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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000280 | 280 | Pestivirus NS3, peptidase S31 | Pestivirus_NS3_S31 | Domain | 950 | false | false | The genome of pestiviruses is a single plus-strand RNA and contains a single large open reading frame (ORF), a 5' untranslated region (5'UTR) and a 3' untranslated region (3'UTR). The ORF encodes a polyprotein, which is processed by viral and cellular proteases into mature proteins (the structural proteins in the N-ter... | [
"GO:0004252"
] | [
"serine-type endopeptidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PROFILE"
] | [
"PF05578",
"PR00729",
"PS51535"
] | [
"Peptidase_S31",
"CDVENDOPTASE",
"PESTIVIRUS_NS3PRO"
] | [
940,
828,
932
] | 3 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.21.113",
"3.4.22.-",
"3.6.1.15",
"3.6.4.13",
"4.6.1.19",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:2.7.7.48",
"EC:3.4.21.113",
"EC:3.4.22.-",
"EC:3.6.1.15",
"EC:3.6.4.13",
"EC:4.6.1.19",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 11 | [
"5mz4",
"5wx1"
] | 2 | [
"PUB00011704",
"PUB00020025",
"PUB00020058",
"PUB00030423",
"PUB00057971",
"PUB00057972",
"PUB00076953"
] | [
"11517925",
"9891971",
"9603310",
"14725770",
"2543956",
"19951725",
"7044372"
] | [
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"Virus-encoded proteinases of the Flaviviridae.",
"The structure of sortase B, a cysteine transpeptidase that tethers surfac... | [
2001,
1998,
1998,
2004,
1989,
2010,
1982
] | 7 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Eukaryota",
"Riboviria",
"viral metagenome"
] | [
2,
4,
943,
1
] | 4 | [] | [] | 0 | true | Domain | Pestivirus NS3, peptidase S31 | Pestivirus NS3, peptidase S31 | Pestivirus_NS3_S31 | 2 |
IPR000281 | 281 | Helix-turn-helix protein RpiR | HTH_RpiR | Domain | 50,376 | false | false | This domain contains a helix-turn-helix motif [ ]. Every member of this family is N-terminal to a SIS domain . Members of this family are probably regulators of genes involved in phosphosugar metobolism. | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF01418",
"PS51071"
] | [
"HTH_6",
"HTH_RPIR"
] | [
48949,
50247
] | 2 | [
"PROSITEDOC"
] | [
"PDOC51071"
] | [
"PROSITEDOC:PDOC51071"
] | 1 | [
"2o3f",
"3iwf",
"4ivn",
"8ju9",
"8k3b",
"8tx9",
"8txl",
"8v4v",
"8v5f",
"9dqn"
] | 10 | [
"PUB00002286"
] | [
"8576032"
] | [
"Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
4,
50151,
40,
181
] | 4 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Domain | Helix-turn-helix protein RpiR | Helix-turn-helix protein RpiR | HTH_RpiR | 3 |
IPR000283 | 283 | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | NADH_UbQ_OxRdtase_75kDa_su_CS | Conserved_site | 22,130 | false | false | This entry represents the 75kDa subunit from NADH:ubiquinone oxidoreductase. Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 75kDa (in mammals), which is the largest subunit of complex I and is a component of the iron-sulphur (IP) fragment of the enzyme. It seems to b... | [
"GO:0008137",
"GO:0042773",
"GO:0016020"
] | [
"NADH dehydrogenase (ubiquinone) activity",
"ATP synthesis coupled electron transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE",
"PROSITE"
] | [
"PS00641",
"PS00642",
"PS00643"
] | [
"COMPLEX1_75K_1",
"COMPLEX1_75K_2",
"COMPLEX1_75K_3"
] | [
19688,
17818,
18594
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1",
"PDOC00554",
"R-BTA-611105",
"R-BTA-6799198",
"R-BTA-9837999",
"R-DDI-6799198",
"R-DDI-9837999",
"R-DME-611105",
"R-DME-6799198",
"R-DME-9837999",
"R-HSA-611105",
"R-HSA-6799198",
"R-HSA-9837999",
"R-MMU-611105",
"R-MMU-6799198",
"R-MMU-9837999",
"R-RNO-611105",
"R-RNO-679... | [
"EC:7.1.1",
"PROSITEDOC:PDOC00554",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-6799198",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DDI-6799198",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-6799198",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-6799198",
... | 19 | [
"2fug",
"2ybb",
"3i9v",
"3iam",
"3ias",
"3m9s",
"4hea",
"5gpn",
"5gup",
"5lc5",
"5ldw",
"5ldx",
"5lnk",
"5o31",
"5xf9",
"5xfa",
"5xtb",
"5xtd",
"5xth",
"5xti",
"6g2j",
"6g72",
"6gcs",
"6h8k",
"6i0d",
"6i1p",
"6q8o",
"6q8w",
"6q8x",
"6q9d",
"6qa9",
"6qbx"... | 332 | [
"PUB00005074",
"PUB00043561",
"PUB00045437"
] | [
"1470679",
"10940377",
"18394423"
] | [
"The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.",
"The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.",
"Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)."
] | [
1992,
2000,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
71,
16401,
5117,
541
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
7,
1,
1,
4,
1,
6,
6,
1,
2,
4,
8
] | 11 | true | Conserved_site | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | NADH:ubiquinone oxidoreductase, 75kDa subunit, conserved site | NADH_UbQ_OxRdtase_75kDa_su_CS | 7 |
IPR000286 | 286 | Histone deacetylase HDAC | HDACs | Family | 61,930 | false | false | Histone deacetylases (HDACs) are a class of enzymes that remove acetyl groups from N(6)-acetyl-lysine residues on histones. This process plays a critical role in transcription regulation, as HDACs facilitate tighter wrapping of DNA around histones. DNA expression is regulated in part by the balance between acetylation ... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR01270"
] | [
"HDASUPER"
] | [
61930
] | 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... | [
"3.5.1",
"3.5.1.98",
"R-BTA-1538133",
"R-BTA-201722",
"R-BTA-2173795",
"R-BTA-3214815",
"R-BTA-350054",
"R-BTA-3769402",
"R-BTA-4551638",
"R-BTA-6804758",
"R-BTA-73762",
"R-BTA-8936459",
"R-BTA-8943724",
"R-BTA-9018519",
"R-BTA-9022692",
"R-BTA-9701898",
"R-BTA-9764725",
"R-BTA-982... | [
"EC:3.5.1",
"EC:3.5.1.98",
"REACTOME:R-BTA-1538133",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-2173795",
"REACTOME:R-BTA-3214815",
"REACTOME:R-BTA-350054",
"REACTOME:R-BTA-3769402",
"REACTOME:R-BTA-4551638",
"REACTOME:R-BTA-6804758",
"REACTOME:R-BTA-73762",
"REACTOME:R-BTA-8936459",
"REACTOME... | 207 | [
"1c3p",
"1c3r",
"1c3s",
"1t64",
"1t67",
"1t69",
"1vkg",
"1w22",
"1zz0",
"1zz1",
"1zz3",
"2gh6",
"2v5w",
"2v5x",
"2vcg",
"2vqj",
"2vqm",
"2vqo",
"2vqq",
"2vqv",
"2vqw",
"3c0y",
"3c0z",
"3c10",
"3ew8",
"3ewf",
"3ezp",
"3ezt",
"3f06",
"3f07",
"3f0r",
"3max"... | 381 | [
"PUB00004480",
"PUB00160366"
] | [
"9278492",
"38822399"
] | [
"Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily.",
"Advances in targeting histone deacetylase for treatment of solid tumors."
] | [
1997,
2024
] | 2 | [] | [
"IPR003084",
"IPR003085"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
890,
23376,
37161,
31,
472
] | 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,
9,
51,
50,
75,
42,
4,
35,
63,
5,
3,
69
] | 12 | true | Family | Histone deacetylase HDAC | Histone deacetylase HDAC | HDACs | 2 |
IPR000289 | 289 | Small ribosomal subunit protein eS28 | Ribosomal_eS28 | Family | 5,479 | false | false | A number of eukaryotic and archaebacterial ribosomal proteins can be grouped on the basis of sequence similarities. Examples are: Mammalian S28 [ , ] Plant S28 [ ] Fungi S33 [ ] Archaebacterial S28e. These proteins have from 64 to 78 amino acids and a highly conserved C-terminal region. S1-like RNA-binding domains are ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"CDD"
] | [
"MF_00292",
"PF01200",
"PTHR10769",
"cd04457"
] | [
"Ribosomal_eS28",
"Ribosomal_S28e",
"",
"S1_S28E"
] | [
3940,
5477,
5190,
4969
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00743",
"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:PDOC00743",
"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"... | 110 | [
"1ne3",
"1ny4",
"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"... | 626 | [
"PUB00000944",
"PUB00004578",
"PUB00005646",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00009424",
"PUB00029026",
"PUB00029269",
"PUB00090043"
] | [
"9008164",
"8278557",
"1481571",
"11297922",
"11290319",
"11114498",
"11875025",
"14627743",
"14627742",
"25957688"
] | [
"The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.",
"Cloning of an Arabidopsis ribosomal protein S28 cDNA.",
"Structure and expression of the ABF1-regulated ribosomal protein S33 gene in Kluyveromyces.",
"Atomic structures at last: the ribosome in 2000.",
... | [
1997,
1993,
1992,
2001,
2001,
2000,
2002,
2003,
2003,
2015
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Candidatus Zambryskibacteria bacterium CG10_big_fil_rev_8_21_14_0_10_34_34",
"Eukaryota",
"ecological metagenomes"
] | [
894,
1,
4546,
38
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
8,
1,
1,
5,
2,
3,
1,
3,
5,
2,
2,
11
] | 12 | true | Family | Small ribosomal subunit protein eS28 | Small ribosomal subunit protein eS28 | Ribosomal_eS28 | 1 |
IPR000290 | 290 | Colicin immunity protein/pyocin immunity protein | Colicin_pyocin | Family | 2,262 | false | false | This family includes bacterial colicin and pyocin immunity proteins [ , ]. These immunity proteins can bind specifically to the DNase-type colicins and pyocins and inhibit their bactericidal activity. The 1.8-angstrom crystal structure of the ImmE7 protein consists of four antiparallel α-helices [ ]. Sequence similarit... | [
"GO:0015643",
"GO:0030153"
] | [
"toxic substance binding",
"bacteriocin immunity"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PRINTS",
"CDD"
] | [
"PF01320",
"PR01299",
"cd16363"
] | [
"Colicin_Pyocin",
"PYOCIN",
"Col_Im_like"
] | [
2262,
1552,
1640
] | 3 | [] | [] | [] | 0 | [
"1ayi",
"1bxi",
"1cei",
"1e0h",
"1emv",
"1fr2",
"1gxg",
"1gxh",
"1imp",
"1imq",
"1mz8",
"1ujz",
"1unk",
"1znv",
"2erh",
"2gyk",
"2gze",
"2gzf",
"2gzg",
"2gzi",
"2gzj",
"2jaz",
"2jb0",
"2jbg",
"2k0d",
"2k5x",
"2no8",
"2vln",
"2vlo",
"2vlp",
"2vlq",
"2wpt"... | 44 | [
"PUB00000437",
"PUB00004893",
"PUB00006228",
"PUB00006230",
"PUB00006233"
] | [
"8755730",
"8692833",
"6253914",
"3892228",
"3936034"
] | [
"Three-dimensional solution structure and 13C nuclear magnetic resonance assignments of the colicin E9 immunity protein Im9.",
"The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.",
"Molecular structure of the immunity gene and immunity protein of the bac... | [
1996,
1996,
1980,
1985,
1985
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Plasmid ColE3-CA38",
"metagenomes"
] | [
2259,
1,
2
] | 3 | [] | [] | 0 | true | Family | Colicin immunity protein/pyocin immunity protein | Colicin immunity protein/pyocin immunity protein | Colicin_pyocin | 6 |
IPR000291 | 291 | D-alanine--D-alanine ligase/VANA/B/C, conserved site | D-Ala_lig_Van_CS | Conserved_site | 32,178 | false | false | D-alanine--D-alanine ligase ( ) is a bacterial enzyme involved in cell-wall biosynthesis. It participates in forming UDP-N-acetylmuramyl pentapeptide, the peptidoglycan precursor. These enzymes are proteins of 300 to 360 amino acids containing many conserved regions. The N-terminal Gly-rich region could be involved in ... | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00843",
"PS00844"
] | [
"DALA_DALA_LIGASE_1",
"DALA_DALA_LIGASE_2"
] | [
30168,
28157
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"6.3.2.4",
"PWY-6386",
"PWY-6387",
"PWY-7953",
"PDOC00659"
] | [
"EC:6.3.2.4",
"METACYC:PWY-6386",
"METACYC:PWY-6387",
"METACYC:PWY-7953",
"PROSITEDOC:PDOC00659"
] | 5 | [
"1e4e",
"1ehi",
"1iov",
"1iow",
"2dln",
"2fb9",
"2i80",
"2i87",
"2i8c",
"2pvp",
"2yzg",
"2yzm",
"2yzn",
"2zdg",
"2zdh",
"2zdq",
"3e5n",
"3i12",
"3k3p",
"3lwb",
"3n8d",
"3q1k",
"3r23",
"3r5f",
"3r5x",
"3rfc",
"3se7",
"3tqt",
"3v4z",
"4c5a",
"4c5b",
"4c5c"... | 66 | [
"PUB00000444"
] | [
"9054558"
] | [
"D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5,
30674,
854,
645
] | 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",
"Zea mays"
] | [
15,
2,
1,
4,
7
] | 5 | true | Conserved_site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | D-alanine--D-alanine ligase/VANA/B/C, conserved site | D-Ala_lig_Van_CS | 1 |
IPR000292 | 292 | Formate/nitrite transporter | For/NO2_transpt | Family | 19,211 | false | false | Proteins in this entry belong to the Formate-Nitrite Transporter (FNT) family (TC 2.A.44), including the nitrite transport protein NirC and formate channel FocA. The prokaryotic proteins of the FNT family function in the transport of the structurally related compounds, formate and nitrite [ , ]. Structures from NirC an... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"PF01226",
"PTHR30520",
"TIGR00790"
] | [
"Form_Nir_trans",
"",
"fnt"
] | [
19196,
19093,
4929
] | 3 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0943",
"PDOC00769"
] | [
"GP:GenProp0943",
"PROSITEDOC:PDOC00769"
] | 2 | [
"3kcu",
"3kcv",
"3kly",
"3klz",
"3q7k",
"3tdo",
"3tdp",
"3tdr",
"3tds",
"3tdx",
"3te0",
"3te1",
"3te2",
"4fc4",
"6vqq",
"6vqr",
"7e26",
"7e27",
"7mxy",
"9g49",
"9g4d",
"9i3k"
] | 22 | [
"PUB00058398",
"PUB00098482"
] | [
"22407320",
"23090993"
] | [
"Identification and characterization of a bacterial hydrosulphide ion channel.",
"Structural and functional characterization of the nitrite channel NirC from Salmonella typhimurium."
] | [
2012,
2012
] | 2 | [] | [
"IPR023999"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
703,
15993,
2365,
7,
143
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
4,
1,
1
] | 3 | true | Family | Formate/nitrite transporter | Formate/nitrite transporter | For/NO2_transpt | 2 |
IPR000293 | 293 | Channel forming colicin, C-terminal cytotoxic | Channel_colicin_C | Domain | 842 | false | false | Colicins are plasmid-encoded polypeptide toxins produced by and active against Escherichia coli and closely related bacteria. Colicins are released into the environment to reduce competition from other bacterial strains. Colicins bind to outer membrane receptors, using them to translocate to the cytoplasm or cytoplasmi... | [
"GO:0140911",
"GO:0031640",
"GO:0050829",
"GO:0016020"
] | [
"pore-forming activity",
"killing of cells of another organism",
"defense response to Gram-negative bacterium",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS",
"PROSITE"
] | [
"PF01024",
"PR00280",
"PS00276"
] | [
"Colicin",
"CHANLCOLICIN",
"CHANNEL_COLICIN"
] | [
639,
607,
685
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00249"
] | [
"PROSITEDOC:PDOC00249"
] | 1 | [
"1a87",
"1cii",
"1col",
"1rh1",
"2i88",
"3few",
"6thk",
"8iom",
"9k2h"
] | 9 | [
"PUB00030669",
"PUB00034705"
] | [
"14731273",
"15519318"
] | [
"Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution.",
"On the role of lipid in colicin pore formation."
] | [
2004,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Halorarum salinum"
] | [
764,
2,
75,
1
] | 4 | [] | [] | 0 | true | Domain | Channel forming colicin, C-terminal cytotoxic | Channel forming colicin, C-terminal cytotoxic | Channel_colicin_C | 6 |
IPR000294 | 294 | Gamma-carboxyglutamic acid-rich (GLA) domain | GLA_domain | Domain | 14,067 | false | false | The GLA (gamma-carboxyglutamic acid-rich) domain contains glutamate residues that have been post-translationally modified by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla) [ , , ]. All glutamic acid (Glu) residues present in the GLA domain are potential carboxylation sites; in coagulation protei... | [
"GO:0005509",
"GO:0005576"
] | [
"calcium ion binding",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00594",
"PR00001",
"PS00011",
"PS50998",
"SM00069"
] | [
"Gla",
"GLABLOOD",
"GLA_1",
"GLA_2",
"GLA"
] | [
12009,
11618,
10840,
13994,
13584
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00011",
"R-BTA-114608",
"R-BTA-140834",
"R-BTA-140837",
"R-BTA-140875",
"R-BTA-159740",
"R-BTA-159763",
"R-BTA-159782",
"R-BTA-202733",
"R-CFA-140875",
"R-CFA-159740",
"R-CFA-159763",
"R-CFA-159782",
"R-CFA-202733",
"R-CFA-381426",
"R-CFA-8957275",
"R-DRE-159763",
"R-DRE-15978... | [
"PROSITEDOC:PDOC00011",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-140834",
"REACTOME:R-BTA-140837",
"REACTOME:R-BTA-140875",
"REACTOME:R-BTA-159740",
"REACTOME:R-BTA-159763",
"REACTOME:R-BTA-159782",
"REACTOME:R-BTA-202733",
"REACTOME:R-CFA-140875",
"REACTOME:R-CFA-159740",
"REACTOME:R-CFA-1597... | 82 | [
"1cfh",
"1cfi",
"1dan",
"1ezq",
"1f0r",
"1f0s",
"1fak",
"1iod",
"1j34",
"1j35",
"1ksn",
"1lpg",
"1lpk",
"1lpz",
"1lqd",
"1lqv",
"1mgx",
"1nfu",
"1nfw",
"1nfx",
"1nfy",
"1nl0",
"1nl1",
"1nl2",
"1o5d",
"1p0s",
"1pfx",
"1q3m",
"1q8h",
"1vzm",
"1w0y",
"1w2k"... | 140 | [
"PUB00004648",
"PUB00015411",
"PUB00015412",
"PUB00044565",
"PUB00044566",
"PUB00044567",
"PUB00044568",
"PUB00044569",
"PUB00044570",
"PUB00044571",
"PUB00044572",
"PUB00044573",
"PUB00044574",
"PUB00044575",
"PUB00044576"
] | [
"3317405",
"7713897",
"8663165",
"18374189",
"11818531",
"18374194",
"18373251",
"17723139",
"18642129",
"18680528",
"16156662",
"16460467",
"2403355",
"18369157",
"9163328"
] | [
"Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase.",
"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.",
"Identification of the phospholipid binding si... | [
1987,
1995,
1996,
2008,
2002,
2008,
2008,
2007,
2008,
2008,
2005,
2006,
1990,
2008,
1997
] | 15 | [] | [
"IPR058704"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
6,
14061
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
27,
67,
48,
59
] | 4 | true | Domain | Gamma-carboxyglutamic acid-rich (GLA) domain | Gamma-carboxyglutamic acid-rich (GLA) domain | GLA_domain | 9 |
IPR000296 | 296 | Cation-dependent mannose-6-phosphate receptor | Man-6-P_rcpt_cation_dep | Family | 1,215 | false | false | The cation dependent mannose-6-phosphate (man-6-P) receptor is one of two transmembrane proteins involved in the transport of lysosomal enzymes from the Golgi complex and the cell surface to lysosomes [ ]. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to man-6-P receptors in the Golgi apparatus a... | [
"GO:0019904",
"GO:0006622",
"GO:0005768",
"GO:0005794"
] | [
"protein domain specific binding",
"protein targeting to lysosome",
"endosome",
"Golgi apparatus"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00715"
] | [
"MAN6PRECEPTR"
] | [
1215
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-432720",
"R-BTA-6811440",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-9840310",
"R-HSA-432720",
"R-HSA-6811440",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9840310",
"R-MMU-432720",
"R-MMU-6811440",
"R-MMU-8856825",
"R-MMU-8856828",
"R-MMU-9840310",
"R-RNO-432720",
"R-RNO-6811440",... | [
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-6811440",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9840310",
"REACTOME:R-HSA-432720",
"REACTOME:R-HSA-6811440",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-9840310",
"REACTOME:R-MMU-432720",
"REACTOME:R... | 20 | [
"1c39",
"1keo",
"1m6p",
"2rl7",
"2rl8",
"2rl9",
"2rlb",
"3cy4",
"3k41",
"3k42",
"3k43"
] | 11 | [
"PUB00000813",
"PUB00002497",
"PUB00002714",
"PUB00010648"
] | [
"2954652",
"2544594",
"1376319",
"12612639"
] | [
"46 kd mannose 6-phosphate receptor: cloning, expression, and homology to the 215 kd mannose 6-phosphate receptor.",
"The cation-dependent mannose 6-phosphate receptor. Structural requirements for mannose 6-phosphate binding and oligomerization.",
"Gene and pseudogene of the mouse cation-dependent mannose 6-pho... | [
1987,
1989,
1992,
2003
] | 4 | [
"IPR028927"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
1215
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
12,
3,
4
] | 4 | true | Family | Cation-dependent mannose-6-phosphate receptor | Cation-dependent mannose-6-phosphate receptor | Man-6-P_rcpt_cation_dep | 7 |
IPR000297 | 297 | Peptidyl-prolyl cis-trans isomerase, PpiC-type | PPIase_PpiC | Domain | 65,447 | false | false | Peptidyl-prolyl cis-trans isomerase ( ) (PPIase or rotamase) is an enzyme that accelerates protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [ ]. Most characterised PPiases belong to two families, the cyclophilin-type and the the FKBP-type. A third family has bee... | [
"GO:0003755"
] | [
"peptidyl-prolyl cis-trans isomerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF00639",
"PF13145",
"PS50198"
] | [
"Rotamase",
"Rotamase_2",
"PPIC_PPIASE_2"
] | [
35124,
13474,
60271
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.2.1.8",
"PDOC00840",
"R-BTA-5668599",
"R-BTA-6804756",
"R-BTA-6811555",
"R-BTA-936440",
"R-DME-6804756",
"R-DME-6811555",
"R-HSA-1169408",
"R-HSA-5668599",
"R-HSA-6804756",
"R-HSA-6811555",
"R-HSA-936440",
"R-HSA-9760173",
"R-MMU-5668599",
"R-MMU-6804756",
"R-MMU-6811555",
"R-MM... | [
"EC:5.2.1.8",
"PROSITEDOC:PDOC00840",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6804756",
"REACTOME:R-BTA-6811555",
"REACTOME:R-BTA-936440",
"REACTOME:R-DME-6804756",
"REACTOME:R-DME-6811555",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-5668599",
"REACTOME:R-HSA-6804756",
"REACTOME:R-HSA-6811555... | 22 | [
"1eq3",
"1f8a",
"1fjd",
"1j6y",
"1jns",
"1jnt",
"1m5y",
"1nmv",
"1nmw",
"1pin",
"1yw5",
"1zcn",
"1zk6",
"2f21",
"2itk",
"2jzv",
"2kgj",
"2lj4",
"2m08",
"2m1i",
"2n87",
"2pv1",
"2pv2",
"2pv3",
"2q5a",
"2rqs",
"2ruc",
"2rud",
"2ruq",
"2rur",
"2xp3",
"2xp4"... | 181 | [
"PUB00000320",
"PUB00001678",
"PUB00097266"
] | [
"2186809",
"7925971",
"19866485"
] | [
"The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.",
"Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin.",
"The prolyl isomera... | [
1990,
1994,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
121,
54548,
9691,
2,
1085
] | 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,
2,
3,
4,
3,
6,
4,
2,
12,
8,
1,
1,
12
] | 13 | true | Domain | Peptidyl-prolyl cis-trans isomerase, PpiC-type | Peptidyl-prolyl cis-trans isomerase, PpiC-type | PPIase_PpiC | 1 |
IPR000298 | 298 | Cytochrome c oxidase subunit III-like | Cyt_c_oxidase-like_su3 | Domain | 72,986 | false | false | This entry represents a structural domain found in cytochrome c and ubiquinol oxidase subunit III. The overall structure of these enzymes is similar [ ]. Cytochrome c oxidase ( ) is the terminal enzyme of the respiratory chain of mitochondria and many aerobic bacteria. It catalyses the transfer of electrons from reduce... | [
"GO:0004129",
"GO:0016020"
] | [
"cytochrome-c oxidase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF00510",
"PS50253"
] | [
"COX3",
"COX3"
] | [
71371,
72355
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"7.1.1.9",
"PWY-3781",
"PWY-4521",
"PWY-6692",
"PWY-7279",
"PWY-7429",
"PWY-8271",
"PDOC50253",
"R-CEL-5419276",
"R-DME-5419276",
"R-DME-5628897",
"R-DME-611105",
"R-DME-9707564",
"R-DME-9864848",
"R-DRE-5628897",
"R-DRE-611105",
"R-DRE-9707564",
"R-GGA-5419276",
"R-GGA-5628897",... | [
"EC:7.1.1.9",
"METACYC:PWY-3781",
"METACYC:PWY-4521",
"METACYC:PWY-6692",
"METACYC:PWY-7279",
"METACYC:PWY-7429",
"METACYC:PWY-8271",
"PROSITEDOC:PDOC50253",
"REACTOME:R-CEL-5419276",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-5628897",
"REACTOME:R-DME-611105",
"REACTOME:R-DME-9707564",
"RE... | 40 | [
"1fft",
"1m56",
"1m57",
"1occ",
"1oco",
"1ocr",
"1ocz",
"1qle",
"1v54",
"1v55",
"2dyr",
"2dys",
"2eij",
"2eik",
"2eil",
"2eim",
"2ein",
"2occ",
"2y69",
"2ybb",
"2yev",
"2zxw",
"3abk",
"3abl",
"3abm",
"3ag1",
"3ag2",
"3ag3",
"3ag4",
"3asn",
"3aso",
"3wg7"... | 182 | [
"PUB00002253",
"PUB00006599",
"PUB00006600",
"PUB00006601",
"PUB00006602",
"PUB00028500",
"PUB00033207"
] | [
"8083153",
"10563795",
"8383670",
"1316894",
"2162835",
"11017202",
"16598262"
] | [
"The superfamily of heme-copper respiratory oxidases.",
"Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping--a discussion.",
"Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cyt... | [
1994,
1999,
1993,
1992,
1990,
2000,
2006
] | 7 | [] | [
"IPR033945",
"IPR033946"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
701,
31776,
39858,
651
] | 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,
4,
1,
14,
1,
746,
9,
1,
2,
6,
1,
1,
6
] | 13 | true | Domain | Cytochrome c oxidase subunit III-like | Cytochrome c oxidase subunit III-like | Cyt_c_oxidase-like_su3 | 4 |
IPR000299 | 299 | FERM domain | FERM_domain | Domain | 99,935 | false | false | The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane [ ]. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma memb... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS50057"
] | [
"FERM_3"
] | [
99935
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00566",
"R-BTA-373752",
"R-BTA-6794361",
"R-CEL-182971",
"R-CEL-2029482",
"R-CEL-2453902",
"R-CEL-354192",
"R-CEL-354194",
"R-CEL-375165",
"R-CEL-3928662",
"R-CEL-418885",
"R-CEL-4420097",
"R-CEL-5663213",
"R-CEL-5673001",
"R-CEL-5675221",
"R-CEL-8874081",
"R-CEL-9009391",
"R-... | [
"PROSITEDOC:PDOC00566",
"REACTOME:R-BTA-373752",
"REACTOME:R-BTA-6794361",
"REACTOME:R-CEL-182971",
"REACTOME:R-CEL-2029482",
"REACTOME:R-CEL-2453902",
"REACTOME:R-CEL-354192",
"REACTOME:R-CEL-354194",
"REACTOME:R-CEL-375165",
"REACTOME:R-CEL-3928662",
"REACTOME:R-CEL-418885",
"REACTOME:R-CEL-... | 335 | [
"1e5w",
"1ef1",
"1gc6",
"1gc7",
"1gg3",
"1h4r",
"1isn",
"1j19",
"1mix",
"1miz",
"1mk7",
"1mk9",
"1ni2",
"1sgh",
"1y19",
"2aeh",
"2al6",
"2d10",
"2d11",
"2d2q",
"2ems",
"2emt",
"2g35",
"2h7d",
"2h7e",
"2he7",
"2hrj",
"2i1j",
"2i1k",
"2j0j",
"2j0k",
"2j0m"... | 198 | [
"PUB00005484",
"PUB00013213",
"PUB00017978"
] | [
"9757824",
"10847681",
"10970839"
] | [
"The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.",
"Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.",
"Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domai... | [
1998,
2000,
2000
] | 3 | [] | [
"IPR057096"
] | 0 | 1 | 0 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
149,
2,
99770,
2,
12
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
6,
57,
570,
69,
305,
227,
1,
253,
42
] | 9 | true | Domain | FERM domain | FERM domain | FERM_domain | 4 |
IPR000300 | 300 | Inositol polyphosphate-related phosphatase | IPPc | Domain | 43,272 | false | false | This domain is found in diverse proteins homologous to inositol monophosphatase [ ]. These proteins are Mg 2+ -dependent/Li + -sensitive phosphatases that catalyse a variety of reactions. | [
"GO:0016791",
"GO:0046856"
] | [
"phosphatase activity",
"phosphatidylinositol dephosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF22669",
"SM00128"
] | [
"Exo_endo_phos2",
"IPPc"
] | [
43079,
39283
] | 2 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTO... | [
"3.1.3",
"3.1.3.36",
"PWY-6368",
"R-CEL-1660499",
"R-CEL-1855183",
"R-CEL-1855204",
"R-CEL-8856828",
"R-CFA-1660499",
"R-CFA-1855204",
"R-CFA-912526",
"R-DRE-1660499",
"R-DRE-1855204",
"R-HSA-1660499",
"R-HSA-1660514",
"R-HSA-1855183",
"R-HSA-1855204",
"R-HSA-202424",
"R-HSA-210990... | [
"EC:3.1.3",
"EC:3.1.3.36",
"METACYC:PWY-6368",
"REACTOME:R-CEL-1660499",
"REACTOME:R-CEL-1855183",
"REACTOME:R-CEL-1855204",
"REACTOME:R-CEL-8856828",
"REACTOME:R-CFA-1660499",
"REACTOME:R-CFA-1855204",
"REACTOME:R-CFA-912526",
"REACTOME:R-DRE-1660499",
"REACTOME:R-DRE-1855204",
"REACTOME:R-... | 57 | [
"1i9y",
"1i9z",
"1ntf",
"1si6",
"1y21",
"1yjh",
"2imq",
"2xsw",
"3mtc",
"3n9v",
"3nr8",
"4a9c",
"4cml",
"4cmn",
"4l1y",
"4l1z",
"4l20",
"4l21",
"5a7i",
"5a7j",
"5okm",
"5okn",
"5oko",
"5okp",
"5rw2",
"5rw3",
"5rw4",
"5rw5",
"5rw6",
"5rw7",
"5rw8",
"5rw9"... | 127 | [
"PUB00001628",
"PUB00004077",
"PUB00004207",
"PUB00023636",
"PUB00024185",
"PUB00024257"
] | [
"1660408",
"2395459",
"7885481",
"9351835",
"10667800",
"1518054"
] | [
"Diverse proteins homologous to inositol monophosphatase.",
"Atomic structure of the actin:DNase I complex.",
"Structure and function of the multifunctional DNA-repair enzyme exonuclease III.",
"The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribo... | [
1991,
1990,
1995,
1997,
2000,
1992
] | 6 | [
"IPR005135"
] | [
"IPR037793"
] | 1 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
723,
42526,
15,
8
] | 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... | [
84,
8,
93,
14,
42,
41,
6,
77,
65,
4,
3,
196
] | 12 | true | Domain | Inositol polyphosphate-related phosphatase | Inositol polyphosphate-related phosphatase | IPPc | 4 |
IPR000301 | 301 | Tetraspanin, animals | Tetraspanin_animals | Family | 33,353 | false | false | Tetraspanins are a distinct family of cell surface proteins, containing four conserved transmembrane domains: a small outer loop (EC1), a larger outer loop (EC2), a small inner loop (IL) and short cytoplasmic tails. They contain characteristic structural features, including 4-6 conserved extracellular cysteine residues... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PIRSF"
] | [
"PIRSF002419"
] | [
"Tetraspanin"
] | [
33353
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00371",
"R-BTA-114608",
"R-BTA-1300645",
"R-BTA-198933",
"R-BTA-6798695",
"R-BTA-977606",
"R-CEL-6798695",
"R-DME-6798695",
"R-DRE-6798695",
"R-HSA-114608",
"R-HSA-1300645",
"R-HSA-198933",
"R-HSA-2022090",
"R-HSA-202733",
"R-HSA-416993",
"R-HSA-446107",
"R-HSA-5336415",
"R-HS... | [
"PROSITEDOC:PDOC00371",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1300645",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DME-6798695",
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1300645",
"REACTOME:R-HS... | 34 | [
"5tcx",
"6k4j",
"7jic",
"8jj5"
] | 4 | [
"PUB00010633"
] | [
"12575999"
] | [
"Functional domains in tetraspanin proteins."
