a novel superfamily of cytokines.",
"Two burgeoning families of platelet factor 4-related proteins: mediators of the inflammatory response."
] | [
1991,
1989,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Orthoherpesviridae"
] | [
6436,
6
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
23,
36,
39,
38
] | 4 | true | Conserved_site | CC chemokine, conserved site | CC chemokine, conserved site | Chemokine_CC_CS | 1 |
IPR000828 | 828 | Monellin, A chain | Monellin_A | Family | 1 | false | false | Monellin is an intensely sweet-tasting protein derived from African berries. 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 protein thaumatin, it neither contains c... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00630"
] | [
"MONELLINA"
] | [
1
] | 1 | [] | [] | [] | 0 | [
"1krl",
"2q33",
"3mon",
"4mon"
] | 4 | [
"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, A chain | Monellin, A chain | Monellin_A | 9 |
IPR000829 | 829 | DAGK family | DAGK | Family | 15,860 | false | false | Prokaryotic diacylglycerol kinase (DAGK) and undecaprenol kinase (UDPK) constitute a family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins and exhibit an unusual structure. Escherichia coli DAGK plays an important role in recycling diacylglycerol produced as a by-p... | [
"GO:0016301",
"GO:0008654",
"GO:0016020"
] | [
"kinase activity",
"phospholipid biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROSITE",
"PANTHER"
] | [
"PF01219",
"PS01069",
"PTHR34299"
] | [
"DAGK_prokar",
"DAGK_PROKAR",
""
] | [
15858,
7208,
15773
] | 3 | [
"EC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"2.7.1.107",
"PWY-7039",
"PWY-7817",
"PDOC00820"
] | [
"EC:2.7.1.107",
"METACYC:PWY-7039",
"METACYC:PWY-7817",
"PROSITEDOC:PDOC00820"
] | 4 | [
"2kdc",
"3ze3",
"3ze4",
"3ze5",
"4bpd",
"4brb",
"4brr",
"4cjz",
"4ck0",
"4d2e",
"4up6",
"4uxw",
"4uxx",
"4uxz",
"4uyo",
"5d56",
"5d57",
"5d6i",
"5dwk",
"7dvm"
] | 20 | [
"PUB00002252",
"PUB00053893",
"PUB00080161"
] | [
"8071224",
"17535816",
"22224599"
] | [
"Membrane topology of Escherichia coli diacylglycerol kinase.",
"Identification of a soluble diacylglycerol kinase required for lipoteichoic acid production in Bacillus subtilis.",
"Prokaryotic diacylglycerol kinase and undecaprenol kinase."
] | [
1994,
2007,
2012
] | 3 | [] | [
"IPR033717",
"IPR033718"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Siphoviridae sp. ctg0K17",
"unclassified sequences"
] | [
15680,
13,
3,
1,
163
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DAGK family | DAGK family | DAGK | 8 |
IPR000831 | 831 | Trp repressor | Trp_repress | Family | 7,107 | false | false | The Trp repressor (TrpR) binds to at least five operators in the Escherichia coli genome, repressing gene expression. The operators at which it binds vary considerably in DNA sequence and location within the promoter; when bound to the Trp operon it recognises the sequence 5'-ACTAGT-3' and acts to prevent the initiatio... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01371"
] | [
"Trp_repressor"
] | [
7107
] | 1 | [] | [] | [] | 0 | [
"1co0",
"1jhg",
"1mi7",
"1rcs",
"1tro",
"1trr",
"1wrp",
"1wrs",
"1wrt",
"1zt9",
"2oz9",
"2xdi",
"3frw",
"3g1c",
"3kor",
"3ssw",
"3ssx",
"3wrp",
"5tm0",
"6ejw",
"6ejz",
"6ekp",
"6elb",
"6elf",
"6elg",
"6eni",
"6enn",
"6f7f",
"6f7g",
"6f9k",
"6fal",
"6st6"... | 34 | [
"PUB00013953"
] | [
"12475235"
] | [
"Trp repressor-operator binding: NMR and electrophoretic mobility shift studies of the effect of DNA sequence and corepressor binding on two Trp repressor-operator complexes."
] | [
2002
] | 1 | [] | [
"IPR013335",
"IPR013368"
] | 0 | 2 | 0 | [
"Bacteria",
"Candidatus Marsarchaeota",
"Opisthokonta",
"unclassified sequences"
] | [
7044,
2,
3,
58
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Trp repressor | Trp repressor | Trp_repress | 2 |
IPR000832 | 832 | GPCR, family 2, secretin-like | GPCR_2_secretin-like | Family | 84,531 | false | false | This entry represents G-protein coupled receptor 2 family. The secretin-like GPCRs include secretin [ ], calcitonin [ ], parathyroid hormone/parathyroid hormone-related peptides [ ] and vasoactive intestinal peptide [ ], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These recepto... | [
"GO:0004930",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF00002",
"PR00249"
] | [
"7tm_2",
"GPCRSECRETIN"
] | [
84322,
65434
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00559",
"R-BTA-418555",
"R-BTA-420092",
"R-CEL-419812",
"R-CFA-373080",
"R-DME-350368",
"R-DME-350376",
"R-DME-350379",
"R-DME-350411",
"R-DME-350480",
"R-DME-373080",
"R-DME-450728",
"R-DME-6798695",
"R-DRE-419812",
"R-DRE-9619665",
"R-HSA-163359",
"R-HSA-187024",
"R-HSA-3730... | [
"PROSITEDOC:PDOC00559",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-420092",
"REACTOME:R-CEL-419812",
"REACTOME:R-CFA-373080",
"REACTOME:R-DME-350368",
"REACTOME:R-DME-350376",
"REACTOME:R-DME-350379",
"REACTOME:R-DME-350411",
"REACTOME:R-DME-350480",
"REACTOME:R-DME-373080",
"REACTOME:R-DME-4507... | 52 | [
"4k5y",
"4l6r",
"4z9g",
"5ee7",
"5nx2",
"5uz7",
"5vai",
"5vew",
"5vex",
"5xez",
"5xf1",
"5yqz",
"6b3j",
"6e3y",
"6fj3",
"6kjv",
"6kk1",
"6kk7",
"6lmk",
"6lml",
"6ln2",
"6lpb",
"6m1h",
"6m1i",
"6nbf",
"6nbh",
"6nbi",
"6niy",
"6orv",
"6p9x",
"6p9y",
"6pb0"... | 214 | [
"PUB00001208",
"PUB00004310",
"PUB00004961",
"PUB00005147",
"PUB00005148",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"1646711",
"1314625",
"8170923",
"1658940",
"1658941",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"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
] | 11 | [] | [
"IPR001740",
"IPR001749",
"IPR002001",
"IPR002144",
"IPR002170",
"IPR002285",
"IPR003051",
"IPR003056",
"IPR003287",
"IPR003290",
"IPR003910",
"IPR003924",
"IPR008077",
"IPR008078"
] | 0 | 14 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
3,
73,
84449,
2,
4
] | 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"
] | [
9,
549,
51,
233,
177,
2,
261
] | 7 | true | Family | GPCR, family 2, secretin-like | GPCR, family 2, secretin-like | GPCR_2_secretin-like | 3 |
IPR000833 | 833 | Alpha-amylase inhibitor | A-amylase_inhib | Family | 582 | false | false | Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases. A crystal structure has been determined for tendamistat, the 74-amino acid inhibitor produced by Streptomyces tenda... | [
"GO:0015066"
] | [
"alpha-amylase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PIRSF",
"SMART"
] | [
"PF01356",
"PIRSF001658",
"SM00783"
] | [
"A_amylase_inhib",
"Amylase_inhib",
"A_amylase_inhib"
] | [
582,
62,
163
] | 3 | [] | [] | [] | 0 | [
"1bvn",
"1hoe",
"1ok0",
"2ait",
"2ker",
"3ait",
"4ait"
] | 7 | [
"PUB00027644"
] | [
"14501112"
] | [
"Structure of the alpha-amylase inhibitor tendamistat at 0.93 A."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
582
] | 1 | [] | [] | 0 | true | Family | Alpha-amylase inhibitor | Alpha-amylase inhibitor | A-amylase_inhib | 2 |
IPR000834 | 834 | Peptidase M14, carboxypeptidase A | Peptidase_M14 | Domain | 77,753 | false | false | This group of sequences contain a diverse range of gene families, which include metallopeptidases belonging to MEROPS peptidase family M14 (carboxypeptidase A, clan MC), subfamilies M14A and M14B. The carboxypeptidase A family can be divided into four subfamilies: M14A (carboxypeptidase A or digestive), M14B (carboxype... | [
"GO:0004181",
"GO:0008270",
"GO:0006508"
] | [
"metallocarboxypeptidase activity",
"zinc ion binding",
"proteolysis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF00246",
"PR00765",
"PS52035",
"SM00631"
] | [
"Peptidase_M14",
"CRBOXYPTASEA",
"PEPTIDASE_M14",
"Zn_pept"
] | [
75257,
33163,
71325,
52658
] | 4 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.4.17",
"GenProp1242",
"PDOC00123",
"R-BTA-2022377",
"R-BTA-977606",
"R-CEL-2022377",
"R-DME-2022377",
"R-DME-432722",
"R-HSA-163125",
"R-HSA-2022377",
"R-HSA-264876",
"R-HSA-432722",
"R-HSA-8955332",
"R-HSA-9696264",
"R-HSA-9696273",
"R-HSA-977606",
"R-HSA-9925561",
"R-MMU-16312... | [
"EC:3.4.17",
"GP:GenProp1242",
"PROSITEDOC:PDOC00123",
"REACTOME:R-BTA-2022377",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-2022377",
"REACTOME:R-DME-2022377",
"REACTOME:R-DME-432722",
"REACTOME:R-HSA-163125",
"REACTOME:R-HSA-2022377",
"REACTOME:R-HSA-264876",
"REACTOME:R-HSA-432722",
"REACTOM... | 28 | [
"1arl",
"1arm",
"1aye",
"1bav",
"1cbx",
"1cpb",
"1cps",
"1cpx",
"1dtd",
"1ee3",
"1ell",
"1elm",
"1f57",
"1h8l",
"1hdq",
"1hdu",
"1hee",
"1iy7",
"1jqg",
"1kwm",
"1m4l",
"1nsa",
"1obr",
"1pca",
"1pyt",
"1qmu",
"1uwy",
"1yme",
"1z5r",
"1zg7",
"1zg8",
"1zg9"... | 161 | [
"PUB00003201",
"PUB00003286",
"PUB00003469",
"PUB00003579",
"PUB00081427",
"PUB00081428",
"PUB00081429",
"PUB00081430",
"PUB00081431",
"PUB00091189",
"PUB00119690",
"PUB00160228"
] | [
"6887246",
"1548696",
"1449602",
"7674922",
"17244817",
"17244818",
"11083920",
"16952463",
"18602413",
"24531462",
"22645247",
"25231992"
] | [
"Refined crystal structure of carboxypeptidase A at 1.54 A resolution.",
"Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.",
"Primary structure of carboxypeptidase T: delineation of functionally re... | [
1983,
1992,
1992,
1995,
2007,
2007,
2000,
2006,
2008,
2014,
2012,
2014
] | 12 | [] | [
"IPR033810",
"IPR033842",
"IPR033843",
"IPR033849",
"IPR033850",
"IPR034224",
"IPR034232",
"IPR034248",
"IPR034253",
"IPR034269",
"IPR034274"
] | 0 | 11 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
220,
28606,
48471,
26,
430
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
24,
104,
65,
1,
94,
39,
2,
6,
90,
1,
1,
35
] | 13 | true | Domain | Peptidase M14, carboxypeptidase A | Peptidase M14, carboxypeptidase A | Peptidase_M14 | 3 |
IPR000835 | 835 | MarR-type HTH domain | HTH_MarR-typ | Domain | 296,683 | false | false | The MarR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 135 amino acids present in transcription regulators of the MarR/SlyA family, involved in the development of antibiotic resistance. The MarR family of transcription regulators is named after Escherichia coli MarR, a repressor of ge... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PFAM",
"PFAM",
"PRINTS",
"PROFILE",
"SMART"
] | [
"PF01047",
"PF12802",
"PF13463",
"PR00598",
"PS50995",
"SM00347"
] | [
"MarR",
"MarR_2",
"HTH_27",
"HTHMARR",
"HTH_MARR_2",
"HTH_MARR"
] | [
115998,
151991,
5312,
159089,
254477,
262072
] | 6 | [
"PROSITEDOC"
] | [
"PDOC00861"
] | [
"PROSITEDOC:PDOC00861"
] | 1 | [
"1jgs",
"1lj9",
"1lnw",
"1p4x",
"1s3j",
"1z91",
"1z9c",
"2a61",
"2bv6",
"2eb7",
"2eth",
"2fa5",
"2fbh",
"2fbi",
"2fbk",
"2fxa",
"2gxg",
"2hr3",
"2nnn",
"2nyx",
"2pex",
"2pfb",
"2qww",
"2rdp",
"2yr2",
"3bdd",
"3bj6",
"3bja",
"3boq",
"3bpv",
"3bpx",
"3bro"... | 200 | [
"PUB00015407",
"PUB00015408",
"PUB00015409",
"PUB00015410"
] | [
"10498949",
"10094687",
"11473263",
"12649270"
] | [
"The mar regulon: multiple resistance to antibiotics and other toxic chemicals.",
"BadR, a new MarR family member, regulates anaerobic benzoate degradation by Rhodopseudomonas palustris in concert with AadR, an Fnr family member.",
"The crystal structure of MarR, a regulator of multiple antibiotic resistance, a... | [
1999,
1999,
2001,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
3789,
290925,
172,
5,
26,
1766
] | 6 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Domain | MarR-type HTH domain | MarR-type HTH domain | HTH_MarR-typ | 9 |
IPR000836 | 836 | Phosphoribosyltransferase domain | PRTase_dom | Domain | 288,911 | false | false | This entry refers to the phosphoribosyl transferase (PRT) type I domain. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrpphosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"CDD"
] | [
"PF00156",
"PF14681",
"cd06223"
] | [
"Pribosyltran",
"UPRTase",
"PRTases_typeI"
] | [
177113,
38011,
284304
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"2.4.2",
"GenProp1268",
"GenProp1418",
"GenProp1611",
"GenProp1614",
"R-BTA-73843",
"R-BTA-74217",
"R-BTA-9748787",
"R-CEL-500753",
"R-CEL-6798695",
"R-CEL-74217",
"R-DDI-500753",
"R-DDI-73614",
"R-DDI-73843",
"R-DDI-74217",
"R-DDI-9748787",
"R-DME-500753",
"R-DME-6798695",
"R-DM... | [
"EC:2.4.2",
"GP:GenProp1268",
"GP:GenProp1418",
"GP:GenProp1611",
"GP:GenProp1614",
"REACTOME:R-BTA-73843",
"REACTOME:R-BTA-74217",
"REACTOME:R-BTA-9748787",
"REACTOME:R-CEL-500753",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-74217",
"REACTOME:R-DDI-500753",
"REACTOME:R-DDI-73614",
"REACTOM... | 53 | [
"1a3c",
"1a4x",
"1a95",
"1a96",
"1a97",
"1a98",
"1ao0",
"1bd3",
"1bd4",
"1bzy",
"1cjb",
"1d6n",
"1dbr",
"1dkr",
"1dku",
"1dqn",
"1dqp",
"1ecb",
"1ecc",
"1ecf",
"1ecg",
"1ecj",
"1fsg",
"1g2p",
"1g2q",
"1g9s",
"1g9t",
"1gph",
"1grv",
"1hgx",
"1hmp",
"1i0i"... | 335 | [
"PUB00028083",
"PUB00038074",
"PUB00046981",
"PUB00060925",
"PUB00060940",
"PUB00080233",
"PUB00080234",
"PUB00080235",
"PUB00080236",
"PUB00080237",
"PUB00080238",
"PUB00080239",
"PUB00080240"
] | [
"11751055",
"15689504",
"18399692",
"22075667",
"17143579",
"18550080",
"12808089",
"8894695",
"15096496",
"7030616",
"6105839",
"21366534",
"18535147"
] | [
"The PRT protein family.",
"Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 A resolution.",
"Structural complexes of human adenine phosphoribosyltransferase reveal novel features of the APRT catalytic mechanism.",
"Molecular, kinetic and thermodynamic ... | [
2001,
2005,
2008,
2012,
2007,
2008,
2003,
1996,
2004,
1981,
1980,
2011,
2008
] | 13 | [] | [
"IPR004467",
"IPR041688"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Birmingham IncP-alpha plasmid",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
6944,
219042,
1,
57802,
700,
4422
] | 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",... | [
100,
16,
30,
30,
8,
46,
29,
13,
54,
60,
14,
11,
165
] | 13 | true | Domain | Phosphoribosyltransferase domain | Phosphoribosyltransferase domain | PRTase_dom | 2 |
IPR000837 | 837 | AP-1 transcription factor | AP-1 | Family | 11,385 | 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 and JDP family members [ ]. They are basic leucine zipper transcription factors that play a central role in regulating gene transcription in various biological processes [ ]. This entry incl... | [
"GO:0003677",
"GO:0003700",
"GO:0006357"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"regulation of transcription by RNA polymerase II"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"PANTHER"
] | [
"PR00042",
"PTHR23351"
] | [
"LEUZIPPRFOS",
""
] | [
9589,
11060
] | 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-2559580",
"R-BTA-2871796",
"R-BTA-450341",
"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-2559580",
"R-GGA-2871796",
"R-GGA-450341",
"R-GGA-9018519",
... | [
"REACTOME:R-BTA-2559580",
"REACTOME:R-BTA-2871796",
"REACTOME:R-BTA-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-D... | 37 | [
"1a02",
"1fos",
"1s9k",
"2wt7",
"5vpa",
"5vpb",
"5vpc",
"5vpd",
"5vpe",
"5vpf",
"6uci",
"6ucl",
"6ucm",
"7ucc",
"7ucd"
] | 15 | [
"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",
"Viruses"
] | [
11038,
347
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
31,
6,
37,
24,
32
] | 6 | true | Family | AP-1 transcription factor | AP-1 transcription factor | AP-1 | 9 |
IPR000838 | 838 | RNA polymerase sigma factor 70, ECF, conserved site | RNA_pol_sigma70_ECF_CS | Conserved_site | 40,315 | false | false | The proteins in this entry are currently known to belong to this sigma factor subfamily, known as ECF; these include Pseudomonas aeruginosa algU; Myxococcus xanthus carQ; Ralstonia eutropha (Alcaligenes eutrophus) plasmid pMOL28-encoded cnrH; Escherichia coli fecI; Pseudomonas syringae hrpL; rpoE from E. coli, Salmonel... | [
"GO:0003677",
"GO:0003700",
"GO:0016987",
"GO:0006352",
"GO:0006355"
] | [
"DNA binding",
"DNA-binding transcription factor activity",
"sigma factor activity",
"DNA-templated transcription initiation",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"PROSITE"
] | [
"PS01063"
] | [
"SIGMA70_ECF"
] | [
40315
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00814"
] | [
"PROSITEDOC:PDOC00814"
] | 1 | [
"1h3l",
"1or7",
"2mao",
"2map",
"2o7g",
"4cxf",
"4lup",
"5or5",
"5uxx",
"5wuq",
"5wur",
"5zx2",
"5zx3",
"6dv9",
"6dvb",
"6dvc",
"6dvd",
"6dve",
"6in7",
"6jbq",
"6jcx",
"6jcy",
"6kon",
"6koo",
"6kop",
"6koq",
"6tye",
"6tyf",
"6tyg",
"7qh5",
"7rwi",
"8z6g"... | 32 | [
"PUB00000061",
"PUB00002181",
"PUB00004340",
"PUB00088319"
] | [
"3052291",
"1597408",
"3092189",
"25596450"
] | [
"Structure and function of bacterial sigma factors.",
"The sigma 70 family: sequence conservation and evolutionary relationships.",
"Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.",
"Plastid sigma factors: Their individual functions and regulation in transcription."... | [
1988,
1992,
1986,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteota archaeon",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
39915,
29,
1,
368,
2
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Conserved_site | RNA polymerase sigma factor 70, ECF, conserved site | RNA polymerase sigma factor 70, ECF, conserved site | RNA_pol_sigma70_ECF_CS | 3 |
IPR000839 | 839 | Porin, Oms28 type | Porin_Oms28 | Family | 31 | false | false | The outer membrane-spanning (Oms) proteins of Borrelia burgdorferi have been isolated and their porin activities characterised; 0.6-nS porin activity was found to reside in a 28kDa protein, designated Oms28 [ ]. The gene sequence of oms28 was found to encode a 257-amino-acid precursor protein with a putative 24-amino-a... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PRINTS"
] | [
"PF03532",
"PIRSF020370",
"PR01027"
] | [
"OMS28_porin",
"Porin_Oms28",
"OMS28PORIN"
] | [
25,
23,
31
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00002301"
] | [
"8759855"
] | [
"Porin activity of the native and recombinant outer membrane protein Oms28 of Borrelia burgdorferi."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
31
] | 1 | [] | [] | 0 | true | Family | Porin, Oms28 type | Porin, Oms28 type | Porin_Oms28 | 3 |
IPR000840 | 840 | Gamma-retroviral matrix protein | G_retro_matrix | Domain | 1,106 | false | false | Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [ ]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01140"
] | [
"Gag_MA"
] | [
1106
] | 1 | [] | [] | [] | 0 | [
"1mn8",
"1uhu"
] | 2 | [
"PUB00014063",
"PUB00016320",
"PUB00016326",
"PUB00016327",
"PUB00055853"
] | [
"9657938",
"12876457",
"12467570",
"9740771",
"18647839"
] | [
"Retroviral matrix proteins: a structural perspective.",
"The evolution, distribution and diversity of endogenous retroviruses.",
"Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.",
"The role of v-Fgr myristoylation and the G... | [
1998,
2003,
2002,
1998,
2008
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses"
] | [
652,
454
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
25,
2
] | 3 | true | Domain | Gamma-retroviral matrix protein | Gamma-retroviral matrix protein | G_retro_matrix | 9 |
IPR000841 | 841 | Peptidase M23A, B-lytic metalloendopeptidase | Pept_M23A_Blytic | Family | 318 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [
"GO:0004222",
"GO:0006508"
] | [
"metalloendopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00933"
] | [
"BLYTICPTASE"
] | [
318
] | 1 | [] | [] | [] | 0 | [
"3it5",
"3it7",
"6ik4",
"8af1"
] | 4 | [
"PUB00002121",
"PUB00003579",
"PUB00069642"
] | [
"2228973",
"7674922",
"1597429"
] | [
"Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus.",
"Evolutionary families of metallopeptidases.",
"Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ions."