] | [
2003
] | 1 | [
"IPR018499"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
33353
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
102,
33,
82,
70,
91
] | 6 | true | Family | Tetraspanin, animals | Tetraspanin, animals | Tetraspanin_animals | 4 |
IPR000304 | 304 | Pyrroline-5-carboxylate reductase-like | Pyrroline-COOH_reductase | Family | 37,529 | false | false | Pyrroline-5-carboxylate reductase (P5CR) ( ) [ , ] is the enzyme that catalyses the terminal step in the biosynthesis of proline from glutamate, the NAD(P) dependent oxidation of 1-pyrroline-5-carboxylate into proline. This enzyme is also able to convert delta-1-piperideine-6-carboxylate (P6C) into pipecolic acid [ ]; ... | [
"GO:0004735",
"GO:0055129"
] | [
"pyrroline-5-carboxylate reductase activity",
"L-proline biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_01925",
"PIRSF000193",
"TIGR00112"
] | [
"P5C_reductase",
"Pyrrol-5-carb_rd",
"proC"
] | [
35839,
35271,
32059
] | 3 | [
"EC",
"GP",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.2",
"GenProp0111",
"PWY-3341",
"PWY-8187",
"PDOC00451",
"R-BTA-8964539",
"R-CEL-8964539",
"R-DDI-8964539",
"R-DRE-8964539",
"R-HSA-8964539",
"R-MMU-8964539",
"R-RNO-8964539",
"R-SCE-8964539",
"R-SPO-8964539"
] | [
"EC:1.5.1.2",
"GP:GenProp0111",
"METACYC:PWY-3341",
"METACYC:PWY-8187",
"PROSITEDOC:PDOC00451",
"REACTOME:R-BTA-8964539",
"REACTOME:R-CEL-8964539",
"REACTOME:R-DDI-8964539",
"REACTOME:R-DRE-8964539",
"REACTOME:R-HSA-8964539",
"REACTOME:R-MMU-8964539",
"REACTOME:R-RNO-8964539",
"REACTOME:R-SC... | 14 | [
"1yqg",
"2ag8",
"2ahr",
"2amf",
"2ger",
"2gr9",
"2gra",
"2izz",
"2rcy",
"3gt0",
"3tri",
"5bse",
"5bsf",
"5bsg",
"5bsh",
"5uat",
"5uau",
"5uav",
"5uaw",
"5uax",
"6lhm",
"6xoz",
"6xp0",
"6xp1",
"6xp2",
"6xp3",
"8dkg",
"8tcu",
"8tcv",
"8tcw",
"8tcx",
"8tcy"... | 51 | [
"PUB00001785",
"PUB00003735",
"PUB00081473",
"PUB00081474",
"PUB00094509",
"PUB00153734",
"PUB00153735"
] | [
"2107123",
"2199815",
"24431009",
"25058475",
"29373009",
"29686660",
"37746209"
] | [
"Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa with their counterparts in Escherichia coli.",
"A soybean gene encoding delta 1-pyrroline-5-carboxylate reductase was isolated by functional complementation in Escherichia coli and is found to be osmoregulated.",
"Human pyrroline-5-carbo... | [
1990,
1990,
2014,
2014,
2018,
2018,
2022
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
477,
28275,
8274,
3,
500
] | 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,
2,
9,
6,
1,
15,
7,
1,
5,
12,
1,
1,
6
] | 13 | true | Family | Pyrroline-5-carboxylate reductase-like | Pyrroline-5-carboxylate reductase-like | Pyrroline-COOH_reductase | 7 |
IPR000305 | 305 | GIY-YIG endonuclease | GIY-YIG_endonuc | Domain | 78,163 | false | false | Nucleases of the GIY-YIG family are involved in many cellular processes, including DNA repair and recombination, transfer of mobile genetic elements, and restriction of incoming foreign DNA. The GIY-YIG superfamily groups together nucleases characterised by the presence of a domain of typically ~100 amino acids, with t... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01541",
"PS50164",
"SM00465"
] | [
"GIY-YIG",
"GIY_YIG",
"GIYc"
] | [
68148,
75054,
48420
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50164",
"R-BTA-5693568",
"R-BTA-6783310",
"R-HSA-5693568",
"R-HSA-6783310",
"R-MMU-5693568",
"R-MMU-6783310",
"R-RNO-5693568",
"R-RNO-6783310"
] | [
"PROSITEDOC:PDOC50164",
"REACTOME:R-BTA-5693568",
"REACTOME:R-BTA-6783310",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-6783310",
"REACTOME:R-MMU-5693568",
"REACTOME:R-MMU-6783310",
"REACTOME:R-RNO-5693568",
"REACTOME:R-RNO-6783310"
] | 9 | [
"1ln0",
"1mk0",
"1ycz",
"1yd0",
"1yd1",
"1yd2",
"1yd3",
"1yd4",
"1yd5",
"1yd6",
"1ywl",
"1zg2",
"2wsh",
"4xlg",
"4xm5",
"6seh",
"6sei",
"7cq2",
"7cq3",
"7cq4",
"7wme"
] | 21 | [
"PUB00017038",
"PUB00019614",
"PUB00032630",
"PUB00044989",
"PUB00063738"
] | [
"12379841",
"10219084",
"15692561",
"16646971",
"19361436"
] | [
"Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI.",
"Configuration of the catalytic GIY-YIG domain of intron endonuclease I-TevI: coincidence of computational and molecular findings.",
"Structural insights into the first incision reaction during nucleotide excision r... | [
2002,
1999,
2005,
2006,
2009
] | 5 | [] | [
"IPR045566",
"IPR047296"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1242,
63570,
10125,
1598,
1628
] | 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,
2,
2,
3,
3,
8,
3,
3,
8,
9,
1,
1,
22
] | 13 | true | Domain | GIY-YIG endonuclease | GIY-YIG endonuclease | GIY-YIG_endonuc | 6 |
IPR000306 | 306 | FYVE zinc finger | Znf_FYVE | Domain | 80,355 | false | false | Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF01363",
"SM00064"
] | [
"FYVE",
"FYVE"
] | [
79283,
78613
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1511",
"R-BTA-182971",
"R-BTA-432720",
"R-BTA-5689880",
"R-BTA-6807004",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-9013420",
"R-BTA-917729",
"R-BTA-9706019",
"R-CEL-1660499",
"R-CEL-1660516",
"R-CEL-1660517",
"R-CEL-9013149",
"R-CEL-9035034",
"R-DME-182971",
"R-DME-432720",
... | [
"GP:GenProp1511",
"REACTOME:R-BTA-182971",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-6807004",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-9013420",
"REACTOME:R-BTA-917729",
"REACTOME:R-BTA-9706019",
"REACTOME:R-CEL-1660499",
"REACTOME:R-CEL-166... | 91 | [
"1dvp",
"1hyi",
"1hyj",
"1joc",
"1vfy",
"1wfk",
"1x4u",
"1z2q",
"2yqm",
"2yw8",
"3mpx",
"3t7l",
"3zyq",
"4avx",
"6w9n",
"8yad",
"9f43",
"9f45"
] | 18 | [
"PUB00002972",
"PUB00014077",
"PUB00018297",
"PUB00032559",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812",
"PUB00042930",
"PUB00042931"
] | [
"8798641",
"12665246",
"11509568",
"15576038",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890",
"11456498",
"11739631"
] | [
"Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger.",
"Zinc fingers--folds for many occasions.",
"Role of the FYVE finger and the RUN domain for the subcellular localization of Rabip4.",
"Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP... | [
1996,
2002,
2001,
2004,
2007,
2005,
2005,
1999,
2001,
2001,
2001
] | 11 | [] | [
"IPR042733",
"IPR042762",
"IPR043269",
"IPR046978",
"IPR047331",
"IPR047333",
"IPR047337",
"IPR047966",
"IPR049764"
] | 0 | 9 | 0 | [
"Eukaryota",
"Pseudomonadati",
"Viruses",
"unclassified sequences"
] | [
80270,
26,
45,
14
] | 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... | [
94,
30,
178,
29,
109,
74,
5,
66,
126,
5,
6,
138
] | 12 | true | Domain | FYVE zinc finger | FYVE zinc finger | Znf_FYVE | 8 |
IPR000307 | 307 | Small ribosomal subunit protein bS16 | Ribosomal_bS16 | Family | 41,737 | false | false | Ribosomal protein S16 (also known as bS16) is one of the proteins from the small ribosomal subunit. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities, groups: Eubacterial S16. Algal and plant chloroplast S16. Cyanelle S16. Neurospora crassa mitochondrial S24 (cyt-21). S16 protein... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00385",
"PF00886",
"PTHR12919",
"TIGR00002"
] | [
"Ribosomal_bS16",
"Ribosomal_S16",
"",
"S16"
] | [
38449,
41111,
41405,
40526
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00600",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-9937383",
"R-DME-5389840",
"R-DME-5419276",
"R-DME-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
... | [
"PROSITEDOC:PDOC00600",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-5389840",
"REACTOME:R-CEL-5419276",
"REACTOME:R-CEL-9937383",
"REACTOME:R-DME-5389840",
"REACTOME:R-DME-5419276",
"REACTOME:R-DME-9937383",
"REACTOME:R-HSA-5368286",
"REACTOME:... | 17 | [
"1emw",
"1fjg",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1xmo",
"1xmq",
"1xnq",
"1xnr",
"2e5l"... | 1,274 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00082325"
] | [
"11297922",
"11290319",
"11114498",
"18453549"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Substitution of the gene for chloroplast RPS16 was assisted by generation of a dual targeting signal."
] | [
2001,
2001,
2000,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Escherichia phage vB_EcoM-613R3",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382M17",
"unclassified sequences"
] | [
23544,
1,
17700,
1,
491
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
1,
1,
1,
1,
2,
1,
1,
6,
2,
1,
1,
4
] | 13 | true | Family | Small ribosomal subunit protein bS16 | Small ribosomal subunit protein bS16 | Ribosomal_bS16 | 3 |
IPR000308 | 308 | 14-3-3 protein | 14-3-3 | Family | 24,302 | false | false | The 14-3-3 proteins are a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells [ , ]. These are structurally similar phospho-binding proteins that regulate multiple signaling pathways [ ]. There is a high degree of sequence identity and conserva... | [] | [] | [] | 0 | [
"PIRSF",
"PRINTS",
"PANTHER"
] | [
"PIRSF000868",
"PR00305",
"PTHR18860"
] | [
"14-3-3",
"1433ZETA",
""
] | [
18442,
23081,
24075
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00633",
"R-BTA-111447",
"R-BTA-2028269",
"R-BTA-205025",
"R-BTA-2565942",
"R-BTA-3371453",
"R-BTA-3371511",
"R-BTA-3769402",
"R-BTA-380259",
"R-BTA-380270",
"R-BTA-380284",
"R-BTA-380320",
"R-BTA-392517",
"R-BTA-430116",
"R-BTA-450604",
"R-BTA-512988",
"R-BTA-5620912",
"R-BTA-... | [
"PROSITEDOC:PDOC00633",
"REACTOME:R-BTA-111447",
"REACTOME:R-BTA-2028269",
"REACTOME:R-BTA-205025",
"REACTOME:R-BTA-2565942",
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-3371511",
"REACTOME:R-BTA-3769402",
"REACTOME:R-BTA-380259",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380284",
"REACTOME:R-BTA... | 243 | [
"1a37",
"1a38",
"1a4o",
"1ib1",
"1o9c",
"1o9d",
"1o9e",
"1o9f",
"1qja",
"1qjb",
"1ywt",
"1yz5",
"2b05",
"2bq0",
"2br9",
"2btp",
"2c1j",
"2c1n",
"2c23",
"2c63",
"2c74",
"2npm",
"2o02",
"2o98",
"2v7d",
"2wh0",
"3axy",
"3cu8",
"3e6y",
"3efz",
"3iqj",
"3iqu"... | 699 | [
"PUB00003264",
"PUB00007085",
"PUB00097184"
] | [
"1671102",
"11911880",
"29915393"
] | [
"Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases.",
"How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis.",
"The dynamic and stress-adaptive signaling hub of 14-3-3: emerging mechanisms of regulation and context-dependent ... | [
1991,
2002,
2018
] | 3 | [] | [
"IPR037435",
"IPR042584"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota"
] | [
5,
24297
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
69,
6,
16,
7,
48,
23,
3,
19,
33,
2,
2,
122
] | 12 | true | Family | 14-3-3 protein | 14-3-3 protein | 14-3-3 | 9 |
IPR000310 | 310 | Orn/Lys/Arg decarboxylase, major domain | Orn/Lys/Arg_deCO2ase_major_dom | Domain | 21,747 | false | false | Pyridoxal-dependent decarboxylases are bacterial proteins acting on ornithine, lysine, arginine and related substrates [ ]. One of the regions of sequence similarity contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group. Ornithine decarboxylase is a dodecamer composed of ... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"CDD"
] | [
"PF01276",
"PS00703",
"cd00615"
] | [
"OKR_DC_1",
"OKR_DC_1",
"Orn_deC_like"
] | [
21744,
13422,
12509
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"PROSITEDOC"
] | [
"4.1.1",
"GenProp1279",
"GenProp1433",
"GenProp1596",
"PDOC00585"
] | [
"EC:4.1.1",
"GP:GenProp1279",
"GP:GenProp1433",
"GP:GenProp1596",
"PROSITEDOC:PDOC00585"
] | 5 | [
"1c4k",
"1ord",
"2vyc",
"2x3l",
"3n75",
"3q16",
"4upb",
"4upf",
"5fkx",
"5fkz",
"5fl2",
"5xx1",
"6q6i",
"6q7l",
"6q7m",
"6y3x",
"6yn5",
"6yn6",
"7p9b",
"7pk6",
"9e0m",
"9e0o",
"9e0q"
] | 23 | [
"PUB00001452",
"PUB00006301",
"PUB00006322",
"PUB00006531",
"PUB00014378",
"PUB00014382",
"PUB00014393",
"PUB00016775",
"PUB00016898",
"PUB00035507",
"PUB00070977",
"PUB00079513",
"PUB00079514",
"PUB00079515"
] | [
"8181483",
"8112347",
"7748903",
"10800595",
"7663340",
"9405048",
"9063963",
"10223296",
"9914259",
"17109392",
"10673430",
"10586514",
"17504214",
"11933250"
] | [
"Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases.",
"Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families.",
"Pyridoxal phosphate-dependent enzymes.",
"The molecular evolution of pyridoxal-5'-phospha... | [
1994,
1994,
1995,
2000,
1995,
1997,
1996,
1999,
1998,
2006,
2000,
1999,
2007,
2001
] | 14 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
45,
20461,
1048,
193
] | 4 | [
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
5,
8
] | 3 | true | Domain | Orn/Lys/Arg decarboxylase, major domain | Orn/Lys/Arg decarboxylase, major domain | Orn/Lys/Arg_deCO2ase_major_dom | 9 |
IPR000312 | 312 | Glycosyl transferase, family 3 | Glycosyl_Trfase_fam3 | Domain | 46,347 | false | false | The glycosyl transferase family includes anthranilate phosphoribosyltransferase (TrpD, ) and thymidine phosphorylase ( ). All these proteins can transfer a phosphorylated ribose substrate. Thymidine phosphorylase ( ) catalyses the reversible phosphorolysis of thymidine, deoxyuridine and their analogues to their respect... | [
"GO:0016757"
] | [
"glycosyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00591"
] | [
"Glycos_transf_3"
] | [
46347
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.4.2",
"2.4.2.18",
"R-HSA-73614",
"R-HSA-73621",
"R-MMU-73614",
"R-MMU-73621",
"R-RNO-73614",
"R-RNO-73621"
] | [
"EC:2.4.2",
"EC:2.4.2.18",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-73621",
"REACTOME:R-MMU-73614",
"REACTOME:R-MMU-73621",
"REACTOME:R-RNO-73614",
"REACTOME:R-RNO-73621"
] | 8 | [
"1azy",
"1brw",
"1gxb",
"1kgz",
"1khd",
"1o17",
"1otp",
"1tpt",
"1uou",
"1v8g",
"1vqu",
"1zvw",
"1zxy",
"1zyk",
"2bpq",
"2dsj",
"2elc",
"2gvq",
"2j0f",
"2tpt",
"2wk5",
"2wk6",
"3gbr",
"3h5q",
"3qqs",
"3qr9",
"3qs8",
"3qsa",
"3r6c",
"3r88",
"3twp",
"3uu1"... | 88 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1578,
39768,
4102,
899
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)... | [
4,
2,
2,
9,
1,
1,
5,
2,
1,
1,
7
] | 11 | true | Domain | Glycosyl transferase, family 3 | Glycosyl transferase, family 3 | Glycosyl_Trfase_fam3 | 5 |
IPR000313 | 313 | PWWP domain | PWWP_dom | Domain | 50,319 | false | false | The PWWP domain is an around 70 amino acids domain that was named after its central core 'Pro-Trp-Trp-Pro'. The PWWP domain is found in one or, less frequently, in two copies in nuclear, often DNA-binding proteins that function as transcription factors regulating developmental processes. Due to its position, the compos... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00855",
"PS50812",
"SM00293"
] | [
"PWWP",
"PWWP",
"PWWP"
] | [
48204,
47725,
40620
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50812",
"R-BTA-9772755",
"R-DME-114608",
"R-DME-5689603",
"R-DME-6804758",
"R-HSA-114608",
"R-HSA-162592",
"R-HSA-164843",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-212300",
"R-HSA-3214841",
"R-HSA-3214847",
"R-HSA-3214858",
"R-HSA-381038",
"R-HSA-... | [
"PROSITEDOC:PDOC50812",
"REACTOME:R-BTA-9772755",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-5689603",
"REACTOME:R-DME-6804758",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177539",
"REACTOME:R-HSA-180689",
"REACTOME:R-HSA-1... | 48 | [
"1h3z",
"1khc",
"1n27",
"1ri0",
"2b8a",
"2daq",
"2gfu",
"2l89",
"2m16",
"2m1h",
"2nas",
"2nlu",
"2x35",
"2x4w",
"2x4x",
"2x4y",
"3eae",
"3flg",
"3l42",
"3llr",
"3lyi",
"3mo8",
"3pfs",
"3qby",
"3qj6",
"3qkj",
"3zeh",
"4cos",
"4fu6",
"4ld6",
"4n4g",
"4n4h"... | 196 | [
"PUB00006532",
"PUB00026733",
"PUB00094286"
] | [
"10802047",
"11836534",
"28645917"
] | [
"The PWWP domain: a potential protein-protein interaction domain in nuclear proteins influencing differentiation?",
"The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds.",
"Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest differentiation."... | [
2000,
2002,
2017
] | 3 | [] | [
"IPR035501",
"IPR035503",
"IPR047268",
"IPR047363",
"IPR047423",
"IPR047434",
"IPR047435",
"IPR047451",
"IPR047453",
"IPR049583"
] | 0 | 10 | 0 | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
14,
50303,
2
] | 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... | [
89,
2,
153,
18,
126,
98,
1,
51,
95,
2,
3,
183
] | 12 | true | Domain | PWWP domain | PWWP domain | PWWP_dom | 4 |
IPR000314 | 314 | Gastrin receptor | Gastrin_rcpt | Family | 1,662 | 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:0015054",
"GO:0007186",
"GO:0016020"
] | [
"gastrin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00527"
] | [
"GASTRINR"
] | [
1662
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"77",
"R-CFA-375276",
"R-CFA-416476",
"R-CFA-881907",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-881907",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-881907",
"R-RNO-375276",
"R-RNO-416476",
"R-RNO-881907"
] | [
"IUPHAR:77",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-416476",
"REACTOME:R-CFA-881907",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-881907",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-881907",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476",
"REA... | 13 | [
"7f8v",
"7f8w",
"7xow",
"8ia7"
] | 4 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR009126"
] | [] | 1 | 0 | 1 | [
"Bilateria",
"bird metagenome"
] | [
1661,
1
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
3,
3,
6,
8
] | 5 | true | Family | Gastrin receptor | Gastrin receptor | Gastrin_rcpt | 8 |
IPR000315 | 315 | B-box-type zinc finger | Znf_B-box | Domain | 122,909 | false | false | This entry represents B-box-type zinc finger domains, which are around 40 residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues. Several proteins contain both types 1 and 2 B-boxes, ... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00643",
"PS50119",
"SM00336"
] | [
"zf-B_box",
"ZF_BBOX",
"BBOX"
] | [
99422,
118505,
100188
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50119",
"R-BTA-3134975",
"R-BTA-9755511",
"R-BTA-983168",
"R-CEL-1660514",
"R-CEL-199992",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-6798695",
"R-CEL-6807878",
"R-CEL-6811434",
"R-DDI-193648",
"R-DDI-4641258",
"R-DDI-5658442",
"R-DDI-8951664",
"R-DDI-9013148",
"R-DDI-9013149",
"R... | [
"PROSITEDOC:PDOC50119",
"REACTOME:R-BTA-3134975",
"REACTOME:R-BTA-9755511",
"REACTOME:R-BTA-983168",
"REACTOME:R-CEL-1660514",
"REACTOME:R-CEL-199992",
"REACTOME:R-CEL-432720",
"REACTOME:R-CEL-432722",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-DD... | 79 | [
"1fre",
"2csv",
"2d8u",
"2did",
"2dif",
"2dja",
"2dq5",
"2egm",
"2ffw",
"2jun",
"2mvw",
"2yrg",
"2yvr",
"3ddt",
"3q1d",
"4tn3",
"5eiu",
"5f7t",
"5iea",
"5jpx",
"5k3q",
"5olm",
"5va4",
"5w9a",
"6h3a",
"6imq",
"6o5k",
"6qaj",
"6qu1",
"7vsp",
"7vsq",
"7wsj"... | 46 | [
"PUB00040284",
"PUB00040653",
"PUB00042940"
] | [
"17428496",
"16529770",
"16434393"
] | [
"Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold.",
"Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING.",
"Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubu... | [
2007,
2006,
2006
] | 3 | [] | [
"IPR020457",
"IPR027727",
"IPR033492",
"IPR037372",
"IPR047051",
"IPR047058",
"IPR047059",
"IPR047063",
"IPR047064",
"IPR047065",
"IPR047095",
"IPR049582",
"IPR049808"
] | 0 | 13 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
25,
381,
122481,
3,
19
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
145,
34,
461,
29,
269,
196,
111,
204,
173
] | 9 | true | Domain | B-box-type zinc finger | B-box-type zinc finger | Znf_B-box | 8 |
IPR000316 | 316 | Plant EC metallothionein-like protein, family 15 | Metallthion_15 | Family | 399 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , , , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] a... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02068",
"PR00877",
"PTHR48198"
] | [
"Metallothio_PEC",
"MTPLANTPEC",
""
] | [
398,
302,
381
] | 3 | [] | [] | [] | 0 | [
"2kak",
"2l61",
"2l62",
"2mfp"
] | 4 | [
"PUB00000300",
"PUB00001490",
"PUB00003570",
"PUB00003571",
"PUB00005944"
] | [
"3064814",
"2959513",
"1779825",
"1779826",
"2959504"
] | [
"Biochemistry of metallothionein.",
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein.",
"Definitions and nomenclature of metallothioneins.",
"Nomenclature of metallothionein."