] | [
1990,
1995,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
318
] | 1 | [] | [] | 0 | true | Family | Peptidase M23A, B-lytic metalloendopeptidase | Peptidase M23A, B-lytic metalloendopeptidase | Pept_M23A_Blytic | 9 |
IPR000842 | 842 | Phosphoribosyl pyrophosphate synthetase, conserved site | PRib_PP_synth_CS | Conserved_site | 30,397 | false | false | Phosphoribosyl pyrophosphate synthetase ( ) (PRib-PP synthetase) catalyses the formation of PRib-PP from ATP and ribose 5-phosphate. PRib-PP is then used in various biosynthetic pathways, for example in the formation of purines, pyrimidines, histidine and tryptophan. PRib-PP synthetase requires inorganic phosphate and ... | [
"GO:0000287",
"GO:0004749",
"GO:0009156"
] | [
"magnesium ion binding",
"ribose phosphate diphosphokinase activity",
"ribonucleoside monophosphate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00114"
] | [
"PRPP_SYNTHASE"
] | [
30397
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.6.1",
"PDOC00105",
"R-BTA-73843",
"R-DDI-73843",
"R-HSA-73843",
"R-MMU-73843",
"R-RNO-73843",
"R-SCE-73843",
"R-SPO-73843",
"R-XTR-73843"
] | [
"EC:2.7.6.1",
"PROSITEDOC:PDOC00105",
"REACTOME:R-BTA-73843",
"REACTOME:R-DDI-73843",
"REACTOME:R-HSA-73843",
"REACTOME:R-MMU-73843",
"REACTOME:R-RNO-73843",
"REACTOME:R-SCE-73843",
"REACTOME:R-SPO-73843",
"REACTOME:R-XTR-73843"
] | 10 | [
"1dkr",
"1dku",
"1ibs",
"2h06",
"2h07",
"2h08",
"2hcr",
"3dah",
"3efh",
"3s5j",
"4f8e",
"4lyg",
"4lzn",
"4lzo",
"4m0p",
"4s2u",
"5mp7",
"6asv",
"6nfe",
"7xmu",
"7xmv",
"7xn3",
"7yk1",
"8dbc",
"8dbd",
"8dbe",
"8dbf",
"8dbg",
"8dbh",
"8dbi",
"8dbj",
"8dbk"... | 40 | [
"PUB00002493"
] | [
"2542328"
] | [
"Characterization of the Escherichia coli prsA1-encoded mutant phosphoribosylpyrophosphate synthetase identifies a divalent cation-nucleotide binding site."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
21925,
4,
8035,
7,
426
] | 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",... | [
13,
4,
4,
8,
1,
10,
9,
3,
9,
10,
5,
3,
14
] | 13 | true | Conserved_site | Phosphoribosyl pyrophosphate synthetase, conserved site | Phosphoribosyl pyrophosphate synthetase, conserved site | PRib_PP_synth_CS | 9 |
IPR000843 | 843 | LacI-type HTH domain | HTH_LacI | Domain | 214,178 | false | false | The lacI-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 residues present in the lacI/galR family of transcriptional regulators involved in metabolic regulation in prokaryotes. Most of these bacterial regulators recognize sugar-inducers. The family is named after the Escherichia coli lact... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00356",
"PR00036",
"PS50932",
"SM00354",
"cd01392"
] | [
"LacI",
"HTHLACI",
"HTH_LACI_2",
"HTH_LACI",
"HTH_LacI"
] | [
210566,
58576,
213434,
213348,
211656
] | 5 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0457",
"PDOC00366"
] | [
"GP:GenProp0457",
"PROSITEDOC:PDOC00366"
] | 2 | [
"1bdh",
"1bdi",
"1cjg",
"1efa",
"1jfs",
"1jft",
"1jh9",
"1jwl",
"1jye",
"1jyf",
"1l1m",
"1lbg",
"1lbh",
"1lbi",
"1lcc",
"1lcd",
"1lqc",
"1osl",
"1pnr",
"1pru",
"1prv",
"1qp0",
"1qp4",
"1qp7",
"1qpz",
"1qqa",
"1qqb",
"1rzr",
"1uxc",
"1uxd",
"1vpw",
"1wet"... | 81 | [
"PUB00001699",
"PUB00002732",
"PUB00005082"
] | [
"8543068",
"1639817",
"1805309"
] | [
"Phylogenetic, structural and functional analyses of the LacI-GalR family of bacterial transcription factors.",
"A family of bacterial regulators homologous to Gal and Lac repressors.",
"Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein posses... | [
1995,
1992,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
9,
213178,
9,
102,
2,
878
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
15
] | 2 | true | Domain | LacI-type HTH domain | LacI-type HTH domain | HTH_LacI | 7 |
IPR000845 | 845 | Nucleoside phosphorylase domain | Nucleoside_phosphorylase_d | Domain | 99,432 | false | false | Phosphorylases with this domain include: Purine nucleoside phosphorylase ( ) (PNP) from most bacteria (gene deoD), which catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ ]. Uridine phosphorylase ( ) (UdRPase) from bacteria (gene udp) and mammals, which catalyses the c... | [
"GO:0003824",
"GO:0009116"
] | [
"catalytic activity",
"nucleoside metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01048"
] | [
"PNP_UDP_1"
] | [
99432
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00946",
"R-BTA-1237112",
"R-CEL-1237112",
"R-CEL-73614",
"R-CEL-73621",
"R-DME-1237112",
"R-DRE-1237112",
"R-HSA-1237112",
"R-HSA-6798695",
"R-HSA-73614",
"R-HSA-73621",
"R-HSA-74217",
"R-HSA-74259",
"R-HSA-8950505",
"R-HSA-9735763",
"R-HSA-9755088",
"R-MMU-1237112",
"R-MMU-67... | [
"PROSITEDOC:PDOC00946",
"REACTOME:R-BTA-1237112",
"REACTOME:R-CEL-1237112",
"REACTOME:R-CEL-73614",
"REACTOME:R-CEL-73621",
"REACTOME:R-DME-1237112",
"REACTOME:R-DRE-1237112",
"REACTOME:R-HSA-1237112",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-73621",
"REACTOME:R-HSA-74... | 39 | [
"1a69",
"1a9o",
"1a9p",
"1a9q",
"1a9r",
"1a9s",
"1a9t",
"1b8n",
"1b8o",
"1c3x",
"1cb0",
"1cg6",
"1ecp",
"1fxu",
"1g2o",
"1i80",
"1jds",
"1jdt",
"1jdu",
"1jdv",
"1jdz",
"1je0",
"1je1",
"1jp7",
"1jpv",
"1jys",
"1k27",
"1k3f",
"1k9s",
"1lv8",
"1lvu",
"1lx7"... | 496 | [
"PUB00000256",
"PUB00000763",
"PUB00002584",
"PUB00002872",
"PUB00002902"
] | [
"8687427",
"8534998",
"2104852",
"7929153",
"7744869"
] | [
"Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA.",
"Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp.",
"Three-dimensional structure of human erythr... | [
1996,
1995,
1990,
1994,
1995
] | 5 | [] | [
"IPR047039"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1961,
70613,
25579,
36,
1243
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
4,
54,
21,
5,
30,
18,
2,
10,
13,
2,
2,
25
] | 13 | true | Domain | Nucleoside phosphorylase domain | Nucleoside phosphorylase domain | Nucleoside_phosphorylase_d | 1 |
IPR000846 | 846 | Dihydrodipicolinate reductase, N-terminal | DapB_N | Domain | 32,450 | false | false | Dihydrodipicolinate reductase catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate [ , , ]. In Escherichia coli and Mycobacterium tuberculosis, dihydrodipicolinate reductase has equal specifici... | [
"GO:0008839",
"GO:0009089"
] | [
"4-hydroxy-tetrahydrodipicolinate reductase activity",
"L-lysine biosynthetic process via diaminopimelate"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01113"
] | [
"DapB_N"
] | [
32450
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"1.17.1.8",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PDOC01000"
] | [
"EC:1.17.1.8",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"PROSITEDOC:PDOC01000"
] | 5 | [
"1arz",
"1b7g",
"1c3v",
"1cf2",
"1dih",
"1dru",
"1drv",
"1drw",
"1p9l",
"1vm6",
"1yl5",
"1yl6",
"1yl7",
"2czc",
"3ijp",
"3qy9",
"3wyb",
"3wyc",
"4f3y",
"4ywj",
"5eer",
"5ees",
"5gz1",
"5gz3",
"5gz6",
"5kt0",
"5tej",
"5tek",
"5tem",
"5ten",
"5tjy",
"5tjz"... | 49 | [
"PUB00000417",
"PUB00019387",
"PUB00019388",
"PUB00043321"
] | [
"7893645",
"8873595",
"9398235",
"18250105"
] | [
"Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase.",
"Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.",
"Three-dimensional structure of Escherichia coli dihydrodipicolinate ... | [
1995,
1996,
1997,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
1239,
28762,
1796,
1,
652
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
11,
19
] | 4 | true | Domain | Dihydrodipicolinate reductase, N-terminal | Dihydrodipicolinate reductase, N-terminal | DapB_N | 3 |
IPR000847 | 847 | LysR, HTH, N-terminal domain | LysR_HTH_N | Domain | 641,420 | false | false | This entry represents the N-terminal domain found in members of the transcription regulator LysR family. This domain acquires a helix-turn-helix fold which is known to be common in proteins that bind DNA . The LysR-type transcriptional regulators (LTTRs) form one of the largest and most diverse families of bacterial re... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00126",
"PR00039",
"PS50931"
] | [
"HTH_1",
"HTHLYSR",
"HTH_LYSR"
] | [
639332,
390356,
633403
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00043"
] | [
"PROSITEDOC:PDOC00043"
] | 1 | [
"1al3",
"1ixc",
"1iz1",
"1utb",
"1uth",
"2esn",
"2h98",
"2h99",
"2h9b",
"2uye",
"2uyf",
"3fxq",
"3fxr",
"3fxu",
"3fzj",
"3fzv",
"3hhg",
"3isp",
"3k1m",
"3k1n",
"3k1p",
"3m1e",
"3mz1",
"3szp",
"3t1b",
"4gwo",
"4ihs",
"4iht",
"4pzj",
"4x6g",
"5ae4",
"5ae5"... | 72 | [
"PUB00002150",
"PUB00002180",
"PUB00003277",
"PUB00004664",
"PUB00004739",
"PUB00117984",
"PUB00160345"
] | [
"1907267",
"1592818",
"1840615",
"3413113",
"2034653",
"12595552",
"37285554"
] | [
"rbcR [correction of rcbR], a gene coding for a member of the LysR family of transcriptional regulators, is located upstream of the expressed set of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in the photosynthetic bacterium Chromatium vinosum.",
"The Escherichia coli K-12 cyn operon is positively regul... | [
1991,
1992,
1991,
1988,
1991,
2003,
2023
] | 7 | [] | [
"IPR003725"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
467,
637120,
15,
970,
10,
2838
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
45
] | 2 | true | Domain | LysR, HTH, N-terminal domain | LysR, HTH, N-terminal domain | LysR_HTH_N | 4 |
IPR000848 | 848 | GPCR, cAMP-type | GPCR_cAMP | Domain | 390 | 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:0030552",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"cAMP binding",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00247"
] | [
"GPCRCAMP"
] | [
390
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001912",
"PUB00001913",
"PUB00004961",
"PUB00005114",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"8436297",
"8382181",
"8170923",
"3047871",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"CAR2, a prestalk cAMP receptor required for normal tip formation and late development of Dictyostelium discoideum.",
"Identification and targeted gene disruption of cAR3, a cAMP receptor subtype expressed during multicellular stages of Dictyostelium development.",
"Fingerprinting G-protein-coupled receptors.",... | [
1993,
1993,
1994,
1988,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR017981"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
390
] | 1 | [
"Danio rerio"
] | [
3
] | 1 | true | Domain | GPCR, cAMP-type | GPCR, cAMP-type | GPCR_cAMP | 2 |
IPR000851 | 851 | Small ribosomal subunit protein uS5 | Ribosomal_uS5 | Family | 39,739 | false | false | Ribosomal protein uS5 is one of the proteins from the small ribosomal subunit, and is a protein of 166 to 254 amino acid residues. In Escherichia coli, uS5 is known to be important in the assembly and function of the 30S ribosomal subunit. Mutations in uS5 have been shown to increase translational error frequencies. It... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PANTHER",
"PANTHER",
"PANTHER"
] | [
"PTHR13718",
"PTHR48277",
"PTHR48432"
] | [
"",
"",
""
] | [
10485,
27067,
2187
] | 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-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-6791226",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CEL-9937383",
"R-DDI-156827",
"R-DDI-... | [
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-6791226",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL... | 115 | [
"1dv4",
"1eg0",
"1fjg",
"1fka",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1pkp",
"1qd7",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo"... | 1,855 | [
"PUB00003665",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00080279"
] | [
"2247072",
"11297922",
"11290319",
"11114498",
"24524803"
] | [
"Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"A new system for naming ribosomal proteins."
... | [
1990,
2001,
2001,
2000,
2014
] | 5 | [] | [
"IPR005711",
"IPR005712"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
940,
23605,
14702,
492
] | 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",... | [
26,
2,
2,
3,
1,
19,
16,
2,
16,
30,
2,
2,
24
] | 13 | true | Family | Small ribosomal subunit protein uS5 | Small ribosomal subunit protein uS5 | Ribosomal_uS5 | 7 |
IPR000852 | 852 | Glycoside hydrolase, family 52 | Glyco_hydro_52 | Family | 351 | 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:0009044",
"GO:0005975"
] | [
"xylan 1,4-beta-xylosidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS"
] | [
"PF03512",
"PR00845"
] | [
"Glyco_hydro_52",
"GLHYDRLASE52"
] | [
351,
329
] | 2 | [
"CAZY"
] | [
"GH52"
] | [
"CAZY:GH52"
] | 1 | [
"4c1o",
"4c1p",
"4rhh",
"8qme"
] | 4 | [
"PUB00000142",
"PUB00004870",
"PUB00005266"
] | [
"8074507",
"7624375",
"8535779"
] | [
"Identification and characterization of clustered genes for thermostable xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus stearothermophilus 21.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of gly... | [
1994,
1995,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"mine drainage metagenome"
] | [
342,
8,
1
] | 3 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 52 | Glycoside hydrolase, family 52 | Glyco_hydro_52 | 7 |
IPR000853 | 853 | Metallothionein, family 6, nematoda | Metalthion_nemt | Family | 26 | 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 [ , , ]. The metallothionein superfamily comprises all polypeptides that resemble equine renal metallothi... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF27649",
"PR00876"
] | [
"Metalthion_nemt",
"MTNEMATODE"
] | [
22,
26
] | 2 | [] | [] | [] | 0 | [
"8ap5",
"8aq9"
] | 2 | [
"PUB00000300",
"PUB00001490",
"PUB00002813",
"PUB00003570"
] | [
"3064814",
"2959513",
"8428932",
"1779825"
] | [
"Biochemistry of metallothionein.",
"Chemistry and biochemistry of metallothionein.",
"The novel metallothionein genes of Caenorhabditis elegans. Structural organization and inducible, cell-specific expression.",
"Overview of metallothionein."
] | [
1988,
1987,
1993,
1991
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
26
] | 1 | [
"Caenorhabditis elegans"
] | [
2
] | 1 | true | Family | Metallothionein, family 6, nematoda | Metallothionein, family 6, nematoda | Metalthion_nemt | 4 |
IPR000855 | 855 | Peptidase C5, adenain | Peptidase_C5 | Family | 393 | false | false | This group of cysteine aminopeptidases belong to the peptidase family C5 (adenain family, clan CE). Several adenovirus proteins are synthesised as precursors, requiring processing by a protease before the virion is assembled [ , ]. Until recently, the adenovirus endopeptidase was classified as a serine protease, having... | [
"GO:0004197",
"GO:0006508"
] | [
"cysteine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"PIRSF",
"PRINTS"
] | [
"MF_04059",
"PF00770",
"PIRSF001218",
"PR00703"
] | [
"ADV_PRO",
"Peptidase_C5",
"Protease_ADV",
"ADVENDOPTASE"
] | [
327,
393,
331,
341
] | 4 | [
"EC"
] | [
"3.4.22.39"
] | [
"EC:3.4.22.39"
] | 1 | [
"1avp",
"1nln",
"4ekf",
"4pid",
"4pie",
"4piq",
"4pis",
"4wx4",
"4wx6",
"4wx7",
"5fgy"
] | 11 | [
"PUB00000060",
"PUB00003577",
"PUB00005559",
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00076953"
] | [
"3052288",
"7845226",
"462815",
"11517925",
"9891971",
"14725770",
"7044372"
] | [
"Viral proteinases.",
"Families of cysteine peptidases.",
"Protease of adenovirus type 2: partial characterization.",
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"T... | [
1988,
1994,
1979,
2001,
1998,
2004,
1982
] | 7 | [] | [] | 0 | 0 | null | [
"Deminuibacter soli",
"Eukaryota",
"Polisuviricotina"
] | [
1,
47,
345
] | 3 | [] | [] | 0 | true | Family | Peptidase C5, adenain | Peptidase C5, adenain | Peptidase_C5 | 5 |
IPR000857 | 857 | MyTH4 domain | MyTH4_dom | Domain | 19,776 | false | false | The microtubule-based kinesin motors and actin-based myosin motors generate movements required for intracellular trafficking, cell division, and muscle contraction. In general, these proteins consist of a motor domain that generates movement and a tail region that varies widely from class to class and is thought to med... | [
"GO:0005856"
] | [
"cytoskeleton"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00784",
"PS51016",
"SM00139"
] | [
"MyTH4",
"MYTH4",
"MyTH4"
] | [
19346,
19695,
19103
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51016",
"R-CEL-2453902",
"R-DDI-9013418",
"R-DDI-9013419",
"R-DDI-9013420",
"R-DDI-9013422",
"R-DDI-9013425",
"R-DME-2453902",
"R-HSA-2029482",
"R-HSA-2453902",
"R-HSA-373752",
"R-HSA-428543",
"R-HSA-8980692",
"R-HSA-9013026",
"R-HSA-9013106",
"R-HSA-9013148",
"R-HSA-9013149",
... | [
"PROSITEDOC:PDOC51016",
"REACTOME:R-CEL-2453902",
"REACTOME:R-DDI-9013418",
"REACTOME:R-DDI-9013419",
"REACTOME:R-DDI-9013420",
"REACTOME:R-DDI-9013422",
"REACTOME:R-DDI-9013425",
"REACTOME:R-DME-2453902",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-2453902",
"REACTOME:R-HSA-373752",
"REACTOME:R... | 38 | [
"3au4",
"3au5",
"3pvl",
"3pzd",
"5ejq",
"5ejr",
"5ejs",
"5ejy",
"5f3y",
"5mv7",
"5mv8",
"5mv9",
"5xbf"
] | 13 | [
"PUB00015330",
"PUB00015331",
"PUB00015332",
"PUB00015333",
"PUB00015337"
] | [
"11212352",
"11401444",
"1074599",
"12062040",
"15372037"
] | [
"Tails of unconventional myosins.",
"Myosin-VIIb, a novel unconventional myosin, is a constituent of microvilli in transporting epithelia.",
"[Study on the hygienic quality of raw milk received in processing plants]",
"MAX-1, a novel PH/MyTH4/FERM domain cytoplasmic protein implicated in netrin-mediated axon ... | [
1999,
2001,
1976,
2002,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobrevibacter smithii",
"organismal metagenomes"
] | [
18,
19752,
4,
2
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
5,
12,
58,
14,
47,
22,
1,
34,
36
] | 9 | true | Domain | MyTH4 domain | MyTH4 domain | MyTH4_dom | 8 |
IPR000858 | 858 | S-locus glycoprotein domain | S_locus_glycoprot_dom | Domain | 37,466 | false | false | In Brassicaceae, self-incompatible plants have a self/non-self recognition system, which involves the inability of flowering plants to achieve self-fertilisation. This is sporophytically controlled by multiple alleles at a single locus (S). There are a total of 50 different S alleles in Brassica oleracea. S-locus glyco... | [
"GO:0048544"
] | [
"recognition of pollen"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00954"
] | [
"S_locus_glycop"
] | [
37466
] | 1 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [
"5gyy",
"6kyw"
] | 2 | [
"PUB00001937"
] | [
"7672580"
] | [
"Evolutionary aspects of the S-related genes of the Brassica self-incompatibility system: synonymous and nonsynonymous base substitutions."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
37466
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
213,
295,
208
] | 3 | true | Domain | S-locus glycoprotein domain | S-locus glycoprotein domain | S_locus_glycoprot_dom | 2 |
IPR000859 | 859 | CUB domain | CUB_dom | Domain | 94,851 | false | false | The CUB domain (for complement C1r/C1s, Uegf, Bmp1) is a structural motif of approximately 110 residues found almost exclusively in extracellular and plasma membrane-associated proteins, many of which are developmentally regulated [ , ]. These proteins are involved in a diverse range of functions, including complement ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00431",
"PS01180",
"SM00042",
"cd00041"
] | [
"CUB",
"CUB",
"CUB",
"CUB"
] | [
86226,
92321,
83634,
86429
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00908",
"R-CEL-1474228",
"R-CEL-1650814",
"R-CEL-196791",
"R-CEL-2214320",
"R-CEL-6798695",
"R-DME-1474228",
"R-DME-1650814",
"R-DME-2243919",
"R-DRE-1650814",
"R-DRE-194306",
"R-DRE-2243919",
"R-DRE-399954",
"R-DRE-399956",
"R-DRE-5362798",
"R-DRE-9619665",
"R-GGA-186797",
"R... | [
"PROSITEDOC:PDOC00908",
"REACTOME:R-CEL-1474228",
"REACTOME:R-CEL-1650814",
"REACTOME:R-CEL-196791",
"REACTOME:R-CEL-2214320",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DME-1474228",
"REACTOME:R-DME-1650814",
"REACTOME:R-DME-2243919",
"REACTOME:R-DRE-1650814",
"REACTOME:R-DRE-194306",
"REACTOME:R-... | 95 | [
"1nt0",
"1nzi",
"1sfp",
"1spp",
"1szb",
"2qqk",
"2qql",
"2qqm",
"2qqo",
"2wno",
"3dem",
"3kq4",
"3pob",
"3poe",
"3pof",
"3pog",
"3poi",
"3poj",
"4aqb",
"4gz9",
"4gza",
"4lmf",
"4lor",
"4los",
"4lot",
"5cis",
"5ckm",
"5ckn",
"5ckq",
"5fws",
"5fwt",
"5fwu"... | 73 | [
"PUB00001610",
"PUB00003306",
"PUB00035659",
"PUB00035660"
] | [
"2026272",
"8510165",
"17446170",
"17335815"
] | [
"Complement components C1r/C1s, bone morphogenic protein 1 and Xenopus laevis developmentally regulated protein UVS.2 share common repeats.",
"The CUB domain. A widespread module in developmentally regulated proteins.",
"Insights into how CUB domains can exert specific functions while sharing a common fold: con... | [
1991,
1993,
2007,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
18,
917,
93883,
9,
24
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
64,
240,
74,
205,
124,
216,
1
] | 7 | true | Domain | CUB domain | CUB domain | CUB_dom | 4 |
IPR000860 | 860 | Porphobilinogen deaminase | HemC | Family | 29,582 | false | false | Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including vitamin B12, haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin [ ]. The first stage in tetrapyrrole synthesi... | [
"GO:0004418",
"GO:0033014"
] | [
"hydroxymethylbilane synthase activity",
"tetrapyrrole biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_00260",
"PIRSF001438",
"PR00151",
"PTHR11557",
"TIGR00212"
] | [
"Porphobil_deam",
"4pyrrol_synth_OHMeBilane_synth",
"PORPHBDMNASE",
"",
"hemC"
] | [
22303,
25843,
28978,
29365,
28584
] | 5 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1.61",
"GenProp0220",
"GenProp1525",
"GenProp1701",
"PWY-5188",
"PWY-5189",
"PDOC00461",
"R-BTA-189451",
"R-HSA-189451",
"R-MMU-189451",
"R-RNO-189451",
"R-SCE-189451",
"R-SPO-189451"
] | [
"EC:2.5.1.61",
"GP:GenProp0220",
"GP:GenProp1525",
"GP:GenProp1701",
"METACYC:PWY-5188",
"METACYC:PWY-5189",
"PROSITEDOC:PDOC00461",
"REACTOME:R-BTA-189451",
"REACTOME:R-HSA-189451",
"REACTOME:R-MMU-189451",
"REACTOME:R-RNO-189451",
"REACTOME:R-SCE-189451",
"REACTOME:R-SPO-189451"
] | 13 | [
"1ah5",
"1gtk",
"1pda",
"1ypn",
"2ypn",
"3ecr",
"3eq1",
"4htg",
"4mlq",
"4mlv",
"5h6o",
"5m6r",
"5m7f",
"5ov4",
"5ov5",
"5ov6",
"7aaj",
"7aak",
"7ccx",
"7ccy",
"7ccz",
"7cd0",
"8pnd"
] | 23 | [
"PUB00009744",
"PUB00025374",
"PUB00029805",
"PUB00035496",
"PUB00035498",
"PUB00035502",
"PUB00074046"
] | [
"11215515",
"12555854",
"1522882",
"17227226",
"16564539",
"16935474",
"23308205"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Time-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthase.",
"Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site.",
"Tetrapyrrole biosynthesis in higher p... | [
2000,
2003,
1992,
2007,
2006,
2006,
2013
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
760,
22644,
5794,
384
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
4,
4,
2,
1,
13,
6,
1,
2,
9,
1,
1,
13
] | 12 | true | Family | Porphobilinogen deaminase | Porphobilinogen deaminase | HemC | 4 |
IPR000863 | 863 | Sulfotransferase domain | Sulfotransferase_dom | Domain | 65,845 | false | false | This entry includes a range of sulfotransferase proteins including flavonol 3-sulfotransferase, aryl sulfotransferases, alcohol sulfotransferases, estrogen sulfotransferases and phenol-sulphate phenol sulfotransferase. These enzymes are responsible for the transfer of sulphate groups to specific compounds [ ] and funct... | [
"GO:0008146"
] | [
"sulfotransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00685"
] | [
"Sulfotransfer_1"
] | [
65845
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.8.2",
"R-BTA-156584",
"R-BTA-9753281",
"R-CEL-156584",
"R-CEL-2022928",
"R-CFA-156584",
"R-CFA-9753281",
"R-DME-2022928",
"R-DRE-156584",
"R-DRE-2022854",
"R-DRE-9753281",
"R-GGA-156584",
"R-HSA-156584",
"R-HSA-1989781",
"R-HSA-2022854",
"R-HSA-2022870",
"R-HSA-2022923",
"R-HSA-... | [
"EC:2.8.2",
"REACTOME:R-BTA-156584",
"REACTOME:R-BTA-9753281",
"REACTOME:R-CEL-156584",
"REACTOME:R-CEL-2022928",
"REACTOME:R-CFA-156584",
"REACTOME:R-CFA-9753281",
"REACTOME:R-DME-2022928",
"REACTOME:R-DRE-156584",
"REACTOME:R-DRE-2022854",
"REACTOME:R-DRE-9753281",
"REACTOME:R-GGA-156584",
... | 36 | [
"1aqu",
"1aqy",
"1bo6",
"1cjm",
"1efh",
"1fmj",
"1fml",
"1g3m",
"1hy3",
"1j99",
"1ls6",
"1nst",
"1ov4",
"1q1q",
"1q1z",
"1q20",
"1q22",
"1q44",
"1t8t",
"1t8u",
"1vkj",
"1x8j",
"1x8k",
"1x8l",
"1z28",
"1z29",
"1zd1",
"1zrh",
"2a3r",
"2ad1",
"2d06",
"2gwh"... | 92 | [
"PUB00020390",
"PUB00160471",
"PUB00160472"
] | [
"9360604",
"35197313",
"38712401"
] | [
"Crystal structure of estrogen sulphotransferase.",
"From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.",
"Polysaccharide sulfotransferases: the identification of putative sequences and respective functional characterisation."
] | [
1997,
2022,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
70,
6432,
59043,
11,
289
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
93,
6,
113,
22,
90,
88,
105,
111,
29
] | 9 | true | Domain | Sulfotransferase domain | Sulfotransferase domain | Sulfotransferase_dom | 2 |
IPR000864 | 864 | Proteinase inhibitor I13, potato inhibitor I | Prot_inh_pot1 | Family | 5,252 | false | false | This family of proteinase inhibitors belong to MEROPS inhibitor family I13, clan IG. They inhibit peptidases of the S1 ( ) and S8 ( ) families [ ]. Potato inhibitor type I sequences are not solely restricted to potatoes but are found in other plant species for example: barley endosperm chymotrypsin inhibitor [ ], and p... | [
"GO:0004867",
"GO:0009611"
] | [
"serine-type endopeptidase inhibitor activity",
"response to wounding"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROSITE",
"PANTHER"
] | [
"PF00280",
"PR00292",
"PS00285",
"PTHR33091"
] | [
"potato_inhibit",
"POTATOINHBTR",
"POTATO_INHIBITOR",
""
] | [
5171,
2854,
3349,
4565
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00257"
] | [
"PROSITEDOC:PDOC00257"
] | 1 | [
"1acb",
"1ciq",
"1cir",
"1cis",
"1coa",
"1cq4",
"1cse",
"1dwm",
"1egl",
"1egp",
"1hym",
"1lw6",
"1mee",
"1mit",
"1sbn",
"1sib",
"1tec",
"1tin",
"1tm1",
"1tm3",
"1tm4",
"1tm5",
"1tm7",
"1tmg",
"1to1",
"1to2",
"1vbw",
"1y1k",
"1y33",
"1y34",
"1y3b",
"1y3c"... | 64 | [
"PUB00001150",
"PUB00001351",
"PUB00014133"
] | [
"3519213",
"3106042",
"14705960"
] | [
"Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.",
"Nucleotide sequence of barley chymotrypsin inhibitor-2 (CI-2) and its expression in normal and high-lysine barley.",
"Evolu... | [
1986,
1987,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Mimiviridae",
"viral metagenome"
] | [
80,
5166,
3,
2,
1
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
28,
37,
59
] | 3 | true | Family | Proteinase inhibitor I13, potato inhibitor I | Proteinase inhibitor I13, potato inhibitor I | Prot_inh_pot1 | 6 |
IPR000866 | 866 | Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant | AhpC/TSA | Domain | 147,491 | false | false | Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels which mediate signal transduction in mammalian cells. Prxs can be regulated by changes to phosphorylation, redox and possibly oligomerisation states. Prxs are divided into three classes: typical 2-Cys... | [
"GO:0016209",
"GO:0016491"
] | [
"antioxidant activity",
"oxidoreductase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00578"
] | [
"AhpC-TSA"
] | [
147491
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"1.11.1",
"1.11.1.24",
"R-BTA-3299685",
"R-BTA-5628897",
"R-BTA-6798695",
"R-BTA-9818027",
"R-CEL-3299685",
"R-CEL-5628897",
"R-CEL-9818027",
"R-DDI-3299685",
"R-DDI-5628897",
"R-DDI-6798695",
"R-DDI-9818027",
"R-DME-3299685",
"R-DME-5628897",
"R-DME-9818027",
"R-GGA-3299685",
"R-G... | [
"EC:1.11.1",
"EC:1.11.1.24",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-5628897",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9818027",
"REACTOME:R-CEL-3299685",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-9818027",
"REACTOME:R-DDI-3299685",
"REACTOME:R-DDI-5628897",
"REACTOME:R-DDI-6798695",
"RE... | 47 | [
"1e2y",
"1lu4",
"1n8j",
"1prx",
"1qmv",
"1qq2",
"1st9",
"1su9",
"1we0",
"1x0r",
"1xcc",
"1xvw",
"1xxu",
"1yep",
"1yex",
"1yf0",
"1yf1",
"1zof",
"1zye",
"2a4v",
"2b5x",
"2b5y",
"2bmx",
"2c0d",
"2cv4",
"2cvb",
"2cx3",
"2cx4",
"2e2g",
"2e2m",
"2f9s",
"2h01"... | 210 | [
"PUB00010128",
"PUB00095135",
"PUB00095136"
] | [
"12517450",
"30657885",
"24424024"
] | [
"Structure, mechanism and regulation of peroxiredoxins.",
"Alkyl hydroperoxide reductase is important for oxidative stress resistance and symbiosis in Azorhizobium caulinodans.",
"The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress."
] | [
2003,
2019,
2014
] | 3 | [
"IPR013766"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3714,
119937,
21157,
10,
2673
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
26,
3,
8,
16,
2,
20,
18,
3,
10,
23,
4,
3,
18
] | 13 | true | Domain | Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant | Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant | AhpC/TSA | 7 |
IPR000867 | 867 | Insulin-like growth factor-binding protein, IGFBP | IGFBP-like | Domain | 19,821 | false | false | This entry represents insulin-like growth factors (IGF-I and IGF-II), which bind with high affinity to specific binding proteins in extracellular fluids [ , , ]. These IGF-binding proteins (IGFBP) prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IG... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00219",
"PS51323",
"SM00121"
] | [
"IGFBP",
"IGFBP_N_2",
"IB"
] | [
17826,
19317,
17374
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00194",
"R-BTA-381426",
"R-BTA-6803211",
"R-BTA-8957275",
"R-DRE-381426",
"R-GGA-381426",
"R-GGA-8957275",
"R-HSA-1474228",
"R-HSA-2032785",
"R-HSA-2559582",
"R-HSA-380994",
"R-HSA-381426",
"R-HSA-6803211",
"R-HSA-8951671",
"R-HSA-8957275",
"R-HSA-9615017",
"R-MMU-1474228",
"R... | [
"PROSITEDOC:PDOC00194",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-6803211",
"REACTOME:R-BTA-8957275",
"REACTOME:R-DRE-381426",
"REACTOME:R-GGA-381426",
"REACTOME:R-GGA-8957275",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-2032785",
"REACTOME:R-HSA-2559582",
"REACTOME:R-HSA-380994",
"REACTOME:R-HS... | 26 | [
"1boe",
"1h59",
"1wqj",
"2dsp",
"2dsq",
"2dsr",
"2jm2",
"3tjq",
"3zxb",
"3zxc",
"7ufg",
"7wrq",
"8ivd"
] | 13 | [
"PUB00003068",
"PUB00003677",
"PUB00004938",
"PUB00005642",
"PUB00013535",
"PUB00013536",
"PUB00013537",
"PUB00013538",
"PUB00013539",
"PUB00013540",
"PUB00013541",
"PUB00013542",
"PUB00015297"
] | [
"1654338",
"1309586",
"1725860",
"7680510",
"11874691",
"9822601",
"9725901",
"7519375",
"9660801",
"12379487",
"12379489",
"7504269",
"2480830"
] | [
"Connective tissue growth factor: a cysteine-rich mitogen secreted by human vascular endothelial cells is related to the SRC-induced immediate early gene product CEF-10.",
"Proviral rearrangements and overexpression of a new cellular gene (nov) in myeloblastosis-associated virus type 1-induced nephroblastomas.",
... | [
1991,
1992,
1991,
1993,
2002,
1998,
1998,
1994,
1998,
2002,
2002,
1993,
1989
] | 13 | [] | [] | 0 | 0 | null | [
"Kangiella spongicola",
"Metazoa"
] | [
1,
19820
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
52,
1,
60,
41,
61
] | 6 | true | Domain | Insulin-like growth factor-binding protein, IGFBP | Insulin-like growth factor-binding protein, IGFBP | IGFBP-like | 5 |
IPR000868 | 868 | Isochorismatase-like domain | Isochorismatase-like_dom | Domain | 102,813 | false | false | This entry represents a domain found in hydrolase enzymes that belong to the isochorismatase family, including Ureidoacrylate amidohydrolase RutB from Escherichia coli and Nicotinamidase from Saccharomyces cerevisiae. Isochorismatase (also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase) catalyses the conversion of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00857"
] | [
"Isochorismatase"
] | [
102813
] | 1 | [
"EC",
"GP",
"GP"
] | [
"3.5.1",
"GenProp1058",
"GenProp1336"
] | [
"EC:3.5.1",
"GP:GenProp1058",
"GP:GenProp1336"
] | 3 | [
"1ilw",
"1im5",
"1j2r",
"1nba",
"1nf8",
"1nf9",
"1x9g",
"1xn4",
"1yac",
"1yzv",
"2a67",
"2b34",
"2fq1",
"2h0r",
"2wt9",
"2wta",
"3eef",
"3hb7",
"3hu5",
"3irv",
"3kl2",
"3lqy",
"3mcw",
"3o90",
"3o91",
"3o92",
"3o93",
"3o94",
"3oqp",
"3ot4",
"3pl1",
"3r2j"... | 74 | [
"PUB00014434",
"PUB00100812"
] | [
"8550523",
"28647364"
] | [
"Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate.",
"Crystal structures of the isochorismatase domains from Vibrio anguillarum."
] | [
1996,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1342,
82079,
18599,
26,
767
] | 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",... | [
16,
4,
4,
3,
5,
5,
6,
3,
12,
14,
1,
1,
19
] | 13 | true | Domain | Isochorismatase-like domain | Isochorismatase-like domain | Isochorismatase-like_dom | 6 |
IPR000869 | 869 | Fungi-IV metallothionein, family 11 | Metalthion_11 | Family | 13 | 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 [ , , ]. The metallothionein superfamily comprises all polypeptides that resemble equine renal metallothi... | [
"GO:0005507"
] | [
"copper ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF02066",
"PR00874"
] | [
"Metallothio_11",
"MTFUNGIIV"
] | [
13,
13
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000300",
"PUB00001490",
"PUB00003570"
] | [
"3064814",
"2959513",
"1779825"
] | [
"Biochemistry of metallothionein.",
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein."
] | [
1988,
1987,
1991
] | 3 | [] | [] | 0 | 0 | null | [
"Yarrowia lipolytica"
] | [
13
] | 1 | [] | [] | 0 | true | Family | Fungi-IV metallothionein, family 11 | Fungi-IV metallothionein, family 11 | Metalthion_11 | 4 |
IPR000870 | 870 | Homoserine kinase | Homoserine_kinase | Family | 17,888 | false | false | Saccharomyces cerevisiae strains containing the erg8-1 mutation are temperature sensitive for growth due to a defect in phosphomevalonate kinase, an enzyme of isoprene and ergosterol biosynthesis. Subcloning and DNA sequencing have defined the functional ERG8 regulon as an 850bp upstream region and an adjacent 1,272bp ... | [
"GO:0004413",
"GO:0005524",
"GO:0006566"
] | [
"homoserine kinase activity",
"ATP binding",
"L-threonine metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00384",
"PIRSF000676",
"TIGR00191"
] | [
"Homoser_kinase",
"Homoser_kin",
"thrB"
] | [
17648,
16767,
17460
] | 3 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"2.7.1.39",
"GenProp0159",
"GenProp1358",
"PWY-702"
] | [
"EC:2.7.1.39",
"GP:GenProp0159",
"GP:GenProp1358",
"METACYC:PWY-702"
] | 4 | [
"1fwk",
"1fwl",
"1h72",
"1h73",
"1h74",
"3hul",
"4p52",
"4rpf",
"5wat",
"6cyz"
] | 10 | [
"PUB00001384",
"PUB00003676"
] | [
"2165904",
"1846667"
] | [
"Yeast homoserine kinase. Characteristics of the corresponding gene, THR1, and the purified enzyme, and evolutionary relationships with other enzymes of threonine metabolism.",
"Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase."