] | [
1988,
1987,
1991,
1991,
1987
] | 5 | [] | [] | 0 | 0 | null | [
"Tracheophyta"
] | [
399
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
8,
1,
2
] | 3 | true | Family | Plant EC metallothionein-like protein, family 15 | Plant EC metallothionein-like protein, family 15 | Metallthion_15 | 9 |
IPR000318 | 318 | Nitrogenase component 1, conserved site | Nase_comp1_CS | Conserved_site | 10,992 | false | false | Nitrogenase ( ) [ ] is the enzyme system responsible for biological nitrogen fixation. Nitrogenase is an oligomeric complex which consists of two components: component 2 is an homodimer of an iron-sulphur protein, while component 1 which contains the active site for the reduction of nitrogen to ammonia exists in three ... | [
"GO:0016163"
] | [
"nitrogenase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00090",
"PS00699"
] | [
"NITROGENASE_1_2",
"NITROGENASE_1_1"
] | [
7995,
10421
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"1.18.6.1",
"PDOC00085"
] | [
"EC:1.18.6.1",
"PROSITEDOC:PDOC00085"
] | 2 | [
"1fp4",
"1g20",
"1g21",
"1h1l",
"1l5h",
"1m1n",
"1m1y",
"1m34",
"1mio",
"1n2c",
"1qgu",
"1qh1",
"1qh8",
"2afh",
"2afi",
"2min",
"3aet",
"3k1a",
"3min",
"3pdi",
"3u7q",
"4nd8",
"4tku",
"4tkv",
"4wes",
"4wn9",
"4wna",
"4wza",
"4wzb",
"4xpi",
"5bvg",
"5bvh"... | 108 | [
"PUB00003737",
"PUB00005343"
] | [
"2266945",
"2672439"
] | [
"The nifEN genes participating in FeMo cofactor biosynthesis and genes encoding dinitrogenase are part of the same operon in Bradyrhizobium species.",
"Nitrogenases without molybdenum."
] | [
1990,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
10260,
75,
522,
135
] | 4 | [] | [] | 0 | true | Conserved_site | Nitrogenase component 1, conserved site | Nitrogenase component 1, conserved site | Nase_comp1_CS | 6 |
IPR000319 | 319 | Aspartate-semialdehyde dehydrogenase, conserved site | Asp-semialdehyde_DH_CS | Conserved_site | 14,739 | false | false | Bacteria, plants and fungi metabolise aspartic acid to produce four amino acids -lysine, threonine, methionine and isoleucine -in a series of reactions known as the aspartate pathway. Additionally, several important metabolic intermediates are produced by these reactions, such as diaminopimelic acid, an essential compo... | [
"GO:0004073",
"GO:0050661",
"GO:0006520"
] | [
"aspartate-semialdehyde dehydrogenase activity",
"NADP binding",
"amino acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS01103"
] | [
"ASD"
] | [
14739
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC"
] | [
"1.2.1.11",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PWY-6160",
"PWY-6559",
"PWY-6562",
"PWY-7153",
"PWY-7977",
"PWY-8088",
"PWY-8179",
"PWY-8296",
"PDOC00847"
] | [
"EC:1.2.1.11",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"METACYC:PWY-6160",
"METACYC:PWY-6559",
"METACYC:PWY-6562",
"METACYC:PWY-7153",
"METACYC:PWY-7977",
"METACYC:PWY-8088",
"METACYC:PWY-8179",
"METACYC:PWY-8296",
"PROSITEDOC:PDOC00847"
] | 13 | [
"1brm",
"1gl3",
"1mb4",
"1mc4",
"1nwc",
"1nwh",
"1nx6",
"1oza",
"1pqp",
"1pr3",
"1pu2",
"1q2x",
"1t4b",
"1t4d",
"1ta4",
"1tb4",
"1ys4",
"2qz9",
"2r00",
"3hsk",
"3pzr",
"3q0e",
"3tz6",
"3uw3",
"3vos",
"4r5m",
"4woj",
"4zhs",
"4zic",
"5bnt",
"5cef",
"6bac"... | 36 | [
"PUB00029242",
"PUB00029661",
"PUB00034672",
"PUB00034673",
"PUB00034674",
"PUB00034675"
] | [
"14559965",
"15272161",
"11352712",
"1673060",
"15388927",
"16225889"
] | [
"Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase.",
"The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.",
"The central enzymes of the aspartate family of amino acid biosynthesis.",
"Chemical and kinetic mechanism... | [
2003,
2004,
2001,
1991,
2004,
2005
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
259,
13018,
1231,
231
] | 4 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1,
1
] | 3 | true | Conserved_site | Aspartate-semialdehyde dehydrogenase, conserved site | Aspartate-semialdehyde dehydrogenase, conserved site | Asp-semialdehyde_DH_CS | 9 |
IPR000320 | 320 | Hedgehog, N-terminal signalling domain | Hedgehog_signalling_dom | Domain | 4,495 | false | false | Hedgehog proteins are a family of secreted signal molecules required for embryonic cell differentiation. They are synthesised as inactive precursors with an N-terminal signalling domain linked to a C-terminal autoprocessing domain. The three-dimensional structure of the autolytic domain of the hedgehog protein of shows... | [
"GO:0007267"
] | [
"cell-cell signaling"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01085"
] | [
"HH_signal"
] | [
4495
] | 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-DME-209338",
"R-DME-209471",
"R-DME-5358346",
"R-DME-5362798",
"R-DME-5632681",
"R-DRE-5358346",
"R-DRE-5362798",
"R-DRE-5632681",
"R-GGA-5358346",
"R-GGA-5362798",
"R-GGA-5632681",
"R-HSA-373080",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5362798",
"R-HSA-5632681",
"R-HSA-5632684"... | [
"REACTOME:R-DME-209338",
"REACTOME:R-DME-209471",
"REACTOME:R-DME-5358346",
"REACTOME:R-DME-5362798",
"REACTOME:R-DME-5632681",
"REACTOME:R-DRE-5358346",
"REACTOME:R-DRE-5362798",
"REACTOME:R-DRE-5632681",
"REACTOME:R-GGA-5358346",
"REACTOME:R-GGA-5362798",
"REACTOME:R-GGA-5632681",
"REACTOME:... | 31 | [
"1vhh",
"2ibg",
"2wfq",
"2wfr",
"2wfx",
"2wg3",
"2wg4",
"3d1m",
"3ho5",
"3k7g",
"3k7h",
"3k7i",
"3k7j",
"3m1n",
"3mxw",
"3n1f",
"3n1g",
"3n1m",
"3n1o",
"3n1p",
"3n1q",
"3n1r",
"4c4m",
"4c4n",
"6dmy",
"6e1h",
"6n7g",
"6n7h",
"6n7k",
"6oev",
"6pjv",
"6rmg"... | 41 | [
"PUB00004222",
"PUB00011705"
] | [
"7477329",
"9489693"
] | [
"A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog.",
"Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution."
] | [
1995,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
12,
4483
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
22,
1,
10,
8,
10
] | 5 | true | Domain | Hedgehog, N-terminal signalling domain | Hedgehog, N-terminal signalling domain | Hedgehog_signalling_dom | 7 |
IPR000321 | 321 | Delta opioid receptor | Delta_opi_rcpt | Family | 585 | 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:0038046",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled enkephalin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00525"
] | [
"DELTAOPIOIDR"
] | [
585
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"317",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-6785807",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594"
] | [
"IUPHAR:317",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6785807",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594"
] | 8 | [
"4n6h",
"4rwa",
"4rwd",
"6pt2",
"6pt3",
"8f7s",
"8y45",
"9cgj",
"9cgk"
] | 9 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR001418"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
585
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
2
] | 3 | true | Family | Delta opioid receptor | Delta opioid receptor | Delta_opi_rcpt | 8 |
IPR000322 | 322 | Glycoside hydrolase family 31, TIM barrel domain | Glyco_hydro_31_TIM | Domain | 55,064 | false | false | This entry corresponds to the second domain of family 31 enzymes and adopts a TIM-barrel fold. 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 h... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01055"
] | [
"Glyco_hydro_31_2nd"
] | [
55064
] | 1 | [
"CAZY",
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"GH31",
"3.2.1",
"GenProp1706",
"PDOC00120",
"R-BTA-6798695",
"R-BTA-70221",
"R-HSA-189085",
"R-HSA-532668",
"R-HSA-5357609",
"R-HSA-5659898",
"R-HSA-6798695",
"R-HSA-70221",
"R-HSA-901042",
"R-HSA-9683686",
"R-HSA-9694548",
"R-HSA-9768727",
"R-MMU-6798695",
"R-MMU-70221",
"R-MMU... | [
"CAZY:GH31",
"EC:3.2.1",
"GP:GenProp1706",
"PROSITEDOC:PDOC00120",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70221",
"REACTOME:R-HSA-189085",
"REACTOME:R-HSA-532668",
"REACTOME:R-HSA-5357609",
"REACTOME:R-HSA-5659898",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70221",
"REACTOME:R-HSA-901042"... | 25 | [
"1we5",
"1xsi",
"1xsj",
"1xsk",
"2f2h",
"2g3m",
"2g3n",
"2qly",
"2qmj",
"2x2h",
"2x2i",
"2x2j",
"2xvg",
"2xvk",
"2xvl",
"3ctt",
"3l4t",
"3l4u",
"3l4v",
"3l4w",
"3l4x",
"3l4y",
"3l4z",
"3lpo",
"3lpp",
"3m46",
"3m6d",
"3mkk",
"3n04",
"3nsx",
"3nuk",
"3pha"... | 171 | [
"PUB00000503",
"PUB00001405",
"PUB00001627",
"PUB00002645",
"PUB00004870",
"PUB00005266"
] | [
"1747104",
"1761061",
"1743281",
"1856189",
"7624375",
"8535779"
] | [
"A classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase.",
"Striking structural and functional simil... | [
1991,
1991,
1991,
1991,
1995,
1995
] | 6 | [] | [
"IPR044112"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctwQg18",
"unclassified sequences"
] | [
230,
23440,
31192,
1,
201
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
28,
6,
32,
13,
2,
25,
19,
6,
23,
40,
1,
4,
74
] | 13 | true | Domain | Glycoside hydrolase family 31, TIM barrel domain | Glycoside hydrolase family 31, TIM barrel domain | Glyco_hydro_31_TIM | 5 |
IPR000323 | 323 | Copper type II, ascorbate-dependent monooxygenase, N-terminal | Cu2_ascorb_mOase_N | Domain | 8,960 | false | false | Copper type II, ascorbate-dependent monooxygenases [ ] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase ( ) and peptidyl-glycine alpha-amidating monooxygenase ( ). There are a few regions of seq... | [
"GO:0004497",
"GO:0005507",
"GO:0016715"
] | [
"monooxygenase activity",
"copper ion binding",
"oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM"
] | [
"PF01082"
] | [
"Cu2_monooxygen"
] | [
8960
] | 1 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.17",
"GenProp1606",
"PDOC00080",
"R-DME-209905",
"R-HSA-209905",
"R-MMU-209905",
"R-RNO-209905"
] | [
"EC:1.14.17",
"GP:GenProp1606",
"PROSITEDOC:PDOC00080",
"REACTOME:R-DME-209905",
"REACTOME:R-HSA-209905",
"REACTOME:R-MMU-209905",
"REACTOME:R-RNO-209905"
] | 7 | [
"1opm",
"1phm",
"1sdw",
"1yi9",
"1yip",
"1yjk",
"1yjl",
"3mib",
"3mic",
"3mid",
"3mie",
"3mif",
"3mig",
"3mih",
"3mlj",
"3mlk",
"3mll",
"3phm",
"4e4z",
"4zel",
"5wja",
"5wkw",
"5wm0",
"6ala",
"6alv",
"6amp",
"6an3",
"6ao6",
"6ay0",
"6nck",
"8dsj",
"8dsl"... | 33 | [
"PUB00001578"
] | [
"2792366"
] | [
"Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain."
] | [
1989
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"freshwater metagenome"
] | [
73,
8885,
2
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
18,
8,
11,
7,
19
] | 6 | true | Domain | Copper type II, ascorbate-dependent monooxygenase, N-terminal | Copper type II, ascorbate-dependent monooxygenase, N-terminal | Cu2_ascorb_mOase_N | 7 |
IPR000324 | 324 | Vitamin D receptor | VitD_rcpt | Family | 1,498 | false | false | null | [
"GO:0003677",
"GO:0004879",
"GO:0006355",
"GO:0005634"
] | [
"DNA binding",
"nuclear receptor activity",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00350"
] | [
"VITAMINDR"
] | [
1498
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-196791",
"R-DRE-4090294",
"R-HSA-196791",
"R-HSA-383280",
"R-HSA-4090294",
"R-MMU-196791",
"R-MMU-383280",
"R-MMU-4090294",
"R-RNO-196791",
"R-RNO-383280",
"R-RNO-4090294",
"R-SSC-196791",
"R-SSC-383280",
"R-SSC-4090294"
] | [
"REACTOME:R-DRE-196791",
"REACTOME:R-DRE-4090294",
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-383280",
"REACTOME:R-HSA-4090294",
"REACTOME:R-MMU-196791",
"REACTOME:R-MMU-383280",
"REACTOME:R-MMU-4090294",
"REACTOME:R-RNO-196791",
"REACTOME:R-RNO-383280",
"REACTOME:R-RNO-4090294",
"REACTOME:R-SSC... | 14 | [
"2hbh",
"2hc4",
"2hcd",
"3dr1",
"3o1d",
"3o1e",
"4fhh",
"4fhi",
"4g1d",
"4g1y",
"4g1z",
"4g20",
"4g21",
"4g2h",
"4ia1",
"4ia2",
"4ia3",
"4ia7",
"4q0a",
"4ruj",
"4ruo",
"4rup",
"5e7v",
"5lga",
"5mx7",
"5nky",
"5nma",
"5nmb",
"5ow7",
"5ow9",
"5owd",
"6fo7"... | 77 | [
"PUB00004464",
"PUB00006168"
] | [
"7899080",
"8165128"
] | [
"Vitamin D receptor contains multiple dimerization interfaces that are functionally different.",
"Human androgen receptor expressed in HeLa cells activates transcription in vitro."
] | [
1995,
1994
] | 2 | [
"IPR001723"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
1498
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
9,
4,
7
] | 4 | true | Family | Vitamin D receptor | Vitamin D receptor | VitD_rcpt | 7 |
IPR000326 | 326 | Phosphatidic acid phosphatase type 2/haloperoxidase | PAP2/HPO | Domain | 119,570 | false | false | This entry represents type 2 phosphatidic acid phosphatase (PAP2; ) enzymes, such as phosphatidylglycerophosphatase B from Escherichia coli. PAP2 enzymes have a core structure consisting of a 5-helical bundle, where the beginning of the third helix binds the cofactor [ ]. PAP2 enzymes catalyse the dephosphorylation of ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF01569",
"SM00014"
] | [
"PAP2",
"acidPPc"
] | [
117155,
102791
] | 2 | [
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp1277",
"GenProp1363",
"GenProp1612",
"R-BTA-191273",
"R-BTA-70263",
"R-BTA-9845614",
"R-CEL-9845614",
"R-DDI-2029485",
"R-DDI-419408",
"R-DDI-446199",
"R-DDI-9845614",
"R-DME-9845614",
"R-DRE-191273",
"R-DRE-70263",
"R-HSA-191273",
"R-HSA-2029485",
"R-HSA-3274531",
"R-HSA-3... | [
"GP:GenProp1277",
"GP:GenProp1363",
"GP:GenProp1612",
"REACTOME:R-BTA-191273",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-9845614",
"REACTOME:R-CEL-9845614",
"REACTOME:R-DDI-2029485",
"REACTOME:R-DDI-419408",
"REACTOME:R-DDI-446199",
"REACTOME:R-DDI-9845614",
"REACTOME:R-DME-9845614",
"REACTOME... | 43 | [
"1d2t",
"1eoi",
"1iw8",
"2a96",
"2akc",
"2ipb",
"4px7",
"5jki",
"5jwy",
"6ebu",
"6fmx",
"7f17",
"7f18",
"8bm3",
"8yc1",
"9htz",
"9ivc",
"9j7u",
"9j7v",
"9jq0",
"9jtl",
"9jtm",
"9jtn",
"9jto"
] | 24 | [
"PUB00010620",
"PUB00024099",
"PUB00036051"
] | [
"12447906",
"10835340",
"17079146"
] | [
"Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.",
"X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.",
"Roles of phosphatidate phosphatase enzymes in lipid metabolism."
] | [
2002,
2000,
2006
] | 3 | [] | [
"IPR033879",
"IPR039667",
"IPR041067"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1511,
72981,
44114,
36,
928
] | 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",... | [
43,
12,
74,
34,
3,
49,
40,
7,
31,
74,
6,
4,
79
] | 13 | true | Domain | Phosphatidic acid phosphatase type 2/haloperoxidase | Phosphatidic acid phosphatase type 2/haloperoxidase | PAP2/HPO | 5 |
IPR000327 | 327 | POU-specific domain | POU_dom | Domain | 17,357 | false | false | This entry represents the POU-specific subunit of the POU domain. The POU domain is a bipartite domain composed of two subunits separated by a non-conserved region of 15-55 aa. The N-terminal subunit is known as the POU-specific (POUs) domain (this entry), while the C-terminal subunit is a homeobox domain ( ). Both sub... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00157",
"PS00035",
"PS00465",
"PS51179",
"SM00352"
] | [
"Pou",
"POU_1",
"POU_2",
"POU_3",
"POU"
] | [
16954,
15497,
15769,
17267,
16807
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00035",
"R-CEL-373752",
"R-CEL-418885",
"R-CEL-418886",
"R-DME-373752",
"R-DME-418885",
"R-DME-418886",
"R-DME-6804759",
"R-DME-6807505",
"R-DME-9018519",
"R-DRE-373752",
"R-DRE-418885",
"R-DRE-418886",
"R-HSA-2892245",
"R-HSA-2892247",
"R-HSA-452723",
"R-HSA-6785807",
"R-HSA-... | [
"PROSITEDOC:PDOC00035",
"REACTOME:R-CEL-373752",
"REACTOME:R-CEL-418885",
"REACTOME:R-CEL-418886",
"REACTOME:R-DME-373752",
"REACTOME:R-DME-418885",
"REACTOME:R-DME-418886",
"REACTOME:R-DME-6804759",
"REACTOME:R-DME-6807505",
"REACTOME:R-DME-9018519",
"REACTOME:R-DRE-373752",
"REACTOME:R-DRE-4... | 42 | [
"1au7",
"1cqt",
"1e3o",
"1gt0",
"1hf0",
"1o4x",
"1oct",
"1pou",
"2xsd",
"3d1n",
"3l1p",
"5wc9",
"6ht5",
"6t90",
"6yov",
"7u0g",
"7u0i",
"7xrc",
"8bx1",
"8bx2",
"8g87",
"8g88",
"8g8b",
"8g8e",
"8g8g",
"8ots",
"8sps",
"8spu",
"9dzm",
"9pfn",
"9pfo",
"9pfp"... | 32 | [
"PUB00000889",
"PUB00000905",
"PUB00001223",
"PUB00004053",
"PUB00004699",
"PUB00007263",
"PUB00007264",
"PUB00007265"
] | [
"8462099",
"8156594",
"1628619",
"1967821",
"1967834",
"11159814",
"11183772",
"9009203"
] | [
"The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain.",
"Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules.",
"Brain 4: a novel mammalian POU domain tran... | [
1993,
1994,
1992,
1990,
1990,
2001,
2000,
1997
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"ecological metagenomes"
] | [
101,
6,
17247,
3
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
116,
28,
127,
49,
65
] | 6 | true | Domain | POU-specific domain | POU-specific domain | POU_dom | 9 |
IPR000329 | 329 | Uteroglobin | Uteroglobin | Family | 275 | false | false | Uteroglobin (blastokinin or Clara cell protein CC10) is a mammalian steroid-inducible secreted protein originally isolated from the uterus of rabbits during early pregnancy [ ]. The mucosal epithelia of several organs that communicate with the external environment express uteroglobin. Its tissue-specific expression is ... | [
"GO:0007165"
] | [
"signal transduction"
] | [
"biological_process"
] | 1 | [
"PRINTS"
] | [
"PR00486"
] | [
"UTEROGLOBIN"
] | [
275
] | 1 | [] | [] | [] | 0 | [
"1ccd",
"1utg",
"1utr",
"2utg",
"7vf3",
"7vg7"
] | 6 | [
"PUB00004962",
"PUB00031900",
"PUB00042584",
"PUB00042585",
"PUB00042586",
"PUB00042590",
"PUB00081689",
"PUB00081692",
"PUB00081693",
"PUB00081696",
"PUB00081698",
"PUB00081699"
] | [
"7770456",
"3656405",
"17916741",
"17928103",
"11193760",
"17163411",
"11193783",
"2378892",
"3319534",
"11193782",
"11193767",
"11193750"
] | [
"Progesterone binding to uteroglobin: two alternative orientations of the ligand.",
"Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution.",
"Uteroglobin: a steroid-inducible immunomodulatory protein that founded the Secretoglobin superfamily.",
"Interaction of antiflammin-1 wit... | [
1995,
1987,
2007,
2007,
2000,
2007,
2000,
1990,
1987,
2000,
2000,
2000
] | 12 | [
"IPR043215"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
275
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
2
] | 3 | true | Family | Uteroglobin | Uteroglobin | Uteroglobin | 6 |
IPR000330 | 330 | SNF2, N-terminal domain | SNF2_N | Domain | 187,873 | false | false | This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54) and chromatin unwinding (e.g., ISWI), as well as several other proteins with limited functional information (e.g... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00176"
] | [
"SNF2-rel_dom"
] | [
187873
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"3.6.4.-",
"PWY-7250",
"R-BTA-1266695",
"R-BTA-141444",
"R-BTA-201722",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-3214858",
"R-BTA-3247509",
"R-BTA-5663220",
"R-BTA-5696395",
"R-BTA-5696400",
"R-BTA-68877",
"R-BTA-8939243",
"R-BTA-9648025",
"R-BTA-9764725",
"R-BTA-9933937",
"R-BTA-9... | [
"EC:3.6.4.-",
"METACYC:PWY-7250",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-3214858",
"REACTOME:R-BTA-3247509",
"REACTOME:R-BTA-5663220",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-5696400",
... | 172 | [
"1z3i",
"1z63",
"1z6a",
"3mwy",
"4s20",
"5gn1",
"5hzr",
"5jxr",
"5jxt",
"5o9g",
"5vvr",
"5x0x",
"5x0y",
"5z3l",
"5z3o",
"5z3u",
"5z3v",
"6bog",
"6eg2",
"6eg3",
"6fhs",
"6fml",
"6ftx",
"6g0l",
"6g7e",
"6gej",
"6gen",
"6hts",
"6igm",
"6iro",
"6iy2",
"6iy3"... | 202 | [
"PUB00014473",
"PUB00014474",
"PUB00095659",
"PUB00096999"
] | [
"7651832",
"14729263",
"21549307",
"16935875"
] | [
"Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions.",
"The SNF2 domain protein family in higher vertebrates displays dynamic expression patterns in Xenopus laevis embryos.",
"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler S... | [
1995,
2004,
2011,
2006
] | 4 | [
"IPR014001"
] | [
"IPR028727",
"IPR031047",
"IPR044753",
"IPR044754",
"IPR044755",
"IPR057342",
"IPR058052"
] | 1 | 7 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
638,
39492,
144820,
1823,
1100
] | 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",... | [
256,
33,
212,
53,
1,
211,
101,
27,
137,
149,
17,
20,
657
] | 13 | true | Domain | SNF2, N-terminal domain | SNF2, N-terminal domain | SNF2_N | 9 |
IPR000331 | 331 | Rap/Ran-GAP domain | Rap/Ran_GAP_dom | Domain | 30,024 | false | false | Structural domains comprising this superfamily share the structure of two shown to be homologous GTPase activating proteins for Rap and Ran. Both are Ras-like guanine-nucleotide-binding proteins (GNBPs) involved in a variety of signal-transduction processes and their activity is regulated by GEFs and GAPs. Rap small G ... | [
"GO:0005096",
"GO:0051056"
] | [
"GTPase activator activity",
"regulation of small GTPase mediated signal transduction"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF02145",
"PS50085"
] | [
"Rap_GAP",
"RAPGAP"
] | [
27189,
29925
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50085",
"R-DDI-392517",
"R-DME-9013407",
"R-HSA-1445148",
"R-HSA-1632852",
"R-HSA-165181",
"R-HSA-198323",
"R-HSA-380972",
"R-HSA-392517",
"R-HSA-5628897",
"R-HSA-5674400",
"R-HSA-6794361",
"R-HSA-8853659",
"R-HSA-8854214",
"R-HSA-9013407",
"R-MMU-1632852",
"R-MMU-165181",
"R-... | [
"PROSITEDOC:PDOC50085",
"REACTOME:R-DDI-392517",
"REACTOME:R-DME-9013407",
"REACTOME:R-HSA-1445148",
"REACTOME:R-HSA-1632852",
"REACTOME:R-HSA-165181",
"REACTOME:R-HSA-198323",
"REACTOME:R-HSA-380972",
"REACTOME:R-HSA-392517",
"REACTOME:R-HSA-5628897",
"REACTOME:R-HSA-5674400",
"REACTOME:R-HSA... | 35 | [
"1srq",
"3brw",
"6ssh",
"7dl2",
"9ce3",
"9qwp"
] | 6 | [
"PUB00007619",
"PUB00018098",
"PUB00018099",
"PUB00018100"
] | [
"9045618",
"11331911",
"9346962",
"10373454"
] | [
"The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis.",
"Rap1 signalling: adhering to new models.",
"Human SPA-1 gene product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2. Segregate e... | [
1997,
2001,
1997,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bird metagenome"
] | [
21,
30002,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
25,
222,
33,
63,
50,
2,
77,
1
] | 8 | true | Domain | Rap/Ran-GAP domain | Rap/Ran-GAP domain | Rap/Ran_GAP_dom | 7 |
IPR000332 | 332 | Beta 2 adrenoceptor | ADRB2_rcpt | Family | 861 | false | false | This entry represents the beta 2 receptor; it mediates relaxation of smooth muscle including vascular beds, bronchus, intestine and uterus [ , ]. Beta 2 adrenoceptors, also mediate glycogenlysis and glucogenesis in the liver [ ], regulate cell metabolism in skeletal muscle [ ] and inhibit the activity of leukocytes and... | [
"GO:0004941",
"GO:0006940",
"GO:0007189",
"GO:0097746",
"GO:0016020"
] | [
"beta2-adrenergic receptor activity",
"regulation of smooth muscle contraction",
"adenylate cyclase-activating G protein-coupled receptor signaling pathway",
"blood vessel diameter maintenance",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS",
"CDD"
] | [
"PR00562",
"cd15957"
] | [
"ADRENRGCB2AR",
"7tmA_Beta2_AR"
] | [
857,
646
] | 2 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"29",
"R-BTA-390696",
"R-BTA-418555",
"R-BTA-5689880",
"R-BTA-8856825",
"R-BTA-8856828",
"R-HSA-390696",
"R-HSA-418555",
"R-HSA-5689880",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-390696",
"R-MMU-418555",
"R-MMU-5689880",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-390696",
"R-RNO-4185... | [
"IUPHAR:29",
"REACTOME:R-BTA-390696",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-HSA-390696",
"REACTOME:R-HSA-418555",
"REACTOME:R-HSA-5689880",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-390696",
... | 21 | [
"2r4r",
"2r4s",
"2rh1",
"3d4s",
"3kj6",
"3ny8",
"3ny9",
"3nya",
"3p0g",
"3pds",
"3sn6",
"4gbr",
"4lde",
"4ldl",
"4ldo",
"4qkx",
"5d5a",
"5d5b",
"5d6l",
"5jqh",
"5x7d",
"6e67",
"6kr8",
"6mxt",
"6n48",
"6ni3",
"6oba",
"6prz",
"6ps0",
"6ps1",
"6ps2",
"6ps3"... | 129 | [
"PUB00066376",
"PUB00066377",
"PUB00066533",
"PUB00066535",
"PUB00066552",
"PUB00066557",
"PUB00066567",
"PUB00066568",
"PUB00066569",
"PUB00066570"
] | [
"18882199",
"2855960",
"11053129",
"15655528",
"14711933",
"12063255",
"15069206",
"1558559",
"18814142",
"11121511"
] | [
"A study of the adrenotropic receptors.",
"Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge.",
"G(i)-dependent localization of beta(2)-adrenergic receptor signaling to L-type Ca(2+) channels.",
"The selectivity of beta-adrenoceptor antagonists at the human beta1, b... | [
1948,
1988,
2000,
2005,
2004,
2002,
2004,
1992,
2009,
2000
] | 10 | [
"IPR002233"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
861
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
5
] | 3 | true | Family | Beta 2 adrenoceptor | Beta 2 adrenoceptor | ADRB2_rcpt | 9 |
IPR000333 | 333 | Ser/Thr protein kinase, TGFB receptor | TGFB_receptor | Family | 22,775 | false | false | Transforming growth factor-beta (TGF-beta) forms a family with other growth factors. The receptors for most of the members of this growth factor family are related. These proteins are receptor-type kinases of Ser/Thr type, which have a single transmembrane domain and a specific hydrophilic Cys-rich ligand-binding domai... | [
"GO:0004675",
"GO:0005524",
"GO:0007178",
"GO:0016020"
] | [
"transmembrane receptor protein serine/threonine kinase activity",
"ATP binding",
"cell surface receptor protein serine/threonine kinase signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"PANTHER"
] | [
"PR00653",
"PTHR23255"
] | [
"ACTIVIN2R",
""
] | [
8575,
22746
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.30",
"R-BTA-1502540",
"R-BTA-201451",
"R-BTA-2173788",
"R-BTA-2173789",
"R-BTA-2173791",
"R-BTA-5689880",
"R-BTA-9839389",
"R-BTA-9839406",
"R-CEL-201451",
"R-CEL-2173788",
"R-CEL-2173789",
"R-CEL-2173791",
"R-CEL-9839389",
"R-DME-1502540",
"R-DME-201451",
"R-DME-2173788",
... | [
"EC:2.7.11.30",
"REACTOME:R-BTA-1502540",
"REACTOME:R-BTA-201451",
"REACTOME:R-BTA-2173788",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-2173791",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-9839389",
"REACTOME:R-BTA-9839406",
"REACTOME:R-CEL-201451",
"REACTOME:R-CEL-2173788",
"REACTOME:R-CEL-2173... | 60 | [
"1b6c",
"1bte",
"1ias",
"1lx5",
"1nys",
"1nyu",
"1py5",
"1rw8",
"1s4y",
"1vjy",
"2goo",
"2h62",
"2h64",
"2hlq",
"2hlr",
"2qlu",
"2wot",
"2wou",
"2x7o",
"3faa",
"3g2f",
"3gxl",
"3h9r",
"3hmm",
"3kcf",
"3mdy",
"3mtf",
"3my0",
"3oom",
"3q4t",
"3q4u",
"3soc"... | 161 | [
"PUB00005725",
"PUB00005768",
"PUB00005778"
] | [
"8047140",
"8909794",
"9023056"
] | [
"Mechanism of activation of the TGF-beta receptor.",
"Serine/threonine kinase receptors: mediators of transforming growth factor beta family signals.",
"Signal transduction by members of the transforming growth factor-beta superfamily."
] | [
1994,
1996,
1996
] | 3 | [] | [
"IPR015771",
"IPR017194"
] | 0 | 2 | 0 | [
"Eukaryota"
] | [
22775
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
88,
25,
64,
39,
67
] | 6 | true | Family | Ser/Thr protein kinase, TGFB receptor | Ser/Thr protein kinase, TGFB receptor | TGFB_receptor | 4 |
IPR000334 | 334 | Glycoside hydrolase, family 45 | Glyco_hydro_45 | Domain | 2,265 | 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:0008810",
"GO:0005975"
] | [
"cellulase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE"
] | [
"PF02015",
"PS01140"
] | [
"Glyco_hydro_45",
"GLYCOSYL_HYDROL_F45"
] | [
2165,
1433
] | 2 | [
"CAZY",
"EC",
"METACYC",
"PROSITEDOC"
] | [
"GH45",
"3.2.1.4",
"PWY-6788",
"PDOC00877"
] | [
"CAZY:GH45",
"EC:3.2.1.4",
"METACYC:PWY-6788",
"PROSITEDOC:PDOC00877"
] | 4 | [
"1hd5",
"1l8f",
"1oa7",
"1oa9",
"2eng",
"3eng",
"4eng",
"5glx",
"5gly",
"5gm9",
"5h4u",
"6mvi",
"6mvj"
] | 13 | [
"PUB00000117",
"PUB00000528",
"PUB00003608",
"PUB00004155",
"PUB00004870",
"PUB00005266"
] | [
"2252383",
"8352747",
"1886523",
"8377830",
"7624375",
"8535779"
] | [
"Molecular biology of cellulose degradation.",
"New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.",
"Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.",
"Structure and function of endoglucanase V.",
"Conserved ... | [
1990,
1993,
1991,
1993,
1995,
1995
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
57,
2206,
2
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Glycoside hydrolase, family 45 | Glycoside hydrolase, family 45 | Glyco_hydro_45 | 1 |
IPR000335 | 335 | Bleomycin resistance protein | Bleomycin-R | Family | 6,660 | false | false | Bleomycin (Blm) is a glycopeptide antibiotic produced naturally by actinomycetes. It is a strong DNA-cutting agent and thus finds use as a potent anti-cancer drug. The DNA-cutting mechanism is complex, involving concomitant oxidation of FeII and reduction of oxygen. In addition to iron, Blm binds other transition metal... | [
"GO:0046677"
] | [
"response to antibiotic"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PRINTS",
"CDD"
] | [
"PF19581",
"PR00311",
"cd08349"
] | [
"Glyoxalase_7",
"BLEOMYCINRST",
"BLMA_like"
] | [
3086,
488,
5406
] | 3 | [] | [] | [] | 0 | [
"1byl",
"1ecs",
"1ewj",
"1jie",
"1jif",
"1mh6",
"1niq",
"1qto",
"1xrk",
"2rk9",
"2zhp",
"3bt3",
"3fcd",
"4iag",
"5cj3"
] | 15 | [
"PUB00001255"
] | [
"7516875"
] | [
"Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid pRL1063a",
"metagenomes",
"virus sp. ct1Hk25"
] | [
5,
6535,
103,
1,
15,
1
] | 6 | [] | [] | 0 | true | Family | Bleomycin resistance protein | Bleomycin resistance protein | Bleomycin-R | 4 |
IPR000336 | 336 | Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily | Flavivir/Alphavir_Ig-like_sf | Homologous_superfamily | 38,144 | false | false | This immuniglobulin-like domain superfamily is found in polyproteins from Flavivirus and Alphavirus. Flaviruses are small, enveloped RNA viruses that use arthropods such as mosquitoes for transmission to their vertebrate hosts, and include Yellow fever virus, West Nile virus, Tick-borne encephalitis virus, Japanese enc... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.60.40.350"
] | [
""
] | [
38144
] | 1 | [
"EC"
] | [
"3.4.21"
] | [
"EC:3.4.21"
] | 1 | [
"1i9w",
"1k4r",
"1ld4",
"1n6g",
"1na4",
"1oan",
"1ok8",
"1oke",
"1p58",
"1pjw",
"1rer",
"1s6n",
"1svb",
"1tg8",
"1tge",
"1thd",
"1urz",
"1uzg",
"1z3r",
"1z66",
"1z8y",
"1ztx",
"2ala",
"2b6b",
"2gg1",
"2h0p",
"2hg0",
"2i69",
"2jqm",
"2jsf",
"2jv6",
"2of6"... | 387 | [
"PUB00015617",
"PUB00015627"
] | [
"15378043",
"12759475"
] | [
"Transmission cycles, host range, evolution and emergence of arboviral disease.",
"A ligand-binding pocket in the dengue virus envelope glycoprotein."
] | [
2004,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Orthornavirae"
] | [
11,
38133
] | 2 | [] | [] | 0 | true | Homologous_superfamily | Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily | Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily | Flavivir/Alphavir_Ig-like_sf | 2 |
IPR000337 | 337 | GPCR, family 3 | GPCR_3 | Family | 46,124 | 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:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00248"
] | [
"GPCRMGR"
] | [
46124
] | 1 | [
"IUPHAR",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"291",
"PDOC00754",
"R-BTA-416476",
"R-BTA-418594",
"R-BTA-420499",
"R-CEL-1296041",
"R-CEL-418594",
"R-CEL-420499",
"R-CEL-977444",
"R-CEL-997272",
"R-DDI-418594",
"R-DDI-420499",
"R-DDI-977444",
"R-DME-418594",
"R-DME-420499",
"R-DRE-416476",
"R-DRE-420499",
"R-HSA-1296041",
"R... | [
"IUPHAR:291",
"PROSITEDOC:PDOC00754",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-420499",
"REACTOME:R-CEL-1296041",
"REACTOME:R-CEL-418594",
"REACTOME:R-CEL-420499",
"REACTOME:R-CEL-977444",
"REACTOME:R-CEL-997272",
"REACTOME:R-DDI-418594",
"REACTOME:R-DDI-420499",
"RE... | 44 | [
"1ewk",
"1ewt",
"1ewv",
"1isr",
"1iss",
"2e4u",
"2e4v",
"2e4w",
"2e4x",
"2e4y",
"2e4z",
"3ks9",
"3lmk",
"3mq4",
"3sm9",
"4f11",
"4f12",
"4mqe",
"4mqf",
"4mr7",
"4mr8",
"4mr9",
"4mrm",
"4ms1",
"4ms3",
"4ms4",
"4or2",
"4xaq",
"4xar",
"4xas",
"5c5c",
"5cni"... | 161 | [
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"8255296",
"1309649",
"8170923",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.",
"A family of metabotropic glutamate receptors.",
"Fingerprinting G-protein-coupled receptors.",
"A new multigene family of putative pheromone receptors.",
"Structure, pharmacology and therapeutic prospects o... | [
1993,
1992,
1994,
1997,
2007,
2000,
2003,
1994,
2005,
2009,
2006,
2013
] | 12 | [] | [
"IPR000162",
"IPR004073"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"ecological metagenomes"
] | [
74,
46007,
26,
17
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
16,
15,
148,
15,
73,
346,
8,
224,
15
] | 9 | true | Family | GPCR, family 3 | GPCR, family 3 | GPCR_3 | 2 |
IPR000340 | 340 | Dual specificity phosphatase, catalytic domain | Dual-sp_phosphatase_cat-dom | Domain | 79,791 | false | false | This entry represents dual specificity protein-tyrosine phosphatases. Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr ( ) and tyrosine specific protein phosphatase ( ) activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a wide range of phosphop... | [
"GO:0016311"
] | [
"dephosphorylation"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF00782"
] | [
"DSPc"
] | [
79791
] | 1 | [
"EC",
"EC",
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"3.1.3",
"3.1.3.16",
"3.1.3.48",
"GenProp1354",
"GenProp1726",
"PDOC00323",
"R-BTA-112409",
"R-BTA-202670",
"R-BTA-5675221",
"R-CEL-112409",
"R-CEL-202670",
"R-CEL-5675221",
"R-CEL-72086",
"R-CEL-77075",
"R-DDI-112409",
"R-DDI-202670",
"R-DDI-5675221",
"R-DDI-8873719",
"R-DME-112... | [
"EC:3.1.3",
"EC:3.1.3.16",
"EC:3.1.3.48",
"GP:GenProp1354",
"GP:GenProp1726",
"PROSITEDOC:PDOC00323",
"REACTOME:R-BTA-112409",
"REACTOME:R-BTA-202670",
"REACTOME:R-BTA-5675221",
"REACTOME:R-CEL-112409",
"REACTOME:R-CEL-202670",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CEL-72086",
"REACTOME:R-... | 58 | [
"1i9s",
"1i9t",
"1j4x",
"1m3g",
"1mkp",
"1vhr",
"1wrm",
"1yn9",
"1yz4",
"1zzw",
"2c46",
"2e0t",
"2esb",
"2g6z",
"2gwo",
"2hcm",
"2hxp",
"2j16",
"2j17",
"2nt2",
"2oud",
"2p4d",
"2pq5",
"2q05",
"2r0b",
"2rf6",
"2wgp",
"2y96",
"3cm3",
"3emu",
"3ezz",
"3f81"... | 134 | [
"PUB00005219",
"PUB00014502",
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"8650541",
"14739250",
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Crystal structure of the dual specificity protein phosphatase VHR.",
"Evolution of the multifunctional protein tyrosine phosphatase family.",
"Protein tyrosine phosphatases: mechanisms of catalysis and regulation.",
"Receptor and nonreceptor protein tyrosine phosphatases in the nervous system.",
"An overvi... | [
1996,
2004,
1998,
2003,
2003,
2006,
1996,
1998
] | 8 | [
"IPR000387"
] | [
"IPR027233",
"IPR045204",
"IPR048035"
] | 1 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
199,
3395,
75583,
410,
204
] | 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",... | [
62,
21,
208,
24,
1,
87,
94,
7,
54,
122,
6,
3,
126
] | 13 | true | Domain | Dual specificity phosphatase, catalytic domain | Dual specificity phosphatase, catalytic domain | Dual-sp_phosphatase_cat-dom | 6 |
IPR000341 | 341 | Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain | PI3K_Ras-bd_dom | Domain | 10,423 | false | false | Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate 4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in turns, initiates a vast array of signaling events. PI3Ks can be grouped into three classes ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00794",
"PS51546",
"SM00144"
] | [
"PI3K_rbd",
"PI3K_RBD",
"PI3K_rbd"
] | [
10130,
10293,
8765
] | 3 | [
"EC",
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.1.137",
"2.7.1.153",
"GenProp1758",
"PWY-6352",
"R-BTA-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-1433557",
"R-BTA-1660499",
"R-BTA-180292",
"R-BTA-186763",
"R-BTA-1963642",
"R-BTA-198203",
"R-BTA-201556",
"R-BTA-202424",
"R-BTA-2029485",... | [
"EC:2.7.1.137",
"EC:2.7.1.153",
"GP:GenProp1758",
"METACYC:PWY-6352",
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-180292",
"REACTOME:R-BTA-18... | 219 | [
"1e7u",
"1e7v",
"1e8w",
"1e8x",
"1e8y",
"1e8z",
"1e90",
"1he8",
"2a4z",
"2a5u",
"2chw",
"2chx",
"2chz",
"2rd0",
"2v4l",
"2wxf",
"2wxg",
"2wxh",
"2wxi",
"2wxj",
"2wxk",
"2wxl",
"2wxm",
"2wxn",
"2wxo",
"2wxp",
"2wxq",
"2wxr",
"2x38",
"2y3a",
"3apc",
"3apd"... | 324 | [
"PUB00043265",
"PUB00046181",
"PUB00049324",
"PUB00054408"
] | [
"17626883",
"10580505",
"18079394",
"20081827"
] | [
"Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.",
"Structural insights into phosphoinositide 3-kinase catalysis and signalling.",
"The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.",
"The p110 delta st... | [
2007,
1999,
2007,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses"
] | [
10421,
2
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
21,
6,
42,
33,
28
] | 6 | true | Domain | Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain | Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain | PI3K_Ras-bd_dom | 2 |
IPR000343 | 343 | Glutamyl-tRNA reductase | 4pyrrol_synth_GluRdtase | Family | 20,489 | false | false | Delta-aminolevulinic acid (ALA) is the obligatory precursor for the synthesis of all tetrapyrroles including porphyrin derivatives such as chlorophyll and heme. ALA can be synthesized via two different pathways: the Shemin (or C4) pathway which involves the single step condensation of succinyl-CoA and glycine and which... | [
"GO:0008883",
"GO:0050661",
"GO:0033014"
] | [
"glutamyl-tRNA reductase activity",
"NADP binding",
"tetrapyrrole biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00087",
"PIRSF000445",
"TIGR01035"
] | [
"Glu_tRNA_reductase",
"4pyrrol_synth_GluRdtase",
"hemA"
] | [
20377,
18054,
19533
] | 3 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"1.2.1.70",
"GenProp0217",
"GenProp1701",
"PWY-5188"
] | [
"EC:1.2.1.70",
"GP:GenProp0217",
"GP:GenProp1701",
"METACYC:PWY-5188"
] | 4 | [
"1gpj",
"4n7r",
"5che",
"5yjl"
] | 4 | [
"PUB00005387",
"PUB00009744",
"PUB00014678"
] | [
"1502723",
"11215515",
"7665501"
] | [
"Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis.",
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui."
] | [
1992,
2000,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
824,
17925,
1477,
263
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
1,
2,
15
] | 4 | true | Family | Glutamyl-tRNA reductase | Glutamyl-tRNA reductase | 4pyrrol_synth_GluRdtase | 1 |
IPR000344 | 344 | 7TM GPCR, serpentine receptor class a (Sra) | 7TM_GPCR_serpentine_rcpt_Sra | Family | 520 | 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:0007606",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"sensory perception of chemical stimulus",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF02117",
"PR00697"
] | [
"7TM_GPCR_Sra",
"TMPROTEINSRA"
] | [
485,
288
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000924",
"PUB00004961",
"PUB00007387",
"PUB00044128",
"PUB00044129",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"7585938",
"8170923",
"10580986",
"18050473",
"15618405",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Divergent seven transmembrane receptors are candidate chemosensory receptors in C. elegans.",
"Fingerprinting G-protein-coupled receptors.",
"Chemosensory signaling in C. elegans.",
"The putative chemoreceptor families of C. elegans.",
"Identification of a nematode chemosensory gene family.",
"The G prot... | [
1995,
1994,
1999,
2006,
2005,
2003,
1994,
2005,
2009,
2006,
2013
] | 11 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Thermoanaerobacterium thermosaccharolyticum"
] | [
518,
2
] | 2 | [
"Caenorhabditis elegans"
] | [
35
] | 1 | true | Family | 7TM GPCR, serpentine receptor class a (Sra) | 7TM GPCR, serpentine receptor class a (Sra) | 7TM_GPCR_serpentine_rcpt_Sra | 6 |
IPR000346 | 346 | Hyperglycemic hormone type 1 | Hyperglycemic1 | Family | 512 | false | false | Hyperglycemic hormone, which controls blood sugar levels, is an abundant peptide in the sinus glands of isopods and decapods [ , ]. The peptide is a potent secretagogue, releasing digestive enzymes from the hepatopancreas. It may act as a stress hormone. The peptide contains around 70 amino acid residues, and includes ... | [
"GO:0005184",
"GO:0005576"
] | [
"neuropeptide hormone activity",
"extracellular region"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00548"
] | [
"HYPRGLYCEMC1"
] | [
512
] | 1 | [] | [] | [] | 0 | [
"5b5i",
"5xs1"
] | 2 | [
"PUB00000190",
"PUB00001435",
"PUB00001577"
] | [
"2169734",
"8436119",
"2792364"
] | [
"Amino acid sequence of a peptide with both molt-inhibiting and hyperglycemic activities in the lobster, Homarus americanus.",
"Isolation and molecular characterization of a hyperglycemic neuropeptide from the sinus gland of the terrestrial isopod Armadillidium vulgare (Crustacea).",
"Amino acid sequence of the... | [
1990,
1993,
1989
] | 3 | [
"IPR001166"
] | [] | 1 | 0 | 1 | [
"Arthropoda"
] | [
512
] | 1 | [
"Drosophila melanogaster"
] | [
1
] | 1 | true | Family | Hyperglycemic hormone type 1 | Hyperglycemic hormone type 1 | Hyperglycemic1 | 1 |
IPR000347 | 347 | Metallothionein, family 15, plant | Metalthion_15p | Family | 2,222 | false | false | Members of this family are metallothioneins. These proteins are cysteine rich proteins that bind to heavy metals. Members of this family appear to be closest to Class II metallothioneins. | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF01439",
"PTHR33543"
] | [
"Metallothio_2",
""
] | [
2222,
2006
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
2217
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
5,
30,
41
] | 3 | true | Family | Metallothionein, family 15, plant | Metallothionein, family 15, plant | Metalthion_15p | 6 |
IPR000349 | 349 | Large envelope protein S | HBV_HBSAG | Family | 62,461 | false | false | This entry represents the large envelope protein S from hepatitis B virus. The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initia... | [
"GO:0016032"
] | [
"viral process"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"PFAM"
] | [
"MF_04075",
"PF00695"
] | [
"HBV_HBSAG",
"vMSA"
] | [
8648,
62461
] | 2 | [] | [] | [] | 0 | [
"1wz4",
"5yax",
"7tuk",
"7tul",
"8rqf",
"8ymj",
"8ymk",
"9iyx",
"9iyy",
"9jt1",
"9u9b",
"9ubq"
] | 12 | [
"PUB00087119",
"PUB00087120",
"PUB00087121"
] | [
"15567498",
"9498079",
"16863502"
] | [
"Envelopment of the hepatitis B virus nucleocapsid.",
"Role of glycan processing in hepatitis B virus envelope protein trafficking.",
"Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and hepatocarcinogenesis."