] | [
1990,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
595,
14489,
2549,
255
] | 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"
] | [
5,
1,
1,
3,
1,
1,
4
] | 7 | true | Family | Homoserine kinase | Homoserine kinase | Homoserine_kinase | 6 |
IPR000871 | 871 | Beta-lactamase, class-A | Beta-lactam_class-A | Family | 33,245 | false | false | Beta-lactamase catalyses the opening and hydrolysis of the beta-lactam ring of beta-lactam antibiotics such as penicillins and cephalosporins. There are four groups, classed A, B, C and D according to sequence, substrate specificity, and kinetic behaviour. Class A (penicillinase-type) is the most common [ ]. The genes ... | [
"GO:0008800",
"GO:0030655",
"GO:0046677"
] | [
"beta-lactamase activity",
"beta-lactam antibiotic catabolic process",
"response to antibiotic"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PRINTS",
"PANTHER"
] | [
"PR00118",
"PTHR35333"
] | [
"BLACTAMASEA",
""
] | [
14554,
33133
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME"
] | [
"3.5.2.6",
"PDOC00134",
"R-HSA-9913143"
] | [
"EC:3.5.2.6",
"PROSITEDOC:PDOC00134",
"REACTOME:R-HSA-9913143"
] | 3 | [
"1alq",
"1axb",
"1blc",
"1blh",
"1blp",
"1bsg",
"1bt5",
"1btl",
"1bue",
"1bul",
"1bza",
"1ck3",
"1dja",
"1djb",
"1djc",
"1dy6",
"1e25",
"1erm",
"1ero",
"1erq",
"1esu",
"1fqg",
"1g68",
"1g6a",
"1ghi",
"1ghm",
"1ghp",
"1htz",
"1hzo",
"1i2s",
"1i2w",
"1iyo"... | 781 | [
"PUB00000464",
"PUB00000477",
"PUB00003270",
"PUB00059638"
] | [
"3128280",
"2788410",
"1856867",
"19100272"
] | [
"The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.",
"The phototrophic bacterium Rhodopseudomonas capsulata sp108 encodes an indigenous class A beta-lactamase.",
"Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 A resolution and analysis... | [
1988,
1989,
1991,
2009
] | 4 | [] | [
"IPR049643",
"IPR058131",
"IPR058132",
"IPR058137",
"IPR058138",
"IPR058139",
"IPR058141",
"IPR058152",
"IPR058160",
"IPR058162",
"IPR058169",
"IPR058170",
"IPR058171",
"IPR058187",
"IPR058197",
"IPR058200",
"IPR058201",
"IPR058202",
"IPR058214",
"IPR058220"
] | 0 | 20 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
21,
32731,
91,
17,
7,
378
] | 6 | [
"Zea mays"
] | [
1
] | 1 | true | Family | Beta-lactamase, class-A | Beta-lactamase, class-A | Beta-lactam_class-A | 2 |
IPR000873 | 873 | AMP-dependent synthetase/ligase domain | AMP-dep_synth/lig_dom | Domain | 586,422 | false | false | This domain is found in a number of prokaryotic and eukaryotic enzymes, which act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ , , ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. This group of enzym... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00501"
] | [
"AMP-binding"
] | [
586422
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"6.2.1",
"GenProp1308",
"GenProp1364",
"GenProp1452",
"GenProp1462",
"GenProp1473",
"GenProp1510",
"GenProp1544",
"GenProp1562",
"GenProp1572",
"GenProp1717",
"PDOC00427",
"R-BTA-75876",
"R-BTA-77111",
"R-BTA-77289",
"R-CEL-77111",
"R-DDI-2046105",
"R-DDI-2046106",
"R-DDI-2151201... | [
"EC:6.2.1",
"GP:GenProp1308",
"GP:GenProp1364",
"GP:GenProp1452",
"GP:GenProp1462",
"GP:GenProp1473",
"GP:GenProp1510",
"GP:GenProp1544",
"GP:GenProp1562",
"GP:GenProp1572",
"GP:GenProp1717",
"PROSITEDOC:PDOC00427",
"REACTOME:R-BTA-75876",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-77289",
... | 111 | [
"1amu",
"1ba3",
"1lci",
"1md9",
"1mdb",
"1mdf",
"1pg3",
"1pg4",
"1ry2",
"1t5d",
"1t5h",
"1ult",
"1v25",
"1v26",
"2d1q",
"2d1r",
"2d1s",
"2d1t",
"2p20",
"2p2b",
"2p2f",
"2p2j",
"2p2m",
"2p2q",
"2qvx",
"2qvy",
"2qvz",
"2qw0",
"2v7b",
"2vsq",
"2vze",
"2wd9"... | 418 | [
"PUB00001189",
"PUB00002125",
"PUB00004359",
"PUB00005277",
"PUB00092576",
"PUB00097529",
"PUB00101120"
] | [
"2118102",
"2254270",
"2911486",
"8805533",
"26473393",
"27908785",
"15699031"
] | [
"The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases.",
"Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708.",
"Prote... | [
1990,
1990,
1989,
1996,
2016,
2017,
2005
] | 7 | [] | [
"IPR010071",
"IPR020459",
"IPR037337",
"IPR048005"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
7505,
389284,
183749,
1,
21,
5862
] | 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",... | [
231,
47,
112,
77,
10,
165,
101,
28,
150,
140,
10,
10,
318
] | 13 | true | Domain | AMP-dependent synthetase/ligase domain | AMP-dependent synthetase/ligase domain | AMP-dep_synth/lig_dom | 4 |
IPR000874 | 874 | Bombesin/neuromedin-B/ranatensin peptide family | Bombesin | Family | 1,496 | false | false | Bombesin-like peptides comprise a large family of peptides which were initially isolated from amphibian skin, where they stimulate smooth muscle contraction. They were later found to be widely distributed in mammalian neural and endocrine cells. The amphibian peptides which belong to this family are currently classifie... | [
"GO:0007218"
] | [
"neuropeptide signaling pathway"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROSITE",
"PANTHER"
] | [
"PF02044",
"PS00257",
"PTHR16866"
] | [
"Bombesin",
"BOMBESIN",
""
] | [
1411,
1426,
1390
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00230",
"R-BTA-375276",
"R-BTA-381771",
"R-BTA-416476",
"R-GGA-375276",
"R-GGA-381771",
"R-GGA-416476",
"R-HSA-375276",
"R-HSA-381771",
"R-HSA-416476",
"R-MMU-375276",
"R-MMU-381771",
"R-MMU-416476",
"R-RNO-375276",
"R-RNO-381771",
"R-RNO-416476",
"R-SSC-375276",
"R-SSC-381771... | [
"PROSITEDOC:PDOC00230",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381771",
"REACTOME:R-BTA-416476",
"REACTOME:R-GGA-375276",
"REACTOME:R-GGA-381771",
"REACTOME:R-GGA-416476",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-381771",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-3817... | 19 | [
"1c98",
"1c9a",
"2n0b",
"2n0c",
"2n0d",
"2n0e",
"2n0f",
"2n0g",
"2n0h",
"4ezu",
"4ezv",
"7w3z",
"8h0p",
"8h0q"
] | 14 | [
"PUB00002463",
"PUB00005958",
"PUB00005959",
"PUB00015298",
"PUB00095214",
"PUB00095215",
"PUB00101168"
] | [
"2458345",
"6141890",
"3868775",
"1726343",
"10840151",
"25796599",
"34610277"
] | [
"Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin.",
"Active peptides in the skins of one hundred amphibian species from Australia and Papua New Guinea.",
"Phyllomedusa skin: a huge factor... | [
1988,
1984,
1985,
1991,
2000,
2015,
2021
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
14,
1482
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
5,
3,
4
] | 4 | true | Family | Bombesin/neuromedin-B/ranatensin peptide family | Bombesin/neuromedin-B/ranatensin peptide family | Bombesin | 5 |
IPR000875 | 875 | Cecropin-like | CecC-like | Family | 532 | false | false | This entry represents antimicrobial peptides such as Cecropins, Sarcotoxins, Aedesins, Andropin and related protins from insects. The andropin gene is closely linked to the cecropin gene cluster of Drosophila melanogaster [ , ]. Cecropins [ , , ] are potent antibacterial proteins that constitute a main part of the cell... | [
"GO:0019731",
"GO:0005576"
] | [
"antibacterial humoral response",
"extracellular region"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00272"
] | [
"Cecropin"
] | [
532
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00241"
] | [
"PROSITEDOC:PDOC00241"
] | 1 | [
"2la2",
"2mmm"
] | 2 | [
"PUB00000112",
"PUB00000851",
"PUB00001402",
"PUB00089381",
"PUB00089384"
] | [
"3318666",
"2015623",
"1915368",
"11965438",
"1899226"
] | [
"Cell-free immunity in insects.",
"Antibacterial peptides: key components needed in immunity.",
"Cell-free immunity in Cecropia. A model system for antibacterial proteins.",
"Rapid evolution of the male-specific antibacterial protein andropin gene in Drosophila.",
"The andropin gene and its product, a male-... | [
1987,
1991,
1991,
2002,
1991
] | 5 | [] | [
"IPR020400"
] | 0 | 1 | 0 | [
"Ecdysozoa"
] | [
532
] | 1 | [
"Drosophila melanogaster"
] | [
9
] | 1 | true | Family | Cecropin-like | Cecropin-like | CecC-like | 6 |
IPR000877 | 877 | Proteinase inhibitor I12, Bowman-Birk | Prot_inh_BBI | Domain | 1,578 | false | false | This family of eukaryotic proteinase inhibitors, belongs to MEROPS inhibitor family I12, clan IF. They predominantly inhibit serine peptidases of the S1 family ( ) [ ]. They play a role in defense response against pathogens and insects, but they also have been studied as therapeutic treatment in cancer and inflammatory... | [
"GO:0004867",
"GO:0005576"
] | [
"serine-type endopeptidase inhibitor activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROSITE",
"SMART",
"CDD"
] | [
"PF00228",
"PS00281",
"SM00269",
"cd00023"
] | [
"Bowman-Birk_leg",
"BOWMAN_BIRK",
"BowB",
"BBI"
] | [
1195,
632,
1540,
1357
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00253"
] | [
"PROSITEDOC:PDOC00253"
] | 1 | [
"1bbi",
"1bi6",
"1c2a",
"1d6r",
"1g9i",
"1h34",
"1jbl",
"1jbn",
"1k9b",
"1mvz",
"1o8y",
"1o8z",
"1pbi",
"1pi2",
"1sbw",
"1sfi",
"1smf",
"1tab",
"1tx6",
"2aih",
"2bbi",
"2bi6",
"2fj8",
"2g81",
"2iln",
"2qn5",
"2r33",
"3myw",
"3p8f",
"3ru4",
"4k8y",
"4ttk"... | 38 | [
"PUB00000032",
"PUB00002332",
"PUB00014133",
"PUB00014484",
"PUB00014485",
"PUB00014486",
"PUB00078839",
"PUB00097957"
] | [
"6996568",
"3667571",
"14705960",
"11375759",
"12325158",
"12643767",
"8873479",
"33666645"
] | [
"Protein inhibitors of proteinases.",
"The complete amino acid sequence of rice bran trypsin inhibitor.",
"Evolutionary families of peptidase inhibitors.",
"Synthetic peptide mimics of the Bowman-Birk inhibitor protein.",
"Peptide mimics of the Bowman-Birk inhibitor reactive site loop.",
"The structural b... | [
1980,
1987,
2004,
2001,
2002,
2003,
1996,
2021
] | 8 | [] | [
"IPR022713"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
3,
1575
] | 2 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
34,
80
] | 2 | true | Domain | Proteinase inhibitor I12, Bowman-Birk | Proteinase inhibitor I12, Bowman-Birk | Prot_inh_BBI | 2 |
IPR000878 | 878 | Tetrapyrrole methylase | 4pyrrol_Mease | Domain | 122,240 | false | false | This entry represents a tetrapyrrole methylase domain, which consist of two non-similar subdomains [ ]. Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway [ ]. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including cobalamin (vitamin... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00590"
] | [
"TP_methylase"
] | [
122240
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1",
"GenProp1215",
"R-BTA-5358493",
"R-DDI-5358493",
"R-HSA-5358493",
"R-MMU-5358493",
"R-SCE-5358493",
"R-SPO-5358493"
] | [
"EC:2.1.1",
"GP:GenProp1215",
"REACTOME:R-BTA-5358493",
"REACTOME:R-DDI-5358493",
"REACTOME:R-HSA-5358493",
"REACTOME:R-MMU-5358493",
"REACTOME:R-SCE-5358493",
"REACTOME:R-SPO-5358493"
] | 8 | [
"1cbf",
"1pjq",
"1pjs",
"1pjt",
"1s4d",
"1v9a",
"1va0",
"1vce",
"1ve2",
"1vhv",
"1wde",
"1wng",
"2bb3",
"2cbf",
"2dek",
"2dsg",
"2dsh",
"2dsi",
"2dv3",
"2dv4",
"2dv5",
"2dv7",
"2dxv",
"2dxw",
"2dxx",
"2e07",
"2e08",
"2e0k",
"2e0n",
"2e15",
"2e16",
"2e17"... | 167 | [
"PUB00009744",
"PUB00029889",
"PUB00030902",
"PUB00035315",
"PUB00035496",
"PUB00035497"
] | [
"11215515",
"14595395",
"15522295",
"16866557",
"17227226",
"17229157"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.",
"Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of... | [
2000,
2003,
2004,
2006,
2007,
2007
] | 6 | [] | [
"IPR006362",
"IPR006363",
"IPR006364",
"IPR006366",
"IPR012818",
"IPR035013"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
4356,
108031,
8300,
1551,
2
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
1,
2,
1,
2,
1,
4,
2,
10,
3,
2,
2,
25
] | 13 | true | Domain | Tetrapyrrole methylase | Tetrapyrrole methylase | 4pyrrol_Mease | 7 |
IPR000881 | 881 | Myotoxin | Myotoxin | Family | 34 | false | false | Myotoxins are small basic peptides (42 to 45 residues) that can cause severe muscle necrosis by a non-enzymatic mechanism. They act extremely rapidly and serve two primary biological functions: limiting the flight of prey by causing instantaneous paralysis of the hind limbs and promoting rapid death by paralysis of the... | [
"GO:0044562"
] | [
"venom-mediated inhibition of voltage-gated potassium channel activity"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS",
"PROSITE"
] | [
"PF00819",
"PR00283",
"PS00459"
] | [
"Myotoxins",
"MYOTOXIN",
"MYOTOXINS_1"
] | [
34,
31,
21
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00435"
] | [
"PROSITEDOC:PDOC00435"
] | 1 | [
"1h5o",
"1z99",
"4gv5"
] | 3 | [
"PUB00001595",
"PUB00005315",
"PUB00068249",
"PUB00068251"
] | [
"2253781",
"1862521",
"22498659",
"16115660"
] | [
"A new small myotoxin from the venom of the prairie rattlesnake (Crotalus viridis viridis).",
"Amino acid sequence of a myotoxin from venom of the eastern diamondback rattlesnake (Crotalus adamanteus).",
"Crotamine pharmacology revisited: novel insights based on the inhibition of KV channels.",
"New view on c... | [
1990,
1991,
2012,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
34
] | 1 | [] | [] | 0 | true | Family | Myotoxin | Myotoxin | Myotoxin | 9 |
IPR000883 | 883 | Cytochrome c oxidase subunit I | Cyt_C_Oxase_1 | Family | 1,781,680 | false | false | Cytochrome c oxidase ( ) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxida... | [
"GO:0004129",
"GO:0020037",
"GO:0009060",
"GO:0016020"
] | [
"cytochrome-c oxidase activity",
"heme binding",
"aerobic respiration",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00115",
"PR01165",
"PTHR10422"
] | [
"COX1",
"CYCOXIDASEI",
""
] | [
1780179,
1743369,
1780090
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"7.1.1.9",
"GenProp1256",
"GenProp1367",
"GenProp1401",
"GenProp1426",
"GenProp1493",
"GenProp1563",
"GenProp1637",
"GenProp1641",
"GenProp1751",
"PWY-3781",
"PWY-4521",
"PWY-6692",
"PWY-7279",
"PWY-7429",
"PWY-8271",
"PDOC00074",
"R-CEL-5419276",
"R-CEL-9837999",
"R-CEL-986484... | [
"EC:7.1.1.9",
"GP:GenProp1256",
"GP:GenProp1367",
"GP:GenProp1401",
"GP:GenProp1426",
"GP:GenProp1493",
"GP:GenProp1563",
"GP:GenProp1637",
"GP:GenProp1641",
"GP:GenProp1751",
"METACYC:PWY-3781",
"METACYC:PWY-4521",
"METACYC:PWY-6692",
"METACYC:PWY-7279",
"METACYC:PWY-7429",
"METACYC:P... | 62 | [
"1ar1",
"1ehk",
"1fft",
"1m56",
"1m57",
"1occ",
"1oco",
"1ocr",
"1ocz",
"1qle",
"1v54",
"1v55",
"1xme",
"2dyr",
"2dys",
"2eij",
"2eik",
"2eil",
"2eim",
"2ein",
"2gsm",
"2occ",
"2qpd",
"2qpe",
"2y69",
"2ybb",
"2yev",
"2zxw",
"3abk",
"3abl",
"3abm",
"3ag1"... | 270 | [
"PUB00000581",
"PUB00001153",
"PUB00001256",
"PUB00002253",
"PUB00006485"
] | [
"6307356",
"2824194",
"8013452",
"8083153",
"8049679"
] | [
"Structure of cytochrome c oxidase.",
"Structural models of the redox centres in cytochrome oxidase.",
"Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen.",
"The superfamily of heme-copper respiratory oxidases.",
"The proton pump of heme-copper oxidases."
] | [
1983,
1987,
1994,
1994,
1994
] | 5 | [] | [
"IPR004677",
"IPR014207",
"IPR014233",
"IPR014241",
"IPR033943"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Flavobacterium phage 6H",
"unclassified sequences"
] | [
1718,
53017,
1725216,
1,
1728
] | 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,
8,
2,
58,
1,
1122,
54,
1,
4,
37,
5,
1,
3
] | 13 | true | Family | Cytochrome c oxidase subunit I | Cytochrome c oxidase subunit I | Cyt_C_Oxase_1 | 2 |
IPR000884 | 884 | Thrombospondin type-1 (TSP1) repeat | TSP1_rpt | Repeat | 109,049 | false | false | This repeat was first described in 1986 by Lawler and Hynes [ ]. It was found in the thrombospondin protein where it is repeated 3 times. Now a number of proteins involved in the complement pathway (properdin, C6, C7, C8A, C8B, C9) [ ] as well as extracellular matrix protein like mindin, F-spondin [ ], SCO-spondin and ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00090",
"PS50092",
"SM00209"
] | [
"TSP_1",
"TSP1",
"TSP1"
] | [
80228,
108415,
101044
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50092",
"R-BTA-1650814",
"R-BTA-166665",
"R-BTA-4641263",
"R-BTA-5173214",
"R-BTA-977606",
"R-CEL-373752",
"R-CEL-418886",
"R-CEL-5173214",
"R-DME-373752",
"R-DME-416700",
"R-DME-418886",
"R-DME-5173214",
"R-DRE-4641263",
"R-DRE-5173214",
"R-GGA-381426",
"R-GGA-8957275",
"R-HS... | [
"PROSITEDOC:PDOC50092",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-4641263",
"REACTOME:R-BTA-5173214",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-373752",
"REACTOME:R-CEL-418886",
"REACTOME:R-CEL-5173214",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-416700",
"REACTOME:R-DME-... | 72 | [
"1lsl",
"1szl",
"1vex",
"1w0r",
"1w0s",
"2bbx",
"2rjq",
"3ghm",
"3ghn",
"3ojy",
"3r6b",
"3t5o",
"3vdj",
"3vdk",
"3vdl",
"3vn4",
"4a5w",
"4e0s",
"4hqf",
"4hql",
"4hqn",
"4hqo",
"4okr",
"4oku",
"4v2a",
"5fmw",
"5foe",
"5ftt",
"6b0s",
"6cxo",
"6dlw",
"6h03"... | 90 | [
"PUB00003230",
"PUB00006208",
"PUB00006209",
"PUB00006210",
"PUB00006211",
"PUB00006212",
"PUB00006213",
"PUB00006214",
"PUB00006215",
"PUB00043707"
] | [
"2459396",
"2430973",
"10508153",
"1501644",
"1417780",
"1868073",
"10409509",
"9135017",
"10500044",
"11687483"
] | [
"Detecting distant homologies of mosaic proteins. Analysis of the sequences of thrombomodulin, thrombospondin complement components C9, C8 alpha and C8 beta, vitronectin and plasma cell membrane glycoprotein PC-1.",
"The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sit... | [
1988,
1986,
1999,
1992,
1992,
1991,
1999,
1997,
1999,
2001
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
114,
3,
108898,
8,
26
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
55,
339,
42,
215,
191,
3,
228,
5
] | 8 | true | Repeat | Thrombospondin type-1 (TSP1) repeat | Thrombospondin type-1 (TSP1) repeat | TSP1_rpt | 2 |
IPR000885 | 885 | Fibrillar collagen, C-terminal | Fib_collagen_C | Domain | 16,614 | false | false | This entry represents the C-terminal non-collagenous domain of animal fibrillar collagens, also named C-propeptide, which is highly conserved from invertebrates to vertebrates (types I-III, V, XI, XXIV and XXVII) [ , , , ]. This domain is involved in both intracellular molecular assembly and extracellular formation of ... | [
"GO:0005201"
] | [
"extracellular matrix structural constituent"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01410",
"PS51461",
"SM00038"
] | [
"COLFI",
"NC1_FIB",
"COLFI"
] | [
16531,
15922,
15400
] | 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-114604",
"R-BTA-1442490",
"R-BTA-1566977",
"R-BTA-1650814",
"R-BTA-186797",
"R-BTA-198933",
"R-BTA-2022090",
"R-BTA-202733",
"R-BTA-216083",
"R-BTA-2243919",
"R-BTA-3000171",
"R-BTA-3000178",
"R-BTA-430116",
"R-BTA-75892",
"R-BTA-76009",
"R-BTA-8874081",
"R-BTA-8948216",
"R-... | [
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1566977",
"REACTOME:R-BTA-1650814",
"REACTOME:R-BTA-186797",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-2022090",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2243919",
"REACTOME:R-BTA-3000171",
"REACTOME:R-B... | 98 | [
"4ae2",
"4aej",
"4ak3",
"5k31",
"6fzv",
"6fzw",
"7e7b",
"7e7d"
] | 8 | [
"PUB00001643",
"PUB00062576",
"PUB00103963",
"PUB00103964",
"PUB00103965",
"PUB00103966"
] | [
"1639194",
"23027749",
"31243143",
"9210465",
"12766169",
"10936452"
] | [
"The modular architecture of vertebrate collagens.",
"Production and crystallization of the C-propeptide trimer from human procollagen III.",
"Roles of the procollagen C-propeptides in health and disease.",
"Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate... | [
1992,
2012,
2019,
1997,
2003,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Ahtivirus sagseatwo",
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota"
] | [
6,
22,
1,
16585
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
64,
50,
39,
70
] | 4 | true | Domain | Fibrillar collagen, C-terminal | Fibrillar collagen, C-terminal | Fib_collagen_C | 3 |
IPR000887 | 887 | KDPG/KHG aldolase | Aldlse_KDPG_KHG | Family | 28,466 | false | false | 4-Hydroxy-2-oxoglutarate aldolase ( ) (KHG-aldolase) catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. Phospho-2-dehydro-3-deoxygluconate aldolase ( ) (KDPG-aldolase) catalyzes the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phospha... | [
"GO:0016829"
] | [
"lyase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PF01081",
"PTHR30246",
"TIGR01182",
"cd00452"
] | [
"Aldolase",
"",
"eda",
"KDPG_aldolase"
] | [
28388,
28337,
18234,
28126
] | 4 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"4.1.2.14",
"GenProp0468",
"GenProp1449",
"GenProp1557",
"GenProp1566",
"GenProp1636",
"GenProp1691",
"PWY-2221",
"PWY-6507",
"PWY-7242",
"PWY-7310",
"PWY-7562",
"PDOC00144"
] | [
"EC:4.1.2.14",
"GP:GenProp0468",
"GP:GenProp1449",
"GP:GenProp1557",
"GP:GenProp1566",
"GP:GenProp1636",
"GP:GenProp1691",
"METACYC:PWY-2221",
"METACYC:PWY-6507",
"METACYC:PWY-7242",
"METACYC:PWY-7310",
"METACYC:PWY-7562",
"PROSITEDOC:PDOC00144"
] | 13 | [
"1eua",
"1eun",
"1fq0",
"1fwr",
"1mxs",
"1vhc",
"1vlw",
"1wa3",
"1wau",
"1wbh",
"2c0a",
"2v81",
"2v82",
"2yw3",
"2yw4",
"3vcr",
"4bk9",
"4e38",
"4qcc",
"5im5",
"5kp9",
"5xse",
"5xsf",
"6ovi",
"6p6f",
"6xh5",
"7b3y",
"7sgd",
"7sge",
"7sgf",
"8a8n",
"8cus"... | 57 | [
"PUB00049619",
"PUB00087307",
"PUB00087308"
] | [
"17981470",
"4894280",
"15659677"
] | [
"Characterization and crystal structure of Escherichia coli KDPGal aldolase.",
"A stereospecific 2-keto-4-hydroxyglutarate aldolase from Escherichia coli.",
"Multiple regulators control expression of the Entner-Doudoroff aldolase (Eda) of Escherichia coli."