] | [
2004,
1998,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Bilateria",
"Hepadnaviridae"
] | [
2,
62459
] | 2 | [] | [] | 0 | true | Family | Large envelope protein S | Large envelope protein S | HBV_HBSAG | 8 |
IPR000351 | 351 | Neuropeptide Y1 receptor | NPY1_rcpt | Family | 857 | false | false | Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01013"
] | [
"NRPEPTIDEY1R"
] | [
857
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"305",
"R-BTA-375276",
"R-BTA-418594",
"R-CFA-375276",
"R-CFA-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594"
] | [
"IUPHAR:305",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418594",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594"
] | 11 | [
"7vgx",
"7x9a",
"8k6m",
"8k6o"
] | 4 | [
"PUB00063739",
"PUB00063740",
"PUB00063741",
"PUB00063742",
"PUB00063743",
"PUB00063744",
"PUB00063745",
"PUB00063746",
"PUB00063747",
"PUB00063748",
"PUB00063749",
"PUB00063750",
"PUB00063751",
"PUB00063752",
"PUB00063753",
"PUB00063754",
"PUB00063755",
"PUB00063756",
"PUB000637... | [
"6549409",
"16874931",
"6547387",
"6549039",
"2821236",
"8395947",
"16190896",
"7529442",
"7644568",
"15337373",
"8685245",
"8369959",
"11287113",
"7629398",
"6133408",
"3855566",
"12678499",
"17222466",
"8013354",
"9833945",
"9389418",
"9446690",
"2453065",
"1661086",
... | [
"Neuropeptide Y: a potent inducer of consummatory behavior in rats.",
"Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.",
"Neuropeptide Y and human pancreatic polypeptide stimulate feeding behavior in rats.",
"Neuropeptide Y: stimulation of feeding and drinking by injection into the... | [
1984,
2006,
1984,
1984,
1987,
1993,
2005,
1994,
1995,
2004,
1996,
1993,
2001,
1995,
1982,
1985,
2003,
2007,
1994,
1998,
1997,
1998,
1988,
1991,
1995,
2003,
2007,
1998,
2004,
2007,
2007,
2007,
2006,
2007,
2006,
2007,
2008,
1996,
1996,
1998... | 46 | [
"IPR000611"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
857
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
2,
4
] | 4 | true | Family | Neuropeptide Y1 receptor | Neuropeptide Y1 receptor | NPY1_rcpt | 7 |
IPR000353 | 353 | MHC class II, beta chain, N-terminal | MHC_II_b_N | Domain | 52,566 | false | false | This entry represents the N-terminal domain (also called beta-1 domain) of the beta chain of class II MHC glycoproteins from vertebrates. Major Histocompatibility Complex (MHC) glycoproteins are heterodimeric cell surface receptors that function to present antigen peptide fragments to T cells responsible for cell-media... | [
"GO:0006955",
"GO:0019882",
"GO:0016020",
"GO:0042613"
] | [
"immune response",
"antigen processing and presentation",
"membrane",
"MHC class II protein complex"
] | [
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PFAM",
"SMART"
] | [
"PF00969",
"SM00921"
] | [
"MHC_II_beta",
"MHC_II_beta"
] | [
52349,
51845
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-202424",
"R-HSA-202427",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-2132295",
"R-HSA-389948",
"R-HSA-877300",
"R-MMU-202424",
"R-MMU-202427",
"R-MMU-202430",
"R-MMU-202433",
"R-MMU-2132295",
"R-MMU-389948",
"R-RNO-202424",
"R-RNO-202427",
"R-RNO-202430",
"R-RNO-202433",
"R-RNO-2... | [
"REACTOME:R-HSA-202424",
"REACTOME:R-HSA-202427",
"REACTOME:R-HSA-202430",
"REACTOME:R-HSA-202433",
"REACTOME:R-HSA-2132295",
"REACTOME:R-HSA-389948",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-202424",
"REACTOME:R-MMU-202427",
"REACTOME:R-MMU-202430",
"REACTOME:R-MMU-202433",
"REACTOME:R-MMU-21... | 19 | [
"1a6a",
"1aqd",
"1bx2",
"1d5m",
"1d5x",
"1d5z",
"1d6e",
"1d9k",
"1dlh",
"1es0",
"1f3j",
"1fne",
"1fng",
"1fv1",
"1fyt",
"1h15",
"1hdm",
"1hqr",
"1hxy",
"1i3r",
"1iak",
"1iao",
"1iea",
"1ieb",
"1j8h",
"1jk8",
"1jl4",
"1jwm",
"1jws",
"1jwu",
"1k2d",
"1k8i"... | 280 | [
"PUB00015254",
"PUB00016273"
] | [
"7612235",
"15120183"
] | [
"The three-dimensional structure of peptide-MHC complexes.",
"Function and regulation of MHC class II molecules in T-lymphocytes: of mice and men."
] | [
1995,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
4,
52562
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
14801,
260,
81
] | 4 | true | Domain | MHC class II, beta chain, N-terminal | MHC class II, beta chain, N-terminal | MHC_II_b_N | 1 |
IPR000354 | 354 | Involucrin repeat | Involucrin_rpt | Repeat | 33 | false | false | Involucrin [ , ] is a protein present in keratinocytes of epidermis and other stratified squamous epithelia. Involucrin first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an insoluble envelope beneath the plasma membrane. Stru... | [
"GO:0031424",
"GO:0005737"
] | [
"keratinization",
"cytoplasm"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00904"
] | [
"Involucrin"
] | [
33
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-6809371",
"R-HSA-9725554"
] | [
"REACTOME:R-HSA-6809371",
"REACTOME:R-HSA-9725554"
] | 2 | [] | 0 | [
"PUB00003634",
"PUB00003636"
] | [
"1359382",
"8277848"
] | [
"Consecutive actions of different gene-altering mechanisms in the evolution of involucrin.",
"The involucrin genes of the mouse and the rat: study of their shared repeats."
] | [
1992,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Simiiformes"
] | [
33
] | 1 | [
"Homo sapiens"
] | [
3
] | 1 | true | Repeat | Involucrin repeat | Involucrin repeat | Involucrin_rpt | 8 |
IPR000355 | 355 | Chemokine receptor family | Chemokine_rcpt | Family | 13,306 | false | false | Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang... | [
"GO:0004950",
"GO:0006935",
"GO:0007186",
"GO:0016020"
] | [
"chemokine receptor activity",
"chemotaxis",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00657"
] | [
"CCCHEMOKINER"
] | [
13306
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-376176",
"R-BTA-380108",
"R-BTA-418594",
"R-CFA-418594",
"R-HSA-1461957",
"R-HSA-173107",
"R-HSA-376176",
"R-HSA-380108",
"R-HSA-418594",
"R-HSA-6783783",
"R-HSA-9609690",
"R-HSA-9823730",
"R-HSA-9827857",
"R-HSA-9937080",
"R-MMU-1461957",
"R-MMU-376176",
"R-MMU-380108",
"R-... | [
"REACTOME:R-BTA-376176",
"REACTOME:R-BTA-380108",
"REACTOME:R-BTA-418594",
"REACTOME:R-CFA-418594",
"REACTOME:R-HSA-1461957",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-376176",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-9609690",
"REACTOME:R-HSA-... | 22 | [
"4mbs",
"4xt1",
"4xt3",
"5lwe",
"5uiw",
"5wb1",
"5wb2",
"6akx",
"6aky",
"6gps",
"6gpx",
"6meo",
"6met",
"6qzh",
"6wwz",
"7rkf",
"7rkm",
"7rkn",
"7vl8",
"7vl9",
"7vla",
"7x9y",
"7xa3",
"8hnn",
"8k2w",
"8k3z",
"8kfx",
"8kfy",
"8kfz",
"8xml",
"8xxy",
"8xxz"... | 49 | [
"PUB00009401",
"PUB00064589",
"PUB00064621",
"PUB00064622",
"PUB00067945",
"PUB00067946"
] | [
"11544102",
"10714678",
"10601351",
"9500790",
"9689100",
"7592998"
] | [
"Chemokine receptors.",
"Chemokines: a new classification system and their role in immunity.",
"Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.",
"Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte... | [
2001,
2000,
1999,
1998,
1998,
1995
] | 6 | [
"IPR050119"
] | [
"IPR000174",
"IPR001053",
"IPR001277",
"IPR001718",
"IPR002235",
"IPR002236",
"IPR002237",
"IPR002238",
"IPR002239",
"IPR002240",
"IPR004067",
"IPR004068",
"IPR004069",
"IPR004070",
"IPR005382",
"IPR005383"
] | 1 | 16 | 0 | [
"Deuterostomia",
"Viruses"
] | [
12974,
332
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
48,
141,
37,
58
] | 4 | true | Family | Chemokine receptor family | Chemokine receptor family | Chemokine_rcpt | 1 |
IPR000356 | 356 | P2Y2 purinoceptor | P2Y2_rcpt | Family | 602 | false | false | There are three distinct families of extracellular receptors for purine and pyrimidine nucleotides [ ], known as P1, P2X and P2Y purinoceptors [ ]. These receptors induce a wide variety of biological effects and are involved in many different cellular functions [ , , ]. P2X receptors are ligand-gated ion channels, wher... | [
"GO:0045028",
"GO:0007200",
"GO:0070257",
"GO:0097746",
"GO:0016020"
] | [
"G protein-coupled purinergic nucleotide receptor activity",
"phospholipase C-activating G protein-coupled receptor signaling pathway",
"positive regulation of mucus secretion",
"blood vessel diameter maintenance",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00594"
] | [
"P2Y2PRNOCPTR"
] | [
602
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"324",
"R-HSA-416476",
"R-HSA-417957",
"R-HSA-5683826",
"R-HSA-9856530",
"R-MMU-416476",
"R-MMU-417957",
"R-MMU-5683826",
"R-MMU-9856530",
"R-RNO-416476",
"R-RNO-417957",
"R-RNO-5683826",
"R-RNO-9856530",
"R-SSC-416476",
"R-SSC-417957",
"R-SSC-5683826",
"R-SSC-9856530"
] | [
"IUPHAR:324",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-417957",
"REACTOME:R-HSA-5683826",
"REACTOME:R-HSA-9856530",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-417957",
"REACTOME:R-MMU-5683826",
"REACTOME:R-MMU-9856530",
"REACTOME:R-RNO-416476",
"REACTOME:R-RNO-417957",
"REACTOME:R-RNO-5683826",
... | 17 | [
"9k0x",
"9k20",
"9k25"
] | 3 | [
"PUB00007054",
"PUB00028347",
"PUB00033968",
"PUB00066193",
"PUB00066194",
"PUB00066195",
"PUB00066196",
"PUB00066197",
"PUB00066198",
"PUB00066203",
"PUB00066204",
"PUB00066205",
"PUB00066206",
"PUB00066207",
"PUB00066208",
"PUB00066209",
"PUB00066210",
"PUB00066211",
"PUB000662... | [
"12270951",
"8872457",
"11111826",
"10629443",
"20471713",
"11099464",
"19921464",
"11734617",
"16257449",
"9364468",
"7724657",
"16968944",
"8508924",
"19386608",
"8921391",
"8702478",
"12724320",
"18404483",
"9755289",
"11794691",
"16914897",
"16934527",
"11004484",
"... | [
"Molecular physiology of P2X receptors.",
"Modelling the P2Y purinoceptor using rhodopsin as template.",
"Molecular pharmacology of P2Y-receptors.",
"Renal vascular reactivity to P(2)-purinoceptor activation in spontaneously hypertensive rats.",
"Purinergic receptor agonists modulate phagocytosis and cleara... | [
2002,
1995,
2000,
2000,
2011,
2000,
2010,
2001,
2006,
1997,
1994,
2006,
1993,
2009,
1996,
1996,
2003,
2006,
1998,
2001,
2006,
2006,
2000,
1995,
2001,
1993,
1996,
2007,
2007,
2005,
2005,
2002,
1996,
1998,
2008,
2005,
2009,
2009,
2005,
2006... | 42 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
602
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
3
] | 3 | true | Family | P2Y2 purinoceptor | P2Y2 purinoceptor | P2Y2_rcpt | 7 |
IPR000357 | 357 | HEAT repeat | HEAT | Repeat | 23,334 | false | false | The HEAT repeat is a tandemly repeated, 37-47 amino acid long module occurring in a number of cytoplasmic proteins, including the four name-giving proteins huntingtin, elongation factor 3 (EF3), the 65 kDa alpha regulatory subunit of protein phosphatase 2A (PP2A) and the yeast PI3-kinase TOR1 [ ]. Arrays of HEAT repeat... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02985"
] | [
"HEAT"
] | [
23334
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50077",
"R-CEL-195253",
"R-CEL-196299",
"R-CEL-198753",
"R-CEL-202670",
"R-CEL-2995383",
"R-CEL-389513",
"R-CEL-5673000",
"R-CEL-5675221",
"R-CEL-6811558",
"R-CEL-69231",
"R-CEL-69273",
"R-CEL-975957",
"R-CEL-9833482",
"R-CEL-9860927",
"R-DDI-113501",
"R-DDI-1632852",
"R-DDI-1... | [
"PROSITEDOC:PDOC50077",
"REACTOME:R-CEL-195253",
"REACTOME:R-CEL-196299",
"REACTOME:R-CEL-198753",
"REACTOME:R-CEL-202670",
"REACTOME:R-CEL-2995383",
"REACTOME:R-CEL-389513",
"REACTOME:R-CEL-5673000",
"REACTOME:R-CEL-5675221",
"REACTOME:R-CEL-6811558",
"REACTOME:R-CEL-69231",
"REACTOME:R-CEL-6... | 218 | [
"1b3u",
"2db0",
"2iae",
"2ie3",
"2ie4",
"2npp",
"2nyl",
"2nym",
"2pf4",
"2pkg",
"3c5w",
"3dw8",
"3fga",
"3k7v",
"3k7w",
"3ltj",
"3ltm",
"4i5l",
"4i5n",
"4jw2",
"4jw3",
"4lac",
"4zv6",
"5h64",
"5w0w",
"6bcu",
"6bcx",
"6bzx",
"6ef4",
"6fsq",
"6ft5",
"6hwp"... | 85 | [
"PUB00006179",
"PUB00006180"
] | [
"7550332",
"9989501"
] | [
"HEAT repeats in the Huntington's disease protein.",
"The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs."
] | [
1995,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
178,
1549,
21558,
49
] | 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... | [
33,
5,
32,
8,
43,
37,
1,
17,
61,
2,
1,
81
] | 12 | true | Repeat | HEAT repeat | HEAT repeat | HEAT | 7 |
IPR000358 | 358 | Ribonucleotide reductase small subunit family | RNR_small_fam | Family | 37,834 | false | false | Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, ( ) [ , ] catalyses the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides: 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H 2 O = ribonucleoside diphosphate + reduced thioredoxin RNR provi... | [
"GO:0009263"
] | [
"deoxyribonucleotide biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF00268",
"PIRSF000355",
"PTHR23409"
] | [
"Ribonuc_red_sm",
"NrdB",
""
] | [
35385,
16824,
35677
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"1.17.4.1",
"GenProp0289",
"GenProp1227",
"GenProp1343",
"GenProp1389",
"GenProp1406",
"GenProp1446",
"GenProp1484",
"GenProp1586",
"GenProp1617",
"GenProp1635",
"PWY-6545",
"PWY-7184",
"PWY-7198",
"PWY-7210",
"PWY-7220",
"PWY-7222",
"PWY-7226",
"PWY-7227",
"PDOC00317",
"R-CE... | [
"EC:1.17.4.1",
"GP:GenProp0289",
"GP:GenProp1227",
"GP:GenProp1343",
"GP:GenProp1389",
"GP:GenProp1406",
"GP:GenProp1446",
"GP:GenProp1484",
"GP:GenProp1586",
"GP:GenProp1617",
"GP:GenProp1635",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"METACYC:PW... | 32 | [
"1av8",
"1biq",
"1h0n",
"1h0o",
"1jk0",
"1jpr",
"1jqc",
"1kgn",
"1kgo",
"1kgp",
"1mrr",
"1mxr",
"1oqu",
"1pfr",
"1pim",
"1piu",
"1piy",
"1piz",
"1pj0",
"1pj1",
"1pm2",
"1r2f",
"1r65",
"1rib",
"1rnr",
"1rsr",
"1rsv",
"1smq",
"1sms",
"1syy",
"1uzr",
"1w68"... | 220 | [
"PUB00000559",
"PUB00004064",
"PUB00005164",
"PUB00007088",
"PUB00051672",
"PUB00062565"
] | [
"3286319",
"2190093",
"8511586",
"11875520",
"19321420",
"22976985"
] | [
"Structure-function studies of the large subunit of ribonucleotide reductase from Escherichia coli.",
"Three-dimensional structure of the free radical protein of ribonucleotide reductase.",
"From RNA to DNA, why so many ribonucleotide reductases?",
"The crystal structure of class II ribonucleotide reductase r... | [
1988,
1990,
1993,
2002,
2009,
2012
] | 6 | [] | [
"IPR033908",
"IPR033909"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
266,
23118,
11224,
2736,
490
] | 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",... | [
12,
2,
9,
1,
2,
8,
10,
1,
5,
8,
2,
1,
8
] | 13 | true | Family | Ribonucleotide reductase small subunit family | Ribonucleotide reductase small subunit family | RNR_small_fam | 5 |
IPR000361 | 361 | Core domain, A-type assembly protein ATAP | ATAP_core_dom | Domain | 49,473 | false | false | This entry represents a common domain in ATAP proteins and related FeS cluster biogenesis proteins. It displays two α-helices and seven β-strands. In SufA from Escherichia coli, the central core consists of two β-sheets, a three-stranded sheet (short A1 and A2-A3) and a four-stranded sheet (strands B1-B4) [ ]. Several ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01521"
] | [
"Fe-S_biosyn"
] | [
49473
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-1362409",
"R-BTA-9854311",
"R-DDI-1362409",
"R-DME-1362409",
"R-HSA-1362409",
"R-HSA-9854311",
"R-MMU-1362409",
"R-MMU-9854311",
"R-RNO-1362409",
"R-SCE-1362409",
"R-SPO-1362409"
] | [
"REACTOME:R-BTA-1362409",
"REACTOME:R-BTA-9854311",
"REACTOME:R-DDI-1362409",
"REACTOME:R-DME-1362409",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-9854311",
"REACTOME:R-MMU-1362409",
"REACTOME:R-MMU-9854311",
"REACTOME:R-RNO-1362409",
"REACTOME:R-SCE-1362409",
"REACTOME:R-SPO-1362409"
] | 11 | [
"1nwb",
"1r94",
"1r95",
"1s98",
"1x0g",
"2apn",
"2d2a",
"2k4z",
"2p2e",
"2qgo"
] | 10 | [
"PUB00003442",
"PUB00003602",
"PUB00028014",
"PUB00030961",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640",
"PUB00040158",
"PUB00058194",
"PUB00160404",
"PUB00160405",
"PUB00160406"
] | [
"8875867",
"10217509",
"11498000",
"15050828",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785",
"16298366",
"17698959",
"23586717",
"32108236",
"33007329"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Organization and expression of nitrogen-fixation genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1.",
"Incorporation of iron-sulphur clusters in membrane-bound protein... | [
1996,
1999,
2001,
2004,
2005,
2005,
2006,
2005,
2007,
2004,
2005,
2007,
2013,
2020,
2021
] | 15 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
537,
38224,
9973,
28,
711
] | 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,
3,
3,
2,
4,
4,
4,
1,
13,
6,
2,
1,
26
] | 13 | true | Domain | Core domain, A-type assembly protein ATAP | Core domain, A-type assembly protein ATAP | ATAP_core_dom | 2 |
IPR000362 | 362 | Fumarate lyase family | Fumarate_lyase_fam | Family | 111,404 | false | false | A number of enzymes, belonging to the lyase class, for which fumarate is a substrate, have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes [ ]. The following are examples of members of this family: : 3-carboxymuconate lacton... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00149"
] | [
"FUMRATELYASE"
] | [
111404
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"4.3.2.1",
"PWY-4983",
"PWY-4984",
"PWY-5",
"PWY-5154",
"PWY-7400",
"PDOC00147",
"R-BTA-70635",
"R-CEL-71403",
"R-CEL-73817",
"R-CEL-9837999",
"R-DDI-71403",
"R-DDI-9837999",
"R-DRE-71403",
"R-GGA-187630",
"R-GGA-419140",
"R-GGA-421203",
"R-GGA-70635",
"R-HSA-70635",
"R-HSA-714... | [
"EC:4.3.2.1",
"METACYC:PWY-4983",
"METACYC:PWY-4984",
"METACYC:PWY-5",
"METACYC:PWY-5154",
"METACYC:PWY-7400",
"PROSITEDOC:PDOC00147",
"REACTOME:R-BTA-70635",
"REACTOME:R-CEL-71403",
"REACTOME:R-CEL-73817",
"REACTOME:R-CEL-9837999",
"REACTOME:R-DDI-71403",
"REACTOME:R-DDI-9837999",
"REACTO... | 39 | [
"1aos",
"1auw",
"1c3c",
"1c3u",
"1dcn",
"1dof",
"1f1o",
"1fuo",
"1fup",
"1fuq",
"1fur",
"1hy0",
"1hy1",
"1i0a",
"1j3u",
"1jsw",
"1k62",
"1k7w",
"1kq7",
"1q5n",
"1re5",
"1tj7",
"1tju",
"1tjv",
"1tjw",
"1u15",
"1u16",
"1vdk",
"1xwo",
"1yfe",
"1yfm",
"1yis"... | 138 | [
"PUB00000374",
"PUB00000586",
"PUB00004940",
"PUB00083219",
"PUB00083220"
] | [
"1390752",
"3282546",
"1574589",
"26639528",
"27750034"
] | [
"3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif.",
"Two biochemically distinct classes of fumarase in Escherichia coli.",
"De novo purine nucleotide biosynthesis.",
"Ustilago maydis pro... | [
1992,
1988,
1992,
2016,
2016
] | 5 | [] | [
"IPR004708",
"IPR004769",
"IPR005677",
"IPR009049",
"IPR012789"
] | 0 | 5 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2247,
90941,
16693,
10,
1513
] | 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",... | [
25,
2,
6,
16,
4,
29,
10,
3,
8,
12,
3,
5,
24
] | 13 | true | Family | Fumarate lyase family | Fumarate lyase family | Fumarate_lyase_fam | 3 |
IPR000366 | 366 | GPCR fungal pheromone mating factor, STE2 | GPCR_STE2 | Family | 1,694 | false | false | This entry represents the STE2-type family of GPCR. The STE2 gene of Saccharomyces cerevisiae (Baker's yeast) is the cell-surface receptor that binds the 13-residue lipopeptide a-factor. GPCR Fungal pheromone mating factor receptors form a distinct family of G-protein-coupled receptors, and are also known as Class D GP... | [
"GO:0004932",
"GO:0007186",
"GO:0016020"
] | [
"mating-type factor pheromone receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02116",
"PR00250",
"PTHR28009"
] | [
"STE2",
"GPCRSTE2",
""
] | [
1281,
1548,
1260
] | 3 | [] | [] | [] | 0 | [
"2k9p",
"7ad3",
"7qa8",
"7qb9",
"7qbc",
"7qbi"
] | 6 | [
"PUB00001139",
"PUB00004338",
"PUB00004657",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"16453635",
"3001640",
"2836861",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae.",
"The yeast alpha-factor receptor: structural properties deduced from the sequence of the STE2 gene.",
"STE2 protein of Saccharomyces kluyveri is a member of the rhodopsin/beta-adrenergic receptor family and... | [
1985,
1985,
1988,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"ecological metagenomes"
] | [
141,
1549,
2,
2
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | GPCR fungal pheromone mating factor, STE2 | GPCR fungal pheromone mating factor, STE2 | GPCR_STE2 | 4 |
IPR000367 | 367 | G-protein alpha subunit, group S | Gprotein_alpha_S | Family | 4,714 | false | false | Guanine nucleotide binding proteins (G-proteins) are membrane-associated, heterotrimeric proteins composed of three subunits: alpha ( ), beta ( ) and gamma ( ) [ ]. G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian cells, regulating systems as diverse as sensory perce... | [
"GO:0003924",
"GO:0005525",
"GO:0031683",
"GO:0007186"
] | [
"GTPase activity",
"GTP binding",
"G-protein beta/gamma-subunit complex binding",
"G protein-coupled receptor signaling pathway"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PRINTS"
] | [
"PR00443"
] | [
"GPROTEINAS"
] | [
4714
] | 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-DME-170660",
"R-DME-170670",
"R-DME-392851",
"R-DME-418555",
"R-HSA-163359",
"R-HSA-164378",
"R-HSA-170660",
"R-HSA-170670",
"R-HSA-381676",
"R-HSA-381753",
"R-HSA-392851",
"R-HSA-418555",
"R-HSA-418594",
"R-HSA-418597",
"R-HSA-420092",
"R-HSA-432040",
"R-HSA-5610787",
"R-HSA-96... | [
"REACTOME:R-DME-170660",
"REACTOME:R-DME-170670",
"REACTOME:R-DME-392851",
"REACTOME:R-DME-418555",
"REACTOME:R-HSA-163359",
"REACTOME:R-HSA-164378",
"REACTOME:R-HSA-170660",
"REACTOME:R-HSA-170670",
"REACTOME:R-HSA-381676",
"REACTOME:R-HSA-381753",
"REACTOME:R-HSA-392851",
"REACTOME:R-HSA-418... | 36 | [
"1azs",
"1azt",
"1cjk",
"1cjt",
"1cju",
"1cjv",
"1cs4",
"1cul",
"1tl7",
"1u0h",
"2gvd",
"2gvz",
"3c14",
"3c15",
"3c16",
"3g82",
"3maa",
"3sn6",
"5g53",
"5uz7",
"5vai",
"6au6",
"6b3j",
"6e3y",
"6eg8",
"6gdg",
"6li3",
"6lmk",
"6lpb",
"6m1h",
"6m1i",
"6nbf"... | 589 | [
"PUB00005142",
"PUB00015166",
"PUB00015168",
"PUB00015169",
"PUB00015170",
"PUB00015171",
"PUB00015172",
"PUB00015173"
] | [
"1902986",
"15294442",
"15119945",
"14762218",
"11313912",
"9278091",
"11882385",
"15331575"
] | [
"Diversity of G proteins in signal transduction.",
"G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?",
"Biochemistry of transmembrane signaling mediated by trimeric G proteins.",
"G protein signaling: insights from new structures.",
"Regulation of G prote... | [
1991,
2004,
2004,
2004,
2001,
1997,
2002,
2004
] | 8 | [
"IPR001019"
] | [] | 1 | 0 | 1 | [
"Metazoa"
] | [
4714
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
7,
2,
24,
12,
16
] | 6 | true | Family | G-protein alpha subunit, group S | G-protein alpha subunit, group S | Gprotein_alpha_S | 8 |
IPR000368 | 368 | Sucrose synthase, first GT-B domain | Sucrose_synth_GT-B1 | Domain | 7,862 | false | false | This entry represents the first GT-B domain (also referred to as GT-BN in [ ] of sucrose synthases, while the second one, at the C-terminal (GT-BC), is represented in [ , ]. The substrates of these proteins (UDP-Glc or UDP and fructose) bound in the cleft between the GT-B domains [ ]. Sucrose synthases catalyse the syn... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00862"
] | [
"GT-B_Sucrose_synth"
] | [
7862
] | 1 | [
"EC",
"METACYC"
] | [
"2.4.1.13",
"PWY-3801"
] | [
"EC:2.4.1.13",
"METACYC:PWY-3801"
] | 2 | [
"2r60",
"2r66",
"2r68",
"3s27",
"3s28",
"3s29",
"4rbn"
] | 7 | [
"PUB00057019",
"PUB00159903"
] | [
"21865170",
"26013491"
] | [
"The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications.",
"The Crystal Structure of Nitrosomonas europaea Sucrose Synthase Reveals Critical Conformational Changes and Insights into Sucrose Metabolism in Prokaryotes."
] | [
2011,
2015
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"ecological metagenomes"
] | [
740,
1,
7103,
18
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
59,
25,
139
] | 3 | true | Domain | Sucrose synthase, first GT-B domain | Sucrose synthase, first GT-B domain | Sucrose_synth_GT-B1 | 8 |
IPR000369 | 369 | Potassium channel, voltage-dependent, beta subunit, KCNE | K_chnl_KCNE | Family | 3,220 | false | false | Two types of beta subunit (KCNE and KCNAB) are presently known to associate with voltage-gated alpha subunits (Kv, KCNQ and eag-like). However, not all combinations of alpha and beta subunits are possible. The KCNE family of K+ channel subunits are membrane glycoproteins that possess a single transmembrane (TM) domain.... | [
"GO:0005249",
"GO:0006811",
"GO:0016020"
] | [
"voltage-gated potassium channel activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02060",
"PR00168",
"PTHR15282"
] | [
"ISK_Channel",
"KCNECHANNEL",
""
] | [
3118,
1915,
3097
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5576890",
"R-HSA-5576893",
"R-MMU-5576890",
"R-MMU-5576893",
"R-RNO-5576890",
"R-RNO-5576893"
] | [
"REACTOME:R-HSA-5576890",
"REACTOME:R-HSA-5576893",
"REACTOME:R-MMU-5576890",
"REACTOME:R-MMU-5576893",
"REACTOME:R-RNO-5576890",
"REACTOME:R-RNO-5576893"
] | 6 | [
"2k21",
"2m0q",
"2ndj",
"6v00",
"6v01",
"9u7f",
"9uc8",
"9vec",
"9vei",
"9wd8"
] | 10 | [
"PUB00001055",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00006577",
"PUB00009378"
] | [
"1772658",
"1879548",
"1373731",
"2448635",
"2451788",
"2555158",
"11178249"
] | [
"The molecular biology of K+ channels.",
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso... | [
1991,
1991,
1992,
1988,
1988,
1989,
2000
] | 7 | [] | [
"IPR005424",
"IPR005425",
"IPR005426"
] | 0 | 3 | 0 | [
"Bilateria"
] | [
3220
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
17,
11,
10
] | 4 | true | Family | Potassium channel, voltage-dependent, beta subunit, KCNE | Potassium channel, voltage-dependent, beta subunit, KCNE | K_chnl_KCNE | 9 |
IPR000370 | 370 | Prostacyclin (prostanoid IP) receptor | Prostglndn_IP_rcpt | Family | 813 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00856"
] | [
"PRSTNOIDIPR"
] | [
813
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"345",
"R-HSA-391908",
"R-HSA-392851",
"R-HSA-418555",
"R-MMU-391908",
"R-MMU-392851",
"R-MMU-418555",
"R-RNO-391908",
"R-RNO-392851"
] | [
"IUPHAR:345",
"REACTOME:R-HSA-391908",
"REACTOME:R-HSA-392851",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-392851",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-391908",
"REACTOME:R-RNO-392851"
] | 9 | [
"8x79",
"8x7a"
] | 2 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR008365"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
813
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
8,
5,
4
] | 4 | true | Family | Prostacyclin (prostanoid IP) receptor | Prostacyclin (prostanoid IP) receptor | Prostglndn_IP_rcpt | 3 |
IPR000371 | 371 | P2Y3 purinoceptor | P2Y3_rcpt | Family | 595 | false | false | There are three distinct families of extracellular receptors for purine and pyrimidine nucleotides [ ], known as P1, P2X and P2Y purinoceptors [ ]. These receptors induce a wide variety of biological effects and are involved in many different cellular functions [ , , ]. P2X receptors are ligand-gated ion channels, wher... | [
"GO:0045028",
"GO:0007200",
"GO:0016020"
] | [
"G protein-coupled purinergic nucleotide receptor activity",
"phospholipase C-activating G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01065"
] | [
"P2Y3PRNOCPTR"
] | [
595
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-GGA-416476",
"R-GGA-417957"
] | [
"REACTOME:R-GGA-416476",
"REACTOME:R-GGA-417957"
] | 2 | [] | 0 | [
"PUB00002928",
"PUB00003886",
"PUB00007054",
"PUB00028347",
"PUB00033968",
"PUB00066193",
"PUB00066194",
"PUB00066195",
"PUB00066196",
"PUB00066197",
"PUB00066198",
"PUB00066203",
"PUB00066204",
"PUB00066205",
"PUB00066206",
"PUB00066207",
"PUB00066208",
"PUB00066209",
"PUB000662... | [
"7592819",
"8700132",
"12270951",
"8872457",
"11111826",
"10629443",
"20471713",
"11099464",
"19921464",
"11734617",
"16257449",
"9364468",
"7724657",
"16968944",
"8508924",
"19386608",
"8921391",
"8702478",
"12724320",
"18404483",
"9755289",
"11794691",
"16914897",
"16... | [
"Molecular cloning and functional analysis of a novel P2 nucleotide receptor.",
"A novel G protein-coupled P2 purinoceptor (P2Y3) activated preferentially by nucleoside diphosphates.",
"Molecular physiology of P2X receptors.",
"Modelling the P2Y purinoceptor using rhodopsin as template.",
"Molecular pharmac... | [
1995,
1996,
2002,
1995,
2000,
2000,
2011,
2000,
2010,
2001,
2006,
1997,
1994,
2006,
1993,
2009,
1996,
1996,
2003,
2006,
1998,
2001,
2006,
2006,
2000,
1998,
1996
] | 27 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
595
] | 1 | [
"Danio rerio",
"Homo sapiens"
] | [
1,
1
] | 2 | true | Family | P2Y3 purinoceptor | P2Y3 purinoceptor | P2Y3_rcpt | 7 |
IPR000375 | 375 | Dynamin stalk domain | Dynamin_stalk | Domain | 39,930 | false | false | Dynamin superfamily members are large GTPases, conserved throughout evolution, that function primarily as mechanochemical enzymes involved in membrane scission events [ , ]. Dynamin itself is a microtubule-associated force-producing protein of approximately 100 kDa, critical for endocytic membrane fission and membrane ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01031"
] | [
"Dynamin_M"
] | [
39930
] | 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-1169408",
"R-BTA-166016",
"R-BTA-190873",
"R-BTA-196025",
"R-BTA-2132295",
"R-BTA-437239",
"R-BTA-75153",
"R-BTA-8856828",
"R-CEL-190873",
"R-CEL-196025",
"R-CEL-3928665",
"R-CEL-432720",
"R-CEL-432722",
"R-CEL-437239",
"R-CEL-75153",
"R-CEL-8856828",
"R-CFA-1169408",
"R-DDI... | [
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-437239",
"REACTOME:R-BTA-75153",
"REACTOME:R-BTA-8856828",
"REACTOME:R-CEL-190873",
"REACTOME:R-CEL-196025",
"REACTOME:R-CEL-3928665",
"REACTOME:R-CEL-... | 74 | [
"1jwy",
"1jx2",
"2aka",
"2x2e",
"2x2f",
"3l43",
"3ljb",
"3snh",
"3szr",
"3t34",
"3t35",
"3w6n",
"3w6o",
"3w6p",
"3zvr",
"3zyc",
"3zys",
"4bej",
"4h1u",
"4h1v",
"4p4s",
"4p4t",
"4p4u",
"4uud",
"4uuk",
"4whj",
"4x0r",
"5a3f",
"5d3q",
"5gtm",
"5uot",
"5wp9"... | 58 | [
"PUB00052601",
"PUB00052602",
"PUB00052603",
"PUB00052604",
"PUB00072539"
] | [
"15004222",
"16403025",
"16938290",
"17533148",
"22233676"
] | [
"An assembly-incompetent mutant establishes a requirement for dynamin self-assembly in clathrin-mediated endocytosis in vivo.",
"Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin.",
"Domain requirements for an endocytosis-independent, isoform-specific function o... | [
2004,
2006,
2006,
2007,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
39908,
16,
6
] | 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... | [
57,
3,
86,
12,
48,
33,
8,
38,
48,
2,
3,
94
] | 12 | true | Domain | Dynamin stalk domain | Dynamin stalk domain | Dynamin_stalk | 4 |
IPR000376 | 376 | Prostaglandin D receptor | Pglndn_D_rcpt | Family | 261 | false | false | DP receptors have a limited distribution. They mediate relaxation in vascular, gastrointestinal and uterine smooth muscle in human and some other species; they inhibit platelet activation, and modify release of hypothalamic and pituitary hormones. The receptors activate adenylyl cyclase through G proteins. Prostanoids ... | [
"GO:0004956",
"GO:0007186",
"GO:0016020"
] | [
"prostaglandin D receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00854"
] | [
"PRSTNOIDDPR"
] | [
261
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"338",
"R-HSA-391908",
"R-HSA-418555",
"R-MMU-391908",
"R-MMU-418555",
"R-RNO-391908"
] | [
"IUPHAR:338",
"REACTOME:R-HSA-391908",
"REACTOME:R-HSA-418555",
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-418555",
"REACTOME:R-RNO-391908"
] | 6 | [
"8zvz",
"8zw0",
"9au0",
"9e9s",
"9ee5",
"9ei5",
"9ekh",
"9uwd"
] | 8 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR008365"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
261
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
4
] | 3 | true | Family | Prostaglandin D receptor | Prostaglandin D receptor | Pglndn_D_rcpt | 8 |
IPR000377 | 377 | 5-Hydroxytryptamine 2C receptor | 5HT2C_rcpt | Family | 463 | false | false | 5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n... | [
"GO:0004993",
"GO:0007186",
"GO:0007626",
"GO:0007631",
"GO:0005886"
] | [
"G protein-coupled serotonin receptor activity",
"G protein-coupled receptor signaling pathway",
"locomotory behavior",
"feeding behavior",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00517"
] | [
"5HT2CRECEPTR"
] | [
463
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"8",
"R-HSA-390666",
"R-HSA-416476",
"R-MMU-390666",
"R-MMU-416476",
"R-RNO-390666",
"R-RNO-416476"
] | [
"IUPHAR:8",
"REACTOME:R-HSA-390666",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-390666",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-390666",
"REACTOME:R-RNO-416476"
] | 7 | [
"8dpf",
"8dpg",
"8dph",
"8dpi"
] | 4 | [
"PUB00064376",
"PUB00064437",
"PUB00064543",
"PUB00064544",
"PUB00064545",
"PUB00064546",
"PUB00064547",
"PUB00064548",
"PUB00064549",
"PUB00064550",
"PUB00064551",
"PUB00064552",
"PUB00064553",
"PUB00064554",
"PUB00064555",
"PUB00064558",
"PUB00066704"
] | [
"18476671",
"16803859",
"8028479",
"9776391",
"10223282",
"10503938",
"15668911",
"7912626",
"9694950",
"10219979",
"11489456",
"11228755",
"9151932",
"11750789",
"8840350",
"9106912",
"11989819"
] | [
"Serotonin receptors.",
"Functional selectivity and classical concepts of quantitative pharmacology.",
"Distribution of the serotonin 5-HT2 receptor family mRNAs: comparison between 5-HT2A and 5-HT2C receptors.",
"Serotonin (5-HT)2C receptors tonically inhibit dopamine (DA) and noradrenaline (NA), but not 5-H... | [
2008,
2007,
1994,
1998,
1999,
1999,
2005,
1994,
1998,
1999,
2001,
1999,
1997,
2001,
1996,
1997,
2002
] | 17 | [
"IPR002231"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
463
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
6,
6
] | 3 | true | Family | 5-Hydroxytryptamine 2C receptor | 5-Hydroxytryptamine 2C receptor | 5HT2C_rcpt | 5 |
IPR000378 | 378 | Opsin red/green sensitive | Opsin_red/grn | Family | 2,401 | false | false | Opsins are the photoreceptors of animal retinas [ ]. Vertebrate rhodopsin is found in rod cells and mediates scotopic vision; red, green and blue opsins are found in cone cells and mediate photopic vision. Red-sensitive opsin has an absorption maximum at 560nm; its deficiency results in protanopia colour blindness [ ].... | [
"GO:0007186",
"GO:0007601",
"GO:0007602",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"visual perception",
"phototransduction",
"membrane"
] | [
"biological_process",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00575"
] | [
"OPSINREDGRN"
] | [
2401
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-2187335",
"R-BTA-418594",
"R-BTA-419771",
"R-CFA-2187335",
"R-CFA-418594",
"R-CFA-419771",
"R-DRE-2187335",
"R-DRE-418594",
"R-DRE-419771",
"R-HSA-2187335",
"R-HSA-418594",
"R-HSA-419771",
"R-HSA-9918436",
"R-HSA-9918450",
"R-MMU-2187335",
"R-MMU-418594",
"R-MMU-419771",
"R-... | [
"REACTOME:R-BTA-2187335",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-419771",
"REACTOME:R-CFA-2187335",
"REACTOME:R-CFA-418594",
"REACTOME:R-CFA-419771",
"REACTOME:R-DRE-2187335",
"REACTOME:R-DRE-418594",
"REACTOME:R-DRE-419771",
"REACTOME:R-HSA-2187335",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA... | 20 | [
"8iu2",
"8y01"
] | 2 | [
"PUB00077993",
"PUB00077994",
"PUB00077995",
"PUB00077996"
] | [
"10349976",
"1302020",
"8185948",
"9860863"
] | [
"Cloning and characterization of six zebrafish photoreceptor opsin cDNAs and immunolocalization of their corresponding proteins.",
"Defective colour vision associated with a missense mutation in the human green visual pigment gene.",
"Molecular determinants of human red/green color discrimination.",
"Mutagene... | [
1999,
1992,
1994,
1998
] | 4 | [
"IPR001760"
] | [] | 1 | 0 | 1 | [
"Bilateria",
"bird metagenome"
] | [
2399,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
11,
4,
3
] | 4 | true | Family | Opsin red/green sensitive | Opsin red/green sensitive | Opsin_red/grn | 2 |
IPR000380 | 380 | DNA topoisomerase, type IA | Topo_IA | Family | 63,254 | false | false | This entry describes the type IA topoisomerases, which are highly conserved enzymes that are structurally distinct from type IB enzymes. The structures of both topoisomerases I and III have been elucidated, and consist of four domains that together form a toroidal molecule with a central hole that is large enough to ac... | [
"GO:0003677",
"GO:0003917",
"GO:0006265"
] | [
"DNA binding",
"DNA topoisomerase type I (single strand cut, ATP-independent) activity",
"DNA topological change"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PANTHER",
"PANTHER"
] | [
"PTHR11390",
"PTHR42785"
] | [
"",
""
] | [
32173,
31081
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.6.2.1",
"PDOC00333",
"R-CEL-5693607",
"R-HSA-5685938",
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"R-HSA-5693579",
"R-HSA-5693607",
"R-HSA-5693616",
"R-HSA-6804756",
"R-HSA-69473",
"R-HSA-912446",
"R-HSA-9701192",
"R-HSA-9704331",
"R-HSA-9704646",
"R-HSA-9709570",
"R-HSA... | [
"EC:5.6.2.1",
"PROSITEDOC:PDOC00333",
"REACTOME:R-CEL-5693607",
"REACTOME:R-HSA-5685938",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693579",
"REACTOME:R-HSA-5693607",
"REACTOME:R-HSA-5693616",
"REACTOME:R-HSA-6804756",
"REACTOME:R-HSA-69473"... | 27 | [
"1cy0",
"1cy1",
"1cy2",
"1cy4",
"1cy6",
"1cy7",
"1cy8",
"1cy9",
"1cyy",
"1d6m",
"1ecl",
"1i7d",
"1mw8",
"1mw9",
"2gai",
"2gaj",
"2o19",
"2o54",
"2o59",
"2o5c",
"2o5e",
"3pwt",
"3px7",
"4cgy",
"4cht",
"4rul",
"5d5h",
"5gvc",
"5gve",
"5uj1",
"5ujy",
"6cq2"... | 55 | [
"PUB00005230",
"PUB00005437",
"PUB00016842",
"PUB00020793",
"PUB00020794",
"PUB00020798",
"PUB00081702",
"PUB00081703",
"PUB00081704",
"PUB00081705"
] | [
"9488644",
"7770916",
"11395412",
"12596227",
"12042765",
"11239459",
"21087076",
"20644584",
"17722649",
"17293019"
] | [
"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA.",
"The mechanisms of DNA topoisomerases.",
"DNA topoisomerases: structure, function, and mechanism.",
"Phylogenomics of type II DNA topoisomerases.",
"Cellular roles of DNA topoisomerases: a molecular perspective.",... | [
1998,
1995,
2001,
2003,
2002,
2001,
2010,
2010,
2007,
2007
] | 10 | [] | [
"IPR005738",
"IPR028612"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
965,
50287,
10642,
60,
10,
1290
] | 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",... | [
18,
4,
3,
6,
3,
21,
19,
1,
12,
3,
1,
1,
78
] | 13 | true | Family | DNA topoisomerase, type IA | DNA topoisomerase, type IA | Topo_IA | 1 |
IPR000381 | 381 | Inhibin, beta B subunit, C-terminal | INHBB_C | Domain | 1,018 | false | false | Inhibins and activins are glycoproteins, secreted by the gonads, that belong to the transforming growth factor beta family [ ]. They participate in differentiation and growth of diverse cell types. Inhibin inhibits secretion of follicle-stimulating hormone by the pituitary [ ]. Inhibin has two isoforms, A and B, with t... | [] | [] | [] | 0 | [
"CDD"
] | [
"cd19405"
] | [
"TGF_beta_INHBB"
] | [
1018
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1502540",
"R-HSA-209822",
"R-HSA-2473224",
"R-MMU-1502540",
"R-MMU-209822",
"R-MMU-2473224",
"R-RNO-1502540",
"R-RNO-209822",
"R-RNO-2473224"
] | [
"REACTOME:R-HSA-1502540",
"REACTOME:R-HSA-209822",
"REACTOME:R-HSA-2473224",
"REACTOME:R-MMU-1502540",
"REACTOME:R-MMU-209822",
"REACTOME:R-MMU-2473224",
"REACTOME:R-RNO-1502540",
"REACTOME:R-RNO-209822",
"REACTOME:R-RNO-2473224"
] | 9 | [] | 0 | [
"PUB00001456",
"PUB00003992",
"PUB00006558",
"PUB00006578"
] | [
"7813465",
"2417121",
"9207855",
"9989858"
] | [
"Genomic cloning and sequence analyses of the bovine alpha-, beta A- and beta B-inhibin/activin genes. Identification of transcription factor AP-2-binding sites in the 5'-flanking regions by DNase I footprinting.",
"Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homol... | [
1994,
1985,
1997,
1998
] | 4 | [
"IPR001839"
] | [] | 1 | 0 | 1 | [
"Gnathostomata",
"bird metagenome"
] | [
1017,
1
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
1,
2
] | 4 | true | Domain | Inhibin, beta B subunit, C-terminal | Inhibin, beta B subunit, C-terminal | INHBB_C | 2 |
IPR000382 | 382 | Peptidase S39B, luteovirus | Peptidase_S39B_luteovirus | Domain | 1,551 | false | false | ORF2 of Potato leafroll virus (PLrV) encodes a polyprotein which is translated following a -1 frameshift. The polyprotein has a putative linear arrangement of membrane achor-VPg-peptidase-polmerase domains. The serine peptidase domain which is found in this group of sequences belongs to MEROPS peptidase family S39 (cla... | [
"GO:0004252",
"GO:0016032",
"GO:0016020"
] | [
"serine-type endopeptidase activity",
"viral process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF02122",
"PS51868"
] | [
"Peptidase_S39",
"PEPTIDASE_S39"
] | [
1455,
1399
] | 2 | [
"EC",
"METACYC"
] | [
"3.4.21.-",
"PWY-7884"
] | [
"EC:3.4.21.-",
"METACYC:PWY-7884"
] | 2 | [
"1zyo",
"6fez",
"6ff0",
"6m78",
"7yzv"
] | 5 | [
"PUB00001567",
"PUB00003126",
"PUB00004354",
"PUB00011866"
] | [
"2466700",
"2732710",
"3194229",
"9714253"
] | [
"Nucleotide sequence and organization of potato leafroll virus genomic RNA.",
"Nucleotide sequence of potato leafroll luteovirus RNA.",
"Nucleotide sequence of beet western yellows virus RNA.",
"Sequencing, genomic localization and initial characterization of the VPg of pea enation mosaic enamovirus."
] | [
1989,
1989,
1988,
1998
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Oliverpabstia intestinalis",
"Viruses"
] | [
3,
1,
1547
] | 3 | [] | [] | 0 | true | Domain | Peptidase S39B, luteovirus | Peptidase S39B, luteovirus | Peptidase_S39B_luteovirus | 8 |
IPR000385 | 385 | MoaA/NifB/PqqE, iron-sulphur binding, conserved site | MoaA_NifB_PqqE_Fe-S-bd_CS | Conserved_site | 33,862 | false | false | A number of proteins involved in the biosynthesis of metallo cofactors have been shown [ , ] to be evolutionary related. These include: Bacterial and archebacterial protein moaA, which is involved in the biosynthesis of the molybdenum cofactor (molybdopterin; MPT). Arabidopsis thaliana (Mouse-ear cress) cnx2, a protein... | [
"GO:0003824",
"GO:0046872",
"GO:0051539"
] | [
"catalytic activity",
"metal ion binding",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PROSITE"
] | [
"PS01305"
] | [
"MOAA_NIFB_PQQE"
] | [
33862
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.99.22",
"PWY-6823",
"PDOC01009",
"R-BTA-947581",
"R-DDI-947581",
"R-DME-947581",
"R-HSA-947581",
"R-MMU-947581"
] | [
"EC:4.1.99.22",
"METACYC:PWY-6823",
"PROSITEDOC:PDOC01009",
"REACTOME:R-BTA-947581",
"REACTOME:R-DDI-947581",
"REACTOME:R-DME-947581",
"REACTOME:R-HSA-947581",
"REACTOME:R-MMU-947581"
] | 8 | [
"1tv7",
"1tv8",
"2fb2",
"2fb3",
"5wgg",
"5why",
"6c8v",
"6efn",
"6y1x",
"8wm2"
] | 10 | [
"PUB00000168",
"PUB00002946",
"PUB00015124"
] | [
"8588735",
"7890743",
"15317939"
] | [
"A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein.",
"Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants.",
... | [
1995,
1995,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
1290,
28055,
34,
3987,
496
] | 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,
3,
2,
1,
1,
4,
4,
1,
10,
4,
3
] | 11 | true | Conserved_site | MoaA/NifB/PqqE, iron-sulphur binding, conserved site | MoaA/NifB/PqqE, iron-sulphur binding, conserved site | MoaA_NifB_PqqE_Fe-S-bd_CS | 3 |
IPR000386 | 386 | Haemagglutinin, influenzavirus B | Hemagglutn_influenz_B | Family | 15,042 | false | false | Haemagglutinin (HA) is one of two main surface fusion glycoproteins embedded in the envelope of influenza viruses, the other being neuraminidase (NA). There are sixteen known HA subtypes (H1-H16) and nine NA subtypes (N1-N9), which together are used to classify influenza viruses (e.g. H5N1). The antigenic variations in... | [
"GO:0046789",
"GO:0019064",
"GO:0019031"
] | [
"host cell surface receptor binding",
"fusion of virus membrane with host plasma membrane",
"viral envelope"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00331"
] | [
"HEMAGGLUTN2"
] | [
15042
] | 1 | [] | [] | [] | 0 | [
"1eo8",
"1hgd",
"1hge",
"1hgf",
"1hgg",
"1hgh",
"1hgi",
"1hgj",
"1htm",
"1jsd",
"1jsh",
"1jsi",
"1jsm",
"1jsn",
"1jso",
"1ken",
"1mql",
"1mqm",
"1mqn",
"1qfu",
"1qu1",
"1rd8",
"1ru7",
"1ruy",
"1ruz",
"1rv0",
"1rvt",
"1rvx",
"1rvz",
"1ti8",
"2fk0",
"2hmg"... | 561 | [
"PUB00033162",
"PUB00033164",
"PUB00033165"
] | [
"16543414",
"15475582",
"16178512"
] | [
"Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus.",
"Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers.",
"The factors of virulence of influenza a virus."