] | [
2008,
1969,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
356,
26944,
869,
2,
295
] | 5 | [
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
4,
6
] | 3 | true | Family | KDPG/KHG aldolase | KDPG/KHG aldolase | Aldlse_KDPG_KHG | 2 |
IPR000888 | 888 | dTDP-4-dehydrorhamnose 3,5-epimerase-like | RmlC-like | Family | 26,466 | false | false | Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase (RmlC, ) is involved in the biosynthesis of dTDP-l-rhamnose, which is an essential component of the bacterial cell wall, converting dTDP-4-keto-6-deoxy-D-glucose to dTDP-4-keto-L-rhamnose. The crystal structure of RmlC from Methanobacterium ther... | [
"GO:0008830"
] | [
"dTDP-4-dehydrorhamnose 3,5-epimerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PF00908",
"PTHR21047",
"TIGR01221",
"cd00438"
] | [
"dTDP_sugar_isom",
"",
"rmlC",
"cupin_RmlC"
] | [
26313,
25087,
18384,
23098
] | 4 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.1.3.13",
"GenProp1032",
"PWY-7301",
"PWY-7814",
"PWY-8380"
] | [
"EC:5.1.3.13",
"GP:GenProp1032",
"METACYC:PWY-7301",
"METACYC:PWY-7814",
"METACYC:PWY-8380"
] | 5 | [
"1dzr",
"1dzt",
"1ep0",
"1epz",
"1nxm",
"1nyw",
"1nzc",
"1ofn",
"1oi6",
"1pm7",
"1rtv",
"1upi",
"1wa4",
"1wlt",
"2b9u",
"2c0z",
"2ixc",
"2ixh",
"2ixi",
"2ixj",
"2ixk",
"2ixl",
"3ejk",
"3ryk",
"4hmz",
"4hn0",
"4hn1",
"5buv",
"6c46",
"6din",
"6ndr",
"7an4"... | 55 | [
"PUB00007928",
"PUB00089648"
] | [
"10827167",
"10770761"
] | [
"Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP.",
"Identification and expression of genes involved in biosynthesis of L-oleandrose and its intermediate L-olivose in the oleandomycin producer Streptomyces antibioticus."
] | [
2000,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
429,
25211,
227,
36,
563
] | 5 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Family | dTDP-4-dehydrorhamnose 3,5-epimerase-like | dTDP-4-dehydrorhamnose 3,5-epimerase-like | RmlC-like | 5 |
IPR000889 | 889 | Glutathione peroxidase | Glutathione_peroxidase | Family | 40,785 | false | false | Glutathione peroxidase (GSHPx) ( ) is an enzyme that catalyses the reduction of hydroperoxides by glutathione [ ]. Its main function is to protect against the damaging effect of endogenously formed hydroperoxides. In higher vertebrates, several forms of GSHPx are known, including a ubiquitous cytosolic form (GSHPx-1), ... | [
"GO:0004601",
"GO:0006979"
] | [
"peroxidase activity",
"response to oxidative stress"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROFILE",
"PANTHER",
"CDD"
] | [
"PF00255",
"PIRSF000303",
"PR01011",
"PS51355",
"PTHR11592",
"cd00340"
] | [
"GSHPx",
"Glutathion_perox",
"GLUTPROXDASE",
"GLUTATHIONE_PEROXID_3",
"",
"GSH_Peroxidase"
] | [
39646,
33550,
36902,
40676,
39472,
36416
] | 6 | [
"EC",
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"1.11.1",
"1.11.1.9",
"GenProp0213",
"GenProp1721",
"PWY-4081",
"PDOC00396",
"R-BTA-2142712",
"R-BTA-3299685",
"R-BTA-9018676",
"R-BTA-9018896",
"R-BTA-9020265",
"R-BTA-9023661",
"R-CEL-3299685",
"R-DRE-3299685",
"R-HSA-2142688",
"R-HSA-2142712",
"R-HSA-2142770",
"R-HSA-3299685",
... | [
"EC:1.11.1",
"EC:1.11.1.9",
"GP:GenProp0213",
"GP:GenProp1721",
"METACYC:PWY-4081",
"PROSITEDOC:PDOC00396",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-9018676",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9020265",
"REACTOME:R-BTA-9023661",
"REACTOME:R-CEL-3299685",
... | 46 | [
"1gp1",
"2f8a",
"2gs3",
"2he3",
"2i3y",
"2obi",
"2p31",
"2p5q",
"2p5r",
"2r37",
"2rm5",
"2rm6",
"2v1m",
"2vup",
"2wgr",
"3cmi",
"3cyn",
"3dwv",
"3e0u",
"3kij",
"5h5q",
"5h5r",
"5h5s",
"5l71",
"6elw",
"6hkq",
"6hn3",
"6vpd",
"7fc2",
"7l8k",
"7l8l",
"7l8m"... | 50 | [
"PUB00000070",
"PUB00001337",
"PUB00003890",
"PUB00004364",
"PUB00004788",
"PUB00095067"
] | [
"2142875",
"6852035",
"7565867",
"2771650",
"1631065",
"23567855"
] | [
"Selenium biochemistry.",
"The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.",
"An investigation of antioxidant status, DNA repair capacity and mutation as a function of age in humans.",
"A human cDNA sequence for a novel glutathione peroxidase-related selenopeptide, GPRP.... | [
1990,
1983,
1995,
1989,
1992,
2013
] | 6 | [] | [
"IPR013376",
"IPR033674"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
19,
23486,
16968,
21,
291
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
10,
13,
6,
1,
44,
24,
1,
19,
27,
3,
1,
27
] | 13 | true | Family | Glutathione peroxidase | Glutathione peroxidase | Glutathione_peroxidase | 1 |
IPR000890 | 890 | Aliphatic acid kinase, short-chain | Aliphatic_acid_kin_short-chain | Family | 29,893 | false | false | Acetate kinase, which is predominantly found in microorganisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation [ , , ]. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a... | [
"GO:0016301",
"GO:0016774",
"GO:0016310"
] | [
"kinase activity",
"phosphotransferase activity, carboxyl group as acceptor",
"phosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00871",
"PR00471",
"PTHR21060"
] | [
"Acetate_kinase",
"ACETATEKNASE",
""
] | [
29855,
29134,
29703
] | 3 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"2.7.2",
"2.7.2.1",
"GenProp1267",
"GenProp1345",
"GenProp1543",
"GenProp1749",
"GenProp1762",
"PWY-5482",
"PWY-5485",
"PWY-5497",
"PWY-8015",
"PWY-8086",
"PWY-8303",
"PWY-8377",
"PDOC00826"
] | [
"EC:2.7.2",
"EC:2.7.2.1",
"GP:GenProp1267",
"GP:GenProp1345",
"GP:GenProp1543",
"GP:GenProp1749",
"GP:GenProp1762",
"METACYC:PWY-5482",
"METACYC:PWY-5485",
"METACYC:PWY-5497",
"METACYC:PWY-8015",
"METACYC:PWY-8086",
"METACYC:PWY-8303",
"METACYC:PWY-8377",
"PROSITEDOC:PDOC00826"
] | 15 | [
"1g99",
"1saz",
"1tuu",
"1tuy",
"1x3m",
"1x3n",
"1x9j",
"2e1y",
"2e1z",
"2e20",
"2iir",
"3khy",
"3p4i",
"3r9p",
"3sk3",
"3slc",
"4dq8",
"4fwk",
"4fwl",
"4fwm",
"4fwn",
"4fwo",
"4fwp",
"4fwq",
"4fwr",
"4fws",
"4h0o",
"4h0p",
"4ijn",
"4iz9",
"4xh1",
"4xh4"... | 41 | [
"PUB00001831",
"PUB00002232",
"PUB00065155"
] | [
"8396545",
"8226682",
"23031654"
] | [
"Cloning and sequence analysis of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB 8052.",
"Regulation of the Bacillus subtilis acetate kinase gene by CcpA.",
"Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identifica... | [
1993,
1993,
2012
] | 3 | [] | [
"IPR004372",
"IPR011245"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Siphoviridae sp. ctX581",
"unclassified sequences"
] | [
27823,
1626,
37,
1,
406
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2,
1
] | 2 | true | Family | Aliphatic acid kinase, short-chain | Aliphatic acid kinase, short-chain | Aliphatic_acid_kin_short-chain | 3 |
IPR000891 | 891 | Pyruvate carboxyltransferase | PYR_CT | Domain | 106,057 | false | false | Pyruvate carboxylase ( ) (PC), a member of the biotin-dependent enzyme family, is involved in gluconeogenesis by mediating the carboxylation of pyruvate to oxaloacetate. Biotin-dependent carboxylase enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl gr... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF00682",
"PS50991"
] | [
"HMGL-like",
"PYR_CT"
] | [
104077,
104709
] | 2 | [
"EC",
"EC",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"2.3.3",
"2.3.3.13",
"GenProp1673",
"PWY-6871",
"PDOC50991",
"R-BTA-196780",
"R-BTA-70263",
"R-BTA-70268",
"R-BTA-77111",
"R-BTA-9033241",
"R-CEL-196780",
"R-CEL-70263",
"R-CEL-70268",
"R-DRE-77111",
"R-HSA-196780",
"R-HSA-3371599",
"R-HSA-70263",
"R-HSA-70268",
"R-HSA-77111",
... | [
"EC:2.3.3",
"EC:2.3.3.13",
"GP:GenProp1673",
"METACYC:PWY-6871",
"PROSITEDOC:PDOC50991",
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-9033241",
"REACTOME:R-CEL-196780",
"REACTOME:R-CEL-70263",
"REACTOME:R-CEL-70268",
"REAC... | 36 | [
"1nvm",
"1rqb",
"1rqe",
"1rqh",
"1rr2",
"1s3h",
"1sr9",
"1u5j",
"1ydn",
"1ydo",
"2cw6",
"2ftp",
"2nx9",
"2qf7",
"2ztj",
"2ztk",
"2zyf",
"3a9i",
"3bg3",
"3bg5",
"3bg9",
"3ble",
"3blf",
"3bli",
"3dxi",
"3eeg",
"3ewb",
"3fig",
"3hb9",
"3hbl",
"3ho8",
"3hps"... | 94 | [
"PUB00015343",
"PUB00015403",
"PUB00015404",
"PUB00016385",
"PUB00095137",
"PUB00155065"
] | [
"11851389",
"7780827",
"10229653",
"12764229",
"23698000",
"38614832"
] | [
"Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.",
"The structure and the mechanism of action of pyruvate carboxylase.",
"Structure, function and regulation of pyruvate carboxylase.",
"Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reac... | [
2002,
1995,
1999,
2003,
2013,
2024
] | 6 | [] | [
"IPR011830",
"IPR035685",
"IPR039371",
"IPR048253"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
2557,
83719,
17949,
1,
5,
1826
] | 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",... | [
33,
3,
10,
7,
2,
10,
15,
5,
17,
16,
6,
3,
61
] | 13 | true | Domain | Pyruvate carboxyltransferase | Pyruvate carboxyltransferase | PYR_CT | 4 |
IPR000892 | 892 | Small ribosomal subunit protein eS26 | Ribosomal_eS26 | Family | 6,196 | false | false | This family represents the small ribosomal subunit protein eS26 (previously known as S26) which is found mainly in eukaryotes and includes mammalian S26 [ ]; Octopus S26 [ ]; Drosophila S26 (DS31) [ ]; plant cytoplasmic S26; and fungal S26 [ ]. S26 may be involved in the attachment of eIF3 and poly (U) [ ]. Disruption ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF01283",
"PTHR12538"
] | [
"Ribosomal_S26e",
""
] | [
6195,
6030
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00601",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-CEL-72706",
"R... | [
"PROSITEDOC:PDOC00601",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827"... | 102 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j7a",
"3j7p",
"3j7r",
"3j80",
"3j81",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jam",
"3jan",
"3jap",
"3jbn",
"3jbo",
"3jbp",
"4bts",
"4d5l",
"4d61",
"4kzx",
"4kzy",
"4kzz",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r"... | 503 | [
"PUB00001126",
"PUB00001852",
"PUB00002326",
"PUB00004355",
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"2731467",
"7821815",
"2993263",
"2928115",
"11297922",
"11290319",
"11114498"
] | [
"[Isolation and structural characteristics of cDNA for octopus proteins which are homologous to rat S26 ribosomal protein]",
"The Saccharomyces cerevisiae homologue of ribosomal protein S26.",
"Molecular cloning and nucleotide sequence of DNA complementary to rat ribosomal protein S26 messenger RNA.",
"The nu... | [
1989,
1994,
1985,
1989,
2001,
2001,
2000
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
232,
2,
5950,
12
] | 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... | [
11,
1,
2,
2,
4,
2,
1,
7,
10,
2,
2,
21
] | 12 | true | Family | Small ribosomal subunit protein eS26 | Small ribosomal subunit protein eS26 | Ribosomal_eS26 | 6 |
IPR000894 | 894 | Ribulose bisphosphate carboxylase small subunit, domain | RuBisCO_ssu_dom | Domain | 6,748 | false | false | RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) is a bifunctional enzyme that catalyses both the carboxylation and oxygenation of ribulose-1,5-bisphosphate (RuBP), thus fixing carbon dioxide as the first step of the Calvin cycle. RuBisCO is the major protein in the stroma of chloroplasts, and in higher plants... | [] | [] | [] | 0 | [
"HAMAP",
"PFAM",
"SMART",
"CDD"
] | [
"MF_00859",
"PF00101",
"SM00961",
"cd03527"
] | [
"RuBisCO_S_bact",
"RuBisCO_small",
"RuBisCO_small",
"RuBisCO_small"
] | [
4841,
6747,
5947,
4970
] | 4 | [
"GP"
] | [
"GenProp1747"
] | [
"GP:GenProp1747"
] | 1 | [
"1aa1",
"1aus",
"1bwv",
"1bxn",
"1ej7",
"1gk8",
"1ir1",
"1ir2",
"1iwa",
"1rbl",
"1rbo",
"1rco",
"1rcx",
"1rlc",
"1rld",
"1rsc",
"1rxo",
"1svd",
"1upm",
"1upp",
"1uw9",
"1uwa",
"1uzd",
"1uzh",
"1wdd",
"2v63",
"2v67",
"2v68",
"2v69",
"2v6a",
"2vdh",
"2vdi"... | 91 | [
"PUB00004339",
"PUB00033007",
"PUB00095138"
] | [
"3010233",
"1512238",
"22811433"
] | [
"The genes encoding the small subunit of ribulose-1,5-bisphosphate carboxylase are expressed differentially in petunia leaves.",
"Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0-A resolution.",
"Availability of Rubisco small subunit up-reg... | [
1986,
1992,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Natronorubrum halalkaliphilum",
"unclassified sequences"
] | [
2468,
4218,
1,
61
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
18,
13,
6
] | 3 | true | Domain | Ribulose bisphosphate carboxylase small subunit, domain | Ribulose bisphosphate carboxylase small subunit, domain | RuBisCO_ssu_dom | 6 |
IPR000895 | 895 | Transthyretin/hydroxyisourate hydrolase | Transthyretin/HIU_hydrolase | Family | 11,690 | false | false | This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyse the conversion of 5-hydroxyisourat... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00189"
] | [
"TRNSTHYRETIN"
] | [
11690
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00617",
"R-BTA-2453902",
"R-BTA-6798695",
"R-BTA-975634",
"R-CEL-3000171",
"R-CEL-6798695",
"R-CEL-975634",
"R-HSA-2453902",
"R-HSA-3000171",
"R-HSA-6798695",
"R-HSA-975634",
"R-HSA-977225",
"R-HSA-9918449",
"R-MMU-2453902",
"R-MMU-6798695",
"R-MMU-975634",
"R-RNO-2453902",
"R... | [
"PROSITEDOC:PDOC00617",
"REACTOME:R-BTA-2453902",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-975634",
"REACTOME:R-CEL-3000171",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-975634",
"REACTOME:R-HSA-2453902",
"REACTOME:R-HSA-3000171",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-975634",
"REACTOME:R-H... | 26 | [
"1bm7",
"1bmz",
"1bz8",
"1bzd",
"1bze",
"1dvq",
"1dvs",
"1dvt",
"1dvu",
"1dvx",
"1dvy",
"1dvz",
"1e3f",
"1e4h",
"1e5a",
"1eta",
"1etb",
"1f41",
"1f86",
"1fh2",
"1fhn",
"1g1o",
"1gke",
"1gko",
"1ict",
"1ie4",
"1iii",
"1iik",
"1ijn",
"1kgi",
"1kgj",
"1oo2"... | 485 | [
"PUB00001401",
"PUB00001752",
"PUB00002809",
"PUB00034597",
"PUB00041243",
"PUB00042841",
"PUB00071851",
"PUB00101389"
] | [
"1833190",
"4054629",
"8428915",
"16098976",
"16952372",
"16462750",
"24422526",
"33001386"
] | [
"Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin. Implications for the evolution of structure and function of transthyretin in vertebrates.",
"Structure of the chromosomal gene for human serum prealbumin.",
"The x-ray crystal structure refinements of normal human transthy... | [
1991,
1985,
1993,
2005,
2006,
2006,
2014,
2020
] | 8 | [] | [
"IPR014306"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
7920,
3676,
34,
1,
59
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
2,
4,
1,
1,
8,
6,
5,
11,
1,
7
] | 11 | true | Family | Transthyretin/hydroxyisourate hydrolase | Transthyretin/hydroxyisourate hydrolase | Transthyretin/HIU_hydrolase | 5 |
IPR000896 | 896 | Hemocyanin/hexamerin middle domain | Hemocyanin/hexamerin_mid_dom | Domain | 4,074 | false | false | This entry represents the middle domain of hemocyanin and hexamerin proteins, which is involved in copper binding in hemocyanins. Crustacean and cheliceratan hemocyanins (oxygen-transport proteins) and insect hexamerins (storage proteins) are homologous gene products, although the latter do not bind oxygen [ ]. Haemocy... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00372"
] | [
"Hemocyanin_M"
] | [
4074
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00184"
] | [
"PROSITEDOC:PDOC00184"
] | 1 | [
"1hc1",
"1hcy",
"1ll1",
"1lla",
"1nol",
"1oxy",
"3gwj",
"3hhs",
"3ixv",
"3ixw",
"3wjm",
"3wky",
"4l37",
"4yzw",
"5yy2",
"5yy3",
"6l8s",
"7ze1",
"8ca9",
"8cad",
"8can",
"8ji8",
"8jib",
"8po9"
] | 24 | [
"PUB00000297",
"PUB00059233",
"PUB00082624",
"PUB00100820"
] | [
"3207675",
"8015442",
"25251934",
"25859931"
] | [
"cDNA cloning of the Octopus dofleini hemocyanin: sequence of the carboxyl-terminal domain.",
"Evolution of arthropod hemocyanins and insect storage proteins (hexamerins).",
"Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems to form the 6,6-quinolone core of viridicatin-type fungal alka... | [
1988,
1994,
2014,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
47,
4027
] | 2 | [
"Drosophila melanogaster"
] | [
15
] | 1 | true | Domain | Hemocyanin/hexamerin middle domain | Hemocyanin/hexamerin middle domain | Hemocyanin/hexamerin_mid_dom | 4 |
IPR000897 | 897 | Signal recognition particle, SRP54 subunit, GTPase domain | SRP54_GTPase_dom | Domain | 73,909 | false | false | The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ , , ]. SRP recognises the signal sequence of the nascent po... | [
"GO:0005525",
"GO:0006614"
] | [
"GTP binding",
"SRP-dependent cotranslational protein targeting to membrane"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE",
"SMART"
] | [
"PF00448",
"PS00300",
"SM00962"
] | [
"SRP54",