] | [
2006,
2005,
2005
] | 3 | [
"IPR001364"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Orthomyxoviridae"
] | [
7,
15035
] | 2 | [] | [] | 0 | true | Family | Haemagglutinin, influenzavirus B | Haemagglutinin, influenzavirus B | Hemagglutn_influenz_B | 5 |
IPR000387 | 387 | Tyrosine-specific protein phosphatases domain | Tyr_Pase_dom | Domain | 216,356 | false | false | Tyrosine specific protein phosphatases (PTPases) contain two conserved cysteines, the second one has been shown to be absolutely required for activity. This entry represents the PTPase domain that centre on the active site cysteine. A number of conserved residues in its immediate vicinity have also been shown to be imp... | [
"GO:0016311"
] | [
"dephosphorylation"
] | [
"biological_process"
] | 1 | [
"PROFILE"
] | [
"PS50056"
] | [
"TYR_PHOSPHATASE_2"
] | [
216356
] | 1 | [
"EC",
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.1.3",
"3.1.3.48",
"PDOC00323",
"R-BTA-112409",
"R-BTA-1483248",
"R-BTA-1660499",
"R-BTA-1660516",
"R-BTA-1660517",
"R-BTA-202670",
"R-BTA-388844",
"R-BTA-5675221",
"R-BTA-77387",
"R-BTA-8849932",
"R-CEL-112409",
"R-CEL-1660499",
"R-CEL-182971",
"R-CEL-1855204",
"R-CEL-199418",
... | [
"EC:3.1.3",
"EC:3.1.3.48",
"PROSITEDOC:PDOC00323",
"REACTOME:R-BTA-112409",
"REACTOME:R-BTA-1483248",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-1660516",
"REACTOME:R-BTA-1660517",
"REACTOME:R-BTA-202670",
"REACTOME:R-BTA-388844",
"REACTOME:R-BTA-5675221",
"REACTOME:R-BTA-77387",
"REACTOME:R-... | 430 | [
"1a5y",
"1aax",
"1bzc",
"1bzh",
"1bzj",
"1c83",
"1c84",
"1c85",
"1c86",
"1c87",
"1c88",
"1d5r",
"1ecv",
"1een",
"1eeo",
"1fpr",
"1fpz",
"1fq1",
"1g1f",
"1g1g",
"1g1h",
"1g4u",
"1g4w",
"1g7f",
"1g7g",
"1gfy",
"1gwz",
"1i57",
"1i9s",
"1i9t",
"1j4x",
"1jf7"... | 918 | [
"PUB00035793",
"PUB00035794",
"PUB00035795",
"PUB00035796",
"PUB00035797",
"PUB00035798"
] | [
"9818190",
"14625689",
"12678841",
"16672235",
"8948575",
"9646865"
] | [
"Protein tyrosine phosphatases: mechanisms of catalysis and regulation.",
"Receptor and nonreceptor protein tyrosine phosphatases in the nervous system.",
"An overview of the protein tyrosine phosphatase superfamily.",
"The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase dom... | [
1998,
2003,
2003,
2006,
1996,
1998
] | 6 | [] | [
"IPR000242",
"IPR000340",
"IPR020422",
"IPR057023"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
473,
18597,
196111,
638,
537
] | 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",... | [
80,
119,
793,
96,
1,
366,
283,
13,
60,
422,
9,
7,
137
] | 13 | true | Domain | Tyrosine-specific protein phosphatases domain | Tyrosine-specific protein phosphatases domain | Tyr_Pase_dom | 2 |
IPR000388 | 388 | ATP-binding cassette sub-family C member 8/9 | ABCC8/9 | Family | 3,780 | false | false | This entry represents the ATP-binding cassette sub-family C member 8 and 9 (ABCC8/9, also known as sulfonylurea receptors SUR1/2), a subunit of the beta cell potassium channel (KATP) that associates with certain K + channel inward rectifier subunits to form ATP-sensitive K + channels (KATP channels) [ , , , , ]. These ... | [
"GO:0005524",
"GO:0008281",
"GO:0006813",
"GO:0016020"
] | [
"ATP binding",
"sulfonylurea receptor activity",
"potassium ion transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01092"
] | [
"SULFNYLUREAR"
] | [
3780
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1296025",
"R-HSA-382556",
"R-HSA-422356",
"R-HSA-5578775",
"R-HSA-5678420",
"R-HSA-5683177",
"R-MMU-1296025",
"R-MMU-382556",
"R-MMU-5578775",
"R-RNO-1296025",
"R-RNO-382556",
"R-RNO-422356",
"R-RNO-5578775"
] | [
"REACTOME:R-HSA-1296025",
"REACTOME:R-HSA-382556",
"REACTOME:R-HSA-422356",
"REACTOME:R-HSA-5578775",
"REACTOME:R-HSA-5678420",
"REACTOME:R-HSA-5683177",
"REACTOME:R-MMU-1296025",
"REACTOME:R-MMU-382556",
"REACTOME:R-MMU-5578775",
"REACTOME:R-RNO-1296025",
"REACTOME:R-RNO-382556",
"REACTOME:R-... | 13 | [
"5twv",
"5wua",
"5yke",
"5ykf",
"5ykg",
"5yw7",
"5yw8",
"5yw9",
"5ywa",
"5ywb",
"5ywc",
"5ywd",
"6baa",
"6c3o",
"6c3p",
"6jb1",
"6jb3",
"6pz9",
"6pza",
"6pzb",
"6pzc",
"6pzi",
"7mit",
"7mjo",
"7mjp",
"7mjq",
"7s5v",
"7s5x",
"7s5y",
"7s5z",
"7s60",
"7s61"... | 59 | [
"PUB00005203",
"PUB00005208",
"PUB00005551",
"PUB00103846",
"PUB00103847",
"PUB00103848"
] | [
"7716547",
"7502040",
"9683320",
"29286281",
"24814349",
"34815345"
] | [
"Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator of insulin secretion.",
"Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor.",
"Correlating structure and function in ATP-sensitive K+ channels.",
"Molecular structure of human KATP in complex with ATP ... | [
1995,
1995,
1998,
2017,
2015,
2021
] | 6 | [] | [
"IPR000844",
"IPR001475"
] | 0 | 2 | 0 | [
"Eumetazoa"
] | [
3780
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
45,
43,
9,
15
] | 4 | true | Family | ATP-binding cassette sub-family C member 8/9 | ATP-binding cassette sub-family C member 8/9 | ABCC8/9 | 5 |
IPR000389 | 389 | Small hydrophilic plant seed protein | Small_hydrophilic_seed_prot | Family | 1,220 | false | false | This entry contains the plant LEA (late embryogenesis abundant) proteins, which are small hydrophilic plant seed proteins that are structurally related. These proteins contains from 83 to 153 amino acid residues and may play a role [ , ] in equipping the seed for survival, maintaining a minimal level of hydration in th... | [] | [] | [] | 0 | [
"PANTHER"
] | [
"PTHR34671"
] | [
""
] | [
1220
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00355"
] | [
"PROSITEDOC:PDOC00355"
] | 1 | [] | 0 | [
"PUB00003758",
"PUB00015278"
] | [
"8492809",
"12231998"
] | [
"Two different Em-like genes are expressed in Arabidopsis thaliana seeds during maturation.",
"Molecular Responses to Water Deficit."
] | [
1993,
1993
] | 2 | [
"IPR038956"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"Pseudomonadota"
] | [
1216,
4
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
6,
6
] | 3 | true | Family | Small hydrophilic plant seed protein | Small hydrophilic plant seed protein | Small_hydrophilic_seed_prot | 6 |
IPR000390 | 390 | Small drug/metabolite transporter protein family | Small_drug/metabolite_transptr | Family | 51,403 | false | false | Members of this family which have been characterised, belong to the small multidrug/metabolite transporter family and are integral membrane proteins. They confer resistance to a wide range of toxic compounds by removing them for the cells. The efflux is coupled to an influx of protons. It includes 4-amino-4-deoxy-L-ara... | [
"GO:0022857",
"GO:0016020"
] | [
"transmembrane transporter activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PANTHER"
] | [
"PTHR30561"
] | [
""
] | [
51403
] | 1 | [
"REACTOME"
] | [
"R-HSA-9913143"
] | [
"REACTOME:R-HSA-9913143"
] | 1 | [
"2i68",
"3b5d",
"3b61",
"3b62",
"6wk5",
"6wk8",
"6wk9",
"7jk8",
"7mgx",
"7mh6",
"7sfq",
"7ssu",
"7sv9",
"7svx",
"7szt",
"7t00",
"8tgy",
"8uoz",
"8uwu",
"8vxu"
] | 20 | [
"PUB00009428",
"PUB00009429",
"PUB00053903",
"PUB00095576",
"PUB00095577",
"PUB00098572"
] | [
"1320256",
"1936950",
"17928292",
"29114048",
"30287687",
"33420032"
] | [
"Cloning and characterization of the mvrC gene of Escherichia coli K-12 which confers resistance against methyl viologen toxicity.",
"Nucleotide sequence of the ethidium efflux gene from Escherichia coli.",
"An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli.... | [
1992,
1991,
2007,
2017,
2018,
2021
] | 6 | [] | [
"IPR022832",
"IPR022883",
"IPR045324"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
443,
50570,
100,
19,
5,
266
] | 6 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Family | Small drug/metabolite transporter protein family | Small drug/metabolite transporter protein family | Small_drug/metabolite_transptr | 9 |
IPR000391 | 391 | Ring-hydroxylating dioxygenase beta subunit | Rng_hydr_dOase-bsu | Family | 8,621 | false | false | This entry represents the ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase. The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonhaem iron-containing dioxygen... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER",
"CDD"
] | [
"PF00866",
"PTHR41534",
"cd00667"
] | [
"Ring_hydroxyl_B",
"",
"ring_hydroxylating_dioxygenases_beta"
] | [
8245,
7430,
7143
] | 3 | [
"EC",
"GP",
"GP"
] | [
"1.14.12",
"GenProp1287",
"GenProp1458"
] | [
"EC:1.14.12",
"GP:GenProp1287",
"GP:GenProp1458"
] | 3 | [
"1eg9",
"1ndo",
"1o7g",
"1o7h",
"1o7m",
"1o7n",
"1o7p",
"1o7w",
"1uli",
"1ulj",
"1uuv",
"1uuw",
"1wql",
"2b1x",
"2b24",
"2bmo",
"2bmq",
"2bmr",
"2ckf",
"2gbw",
"2gbx",
"2hmj",
"2hmk",
"2hml",
"2hmm",
"2hmn",
"2hmo",
"2xr8",
"2xrx",
"2xsh",
"2xso",
"2yfi"... | 59 | [
"PUB00000122",
"PUB00005305"
] | [
"1444257",
"9634695"
] | [
"The electron-transport proteins of hydroxylating bacterial dioxygenases.",
"Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase."
] | [
1992,
1998
] | 2 | [] | [
"IPR017640",
"IPR017641",
"IPR023712"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"plasmids",
"unclassified sequences"
] | [
71,
8464,
27,
2,
57
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ring-hydroxylating dioxygenase beta subunit | Ring-hydroxylating dioxygenase beta subunit | Rng_hydr_dOase-bsu | 3 |
IPR000392 | 392 | NifH/frxC family | NifH/frxC | Family | 24,882 | false | false | This entry includes the bacterial nitrogenase iron protein NifH [ ], chloroplast encoded chlL (or frxC) [ ], and archaeal Ni-sirohydrochlorin a,c-diamide reductive cyclase complex component CfbC [ ]. Nitrogenase ( ) is responsible for biological nitrogen fixation. Nitrogenase is an oligomeric complex which consists of ... | [
"GO:0005524",
"GO:0016491"
] | [
"ATP binding",
"oxidoreductase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PIRSF",
"PROFILE",
"PANTHER"
] | [
"PF00142",
"PIRSF000363",
"PS51026",
"PTHR42864"
] | [
"Fer4_NifH",
"Nitrogenase_iron",
"NIFH_FRXC_3",
""
] | [
24698,
6892,
24719,
24627
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00580"
] | [
"PROSITEDOC:PDOC00580"
] | 1 | [
"1cp2",
"1de0",
"1fp6",
"1g1m",
"1g20",
"1g21",
"1g5p",
"1m1y",
"1m34",
"1n2c",
"1nip",
"1rw4",
"1xcp",
"1xd8",
"1xd9",
"1xdb",
"2afh",
"2afi",
"2c8v",
"2nip",
"2ynm",
"3fwy",
"4wza",
"4wzb",
"6n4j",
"6n4k",
"6n4l",
"6n4m",
"6nzj",
"6o0b",
"6q93",
"6uyk"... | 71 | [
"PUB00002054",
"PUB00004532",
"PUB00005343",
"PUB00046139",
"PUB00087319"
] | [
"6327620",
"2491672",
"2672439",
"16889380",
"28225763"
] | [
"Rhizobium japonicum nitrogenase Fe protein gene (nifH).",
"Identification of a novel nifH-like (frxC) protein in chloroplasts of the liverwort Marchantia polymorpha.",
"Nitrogenases without molybdenum.",
"Characterization of three genes encoding the subunits of light-independent protochlorophyllide reductase... | [
1984,
1989,
1989,
2006,
2017
] | 5 | [] | [
"IPR005971",
"IPR005977",
"IPR010246"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
481,
18191,
1541,
4669
] | 4 | [] | [] | 0 | true | Family | NifH/frxC family | NifH/frxC family | NifH/frxC | 1 |
IPR000393 | 393 | Neuropeptide Y5 receptor | NPY5_rcpt | Family | 585 | false | false | Neuropeptide Y (NPY) acts as a neurotransmitter in the brain and in the autonomic nervous system. In the brain it is thought to have several functions, including increasing food intake and storage of energy as fat [ , , , ], facilitation of learning and memory via the modulation of hippocampal activity [ , , ], inhibit... | [
"GO:0004983",
"GO:0007186",
"GO:0016020"
] | [
"neuropeptide Y receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"CDD"
] | [
"PR01016",
"cd15398"
] | [
"NRPEPTIDEY5R",
"7tmA_NPY5R"
] | [
583,
362
] | 2 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"308",
"R-CFA-375276",
"R-CFA-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594",
"R-SSC-375276",
"R-SSC-418594"
] | [
"IUPHAR:308",
"REACTOME:R-CFA-375276",
"REACTOME:R-CFA-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594",
"REACTOME:R-SSC-375276",
"REACTOME:R-SSC-418594"
] | 11 | [] | 0 | [
"PUB00004236",
"PUB00063739",
"PUB00063740",
"PUB00063741",
"PUB00063742",
"PUB00063743",
"PUB00063744",
"PUB00063745",
"PUB00063746",
"PUB00063747",
"PUB00063748",
"PUB00063749",
"PUB00063750",
"PUB00063751",
"PUB00063752",
"PUB00063753",
"PUB00063754",
"PUB00063755",
"PUB000637... | [
"8700207",
"6549409",
"16874931",
"6547387",
"6549039",
"2821236",
"8395947",
"16190896",
"7529442",
"7644568",
"15337373",
"8685245",
"8369959",
"11287113",
"7629398",
"6133408",
"3855566",
"12678499",
"17222466",
"8013354",
"9833945",
"9389418",
"9446690",
"2453065",
... | [
"A receptor subtype involved in neuropeptide-Y-induced food intake.",
"Neuropeptide Y: a potent inducer of consummatory behavior in rats.",
"Neuropeptide Y in normal eating and in genetic and dietary-induced obesity.",
"Neuropeptide Y and human pancreatic polypeptide stimulate feeding behavior in rats.",
"N... | [
1996,
1984,
2006,
1984,
1984,
1987,
1993,
2005,
1994,
1995,
2004,
1996,
1993,
2001,
1995,
1982,
1985,
2003,
2007,
1994,
1998,
1997,
1998,
1988,
1991,
1995,
2003,
2007,
1998,
2004,
2007,
2007,
2007,
2006,
2007,
2006,
2007,
2008,
1996,
1996... | 46 | [
"IPR000611"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
585
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
3
] | 3 | true | Family | Neuropeptide Y5 receptor | Neuropeptide Y5 receptor | NPY5_rcpt | 8 |
IPR000394 | 394 | RNA polymerase sigma factor 54 | RNA_pol_sigma_54 | Family | 17,988 | false | false | Sigma factors [ ] are bacterial transcription initiation factors that promote the attachment of the core RNA polymerase to specific initiation sites and are then released. They alter the specificity of promoter recognition. Most bacteria express a multiplicity of sigma factors. Two of these factors, sigma-70 (gene rpoD... | [
"GO:0001216",
"GO:0016987"
] | [
"DNA-binding transcription activator activity",
"sigma factor activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROSITE",
"PROSITE",
"PANTHER",
"NCBIFAM"
] | [
"PF00309",
"PIRSF000774",
"PR00045",
"PS00717",
"PS00718",
"PTHR32248",
"TIGR02395"
] | [
"Sigma54_AID",
"RpoN",
"SIGMA54FCT",
"SIGMA54_1",
"SIGMA54_2",
"",
"rpoN_sigma"
] | [
16740,
16719,
16919,
12389,
16040,
17563,
16455
] | 7 | [
"GP",
"PROSITEDOC"
] | [
"GenProp0634",
"PDOC00593"
] | [
"GP:GenProp0634",
"PROSITEDOC:PDOC00593"
] | 2 | [
"2ahq",
"2k9m",
"2mt3",
"2o8k",
"2o9l",
"5nsr",
"5nss",
"5nwt",
"5ui5",
"5ui8",
"6gfw",
"6gh5",
"6gh6",
"7qv9",
"7qwp",
"7qxi",
"8f1i",
"8f1j",
"8f1k",
"8re4",
"8rea",
"8reb",
"8rec",
"8red",
"8ree",
"9mse",
"9msf",
"9msg",
"9msh",
"9msj",
"9q90",
"9q91"... | 39 | [
"PUB00000061",
"PUB00001740",
"PUB00003853"
] | [
"3052291",
"2517036",
"7934866"
] | [
"Structure and function of bacterial sigma factors.",
"The -24/-12 promoter comes of age.",
"In a class of its own--the RNA polymerase sigma factor sigma 54 (sigma N)."
] | [
1988,
1989,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2,
17577,
46,
363
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | RNA polymerase sigma factor 54 | RNA polymerase sigma factor 54 | RNA_pol_sigma_54 | 9 |
IPR000395 | 395 | Botulinum/Tetanus toxin, catalytic chain | Bot/tetX_LC | Domain | 315 | false | false | The Clostridium neurotoxin family is composed of tetanus neurotoxin (TeNT) and seven serotypes of botulinum neurotoxin (BoNT). It also includes the Botulinum non-toxic non-hemagglutinin (NTNHA) component, which forms a binary complex with BoNT to protect it from gastrointestinal degradation [ ]. These toxins act as inh... | [
"GO:0004222",
"GO:0008270",
"GO:0006508"
] | [
"metalloendopeptidase activity",
"zinc ion binding",
"proteolysis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF01742",
"PR00760"
] | [
"Peptidase_M27",
"BONTOXILYSIN"
] | [
310,
313
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24.69",
"R-HSA-5250955",
"R-HSA-5250958",
"R-HSA-5250968",
"R-HSA-5250971",
"R-HSA-5250981",
"R-HSA-5250982",
"R-HSA-5250989",
"R-HSA-5250992"
] | [
"EC:3.4.24.69",
"REACTOME:R-HSA-5250955",
"REACTOME:R-HSA-5250958",
"REACTOME:R-HSA-5250968",
"REACTOME:R-HSA-5250971",
"REACTOME:R-HSA-5250981",
"REACTOME:R-HSA-5250982",
"REACTOME:R-HSA-5250989",
"REACTOME:R-HSA-5250992"
] | 9 | [
"1e1h",
"1epw",
"1f31",
"1f82",
"1g9a",
"1g9b",
"1g9c",
"1g9d",
"1i1e",
"1s0b",
"1s0c",
"1s0d",
"1s0e",
"1s0f",
"1s0g",
"1t3a",
"1t3c",
"1xtf",
"1xtg",
"1yvg",
"1z7h",
"1zb7",
"1zkw",
"1zkx",
"1zl5",
"1zl6",
"1zn3",
"2a8a",
"2a97",
"2etf",
"2fpq",
"2g7k"... | 154 | [
"PUB00003782",
"PUB00005402",
"PUB00088575",
"PUB00088576",
"PUB00088602",
"PUB00088603"
] | [
"8897436",
"7901925",
"1328520",
"23435179",
"25895970",
"26363288"
] | [
"Botulinum neurotoxins: mechanism of action and therapeutic applications.",
"Tetanus and botulism neurotoxins: a new group of zinc proteases.",
"Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation.",
"Bot... | [
1996,
1993,
1992,
2013,
2015,
2015
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified Caudoviricetes"
] | [
306,
9
] | 2 | [] | [] | 0 | true | Domain | Botulinum/Tetanus toxin, catalytic chain | Botulinum/Tetanus toxin, catalytic chain | Bot/tetX_LC | 4 |
IPR000396 | 396 | Cyclic-AMP phosphodiesterase, class-II | Pdiesterase2 | Family | 3,269 | false | false | Cyclic-AMP phosphodiesterase ( ) (PDE) catalyses the hydrolysis of cAMP to the corresponding nucleoside 5' monophosphate. On the basis of sequence similarity, most PDEs can be grouped together [ ], but some enzymes lie apart from the main family and represent a second distinct class [ ] that includes PDEs from Dictyost... | [
"GO:0004115",
"GO:0006198"
] | [
"3',5'-cyclic-AMP phosphodiesterase activity",
"cAMP catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER",
"CDD"
] | [
"PF02112",
"PIRSF000962",
"PR00388",
"PTHR28283",
"cd07735"
] | [
"PDEase_II",
"Cyc_nuc_PDEase",
"PDIESTERASE2",
"",
"class_II_PDE_MBL-fold"
] | [
2417,
978,
3143,
2883,
3099
] | 5 | [
"EC",
"PROSITEDOC"
] | [
"3.1.4.17",
"PDOC00530"
] | [
"EC:3.1.4.17",
"PROSITEDOC:PDOC00530"
] | 2 | [
"4ojv",
"4ojx"
] | 2 | [
"PUB00003649",
"PUB00005554"
] | [
"2824992",
"2159198"
] | [
"Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.",
"Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors."
] | [
1987,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1634,
1598,
37
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | Cyclic-AMP phosphodiesterase, class-II | Cyclic-AMP phosphodiesterase, class-II | Pdiesterase2 | 3 |
IPR000397 | 397 | Heat shock protein Hsp33 | Heat_shock_Hsp33 | Family | 16,120 | false | false | Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H 2 O 2 cau... | [
"GO:0051082",
"GO:0006457",
"GO:0005737"
] | [
"unfolded protein binding",
"protein folding",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"MF_00117",
"PF01430",
"PIRSF005261",
"PTHR30111",
"cd00498"
] | [
"HslO",
"HSP33",
"Heat_shock_Hsp33",
"",
"Hsp33"
] | [
9634,
16112,
15257,
15938,
15033
] | 5 | [] | [] | [] | 0 | [
"1hw7",
"1i7f",
"1vq0",
"1vzy",
"1xjh",
"3m7m"
] | 6 | [
"PUB00000967",
"PUB00036944",
"PUB00079556",
"PUB00079557"
] | [
"10025400",
"11323724",
"10102262",
"10359689"
] | [
"Chaperone activity with a redox switch.",
"Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity.",
"Bridge over troubled waters: sensing stress by disulfide bond formation.",
"Oxidative stress: Protein folding with a novel redox switch."
] | [
1999,
2001,
1999,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
15614,
370,
136
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Heat shock protein Hsp33 | Heat shock protein Hsp33 | Heat_shock_Hsp33 | 3 |
IPR000398 | 398 | Thymidylate synthase | Thymidylate_synthase | Family | 27,345 | false | false | Thymidylate synthase ( ) [ , ] catalyzes the reductive methylation of dUMP to dTMP with concomitant conversion of 5,10-methylenetetrahydrofolate to dihydrofolate: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP This provides the sole de novo pathway for production of dTMP and is the only enzyme in folate m... | [
"GO:0004799",
"GO:0006231"
] | [
"thymidylate synthase activity",
"dTMP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PRINTS",
"NCBIFAM"
] | [
"MF_00008",
"PR00108",
"TIGR03284"
] | [
"Thymidy_synth_bact",
"THYMDSNTHASE",
"thym_sym"
] | [
24726,
26973,
25915
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.45",
"GenProp1221",
"GenProp1264",
"GenProp1356",
"GenProp1616",
"GenProp1617",
"GenProp1621",
"PWY-3841",
"PWY-7184",
"PWY-7187",
"PWY-7198",
"PWY-7199",
"PWY-7210",
"PDOC00086",
"R-DME-499943",
"R-HSA-499943",
"R-HSA-69205",
"R-MMU-499943",
"R-RNO-499943",
"R-SCE-49994... | [
"EC:2.1.1.45",
"GP:GenProp1221",
"GP:GenProp1264",
"GP:GenProp1356",
"GP:GenProp1616",
"GP:GenProp1617",
"GP:GenProp1621",
"METACYC:PWY-3841",
"METACYC:PWY-7184",
"METACYC:PWY-7187",
"METACYC:PWY-7198",
"METACYC:PWY-7199",
"METACYC:PWY-7210",
"PROSITEDOC:PDOC00086",
"REACTOME:R-DME-49994... | 21 | [
"1aiq",
"1ajm",
"1an5",
"1aob",
"1axw",
"1b02",
"1bdu",
"1bid",
"1bjg",
"1bko",
"1bkp",
"1bo7",
"1bo8",
"1bp0",
"1bp6",
"1bpj",
"1bq1",
"1bq2",
"1bsf",
"1bsp",
"1ci7",
"1ddu",
"1dna",
"1ev5",
"1ev8",
"1evf",
"1evg",
"1f28",
"1f4b",
"1f4c",
"1f4d",
"1f4e"... | 334 | [
"PUB00000031",
"PUB00000137",
"PUB00002591",
"PUB00005100",
"PUB00030463",
"PUB00036705",
"PUB00037605",
"PUB00081476",
"PUB00081477",
"PUB00081481"
] | [
"6996564",
"2117882",
"2243092",
"3099389",
"14555647",
"16615077",
"16511011",
"16162288",
"16178783",
"7574499"
] | [
"On the mechanism of action of folate- and biopterin-requiring enzymes.",
"Cloning and characterization of the thymidylate synthase gene from Lactococcus lactis subsp. lactis.",
"Structural and functional analysis of the human thymidylate synthase gene.",
"Atomic structure of thymidylate synthase: target for ... | [
1980,
1990,
1990,
1987,
2003,
2006,
2005,
2005,
2005,
1995
] | 10 | [
"IPR045097"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
266,
19798,
5605,
1289,
387
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
17,
2,
1,
2,
1,
4,
7,
1,
8,
3,
1,
1,
14
] | 13 | true | Family | Thymidylate synthase | Thymidylate synthase | Thymidylate_synthase | 8 |
IPR000399 | 399 | TPP-binding enzyme, conserved site | TPP-bd_CS | Conserved_site | 65,808 | false | false | A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [ ] that some of these enzymes are structurally related. Enzymes with a TPP-binding domain include: Pyruvate oxidase (POX) ( ). Reaction catalysed: pyruvate + orthophosphate + O(2) + H(2)O = acetyl phosphate + CO(2) +... | [
"GO:0000287",
"GO:0030976"
] | [
"magnesium ion binding",
"thiamine pyrophosphate binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00187"
] | [
"TPP_ENZYMES"
] | [
65808
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00166",
"R-DDI-389599",
"R-DDI-9033241",
"R-SCE-389599",
"R-SCE-9033241"
] | [
"PROSITEDOC:PDOC00166",
"REACTOME:R-DDI-389599",
"REACTOME:R-DDI-9033241",
"REACTOME:R-SCE-389599",
"REACTOME:R-SCE-9033241"
] | 5 | [
"1bfd",
"1jsc",
"1mcz",
"1n0h",
"1ovm",
"1ozf",
"1ozg",
"1ozh",
"1pi3",
"1po7",
"1pow",
"1pox",
"1pvd",
"1pyd",
"1q6z",
"1qpb",
"1t9a",
"1t9b",
"1t9c",
"1t9d",
"1upa",
"1upb",
"1upc",
"1v5e",
"1v5f",
"1v5g",
"1y9d",
"1ybh",
"1yhy",
"1yhz",
"1yi0",
"1yi1"... | 184 | [
"PUB00015103",
"PUB00016247",
"PUB00016248"
] | [
"8604141",
"1639814",
"12590569"
] | [
"Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution.",
"Purification and characterization of indolepyruvate decarboxylase. A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae.",
"Structural and... | [
1996,
1992,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Terrestrivirus sp.",
"unclassified sequences"
] | [
1068,
56898,
6972,
1,
869
] | 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",... | [
20,
1,
2,
1,
4,
2,
2,
3,
3,
7,
5,
3,
4
] | 13 | true | Conserved_site | TPP-binding enzyme, conserved site | TPP-binding enzyme, conserved site | TPP-bd_CS | 2 |
IPR000400 | 400 | Glycoside hydrolase, family 46 | Glyco_hydro_46 | Family | 2,220 | 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:0016977",
"GO:0005975",
"GO:0005576"
] | [
"chitosanase activity",
"carbohydrate metabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PIRSF",
"PROSITE",
"CDD"
] | [
"PF01374",
"PIRSF036551",
"PS60000",
"cd00978"
] | [
"Glyco_hydro_46",
"Chitosanase",
"CHITOSANASE_46_80",
"chitosanase_GH46"
] | [
2204,
1297,
1132,
1721
] | 4 | [
"CAZY",
"EC",
"PROSITEDOC"
] | [
"GH46",
"3.2.1.132",
"PDOC60000"
] | [
"CAZY:GH46",
"EC:3.2.1.132",
"PROSITEDOC:PDOC60000"
] | 3 | [
"1chk",
"1qgi",
"2d05",
"4ily",
"4olt",
"4qwp",
"5b4s",
"5hwa",
"6lwu",
"6x2q",
"7c6c",
"7c6d",
"7xh0"
] | 13 | [
"PUB00004870",
"PUB00005266",
"PUB00036505",
"PUB00079509",
"PUB00079510",
"PUB00079511"
] | [
"7624375",
"8535779",
"8564542",
"9723170",
"8564539",
"12369923"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"X-ray structure of an anti-fungal chitosanase from streptomyces N174.",
"Structural analysis shows five glycohydrolase families diverged from ... | [
1995,
1995,
1996,
1998,
1996,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina",
"Viruses",
"unclassified sequences"
] | [
1821,
358,
7,
30,
4
] | 5 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 46 | Glycoside hydrolase, family 46 | Glyco_hydro_46 | 5 |
IPR000401 | 401 | [Phe13]-bombesin receptor | BRS4 | Family | 8 | 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... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00638"
] | [
"BOMBESIN4R"
] | [
8
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000131",
"PUB00002477",
"PUB00004867",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816",
"PUB00099716",
"PUB00099719"
] | [
"2111655",
"2830256",
"7597102",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293",
"34539578",
"25517020"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Cloning of a receptor for amphibian [Phe13]bombesin distinct from the receptor for gastrin-releasing peptide: identification of a fourth bombesin receptor subtype (BB4).",
"Design of a discriminating fingerprint for... | [
1990,
1988,
1995,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013,
2021,
2015
] | 13 | [
"IPR001556"
] | [] | 1 | 0 | 1 | [
"Anura"
] | [
8
] | 1 | [] | [] | 0 | true | Family | [Phe13]-bombesin receptor | [Phe13]-bombesin receptor | BRS4 | 4 |
IPR000402 | 402 | Sodium/potassium-transporting ATPase subunit beta | Na/K_ATPase_sub_beta | Family | 8,448 | false | false | This entry represents the sodium/potassium-transporting ATPase subunit beta. This is the non-catalytic component of the active enzyme, which catalyses the hydrolysis of ATP coupled with the exchange of Na + and K + ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers,... | [
"GO:0006813",
"GO:0006814",
"GO:0005890"
] | [
"potassium ion transport",
"sodium ion transport",
"sodium:potassium-exchanging ATPase complex"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROSITE",
"PROSITE",
"PANTHER",
"NCBIFAM"
] | [
"PF00287",
"PS00390",
"PS00391",
"PTHR11523",
"TIGR01107"
] | [
"Na_K-ATPase",
"ATPASE_NA_K_BETA_1",
"ATPASE_NA_K_BETA_2",
"",
"Na_K_ATPase_bet"
] | [
8436,
3284,
4394,
8187,
4854
] | 5 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp2099",
"PDOC00328",
"R-BTA-210991",
"R-BTA-2173795",
"R-BTA-5578775",
"R-BTA-936837",
"R-CEL-210991",
"R-CEL-2173795",
"R-CFA-936837",
"R-DME-210991",
"R-DME-2173795",
"R-GGA-210991",
"R-GGA-2173795",
"R-GGA-5578775",
"R-GGA-936837",
"R-HSA-210991",
"R-HSA-2173795",
"R-HSA-... | [
"GP:GenProp2099",
"PROSITEDOC:PDOC00328",
"REACTOME:R-BTA-210991",
"REACTOME:R-BTA-2173795",
"REACTOME:R-BTA-5578775",
"REACTOME:R-BTA-936837",
"REACTOME:R-CEL-210991",
"REACTOME:R-CEL-2173795",
"REACTOME:R-CFA-936837",
"REACTOME:R-DME-210991",
"REACTOME:R-DME-2173795",
"REACTOME:R-GGA-210991"... | 32 | [
"2xzb",
"2yn9",
"2zxe",
"3a3y",
"3b8e",
"3ixz",
"3kdp",
"3n23",
"3wgu",
"3wgv",
"4hqj",
"4hyt",
"4res",
"4ret",
"4ux1",
"4ux2",
"4xe5",
"5avq",
"5avr",
"5avs",
"5avt",
"5avu",
"5avv",
"5avw",
"5avx",
"5avy",
"5avz",
"5aw0",
"5aw1",
"5aw2",
"5aw3",
"5aw4"... | 113 | [
"PUB00063564"
] | [
"9648860"
] | [
"Functional analysis and tissue-specific expression of Drosophila Na+,K+-ATPase subunits."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"bird metagenome"
] | [
8443,
4,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
13,
12,
24,
21,
27
] | 6 | true | Family | Sodium/potassium-transporting ATPase subunit beta | Sodium/potassium-transporting ATPase subunit beta | Na/K_ATPase_sub_beta | 5 |
IPR000403 | 403 | Phosphatidylinositol 3-/4-kinase, catalytic domain | PI3/4_kinase_cat_dom | Domain | 67,103 | false | false | This entry represents the catalytic domain of PI3 and PI-4 kinases. This domain is also found in a number of pseudokinases, where a lack of typical motifs at the catalytic site suggest a lack of kinase activity. Phosphatidylinositol 3-kinase (PI3-kinase) ( ) [ ] is an enzyme that phosphorylates phosphoinositides on the... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00454",
"PS50290",
"SM00146"
] | [
"PI3_PI4_kinase",
"PI3_4_KINASE_3",
"PI3Kc"
] | [
65800,
66036,
53297
] | 3 | [
"EC",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"2.7.1",
"GenProp1548",
"GenProp1758",
"PDOC00710",
"R-BTA-109704",
"R-BTA-112399",
"R-BTA-114604",
"R-BTA-1250342",
"R-BTA-1257604",
"R-BTA-1433557",
"R-BTA-1660499",
"R-BTA-180292",
"R-BTA-186763",
"R-BTA-1963642",
"R-BTA-198203",
"R-BTA-201556",
"R-BTA-202424",
"R-BTA-2029485",
... | [
"EC:2.7.1",
"GP:GenProp1548",
"GP:GenProp1758",
"PROSITEDOC:PDOC00710",
"REACTOME:R-BTA-109704",
"REACTOME:R-BTA-112399",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1250342",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1660499",
"REACTOME:R-BTA-180292",
"REACTOME:R-BTA-... | 450 | [
"1e7u",
"1e7v",
"1e8w",
"1e8x",
"1e8y",
"1e8z",
"1e90",
"1he8",
"2a4z",
"2a5u",
"2chw",
"2chx",
"2chz",
"2rd0",
"2v4l",
"2wxf",
"2wxg",
"2wxh",
"2wxi",
"2wxj",
"2wxk",
"2wxl",
"2wxm",
"2wxn",
"2wxo",
"2wxp",
"2wxq",
"2wxr",
"2x38",
"2x6f",
"2x6h",
"2x6i"... | 532 | [
"PUB00000875",
"PUB00000893",
"PUB00001254",
"PUB00007087",
"PUB00014536",
"PUB00090062"
] | [
"1322797",
"8387896",
"8194527",
"12151228",
"12456783",
"24675427"
] | [
"Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit.",
"Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression.",
"PIK1, an essential phosphatidylinositol 4-kinase associated with the yeast nucleus.",
"Structural... | [
1992,
1993,
1994,
2002,
2002,
2014
] | 6 | [] | [
"IPR026683",
"IPR037702",
"IPR037703",
"IPR037704",
"IPR037705",
"IPR037706",
"IPR037707",
"IPR039414",
"IPR044107",
"IPR057754",
"IPR057756"
] | 0 | 11 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
201,
66809,
43,
50
] | 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... | [
104,
14,
59,
33,
96,
62,
8,
67,
81,
9,
10,
143
] | 12 | true | Domain | Phosphatidylinositol 3-/4-kinase, catalytic domain | Phosphatidylinositol 3-/4-kinase, catalytic domain | PI3/4_kinase_cat_dom | 9 |
IPR000404 | 404 | Flavivirus non-structural protein NS4A | Flavi_NS4A | Domain | 11,398 | false | false | Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4A protein is small and poorly conserved among the Flaviviruses. NS4A contains multiple hydrophobic potential membrane spanning regions [ ]. NS4A has only been found in cells infected by Kunjin virus... | [
"GO:0016032",
"GO:0016070",
"GO:0044423"
] | [
"viral process",
"RNA metabolic process",
"virion component"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF01350"
] | [
"Flavi_NS4A"
] | [
11398
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.56",
"2.1.1.57",
"2.7.7.48",
"3.4.21.91",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"PWY-7375",
"PWY-7379"
] | [
"EC:2.1.1.56",
"EC:2.1.1.57",
"EC:2.7.7.48",
"EC:3.4.21.91",
"EC:3.6.1.15",
"EC:3.6.4.13",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"METACYC:PWY-7375",
"METACYC:PWY-7379"
] | 13 | [
"8cxg",
"8cxh",
"8cxi"
] | 3 | [
"PUB00000118",
"PUB00005567"
] | [
"2174669",
"2541547"
] | [
"Flavivirus genome organization, expression, and replication.",
"Positive identification of NS4A, the last of the hypothetical nonstructural proteins of flaviviruses."
] | [
1990,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Levilactobacillus bambusae",
"Orthornavirae"
] | [
1,
11397
] | 2 | [] | [] | 0 | true | Domain | Flavivirus non-structural protein NS4A | Flavivirus non-structural protein NS4A | Flavi_NS4A | 5 |
IPR000405 | 405 | Galanin receptor family | Galanin_rcpt | Family | 4,420 | false | false | Galanin is involved in a variety of physiological mechanisms and disease states, from appetite and neuroregeneration to seizures and pain [ , ]. The actions of galanin are mediated through interaction with specific membrane receptors. Three receptor subtypes have been identified; Galanin receptor 1 (GALR1), Galanin rec... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00663"
] | [
"GALANINR"
] | [
4420
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-375276",
"R-DRE-418594",
"R-HSA-375276",
"R-HSA-418594",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-375276",
"R-RNO-418594"
] | [
"REACTOME:R-DRE-375276",
"REACTOME:R-DRE-418594",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-418594"
] | 8 | [
"7wq3",
"7wq4",
"7xbd",
"7xjj",
"7xjk",
"7xjl"
] | 6 | [
"PUB00007607",
"PUB00007608",
"PUB00063814",
"PUB00066627",
"PUB00066628",
"PUB00066629",
"PUB00066630",
"PUB00066631",
"PUB00066632",
"PUB00066633",
"PUB00066634",
"PUB00066635",
"PUB00066636",
"PUB00066637",
"PUB00066647",
"PUB00066648",
"PUB00066988"
] | [
"9578554",
"10689365",
"8750821",
"17604107",
"16052044",
"9126874",
"7682064",
"2417156",
"10619483",
"15670772",
"1281259",
"8734340",
"12769595",
"23233848",
"2463283",
"2471574",
"11381038"
] | [
"Differential intracellular signaling of the GalR1 and GalR2 galanin receptor subtypes.",
"Galanin receptor subtypes.",
"Cloning and characterization of the rat GALR1 galanin receptor from Rin14B insulinoma cells.",
"The galanin peptide family: receptor pharmacology, pleiotropic biological actions, and implic... | [
1998,
2000,
1995,
2007,
2005,
1997,
1993,
1985,
2000,
2005,
1992,
1996,
2002,
2012,
1988,
1989,
2001
] | 17 | [
"IPR000276"
] | [
"IPR003906",
"IPR003907",
"IPR003908"
] | 1 | 3 | 0 | [
"Eumetazoa",
"bird metagenome"
] | [
4419,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
7,
4,
3,
4,
9
] | 6 | true | Family | Galanin receptor family | Galanin receptor family | Galanin_rcpt | 8 |
IPR000406 | 406 | Rho protein GDP-dissociation inhibitor | Rho_GDI | Family | 8,123 | false | false | The GDP dissociation inhibitor for rho proteins, rho GDI, regulates GDP/GTP exchange by inhibiting the dissociation of GDP from them. The protein contains 204 amino acids, with a calculated Mr value of 23,421. Hydropathy analysis shows it to be largely hydrophilic, with a single hydrophobic region. The protein plays an... | [
"GO:0005094",
"GO:0005515",
"GO:0007266",
"GO:0005737"
] | [
"Rho GDP-dissociation inhibitor activity",
"protein binding",
"Rho protein signal transduction",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF02115",
"PR00492",
"PTHR10980"
] | [
"Rho_GDI",
"RHOGDI",
""
] | [
8117,
6348,
7926
] | 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-9013148",
"R-BTA-9013407",
"R-BTA-9013408",
"R-CEL-8980692",
"R-CEL-9013026",
"R-CEL-9013148",
"R-CEL-9013149",
"R-CEL-9013404",
"R-CEL-9013407",
"R-CEL-9013408",
"R-CEL-9013423",
"R-DDI-9013148",
"R-DDI-9013149",
"R-DDI-9013404",
"R-DDI-9013407",
"R-DDI-9013408",
"R-DDI-90134... | [
"REACTOME:R-BTA-9013148",
"REACTOME:R-BTA-9013407",
"REACTOME:R-BTA-9013408",
"REACTOME:R-CEL-8980692",
"REACTOME:R-CEL-9013026",
"REACTOME:R-CEL-9013148",
"REACTOME:R-CEL-9013149",
"REACTOME:R-CEL-9013404",
"REACTOME:R-CEL-9013407",
"REACTOME:R-CEL-9013408",
"REACTOME:R-CEL-9013423",
"REACTOM... | 55 | [
"1ajw",
"1cc0",
"1doa",
"1ds6",
"1fso",
"1fst",
"1ft0",
"1ft3",
"1gdf",
"1hh4",
"1kmt",
"1qvy",
"1rho",
"2bxw",
"2jhs",
"2jht",
"2jhu",
"2jhv",
"2jhw",
"2jhx",
"2jhy",
"2jhz",
"2ji0",
"2n80",
"4f38",
"5fr1",
"5fr2",
"5h1d",
"8x8t",
"9x53",
"9x54",
"9x55"... | 34 | [
"PUB00001445",
"PUB00003781",
"PUB00101427",
"PUB00101428",
"PUB00101429",
"PUB00101430"
] | [
"8223583",
"8796870",
"12198156",
"24554735",
"9242378",
"12163018"
] | [
"Role of the rac1 p21-GDP-dissociation inhibitor for rho heterodimer in the activation of the superoxide-forming NADPH oxidase of macrophages.",
"The NADPH oxidase and chronic granulomatous disease.",
"Defects in cytokinesis, actin reorganization and the contractile vacuole in cells deficient in RhoGDI.",
"Rh... | [
1993,
1996,
2002,
2014,
1997,
2002
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
27,
8096
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
11,
2,
2,
1,
22,
7,
1,
11,
8,
1,
1,
23
] | 12 | true | Family | Rho protein GDP-dissociation inhibitor | Rho protein GDP-dissociation inhibitor | Rho_GDI | 4 |
IPR000407 | 407 | Nucleoside phosphatase GDA1/CD39 | GDA1_CD39_NTPase | Family | 22,377 | false | false | A number of nucleoside diphosphate and triphosphate hydrolases as well as some yet uncharacterised proteins have been found to belong to the same family [ , ]. The uncharacterised proteins all seem to be membrane-bound. | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROSITE",
"PANTHER"
] | [
"PF01150",
"PS01238",
"PTHR11782"
] | [
"GDA1_CD39",
"GDA1_CD39_NTPASE",
""
] | [
22292,
14825,
21808
] | 3 | [
"EC",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.1",
"GenProp1396",
"PDOC00952",
"R-CEL-8850843",
"R-HSA-8850843",
"R-HSA-9660826",
"R-MMU-8850843",
"R-RNO-8850843",
"R-SCE-8850843",
"R-SPO-8850843",
"R-XTR-8850843"
] | [
"EC:3.6.1",
"GP:GenProp1396",
"PROSITEDOC:PDOC00952",
"REACTOME:R-CEL-8850843",
"REACTOME:R-HSA-8850843",
"REACTOME:R-HSA-9660826",
"REACTOME:R-MMU-8850843",
"REACTOME:R-RNO-8850843",
"REACTOME:R-SCE-8850843",
"REACTOME:R-SPO-8850843",
"REACTOME:R-XTR-8850843"
] | 11 | [
"3aap",
"3aaq",
"3aar",
"3agr",
"3cj1",
"3cj7",
"3cj9",
"3cja",
"3zx0",
"3zx2",
"3zx3",
"4a57",
"4a59",
"4a5a",
"4a5b",
"4bqz",
"4br0",
"4br2",
"4br4",
"4br5",
"4br7",
"4br9",
"4bra",
"4brc",
"4brd",
"4bre",
"4brf",
"4brg",
"4brh",
"4bri",
"4brk",
"4brl"... | 50 | [
"PUB00000253",
"PUB00002967"
] | [
"8579614",
"8703025"
] | [
"Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum).",
"Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside tri... | [
1996,
1996
] | 2 | [] | [
"IPR017227"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Manticavirus",
"freshwater metagenome"
] | [
186,
22188,
2,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
3,
33,
5,
40,
25,
2,
40,
39,
2,
2,
99
] | 12 | true | Family | Nucleoside phosphatase GDA1/CD39 | Nucleoside phosphatase GDA1/CD39 | GDA1_CD39_NTPase | 5 |
IPR000408 | 408 | Regulator of chromosome condensation, RCC1 | Reg_chr_condens | Repeat | 86,628 | false | false | The regulator of chromosome condensation (RCC1) [ ] is a eukaryotic protein which binds to chromatin and interacts with ran, a nuclear GTP-binding protein , to promote the loss of bound GDP and the uptake of fresh GTP, thus acting as a guanine-nucleotide dissociation stimulator (GDS). The interaction of RCC1 with ran p... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROSITE",
"PROFILE"
] | [
"PF00415",
"PR00633",
"PS00625",
"PS00626",
"PS50012"
] | [
"RCC1",
"RCCNDNSATION",
"RCC1_1",
"RCC1_2",
"RCC1_3"
] | [
38842,
63163,
3287,
57569,
83931
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00544",
"R-CEL-1169408",
"R-CEL-936440",
"R-CEL-9615933",
"R-CEL-983168",
"R-CEL-9833482",
"R-CEL-9909505",
"R-DDI-1169408",
"R-DDI-936440",
"R-DDI-983168",
"R-DDI-9909505",
"R-DME-5693565",
"R-DME-8876198",
"R-DME-9013149",
"R-DME-9615933",
"R-DME-983168",
"R-HSA-1169408",
"R... | [
"PROSITEDOC:PDOC00544",
"REACTOME:R-CEL-1169408",
"REACTOME:R-CEL-936440",
"REACTOME:R-CEL-9615933",
"REACTOME:R-CEL-983168",
"REACTOME:R-CEL-9833482",
"REACTOME:R-CEL-9909505",
"REACTOME:R-DDI-1169408",
"REACTOME:R-DDI-936440",
"REACTOME:R-DDI-983168",
"REACTOME:R-DDI-9909505",
"REACTOME:R-DM... | 66 | [
"1a12",
"1i2m",
"1jtd",
"3kci",
"3mvd",
"3of7",
"3qhy",
"3qi0",
"4d4o",
"4d4p",
"4d4q",
"4d9s",
"4dnu",
"4dnv",
"4dnw",
"4jhn",
"4jhp",
"4l1m",
"4naa",
"4nbm",
"4nc4",
"4o2w",
"4qam",
"4x33",
"5gwn",
"5hq2",
"5t94",
"5tbk",
"5xgs",
"6dd7",
"6xzl",
"6xzm"... | 48 | [
"PUB00002001",
"PUB00005411"
] | [
"8817343",
"8480369"
] | [
"Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1.",
"RCC1 in the cell cycle: the regulator of chromosome condensation takes on new roles."
] | [
1996,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
65,
8685,
77261,
316,
301
] | 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... | [
147,
11,
173,
23,
136,
67,
6,
87,
76,
4,
4,
232
] | 12 | true | Repeat | Regulator of chromosome condensation, RCC1 | Regulator of chromosome condensation, RCC1 | Reg_chr_condens | 2 |
IPR000409 | 409 | BEACH domain | BEACH_dom | Domain | 26,765 | false | false | The BEACH domain is usually followed by a series of WD repeats. BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF02138",
"PS50197",
"SM01026",
"cd06071"
] | [
"Beach",
"BEACH",
"Beach",
"Beach"
] | [
26386,
26474,
26037,
24611
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50197",
"R-DDI-6798695",
"R-DRE-6798695",
"R-HSA-112314",
"R-HSA-163615",
"R-HSA-2122947",
"R-HSA-5626978",
"R-HSA-6798695",
"R-HSA-9013148",
"R-HSA-9609736",
"R-MMU-5626978",
"R-MMU-6798695"
] | [
"PROSITEDOC:PDOC50197",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-112314",
"REACTOME:R-HSA-163615",
"REACTOME:R-HSA-2122947",
"REACTOME:R-HSA-5626978",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9609736",
"REACTOME:R-MMU-5626978",
"REACTOME:R-... | 12 | [
"1mi1",
"1t77"
] | 2 | [
"PUB00054617",
"PUB00062010",
"PUB00075926",
"PUB00079623",
"PUB00079624",
"PUB00079625",
"PUB00079626",
"PUB00079627"
] | [
"12535270",
"15193433",
"11102458",
"17079274",
"15086784",
"12125812",
"15342963",
"12210762"
] | [
"The role of BEACH proteins in Dictyostelium.",
"Identification and characterization of NBEAL1, a novel human neurobeachin-like 1 protein gene from fetal brain, which is up regulated in glioma.",
"Neurobeachin: A protein kinase A-anchoring, beige/Chediak-higashi protein homolog implicated in neuronal membrane t... | [
2003,
2004,
2000,
2006,
2004,
2002,
2004,
2002
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halorubrum",
"Siphoviridae sp. ctWuM9",
"metagenomes"
] | [
95,
26662,
3,
1,
4
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
34,
8,
114,
12,
66,
36,
1,
20,
44,
1,
1,
73
] | 12 | true | Domain | BEACH domain | BEACH domain | BEACH_dom | 7 |
IPR000412 | 412 | ABC-2 transporter | ABC_2_transport | Family | 76,971 | false | false | This entry includes a varied group of ABC2-type transporters from bacteria and archaea, including Nodulation protein J (NodJ), Doxorubicin resistance ABC transporter permease protein DrrB, Daunorubicin resistance ABC transporter permease protein DrrB1-3, among others. NodJ is part of the NodIJ complex involved in the e... | [
"GO:0140359",
"GO:0055085",
"GO:0016020",
"GO:0043190"
] | [
"ABC-type transporter activity",
"transmembrane transport",
"membrane",
"ATP-binding cassette (ABC) transporter complex"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PIRSF",
"PRINTS"
] | [
"PIRSF006648",
"PR00164"
] | [
"DrrB",
"ABC2TRNSPORT"
] | [
64434,
38521
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00692"
] | [
"PROSITEDOC:PDOC00692"
] | 1 | [
"8tsh",
"8tsi",
"8tsl",
"8tsw",
"8tt3",
"8tun",
"8yzp",
"8z00",
"8z01",
"8z0b",
"8z0i",
"8z0j",
"9ju6"
] | 13 | [
"PUB00014769",
"PUB00018398",
"PUB00158909"
] | [
"9873074",
"10331089",
"39375957"
] | [
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"Biochemical, cellular, and pharmacological aspects of the multidrug transporter.",
"The involvement of multiple ABC transporters in daunorubicin efflux in Streptomyces coeruleoru... | [
1999,
1999,
2024
] | 3 | [] | [
"IPR005942",
"IPR005943",
"IPR005981",
"IPR022403"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2190,
72623,
1023,
1135
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)"
] | [
2,
1,
2
] | 3 | true | Family | ABC-2 transporter | ABC-2 transporter | ABC_2_transport | 9 |
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