"SRP54",
"SRP54"
] | [
73546,
56041,
72765
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.5.4",
"PDOC00272",
"R-BTA-1799339",
"R-CFA-1799339",
"R-DDI-1799339",
"R-DRE-1799339",
"R-HSA-1799339",
"R-HSA-381038",
"R-MMU-1799339",
"R-RNO-1799339",
"R-SCE-1799339",
"R-SPO-1799339"
] | [
"EC:3.6.5.4",
"PROSITEDOC:PDOC00272",
"REACTOME:R-BTA-1799339",
"REACTOME:R-CFA-1799339",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DRE-1799339",
"REACTOME:R-HSA-1799339",
"REACTOME:R-HSA-381038",
"REACTOME:R-MMU-1799339",
"REACTOME:R-RNO-1799339",
"REACTOME:R-SCE-1799339",
"REACTOME:R-SPO-1799339... | 12 | [
"1ffh",
"1fts",
"1j8m",
"1j8y",
"1jpj",
"1jpn",
"1ls1",
"1ng1",
"1o87",
"1okk",
"1qzw",
"1qzx",
"1rj9",
"1ry1",
"1vma",
"1zu4",
"1zu5",
"2c03",
"2c04",
"2cnw",
"2ffh",
"2iy3",
"2iyl",
"2j28",
"2j37",
"2j45",
"2j46",
"2j7p",
"2ng1",
"2og2",
"2px0",
"2px3"... | 97 | [
"PUB00004449",
"PUB00028143",
"PUB00035998",
"PUB00035999",
"PUB00041125",
"PUB00053948",
"PUB00063486",
"PUB00100261",
"PUB00103723",
"PUB00103724",
"PUB00103725"
] | [
"7518075",
"16469117",
"17622352",
"17507650",
"16675701",
"12364595",
"12605305",
"34020957",
"15148364",
"9922234",
"7511896"
] | [
"Molecular evolution of SRP cycle components: functional implications.",
"Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.",
"X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.",
"The signal re... | [
1994,
2006,
2007,
2007,
2006,
2002,
2003,
2021,
2004,
1999,
1994
] | 11 | [] | [
"IPR047040"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1910,
57060,
13560,
8,
1371
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
31,
2,
2,
4,
2,
10,
6,
3,
21,
6,
2,
2,
44
] | 13 | true | Domain | Signal recognition particle, SRP54 subunit, GTPase domain | Signal recognition particle, SRP54 subunit, GTPase domain | SRP54_GTPase_dom | 4 |
IPR000898 | 898 | Indoleamine 2,3-dioxygenase | Indolamine_dOase | Family | 7,919 | false | false | Indoleamine 2,3-dioxgyenase (IDO, ) [ , ] is a cytosolic heme protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyses the conversion of tryptophan and other indole derivatives to kynurenines. It is widely distributed in human tissues, involved in the peripheral immune tolerance, contributi... | [
"GO:0020037"
] | [
"heme binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PF01231",
"PS00876",
"PS00877",
"PTHR28657"
] | [
"IDO",
"IDO_1",
"IDO_2",
""
] | [
7721,
2515,
203,
7333
] | 4 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.13.11",
"GenProp1503",
"PDOC00684",
"R-HSA-71240",
"R-MMU-71240",
"R-RNO-71240",
"R-SCE-71240"
] | [
"EC:1.13.11",
"GP:GenProp1503",
"PROSITEDOC:PDOC00684",
"REACTOME:R-HSA-71240",
"REACTOME:R-MMU-71240",
"REACTOME:R-RNO-71240",
"REACTOME:R-SCE-71240"
] | 7 | [
"2d0t",
"2d0u",
"4pk5",
"4pk6",
"4u72",
"4u74",
"5ek2",
"5ek3",
"5ek4",
"5etw",
"5whr",
"5wmu",
"5wmv",
"5wmw",
"5wmx",
"5wn8",
"5xe1",
"6azu",
"6azv",
"6azw",
"6cxu",
"6cxv",
"6dpq",
"6dpr",
"6e35",
"6e40",
"6e41",
"6e42",
"6e43",
"6e44",
"6e45",
"6e46"... | 81 | [
"PUB00001509",
"PUB00003470",
"PUB00015433",
"PUB00015434",
"PUB00097837",
"PUB00097838",
"PUB00097839",
"PUB00097840",
"PUB00097841",
"PUB00097842",
"PUB00097843",
"PUB00097844"
] | [
"1907934",
"8011076",
"12711393",
"12766158",
"21170645",
"25691885",
"25950090",
"18418598",
"25394548",
"23103127",
"25157255",
"18828915"
] | [
"Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism.",
"Abalone myoglobins evolved from indoleamine dioxygenase: the cDNA-derived amino acid sequence of myoglobin from Nordotis madaka.",
"Comparison of the sequences of Turbo and Sulculus indoleamine dioxygenase-like my... | [
1991,
1994,
2003,
2003,
2011,
2015,
2015,
2009,
2014,
2013,
2014,
2008
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Imitervirales",
"metagenomes"
] | [
288,
7557,
14,
3,
57
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
4,
6,
4,
3,
7,
1
] | 6 | true | Family | Indoleamine 2,3-dioxygenase | Indoleamine 2,3-dioxygenase | Indolamine_dOase | 8 |
IPR000900 | 900 | Nebulin repeat | Nebulin_repeat | Repeat | 10,655 | false | false | The nebulin-like motif or nebulin repeat is a tandemly repeated actin-binding module of about 35 amino acids. The repeat is named after the nebulin protein, which is a large protein specific for vertebrate skeletal muscle that may regulate the length of thin filaments. Nebulin contains about 185 copies of the repeat an... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00880",
"PS51216",
"SM00227"
] | [
"Nebulin",
"NEBULIN",
"NEBU"
] | [
10561,
10531,
10574
] | 3 | [
"PROSITEDOC",
"REACTOME"
] | [
"PDOC51216",
"R-HSA-390522"
] | [
"PROSITEDOC:PDOC51216",
"REACTOME:R-HSA-390522"
] | 2 | [] | 0 | [
"PUB00001250",
"PUB00033737",
"PUB00033738"
] | [
"8168478",
"9733644",
"12446728"
] | [
"Nebulin, a helical actin binding protein.",
"Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs.",
"Interactions between nebulin-like motifs and thin filament regulatory proteins."
] | [
1994,
1998,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
7,
10648
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
18,
3,
45,
42,
31
] | 6 | true | Repeat | Nebulin repeat | Nebulin repeat | Nebulin_repeat | 6 |
IPR000903 | 903 | Glycylpeptide N-tetradecanoyltransferase | NMT | Family | 7,388 | false | false | Glycylpeptide N-tetradecanoyltransferase, also known as Myristoyl-CoA:protein N-myristoyltransferase ( ) (Nmt), is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins [ ]. Nmt is a monomeric protein of about 50 to 60kDa whose sequenc... | [
"GO:0004379",
"GO:0006499"
] | [
"glycylpeptide N-tetradecanoyltransferase activity",
"N-terminal protein myristoylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF015892",
"PTHR11377"
] | [
"N-myristl_transf",
""
] | [
5459,
7388
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.97",
"PDOC00752",
"R-BTA-2514859",
"R-DDI-2514859",
"R-DRE-2514859",
"R-HSA-162599",
"R-HSA-174490",
"R-HSA-203615",
"R-HSA-2514859",
"R-HSA-75108",
"R-MMU-2514859",
"R-MMU-75108",
"R-RNO-2514859",
"R-RNO-75108",
"R-SCE-2514859",
"R-SPO-2514859"
] | [
"EC:2.3.1.97",
"PROSITEDOC:PDOC00752",
"REACTOME:R-BTA-2514859",
"REACTOME:R-DDI-2514859",
"REACTOME:R-DRE-2514859",
"REACTOME:R-HSA-162599",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-203615",
"REACTOME:R-HSA-2514859",
"REACTOME:R-HSA-75108",
"REACTOME:R-MMU-2514859",
"REACTOME:R-MMU-75108",
... | 16 | [
"1iic",
"1iid",
"1iyk",
"1iyl",
"1nmt",
"1rxt",
"2nmt",
"2p6e",
"2p6f",
"2p6g",
"2wsa",
"2wuu",
"2ync",
"2ynd",
"2yne",
"3h5z",
"3iu1",
"3iu2",
"3iwe",
"3jtk",
"4a2z",
"4a30",
"4a31",
"4a32",
"4a33",
"4a95",
"4b10",
"4b11",
"4b12",
"4b13",
"4b14",
"4bbh"... | 157 | [
"PUB00000005",
"PUB00100072"
] | [
"8322618",
"11139338"
] | [
"MyristoylCoA:protein N-myristoyltransferase.",
"Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects."
] | [
1993,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Nucleocytoviricota",
"metagenomes"
] | [
7323,
51,
14
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
10,
2,
8,
1,
16,
6,
1,
4,
11,
1,
1,
7
] | 12 | true | Family | Glycylpeptide N-tetradecanoyltransferase | Glycylpeptide N-tetradecanoyltransferase | NMT | 2 |
IPR000904 | 904 | Sec7 domain | Sec7_dom | Domain | 46,503 | false | false | Protein containing this domain are highly divergent in their overall sequence, however, they share a common region of roughly 200 amino acids known as the SEC7 domain [ , ]. The 3D structure of the domain displays several α-helices [ ]. It was found to be associated with other domains involved in guanine nucleotide exc... | [
"GO:0005085",
"GO:0032012"
] | [
"guanyl-nucleotide exchange factor activity",
"regulation of ARF protein signal transduction"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF01369",
"PS50190",
"SM00222",
"cd00171"
] | [
"Sec7",
"SEC7",
"Sec7",
"Sec7"
] | [
44865,
44336,
45028,
39581
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50190",
"R-CEL-199992",
"R-CEL-6807878",
"R-CEL-6811434",
"R-HSA-199992",
"R-HSA-390471",
"R-HSA-5620916",
"R-HSA-6807878",
"R-HSA-6811434",
"R-HSA-6811438",
"R-HSA-9768919",
"R-MMU-199992",
"R-MMU-5620916",
"R-MMU-6807878",
"R-MMU-6811434",
"R-MMU-6811438",
"R-RNO-6811438",
"... | [
"PROSITEDOC:PDOC50190",
"REACTOME:R-CEL-199992",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-HSA-199992",
"REACTOME:R-HSA-390471",
"REACTOME:R-HSA-5620916",
"REACTOME:R-HSA-6807878",
"REACTOME:R-HSA-6811434",
"REACTOME:R-HSA-6811438",
"REACTOME:R-HSA-9768919",
"REACTOME:R-M... | 27 | [
"1bc9",
"1ku1",
"1pbv",
"1r8m",
"1r8q",
"1r8s",
"1re0",
"1s9d",
"1xsz",
"1xt0",
"2r09",
"2r0d",
"3l8n",
"3ltl",
"3swv",
"4a4p",
"4c0a",
"4c7p",
"4d7q",
"4d7r",
"4jmi",
"4jmo",
"4jwl",
"4jxh",
"4l5m",
"4oiy",
"4z21",
"5nlv",
"5nly",
"6bbp",
"6bbq",
"6fae"... | 43 | [
"PUB00005826",
"PUB00005838",
"PUB00076749",
"PUB00076750",
"PUB00101184",
"PUB00101185"
] | [
"9653114",
"9868368",
"19669794",
"24728583",
"26765562",
"27373159"
] | [
"Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.",
"Triple association of CDC25-, Dbl- and Sec7-related domains in mammalian guanine-nucleotide-exchange factors.",
"Large Arf1 guanine nucleotide exchange factors: evolution, domain structure... | [
1998,
1998,
2009,
2014,
2016,
2016
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
52,
46446,
5
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
39,
10,
147,
15,
97,
70,
5,
23,
84,
5,
7,
215
] | 12 | true | Domain | Sec7 domain | Sec7 domain | Sec7_dom | 8 |
IPR000905 | 905 | Gcp-like domain | Gcp-like_dom | Domain | 64,269 | false | false | This domain was identified in proteins including Kae1 and Gcp (YgjD), which were originally thought to be endopeptidases belonging to the peptidase M22 family [ ]. However, there is a lack of experimental evidence to support peptidase activity as a general property, and this has not been confirmed in other orthologues ... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF00814",
"PTHR11735"
] | [
"TsaD",
""
] | [
64161,
59101
] | 2 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"2.3.1.234",
"R-HSA-6782315",
"R-HSA-6787450"
] | [
"EC:2.3.1.234",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-6787450"
] | 3 | [
"1okj",
"2a6a",
"2gel",
"2gem",
"2ivn",
"2ivo",
"2ivp",
"2vwb",
"3en9",
"3enh",
"3eno",
"3r6m",
"3wuh",
"3zet",
"3zeu",
"4k25",
"4wq4",
"4wq5",
"4y0w",
"4ydu",
"5br9",
"5jmv",
"6gwj",
"6n9a",
"6nak",
"6nbj",
"6s84",
"6z81",
"8ide",
"8iey",
"8ifx",
"8k20"... | 35 | [
"PUB00002152",
"PUB00047751",
"PUB00059910",
"PUB00059911",
"PUB00063355",
"PUB00063366"
] | [
"1885539",
"17766251",
"21183954",
"21285948",
"22378793",
"23072323"
] | [
"Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.",
"An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro.",
"The highly conserved KEOPS/EKC comp... | [
1991,
2007,
2011,
2011,
2012,
2012
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
951,
51858,
10164,
9,
1287
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
2,
5,
3,
2,
8,
10,
2,
12,
8,
2,
2,
40
] | 13 | true | Domain | Gcp-like domain | Gcp-like domain | Gcp-like_dom | 5 |
IPR000907 | 907 | Lipoxygenase | LipOase | Family | 18,947 | false | false | Lipoxygenases ([ec:1.13.11.-]) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resist... | [
"GO:0016702",
"GO:0046872",
"GO:0034440"
] | [
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen",
"metal ion binding",
"lipid oxidation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PANTHER"
] | [
"PTHR11771"
] | [
""
] | [
18947
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.13.11",
"R-BTA-2142691",
"R-BTA-2142712",
"R-BTA-2142770",
"R-BTA-9018677",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9023661",
"R-BTA-9025106",
"R-BTA-9026286",
"R-HSA-2142688",
"R-HSA-2142691",
"R-HSA-2142696",
"R-HSA-2142700",
"R-HSA-2142712",
"R-HSA-2142770",
"R-HSA-6785807",
... | [
"EC:1.13.11",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-2142770",
"REACTOME:R-BTA-9018677",
"REACTOME:R-BTA-9018681",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9023661",
"REACTOME:R-BTA-9025106",
"REACTOME:R-BTA-9026286",
"REACTOME:R-HSA-2142688",
"REACTOME:R-HSA-2142... | 78 | [
"1f8n",
"1fgm",
"1fgo",
"1fgq",
"1fgr",
"1fgt",
"1hu9",
"1ik3",
"1jnq",
"1lnh",
"1lox",
"1n8q",
"1no3",
"1rov",
"1rrh",
"1rrl",
"1y4k",
"1yge",
"2fnq",
"2iuj",
"2iuk",
"2p0m",
"2sbl",
"3bnb",
"3bnc",
"3bnd",
"3bne",
"3d3l",
"3dy5",
"3fg1",
"3fg3",
"3fg4"... | 84 | [
"PUB00000045",
"PUB00000363",
"PUB00002887",
"PUB00005162"
] | [
"3017195",
"1567851",
"7508918",
"8502991"
] | [
"Arachidonic acid metabolism.",
"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.",
"A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus.",
"The three-dimensional structure of an arachid... | [
1986,
1992,
1994,
1993
] | 4 | [] | [
"IPR001246",
"IPR001885"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Sylvanvirus sp.",
"hydrothermal vent metagenome"
] | [
558,
18387,
1,
1
] | 4 | [
"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",
"Zea mays"
] | [
29,
44,
23,
25,
1,
65,
30,
182
] | 8 | true | Family | Lipoxygenase | Lipoxygenase | LipOase | 3 |
IPR000908 | 908 | Acetylcholinesterase, fish/snake | Acylcholinesterase_fish/snake | Family | 10 | false | false | Cholinesterase enzymes are members of the broader alpha/beta hydrolase family and can be dividied into two distinct groups: those that catalyse the hydrolysis of acetylcholine to choline and acetate (acetylcholinesterases ) acetylcholine + H 2 O ->choline + acetate and those that catalyse the conversion of other acylch... | [
"GO:0003990",
"GO:0001507"
] | [
"acetylcholinesterase activity",
"acetylcholine catabolic process in synaptic cleft"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00879"
] | [
"ACHEFISH"
] | [
10
] | 1 | [
"EC"
] | [
"3.1.1.7"
] | [
"EC:3.1.1.7"
] | 1 | [
"1acj",
"1acl",
"1amn",
"1ax9",
"1cfj",
"1dx6",
"1e3q",
"1e66",
"1ea5",
"1eea",
"1eve",
"1fss",
"1gpk",
"1gpn",
"1gqr",
"1gqs",
"1h22",
"1h23",
"1hbj",
"1jjb",
"1oce",
"1odc",
"1qid",
"1qie",
"1qif",
"1qig",
"1qih",
"1qii",
"1qij",
"1qik",
"1qim",
"1qti"... | 124 | [
"PUB00010129",
"PUB00029676",
"PUB00036069",
"PUB00036070",
"PUB00036071",
"PUB00036072",
"PUB00036073"
] | [
"1678899",
"12869558",
"15907917",
"8161450",
"8890157",
"8608006",
"11169626"
] | [
"Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.",
"Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.",
"Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology.",
"Acetylch... | [
1991,
2003,
2005,
1994,
1996,
1996,
2001
] | 7 | [
"IPR000997"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
10
] | 1 | [] | [] | 0 | true | Family | Acetylcholinesterase, fish/snake | Acetylcholinesterase, fish/snake | Acylcholinesterase_fish/snake | 9 |
IPR000909 | 909 | Phosphatidylinositol-specific phospholipase C, X domain | PLipase_C_PInositol-sp_X_dom | Domain | 46,687 | false | false | Phosphatidylinositol-specific phospholipase C, a eukaryotic intracellular enzyme, plays an important role in signal transduction processes [ ]. It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3,4,5-triphosphate into the second messenger molecules diacylglycerol and inositol-1,4,5-triphosphate. This catalyt... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00388",
"SM00148"
] | [
"PI-PLC-X",
"PLCXc"
] | [
44974,
45538
] | 2 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.4.11",
"GenProp1511",
"GenProp1548",
"PWY-6351",
"PWY-6367",
"PWY-7039",
"PWY-8052",
"PDOC50007",
"R-BTA-112043",
"R-BTA-1855204",
"R-BTA-399997",
"R-BTA-4086398",
"R-BTA-416476",
"R-BTA-418217",
"R-BTA-434316",
"R-BTA-500657",
"R-CEL-112043",
"R-CEL-1855204",
"R-CEL-416476"... | [
"EC:3.1.4.11",
"GP:GenProp1511",
"GP:GenProp1548",
"METACYC:PWY-6351",
"METACYC:PWY-6367",
"METACYC:PWY-7039",
"METACYC:PWY-8052",
"PROSITEDOC:PDOC50007",
"REACTOME:R-BTA-112043",
"REACTOME:R-BTA-1855204",
"REACTOME:R-BTA-399997",
"REACTOME:R-BTA-4086398",
"REACTOME:R-BTA-416476",
"REACTOM... | 167 | [
"1aod",
"1djg",
"1djh",
"1dji",
"1djw",
"1djx",
"1djy",
"1djz",
"1gym",
"1ptd",
"1ptg",
"1qas",
"1qat",
"1t6m",
"2fju",
"2isd",
"2or2",
"2plc",
"2ptd",
"2zkm",
"3ea1",
"3ea2",
"3ea3",
"3ptd",
"3qr0",
"3qr1",
"3v16",
"3v18",
"3v1h",
"4f2b",
"4f2t",
"4f2u"... | 67 | [
"PUB00000014",
"PUB00000624",
"PUB00002715",
"PUB00005394"
] | [
"1419362",
"1849017",
"1319994",
"1335185"
] | [
"Multiple forms of phospholipase C isozymes and their activation mechanisms.",
"The PtdIns-PLC superfamily and signal transduction.",
"Regulation of inositol phospholipid-specific phospholipase C isozymes.",
"Regulation of phospholipase C by G proteins."
] | [
1992,
1991,
1992,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanococcus maripaludis",
"Viruses",
"metagenomes"
] | [
2075,
44490,
3,
5,
114
] | 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... | [
50,
36,
127,
9,
89,
55,
5,
16,
85,
1,
1,
43
] | 12 | true | Domain | Phosphatidylinositol-specific phospholipase C, X domain | Phosphatidylinositol-specific phospholipase C, X domain | PLipase_C_PInositol-sp_X_dom | 8 |
IPR000911 | 911 | Ribosomal protein uL11 | Ribosomal_uL11 | Family | 36,583 | false | false | Ribosomal protein uL11, together with proteins L10 and L7/L12, and 23S rRNA, form the L7/L12 stalk on the surface of the large subunit of the ribosome. The homologous eukaryotic cytoplasmic protein uL11 was called in the past 60S ribosomal protein L12, which is distinct from the L12 involved in the formation of the L7/... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PANTHER",
"SMART",
"CDD"
] | [
"MF_00736",
"PTHR11661",
"SM00649",
"cd00349"
] | [
"Ribosomal_uL11",
"",
"RL11",
"Ribosomal_L11"
] | [
34922,
36197,
36324,
34457
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00310",
"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-5389840",
"R-CEL-5419276",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-97... | [
"PROSITEDOC:PDOC00310",
"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-1... | 85 | [
"1aci",
"1c04",
"1eg0",
"1fow",
"1fox",
"1foy",
"1hc8",
"1jqm",
"1jqs",
"1jqt",
"1mj1",
"1ml5",
"1mms",
"1mvr",
"1nkw",
"1nwx",
"1nwy",
"1oln",
"1pn7",
"1pn8",
"1qa6",
"1r2w",
"1r2x",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 901 | [
"PUB00000269",
"PUB00004378",
"PUB00022183",
"PUB00029489",
"PUB00030943",
"PUB00041959",
"PUB00042066",
"PUB00045897",
"PUB00050356",
"PUB00051026",
"PUB00079997",
"PUB00079998",
"PUB00079999",
"PUB00080000",
"PUB00080001",
"PUB00080002"
] | [
"2483975",
"2167467",
"10338213",
"12954336",
"15184028",
"17169991",
"17215866",
"17599351",
"18406324",
"18611379",
"17095013",
"17015650",
"16803902",
"16371360",
"15492007",
"15152193"
] | [
"Structural properties of ribosomal protein L11 from Escherichia coli.",
"The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae.",
"A detailed view of a ribosomal active site: the structure of the L11-RNA complex.",
"Str... | [
1989,
1990,
1999,
2003,
2004,
2007,
2007,
2007,
2008,
2008,
2007,
2006,
2006,
2006,
2005,
2004
] | 16 | [] | [
"IPR006519"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
903,
23551,
11638,
491
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
16,
2,
4,
3,
1,
6,
9,
2,
10,
12,
3,
3,
31
] | 13 | true | Family | Ribosomal protein uL11 | Ribosomal protein uL11 | Ribosomal_uL11 | 8 |
IPR000912 | 912 | Herpesvirus major capsid protein | Herpes_MCP | Family | 675 | false | false | The Herpesvirus major capsid protein (MCP) is the principal protein of the icosahedral capsid, forming the main component of the hexavalent and probably the pentavalent capsomeres. The capsid shell consists of 150 MCP hexamers and 12 MCP pentamers. One pentamer is found at each of the 12 apices of the icosahedral shell... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"PRINTS"
] | [
"MF_04016",
"PF03122",
"PR00235"
] | [
"HSV_MCP",
"Herpes_MCP",
"HSVCAPSIDMCP"
] | [
536,
675,
622
] | 3 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-9609690",
"R-HSA-9610379"
] | [
"REACTOME:R-HSA-9609690",
"REACTOME:R-HSA-9610379"
] | 2 | [
"1no7",
"5vku",
"5zap",
"5zz8",
"6b43",
"6cgr",
"6lgl",
"6lgn",
"6m6g",
"6m6h",
"6m6i",
"6nhj",
"6odm",
"6ppb",
"6ppd",
"6pph",
"6q1f",
"6w19",
"6w2d",
"6w2e",
"7bqx",
"7br7",
"7br8",
"7bsi",
"7bw6",
"7et3",
"7etj",
"7eto",
"7fj1",
"7fj3",
"7liv",
"8hex"... | 46 | [
"PUB00019684",
"PUB00054081",
"PUB00054082"
] | [
"11222712",
"7583656",
"10797014"
] | [
"Lytic replication of Kaposi's sarcoma-associated herpesvirus results in the formation of multiple capsid species: isolation and molecular characterization of A, B, and C capsids from a gammaherpesvirus.",
"Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids.",... | [
2001,
1995,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Corallococcus aberystwythensis",
"Herpesvirales",
"Homo sapiens"
] | [
1,
673,
1
] | 3 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Herpesvirus major capsid protein | Herpesvirus major capsid protein | Herpes_MCP | 5 |
IPR000913 | 913 | Neurokinin NK2 receptor | NK2_rcpt | Family | 593 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004995",
"GO:0007186",
"GO:0005886",
"GO:0016020"
] | [
"tachykinin receptor activity",
"G protein-coupled receptor signaling pathway",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01025"
] | [
"NEUROKININ2R"
] | [
593
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"361",
"R-BTA-380095",
"R-BTA-416476",
"R-CFA-380095",
"R-CFA-416476",
"R-HSA-380095",
"R-HSA-416476",
"R-MMU-380095",
"R-MMU-416476",
"R-RNO-380095",
"R-RNO-416476"
] | [
"IUPHAR:361",
"REACTOME:R-BTA-380095",
"REACTOME:R-BTA-416476",
"REACTOME:R-CFA-380095",
"REACTOME:R-CFA-416476",
"REACTOME:R-HSA-380095",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-380095",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-380095",
"REACTOME:R-RNO-416476"
] | 11 | [
"7xwo"
] | 1 | [
"PUB00000131",
"PUB00002477",
"PUB00002518",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"2478537",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Molecular characterization of a functional cDNA for rat substance P receptor.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G pr... | [
1990,
1988,
1989,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 11 | [
"IPR001681"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
593
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
5,
4,
2
] | 4 | true | Family | Neurokinin NK2 receptor | Neurokinin NK2 receptor | NK2_rcpt | 4 |
IPR000914 | 914 | Solute-binding protein family 5 domain | SBP_5_dom | Domain | 184,950 | false | false | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-bi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00496"
] | [
"SBP_bac_5"
] | [
184950
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC00799",
"R-HSA-1222538",
"R-HSA-9927020"
] | [
"PROSITEDOC:PDOC00799",
"REACTOME:R-HSA-1222538",
"REACTOME:R-HSA-9927020"
] | 3 | [
"1b05",
"1b0h",
"1b1h",
"1b2h",
"1b32",
"1b3f",
"1b3g",
"1b3h",
"1b3l",
"1b40",
"1b46",
"1b4h",
"1b4z",
"1b51",
"1b52",
"1b58",
"1b5h",
"1b5i",
"1b5j",
"1b6h",
"1b7h",
"1b9j",
"1dpe",
"1dpp",
"1jet",
"1jeu",
"1jev",
"1ola",
"1olc",
"1qka",
"1qkb",
"1rkm"... | 254 | [
"PUB00003610",
"PUB00057335",
"PUB00071925",
"PUB00071938",
"PUB00097270",
"PUB00153772"
] | [
"8336670",
"17209026",
"18310026",
"8003968",
"25338022",
"36566216"
] | [
"Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria.",
"The novel transcription factor SgrR coordinates the response to glucose-phosphate stress.",
"Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic amino acid upta... | [
1993,
2007,
2008,
1994,
2014,
2022
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Plasmid pAD1",
"unclassified sequences"
] | [
4055,
178100,
3,
517,
1,
2274
] | 6 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
12
] | 2 | true | Domain | Solute-binding protein family 5 domain | Solute-binding protein family 5 domain | SBP_5_dom | 4 |
IPR000915 | 915 | Large ribosomal subunit protein eL6 | 60S_ribosomal_eL6 | Family | 6,940 | false | false | This family represents large ribosomal subunit protein eL6 which are found in eukaryotes, including mammalian eL6 (which was previously known as L6 and TAX-responsive enhancer element binding protein 107 [ ]) [ , ], Saccharomyces cerevisiae (Baker's yeast) ribosomal protein eL6A/B (also known as YL16A/YL16B); and Mesem... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF01159",
"PTHR10715"
] | [
"Ribosomal_L6e",
""
] | [
6675,
6768
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00900",
"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:PDOC00900",
"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... | 66 | [
"3j6x",
"3j6y",
"3j77",
"3j78",
"3j79",
"3j7o",
"3j7p",
"3j7q",
"3j7r",
"3j92",
"3jag",
"3jah",
"3jai",
"3jaj",
"3jan",
"3jbn",
"3jbo",
"3jbp",
"3jbs",
"3jcs",
"3jct",
"4d5y",
"4d67",
"4u3m",
"4u3n",
"4u3u",
"4u4n",
"4u4o",
"4u4q",
"4u4r",
"4u4u",
"4u4y"... | 579 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00101554",
"PUB00110894",
"PUB00151131"
] | [
"11297922",
"11290319",
"11114498",
"32669547",
"23636399",
"8457378"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Structural snapshots of human pre-60S ribosomal particles before and after nuclear export.",
"Structures of the human and Drosophila 80S ribosome.",
"Isolat... | [
2001,
2001,
2000,
2020,
2013,
1993
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Hepatitis E virus"
] | [
4,
6935,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
14,
1,
1,
2,
11,
4,
1,
6,
9,
2,
1,
20
] | 12 | true | Family | Large ribosomal subunit protein eL6 | Large ribosomal subunit protein eL6 | 60S_ribosomal_eL6 | 9 |
IPR000916 | 916 | Bet v I/Major latex protein | Bet_v_I/MLP | Domain | 16,493 | false | false | This domain is named after Bet v 1, the major birch pollen allergen. Bet v 1 belongs to family 10 of plant pathogenesis-related proteins (PR-10), cytoplasmic proteins of 15-17 kd that are wide-spread among dicotyledonous plants [ ]. In recent years, a number of diverse plant proteins with low sequence similarity to Bet... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00407",
"SM01037"
] | [
"Bet_v_1",
"Bet_v_1"
] | [
16451,
9602
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00437"
] | [
"PROSITEDOC:PDOC00437"
] | 1 | [
"1b6f",
"1btv",
"1bv1",
"1e09",
"1fm4",
"1fsk",
"1h2o",
"1icx",
"1ifv",
"1llt",
"1qmr",
"1tw0",
"1txc",
"1vjh",
"1xdf",
"2bk0",
"2flh",
"2i9y",
"2k7h",
"2lpx",
"2q3q",
"2qim",
"2vne",
"2vq5",
"2wql",
"3c0v",
"3e85",
"3ie5",
"4a80",
"4a81",
"4a83",
"4a84"... | 131 | [
"PUB00047452",
"PUB00053295",
"PUB00056876",
"PUB00056877"
] | [
"9874249",
"18922149",
"9417891",
"15447655"
] | [
"Purification and cDNA cloning of cytokinin-specific binding protein from mung bean (Vigna radiata).",
"The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands.",
"The potential of Betv1 homologues, a nuclear multigene family, as phylogenetic markers in flowering plants.",
"... | [
1998,
2008,
1997,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
16488
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
109,
21,
21
] | 3 | true | Domain | Bet v I/Major latex protein | Bet v I/Major latex protein | Bet_v_I/MLP | 6 |
IPR000917 | 917 | Sulfatase, N-terminal | Sulfatase_N | Domain | 160,337 | false | false | This entry represents a domain found in sulphatases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00884"
] | [
"Sulfatase"
] | [
160337
] | 1 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp0918",
"PDOC00117",
"R-BTA-1663150",
"R-BTA-6798695",
"R-BTA-9840310",
"R-CFA-1663150",
"R-CFA-2022857",
"R-CFA-6798695",
"R-CFA-9840310",
"R-HSA-1663150",
"R-HSA-196071",
"R-HSA-2022857",
"R-HSA-2024096",
"R-HSA-2024101",
"R-HSA-2206285",
"R-HSA-2206290",
"R-HSA-2206296",
... | [
"GP:GenProp0918",
"PROSITEDOC:PDOC00117",
"REACTOME:R-BTA-1663150",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9840310",
"REACTOME:R-CFA-1663150",
"REACTOME:R-CFA-2022857",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-9840310",
"REACTOME:R-HSA-1663150",
"REACTOME:R-HSA-196071",
"REACTOME:R-HSA-202... | 42 | [
"1auk",
"1e1z",
"1e2s",
"1e33",
"1e3c",
"1fsu",
"1hdh",
"1n2k",
"1n2l",
"1p49",
"2qzu",
"2vqr",
"2w5q",
"2w5r",
"2w5s",
"2w5t",
"2w8d",
"2w8s",
"3b5q",
"3ed4",
"3lxq",
"4cxk",
"4cxs",
"4cxu",
"4cyr",
"4cys",
"4fdi",
"4fdj",
"4kav",
"4kay",
"4mhx",
"4miv"... | 148 | [
"PUB00002603",
"PUB00003733",
"PUB00004716"
] | [
"2303452",
"2476654",
"2122463"
] | [
"Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.",
"Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii.",
"Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA."
] | [
1990,
1989,
1990
] | 3 | [] | [
"IPR058130"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2523,
115442,
39052,
20,
3300
] | 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)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (stra... | [
7,
4,
129,
18,
10,
100,
36,
3,
52,
1,
1,
1
] | 12 | true | Domain | Sulfatase, N-terminal | Sulfatase, N-terminal | Sulfatase_N | 9 |
IPR000919 | 919 | Neutrophil cytosol factor P40 | p40phox | Family | 1,011 | false | false | Phagocytes form the first line of defence against invasion by microorganisms. Engulfing of bacteria by neutrophils is accompanied by the consumption of large amounts of oxygen, a so-called respiratory burst. Defects in phagocytosis involving the lack of a respiratory burst give rise to chronic granulomatous disease (CG... | [
"GO:0016176",
"GO:0006909",
"GO:0045730",
"GO:0043020"
] | [
"superoxide-generating NADPH oxidase activator activity",
"phagocytosis",
"respiratory burst",
"NADPH oxidase complex"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00497"
] | [
"P40PHOX"
] | [
1011
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1222556",
"R-HSA-1236973",
"R-HSA-3299685",
"R-HSA-4420097",
"R-HSA-5668599",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013423",
"R-MMU-1222556",
"R-MMU-1236973",
"R-MMU-3299685",
"R-MMU-4420097",
"R-MMU-5668599",
"R-MMU-9013149",
"R-MMU-9013404",
"R-MMU-9013423"
] | [
"REACTOME:R-HSA-1222556",
"REACTOME:R-HSA-1236973",
"REACTOME:R-HSA-3299685",
"REACTOME:R-HSA-4420097",
"REACTOME:R-HSA-5668599",
"REACTOME:R-HSA-9013149",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013423",
"REACTOME:R-MMU-1222556",
"REACTOME:R-MMU-1236973",
"REACTOME:R-MMU-3299685",
"REACTOM... | 16 | [
"1h6h",
"1oey",
"2dyb"
] | 3 | [
"PUB00003781"
] | [
"8796870"
] | [
"The NADPH oxidase and chronic granulomatous disease."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Chordata"
] | [
1011
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
7,
4,
5
] | 4 | true | Family | Neutrophil cytosol factor P40 | Neutrophil cytosol factor P40 | p40phox | 4 |
IPR000920 | 920 | Myelin P0 protein-related | Myelin_P0-rel | Family | 7,946 | false | false | This entry represents a group of transmembrane proteins, including myelin protein P0, myelin protein zero-like protein 1/2/3, sodium channel subunit beta-2 and v-set and immunoglobulin domain-containing protein 1. Myelin protein P0 is required for normal myelination in the peripheral nervous system. It mediates adhesio... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PRINTS",
"PANTHER"
] | [
"PR00213",
"PTHR13869"
] | [
"MYELINP0",
""
] | [
5852,
7703
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00491",
"R-BTA-5576892",
"R-HSA-198933",
"R-HSA-202733",
"R-HSA-445095",
"R-HSA-5576892",
"R-HSA-9619665",
"R-HSA-9717207",
"R-MMU-198933",
"R-MMU-202733"
] | [
"PROSITEDOC:PDOC00491",
"REACTOME:R-BTA-5576892",
"REACTOME:R-HSA-198933",
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-445095",
"REACTOME:R-HSA-5576892",
"REACTOME:R-HSA-9619665",
"REACTOME:R-HSA-9717207",
"REACTOME:R-MMU-198933",
"REACTOME:R-MMU-202733"
] | 10 | [
"1neu",
"3mj6",
"3mj7",
"3mj9",
"4mz2",
"4mz3",
"5ayq",
"5fdy",
"5feb",
"5xaw",
"5xax",
"6igo",
"6igt",
"6igw",
"6j8e",
"6j8g",
"6j8h",
"6j8i",
"6j8j",
"6vrr",
"6vsv",
"7dtd",
"7w77",
"7w7f",
"7w9k",
"7w9l",
"7w9m",
"7w9p",
"7w9t",
"7xm9",
"7xmf",
"7xmg"... | 48 | [
"PUB00072468",
"PUB00099904",
"PUB00154961",
"PUB00154962",
"PUB00154963",
"PUB00154964"
] | [
"12869515",
"18337304",
"18948633",
"19808477",
"23559163",
"26894959"
] | [
"JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells.",
"Different cellular and molecular mechanisms for early and late-onset myelin protein zero mutations.",
"Role of junctional adhesion molecule-like protein in mediating mon... | [
2003,
2008,
2009,
2009,
2013,
2016
] | 6 | [] | [
"IPR029861"
] | 0 | 1 | 0 | [
"Eukaryota",
"bird metagenome"
] | [
7945,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus"
] | [
20,
30,
25,
1,
40
] | 5 | true | Family | Myelin P0 protein-related | Myelin P0 protein-related | Myelin_P0-rel | 8 |
IPR000921 | 921 | Histamine H1 receptor | Histamine_H1_rcpt | Family | 763 | false | false | Histamine plays an important role in a variety of pathophysiological conditions. In allergic conditions, histamine is released from basophils and mast cells and is responsible for symptoms of allergic conditions of the skin and airways. In the gastric mucosa, gastric induced histamine release stimulates parietal cells ... | [
"GO:0004969",
"GO:0007186",
"GO:0043114",
"GO:0045907",
"GO:0016020"
] | [
"histamine receptor activity",
"G protein-coupled receptor signaling pathway",
"regulation of vascular permeability",
"positive regulation of vasoconstriction",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00530"
] | [
"HISTAMINEH1R"
] | [
763
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"262",
"R-HSA-390650",
"R-HSA-416476",
"R-MMU-390650",
"R-MMU-416476",
"R-RNO-390650",
"R-RNO-416476"
] | [
"IUPHAR:262",
"REACTOME:R-HSA-390650",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-390650",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-390650",
"REACTOME:R-RNO-416476"
] | 7 | [
"7dfl",
"8x5x",
"8x5y",
"8x63",
"8x64",
"8yn2"
] | 6 | [
"PUB00010558",
"PUB00063500",
"PUB00063501",
"PUB00063502",
"PUB00063503",
"PUB00063504",
"PUB00063506",
"PUB00063507",
"PUB00063514",
"PUB00063515",
"PUB00063516",
"PUB00063517"
] | [
"11179434",
"16402096",
"19772756",
"12113221",
"17490952",
"19843401",
"9311023",
"12626656",
"21618887",
"7644667",
"11972592",
"8008209"
] | [
"Cloning and pharmacological characterization of a fourth histamine receptor (H(4)) expressed in bone marrow.",
"Histamine and its receptors.",
"Intranasal antihistamines for allergic rhinitis: mechanism of action.",
"Histamine and antihistamines in anaphylaxis.",
"Histamine and histamine intolerance.",
"... | [
2001,
2006,
2009,
2002,
2007,
2009,
1997,
2003,
2010,
1995,
2002,
1994
] | 12 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
763
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
3,
2,
10
] | 4 | true | Family | Histamine H1 receptor | Histamine H1 receptor | Histamine_H1_rcpt | 6 |
IPR000922 | 922 | D-galactoside/L-rhamnose binding SUEL lectin domain | Lectin_gal-bd_dom | Domain | 25,714 | false | false | The D-galactoside binding lectin purified from sea urchin (Anthocidaris crassispina) eggs exists as a disulphide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity [ ]. The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galac... | [
"GO:0030246"
] | [
"carbohydrate binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF02140",
"PS50228"
] | [
"SUEL_Lectin",
"SUEL_LECTIN"
] | [
25167,
25122
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC50228",
"R-DME-373080",
"R-DME-6798695"
] | [
"PROSITEDOC:PDOC50228",
"REACTOME:R-DME-373080",
"REACTOME:R-DME-6798695"
] | 3 | [
"2jx9",
"2jxa",
"2zx0",
"2zx1",
"2zx2",
"2zx3",
"2zx4",
"5afb",
"5ftt",
"5ftu",
"5h4s",
"5iaz",
"6ska",
"6ske",
"6vhh",
"7wy5",
"7wy8",
"7wyb",
"7x10",
"8djg",
"8gl6",
"8suf"
] | 22 | [
"PUB00005840",
"PUB00006605",
"PUB00006606",
"PUB00006607",
"PUB00006608"
] | [
"9920906",
"2001368",
"10564781",
"9261169",
"9668106"
] | [
"Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants.",
"Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris cr... | [
1999,
1991,
1999,
1997,
1998
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"ecological metagenomes"
] | [
25606,
93,
10,
5
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
64,
4,
198,
10,
36,
39,
35,
49,
127
] | 9 | true | Domain | D-galactoside/L-rhamnose binding SUEL lectin domain | D-galactoside/L-rhamnose binding SUEL lectin domain | Lectin_gal-bd_dom | 1 |
IPR000923 | 923 | Blue (type 1) copper domain | BlueCu_1 | Domain | 17,064 | false | false | The small blue proteins are single-domain proteins. The domain consists of a β-sheet sandwich, composed of eight strands in two sheets, and has predominantly antiparallel β-strand topology [ ]. This entry represents the blue copper domain. Blue (type 1) copper proteins constitute a diverse class of proteins, including ... | [
"GO:0005507",
"GO:0009055"
] | [
"copper ion binding",
"electron transfer activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00127"
] | [
"Copper-bind"
] | [
17064
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00174"
] | [
"PROSITEDOC:PDOC00174"
] | 1 | [
"1a3z",
"1a4a",
"1a4b",
"1a4c",
"1aac",
"1aaj",
"1aan",
"1adw",
"1ag0",
"1ag6",
"1aiz",
"1azb",
"1azc",
"1azn",
"1azr",
"1azu",
"1b3i",
"1baw",
"1bex",
"1bqk",
"1bqr",
"1bxa",
"1bxu",
"1bxv",
"1byo",
"1byp",
"1cc3",
"1cuo",
"1cur",
"1dyz",
"1dz0",
"1e5y"... | 300 | [
"PUB00001602",
"PUB00001621",
"PUB00001648",
"PUB00002400",
"PUB00002762",
"PUB00002847",
"PUB00003425"
] | [
"1995346",
"1879547",
"1468551",
"6698995",
"1313011",
"8195126",
"8433378"
] | [
"A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins.",
"The amino acid sequence of rusticyanin isolated from Thiobacillus ferrooxidans.",
"The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-termi... | [
1991,
1991,
1992,
1984,
1992,
1994,
1993
] | 7 | [] | [
"IPR017533"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3674,
11718,
1357,
89,
226
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
6
] | 3 | true | Domain | Blue (type 1) copper domain | Blue (type 1) copper domain | BlueCu_1 | 9 |
IPR000924 | 924 | Glutamyl/glutaminyl-tRNA synthetase | Glu/Gln-tRNA-synth | Family | 70,147 | false | false | Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase; ) is a class I aminoacyl-tRNA synthetase. This enzyme shares similarities with glutaminyl-tRNA synthetase in terms of structure and catalytic properties. Glutamyl-tRNA synthetase (GluRS) and glutaminyl-tRNA synthetase (GlnRS) are grouped in the GlxRS subcla... | [
"GO:0000166",
"GO:0004812",
"GO:0005524",
"GO:0043039"
] | [
"nucleotide binding",
"aminoacyl-tRNA ligase activity",
"ATP binding",
"tRNA aminoacylation"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR00987"
] | [
"TRNASYNTHGLU"
] | [
70147
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"6.1.1.17",
"PWY-5188",
"R-BTA-9856649",
"R-DDI-9856649",
"R-DME-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-6782315",
"R-HSA-9856649",
"R-MMU-9856649",
"R-RNO-9856649"
] | [
"EC:6.1.1",
"EC:6.1.1.17",
"METACYC:PWY-5188",
"REACTOME:R-BTA-9856649",
"REACTOME:R-DDI-9856649",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-6782315",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9856649",
"REACTOME:R-R... | 13 | [
"1euq",
"1euy",
"1exd",
"1g59",
"1gln",
"1gsg",
"1gtr",
"1gts",
"1j09",
"1n75",
"1n77",
"1n78",
"1nyl",
"1nzj",
"1o0b",
"1o0c",
"1qrs",
"1qrt",
"1qru",
"1qtq",
"1zjw",
"2cfo",
"2cuz",
"2cv0",
"2cv1",
"2cv2",
"2dxi",
"2hz7",
"2ja2",
"2o5r",
"2rd2",
"2re8"... | 73 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006397",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873",
"PUB00103850",
"PUB00103851"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"9426192",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790",
"9746349",
"8078941"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
1997,
2000,
1990,
1999,
2000,
2002,
1998,
1994
] | 12 | [] | [
"IPR004514",
"IPR004526",
"IPR049940"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
948,
53367,
14820,
19,
993
] | 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",... | [
13,
4,
6,
5,
3,
18,
12,
3,
10,
14,
3,
3,
39
] | 13 | true | Family | Glutamyl/glutaminyl-tRNA synthetase | Glutamyl/glutaminyl-tRNA synthetase | Glu/Gln-tRNA-synth | 8 |
IPR000925 | 925 | Major surface glycoprotein G | G_prot | Family | 21,098 | false | false | Respiratory synctial virus (RSV) has two major virion envelope proteins, the fusion F and major attachment G glycoproteins, which are the two viral neutralisation antigens [ ]. This entry represents the major surface glycoprotein G from RSV. G glycoprotein interacts with host CX3CR1, the receptor for the CX3C chemokine... | [
"GO:0055036"
] | [
"virion membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF00802"
] | [
"Glycoprotein_G"
] | [
21098
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-9820960",
"R-HSA-9820962",
"R-HSA-9828721",
"R-HSA-9828806",
"R-HSA-9833110"
] | [
"REACTOME:R-HSA-9820960",
"REACTOME:R-HSA-9820962",
"REACTOME:R-HSA-9828721",
"REACTOME:R-HSA-9828806",
"REACTOME:R-HSA-9833110"
] | 5 | [
"1brv",
"5wn9",
"5wna",
"6blh",
"6bli",
"6uvo",
"7t8w",
"9cqa",
"9cqb",
"9cqd"
] | 10 | [
"PUB00070952",
"PUB00070953",
"PUB00070954"
] | [
"18842713",
"11477410",
"16424189"
] | [
"The secreted form of respiratory syncytial virus G glycoprotein helps the virus evade antibody-mediated restriction of replication by acting as an antigen decoy and through effects on Fc receptor-bearing leukocytes.",
"CX3C chemokine mimicry by respiratory syncytial virus G glycoprotein.",
"Respiratory syncyti... | [
2008,
2001,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Pneumoviridae"
] | [
21098
] | 1 | [] | [] | 0 | true | Family | Major surface glycoprotein G | Major surface glycoprotein G | G_prot | 7 |
IPR000926 | 926 | GTP cyclohydrolase II, RibA | RibA | Family | 28,167 | false | false | GTP cyclohydrolase II (also known as ribA) catalyses the first committed step in the biosynthesis of riboflavin (vitamin b2). The enzyme converts GTP to 2,5-diamino-6-beta-ribosyl-4(3H)-pyrimidinone 5'-phosphate (APy), formate and pyrophosphate, and requires magnesium as a cofactor. In numerous bacteria and in plants, ... | [
"GO:0003935",
"GO:0009231"
] | [
"GTP cyclohydrolase II activity",
"riboflavin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00179",
"TIGR00505",
"cd00641"
] | [
"RibA",
"ribA",
"GTP_cyclohydro2"
] | [
22007,
20784,
28167
] | 3 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.5.4.25",
"GenProp1734",
"PWY-6168",
"PWY-7539",
"PWY-7991"
] | [
"EC:3.5.4.25",
"GP:GenProp1734",
"METACYC:PWY-6168",
"METACYC:PWY-7539",
"METACYC:PWY-7991"
] | 5 | [
"2bz0",
"2bz1",
"4i14",
"4rl4",
"7eev",
"7ej3"
] | 6 | [
"PUB00076431",
"PUB00080016"
] | [
"10940330",
"17002314"
] | [
"Biosynthesis of vitamin b2 (riboflavin).",
"Evolution of new function in the GTP cyclohydrolase II proteins of Streptomyces coelicolor."
] | [
2000,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
98,
22451,
5231,
387
] | 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"
] | [
11,
1,
2,
5,
1,
2,
33
] | 7 | true | Family | GTP cyclohydrolase II, RibA | GTP cyclohydrolase II, RibA | RibA | 8 |
IPR000928 | 928 | SNAP-25 domain | SNAP-25_dom | Domain | 3,964 | false | false | This entry represents a domain found in the SNAP-25 family members. SNAP-25 (synaptosome-associated protein 25kDa) proteins are components of SNARE complexes, which are proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex (the SNARE or core complex) that b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00835"
] | [
"SNAP-25"
] | [
3964
] | 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-181429",
"R-BTA-181430",
"R-BTA-210500",
"R-BTA-212676",
"R-BTA-264642",
"R-BTA-449836",
"R-BTA-6798695",
"R-BTA-888590",
"R-DME-181429",
"R-DME-181430",
"R-DME-199992",
"R-DME-210500",
"R-DME-212676",
"R-DME-264642",
"R-DME-449836",
"R-DME-6798695",
"R-DME-888590",
"R-DME-8... | [
"REACTOME:R-BTA-181429",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-212676",
"REACTOME:R-BTA-264642",
"REACTOME:R-BTA-449836",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-888590",
"REACTOME:R-DME-181429",
"REACTOME:R-DME-181430",
"REACTOME:R-DME-199992",
"REACTOME:R-DME-21... | 83 | [
"1l4a",
"1sfc",
"3j96",
"3j97",
"3j98",
"3j99",
"6ip1",
"6mdm",
"6mdn",
"6mdo",
"6mdp",
"9ojz",
"9ok3",
"9olo",
"9om6",
"9paf",
"9pag",
"9pb9",
"9pba",
"9pbf",
"9pbv",
"9pc3",
"9pcx",
"9pcz",
"9pd1",
"9pd8"
] | 26 | [
"PUB00002810",
"PUB00010661"
] | [
"8226991",
"12154365"
] | [
"Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones.",
"Snares and Munc18 in synaptic vesicle fusion."
] | [
1993,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
3964
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
18,
2,
8,
5,
10
] | 6 | true | Domain | SNAP-25 domain | SNAP-25 domain | SNAP-25_dom | 9 |
IPR000929 | 929 | Dopamine receptor family | Dopamine_rcpt | Family | 6,797 | false | false | Dopamine receptors are members of the rhodopsin-like G-protein coupled receptor family and are prominent in the vertebrate central nervous system (CNS). Dysfunction of dopaminergic neurotransmission in the CNS has been implicated in a variety of neuropsychiatric disorders [ ], including social phobia [ ], Tourette's sy... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00242"
] | [
"DOPAMINER"
] | [
6797
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-390651",
"R-BTA-418555",
"R-DME-390666",
"R-DME-418555",
"R-DME-9706019",
"R-HSA-390651",
"R-HSA-418555",
"R-HSA-418594",
"R-MMU-390651",
"R-MMU-418555",
"R-MMU-418594",
"R-RNO-390651",
"R-RNO-418594"
] | [
"REACTOME:R-BTA-390651",
"REACTOME:R-BTA-418555",
"REACTOME:R-DME-390666",
"REACTOME:R-DME-418555",
"REACTOME:R-DME-9706019",
"REACTOME:R-HSA-390651",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-390651",
"REACTOME:R-MMU-418555",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-39... | 13 | [
"5wiu",
"5wiv",
"6iql",
"7ckw",
"7ckx",
"7cky",
"7ckz",
"7cmu",
"7cmv",
"7crh",
"7dfp",
"7f0t",
"7f1o",
"7f1z",
"7f23",
"7f24",
"7jv5",
"7jvp",
"7jvq",
"7jvr",
"7ljc",
"7ljd",
"7x2c",
"7x2d",
"7x2f",
"8irr",
"8irs",
"8irt",
"8iru",
"8irv",
"8jxr",
"8jxs"... | 38 | [
"PUB00064281",
"PUB00064282",
"PUB00064283",
"PUB00064284",
"PUB00064285",
"PUB00064286",
"PUB00064287",
"PUB00064288",
"PUB00064289",
"PUB00064290",
"PUB00064291",
"PUB00064292",
"PUB00064293",
"PUB00067001"
] | [
"15148138",
"10698826",
"16613557",
"17017512",
"12555236",
"16961425",
"11920678",
"9633679",
"16433053",
"14060771",
"1060115",
"12836695",
"9457173",
"16458973"
] | [
"The neurobiology of dopamine signaling.",
"Low dopamine D(2) receptor binding potential in social phobia.",
"Dopamine and the diseased brain.",
"The nigrostriatal DA pathway and Parkinson's disease.",
"Relationship between functional dopamine D2 and D3 receptors gene polymorphisms and neuroleptic malignant... | [
2004,
2000,
2006,
2006,
2003,
2006,
2002,
1998,
2005,
1963,
1975,
2003,
1998,
2006
] | 14 | [
"IPR000276"
] | [
"IPR000497",
"IPR001413",
"IPR001620",
"IPR001922",
"IPR002185"
] | 1 | 5 | 0 | [
"Eumetazoa"
] | [
6797
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
32,
6,
16,
10,
16
] | 5 | true | Family | Dopamine receptor family | Dopamine receptor family | Dopamine_rcpt | 9 |
IPR000930 | 930 | Peptidase S3, togavirin | Peptidase_S3 | Domain | 2,263 | false | false | Togavirin, also known as Sindbis virus core endopeptidase, is a serine protease resident at the N terminus of the p130 polyprotein of togaviruses [ ]. The endopeptidase signature identifies the peptidase as belonging to the MEROPS peptidase family S3 (togavirin family, clan PA(S)). The polyprotein also includes structu... | [
"GO:0004252",
"GO:0006508"
] | [
"serine-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF00944",
"PR00798",
"PS51690"
] | [
"Peptidase_S3",
"TOGAVIRIN",
"ALPHAVIRUS_CP"
] | [
2242,
2186,
2257
] | 3 | [
"EC"
] | [
"3.4.21.90"
] | [
"EC:3.4.21.90"
] | 1 | [
"1dyl",
"1ep5",
"1ep6",
"1kxa",
"1kxb",
"1kxc",
"1kxd",
"1kxe",
"1kxf",
"1ld4",
"1svp",
"1vcp",
"1vcq",
"1wyk",
"1z8y",
"2snv",
"2snw",
"2yew",
"3j0c",
"3j0f",
"3j2w",
"4agj",
"4agk",
"4uon",
"5g4b",
"5h23",
"5vu2",
"6mx4",
"6mx7",
"6nk5",
"6nk6",
"6nk7"... | 98 | [
"PUB00003576",
"PUB00004110"
] | [
"7845208",
"1944569"
] | [
"Families of serine peptidases.",
"Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion."
] | [
1994,
1991
] | 2 | [] | [] | 0 | 0 | null | [
"Alphavirus",
"Fungi",
"Salinirubellus salinus"
] | [
2259,
3,
1
] | 3 | [] | [] | 0 | true | Domain | Peptidase S3, togavirin | Peptidase S3, togavirin | Peptidase_S3 | 3 |
IPR000931 | 931 | Adenovirus fibre protein | Adeno_fibre | Family | 1,446 | false | false | Adenoviruses are responsible for diseases such as pneumonia, cystitis, conjunctivitis and diarrhoea, all of which can be fatal to patients who are immunocompromised [ ]. Viral infection commences with recognition of host cell receptors by means of specialised proteins on viral surfaces. The adenovirus fibre protein `kn... | [
"GO:0007155",
"GO:0019058",
"GO:0019062"
] | [
"cell adhesion",
"viral life cycle",
"virion attachment to host cell"
] | [
"biological_process",
"biological_process",
"biological_process"
] | 3 | [
"PRINTS"
] | [
"PR00307"
] | [
"ADENOVSFIBRE"
] | [
1446
] | 1 | [] | [] | [] | 0 | [
"1h7z",
"1kac",
"1knb",
"1nob",
"1p69",
"1p6a",
"1qhv",
"1qiu",
"1uxa",
"1uxb",
"1uxe",
"2bzu",
"2bzv",
"2j12",
"2o39",
"2qlk",
"2wbw",
"2wgt",
"2wgu",
"2wst",
"3bq4",
"3cnc",
"3exv",
"3exw",
"3f0y",
"3izo",
"3l88",
"3l89",
"3n0i",
"3o8e",
"3qnd",
"4atz"... | 79 | [
"PUB00005244"
] | [
"7704534"
] | [
"Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Adenoviridae",
"Eukaryota"
] | [
1443,
3
] | 2 | [] | [] | 0 | true | Family | Adenovirus fibre protein | Adenovirus fibre protein | Adeno_fibre | 6 |
IPR000932 | 932 | Photosystem antenna protein-like | PS_antenna-like | Family | 35,844 | false | false | This entry represents the intrinsic antenna proteins CP43 (PsbC) and CP47 (PsbB) found in the reaction centre of PSII. These polypeptides bind to chlorophyll a and beta-carotene and pass the excitation energy on to the reaction centre [ ]. This entry also includes the iron-stress induced chlorophyll-binding protein CP4... | [
"GO:0016168",
"GO:0009767",
"GO:0019684",
"GO:0009521",
"GO:0016020"
] | [
"chlorophyll binding",
"photosynthetic electron transport chain",
"photosynthesis, light reaction",
"photosystem",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 5 | [
"PFAM"
] | [
"PF00421"
] | [
"PSII"
] | [
35844
] | 1 | [] | [] | [] | 0 | [
"1izl",
"1s5l",
"1w5c",
"2axt",
"3a0b",
"3a0h",
"3jcu",
"3kzi",
"3wu2",
"4fby",
"4il6",
"4ixq",
"4ixr",
"4pbu",
"4pj0",
"4rvy",
"4tnh",
"4tni",
"4tnj",
"4tnk",
"4ub6",
"4ub8",
"4v62",
"4v82",
"4yuu",
"5b5e",
"5b66",
"5e79",
"5e7c",
"5gth",
"5gti",
"5h2f"... | 172 | [
"PUB00015357",
"PUB00015358",
"PUB00015359",
"PUB00015360",
"PUB00015361",
"PUB00097583",
"PUB00152828"
] | [
"12518057",
"15100025",
"14871485",
"12163077",
"15301529",
"30076221",
"33846594"
] | [
"Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.",
"The evolutionary development of the protein complement of photosystem 2.",
"The low molecular mass subunits of the photosynthetic supracomplex, photosystem II.",
"Photosystem II: a multisubunit membr... | [
2003,
2004,
2004,
2002,
2004,
2018,
2021
] | 7 | [] | [
"IPR005869",
"IPR017486"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1683,
34158,
3
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
14,
12
] | 3 | true | Family | Photosystem antenna protein-like | Photosystem antenna protein-like | PS_antenna-like | 5 |
IPR000933 | 933 | Glycoside hydrolase, family 29 | Glyco_hydro_29 | Family | 24,418 | false | false | O-Glycosyl hydrolases family 29 ( ) encompasses alpha-L-fucosidases ( ) [ ], which is a lysosomal enzyme responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-l... | [
"GO:0004560",
"GO:0005975"
] | [
"alpha-L-fucosidase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"SMART"
] | [
"PTHR10030",
"SM00812"
] | [
"",
"Alpha_L_fucos"
] | [
24208,
23883
] | 2 | [
"CAZY",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"GH29",
"3.2.1.51",
"PWY-6807",
"PDOC00324",
"R-BTA-6798695",
"R-BTA-975578",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-CEL-975578",
"R-DDI-6798695",
"R-DDI-975578",
"R-DME-381426",
"R-DME-6798695",
"R-DME-8957275",
"R-DME-975578",
"R-HSA-381426",
"R-HSA-6798695",
"R-H... | [
"CAZY:GH29",
"EC:3.2.1.51",
"METACYC:PWY-6807",
"PROSITEDOC:PDOC00324",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-975578",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8957275",
"REACTOME:R-CEL-975578",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-975578",
"REACTOME:R-DME-... | 28 | [
"1hl8",
"1hl9",
"1odu",
"2wsp",
"2wvs",
"2wvt",
"2wvu",
"2wvv",
"2xib",
"2xii",
"2zwy",
"2zwz",
"2zx5",
"2zx6",
"2zx7",
"2zx8",
"2zx9",
"2zxa",
"2zxb",
"2zxd",
"3eyp",
"3gza",
"3mo4",
"3ues",
"3uet",
"4j27",
"4j28",
"4jfs",
"4jft",
"4jfu",
"4jfv",
"4jfw"... | 87 | [
"PUB00000482",
"PUB00004870",
"PUB00005266",
"PUB00021761",
"PUB00043486",
"PUB00043487"
] | [
"2482732",
"7624375",
"8535779",
"14715651",
"18556148",
"18522672"
] | [
"Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Crystal structure of Thermotoga maritima alpha-L-fucosidas... | [
1989,
1995,
1995,
2004,
2008,
2008
] | 6 | [] | [
"IPR016286"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
79,
17183,
6827,
5,
324
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
4,
1,
4,
1,
5,
5,
5,
7,
13
] | 9 | true | Family | Glycoside hydrolase, family 29 | Glycoside hydrolase, family 29 | Glyco_hydro_29 | 2 |
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