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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR020621 | 20,621 | ATP phosphoribosyltransferase HisG, long form | ATP-PRT_HisG_long | Family | 13,362 | false | false | ATP phosphoribosyltransferase (ATP-PRT, ) is the enzyme that catalyses the first step in the biosynthesis of histidine in bacteria, fungi and plants as shown below. It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate wit... | [
"GO:0003879",
"GO:0000105"
] | [
"ATP phosphoribosyltransferase activity",
"L-histidine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00079"
] | [
"HisG_Long"
] | [
13362
] | 1 | [
"EC"
] | [
"2.4.2.17"
] | [
"EC:2.4.2.17"
] | 1 | [
"1h3d",
"1nh7",
"1nh8",
"1q1k",
"2vd3",
"4yb5",
"4yb6",
"4yb7",
"5lht",
"5lhu",
"5u99",
"7dah",
"7dam"
] | 13 | [
"PUB00022501",
"PUB00028083",
"PUB00028134",
"PUB00028139",
"PUB00103843",
"PUB00103844",
"PUB00103845"
] | [
"14741209",
"11751055",
"12511575",
"10430882",
"22989207",
"27191057",
"28781362"
] | [
"The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.",
"The PRT protein family.",
"Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis.",
"An aminoacyl-tRNA synthetase paralog with a catalytic rol... | [
2004,
2001,
2003,
1999,
2012,
2016,
2017
] | 7 | [
"IPR001348"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
688,
10566,
1867,
241
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
1,
1,
1,
1,
3
] | 7 | true | Family | ATP phosphoribosyltransferase HisG, long form | ATP phosphoribosyltransferase HisG, long form | ATP-PRT_HisG_long | 1 |
IPR020622 | 20,622 | Alanine racemase, pyridoxal-phosphate attachment site | Ala_racemase_pyridoxalP-BS | Binding_site | 25,420 | false | false | Alanine racemase catalyses the pyridoxal-dependent conversion of L-alanine into D-alanine, a key component of bacterial peptidoglycan [ ]. In bacteria such as Escherichia coli and Salmonella typhimurium, there are two alanine racemase isoforms synthesised by the genes alr and dadX, where the first is a biosynthetic for... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00395"
] | [
"ALANINE_RACEMASE"
] | [
25420
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.1.1",
"5.1.1.1",
"PWY-7383",
"PWY-8040",
"PWY-8072",
"PWY-8443"
] | [
"EC:5.1.1",
"EC:5.1.1.1",
"METACYC:PWY-7383",
"METACYC:PWY-8040",
"METACYC:PWY-8072",
"METACYC:PWY-8443"
] | 6 | [
"1bd0",
"1epv",
"1ftx",
"1l6f",
"1l6g",
"1niu",
"1rcq",
"1sft",
"1vfh",
"1vfs",
"1vft",
"1xfc",
"1xqk",
"1xql",
"2odo",
"2rjg",
"2rjh",
"2sfp",
"2vd8",
"2vd9",
"3b8t",
"3b8u",
"3b8v",
"3b8w",
"3co8",
"3e5p",
"3e6e",
"3ha1",
"3hur",
"3kw3",
"3oo2",
"3s46"... | 68 | [
"PUB00000074",
"PUB00000440",
"PUB00163391",
"PUB00163392",
"PUB00163393"
] | [
"2197992",
"9063881",
"20971724",
"28042035",
"37129190"
] | [
"Recent topics in pyridoxal 5'-phosphate enzyme studies.",
"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.",
"Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases.",
"Structural and functional characteriza... | [
1990,
1997,
2011,
2017,
2023
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanococcus",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
24824,
143,
19,
2,
432
] | 5 | [
"Escherichia coli (strain K12)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2
] | 2 | true | Binding_site | Alanine racemase, pyridoxal-phosphate attachment site | Alanine racemase, pyridoxal-phosphate attachment site | Ala_racemase_pyridoxalP-BS | 8 |
IPR020624 | 20,624 | Schiff base-forming aldolase, conserved site | Schiff_base-form_aldolases_CS | Conserved_site | 25,536 | false | false | This entry represents an conserved site found in members of a structural superfamily of Schiff base-forming aldolases that catalyse reactions in different biological pathways. This superfamily includes members such as dihydrodipicolinate synthase (DHDPS), N-acetylneuraminate lyase (NAL) and 2-keto-3-deoxygluconate aldo... | [
"GO:0016829"
] | [
"lyase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00665"
] | [
"DHDPS_1"
] | [
25536
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME"
] | [
"4.3.3.7",
"PWY-2941",
"PWY-2942",
"PWY-5097",
"PWY-8088",
"R-DRE-4085001"
] | [
"EC:4.3.3.7",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097",
"METACYC:PWY-8088",
"REACTOME:R-DRE-4085001"
] | 6 | [
"1dhp",
"1f5z",
"1f6k",
"1f6p",
"1f73",
"1f74",
"1f7b",
"1fdy",
"1fdz",
"1hl2",
"1nal",
"1o5k",
"1s5v",
"1s5w",
"1xky",
"1xl9",
"1xxx",
"1yxc",
"1yxd",
"2a6l",
"2a6n",
"2ats",
"2ehh",
"2ojp",
"2pur",
"2rfg",
"2v8z",
"2v9d",
"2vc6",
"2wkj",
"2wnn",
"2wnq"... | 185 | [
"PUB00000520",
"PUB00072988",
"PUB00072990"
] | [
"1463470",
"24677246",
"20503968"
] | [
"Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.",
"Identification of the bona fide DHDPS from a common plant pathogen.",
"NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehy... | [
1992,
2014,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviridae environmental sample",
"unclassified sequences"
] | [
735,
21660,
2738,
1,
402
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
2,
4,
1,
7,
9
] | 6 | true | Conserved_site | Schiff base-forming aldolase, conserved site | Schiff base-forming aldolase, conserved site | Schiff_base-form_aldolases_CS | 4 |
IPR020626 | 20,626 | L-aspartate dehydrogenase, prokaryotic | Asp_DH_prok | Family | 3,026 | false | false | This group contains aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P) + cofactor) and a C-terminal α/β domain [ ]. This suggested that TM1643 may be a dehyd... | [
"GO:0033735",
"GO:0009435"
] | [
"aspartate dehydrogenase [NAD(P)+] activity",
"NAD+ biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01265"
] | [
"NadX"
] | [
3026
] | 1 | [
"EC"
] | [
"1.4.1.21"
] | [
"EC:1.4.1.21"
] | 1 | [
"1h2h",
"1j5p",
"2dc1"
] | 3 | [
"PUB00014412"
] | [
"12496312"
] | [
"Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643."
] | [
2003
] | 1 | [
"IPR011182"
] | [
"IPR022487"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
348,
2625,
16,
37
] | 4 | [] | [] | 0 | true | Family | L-aspartate dehydrogenase, prokaryotic | L-aspartate dehydrogenase, prokaryotic | Asp_DH_prok | 2 |
IPR020627 | 20,627 | RNA-binding protein KhpA | KhpA | Family | 11,563 | false | false | This family represents the RNA-binding protein KhpA, a probable RNA chaperone. It forms a complex with KhpB (also known as Jag or EloR) which binds to cellular RNA and controls its expression. KhpA plays a role in peptidoglycan (PG) homeostasis and cell length regulation [ ]. The KhpA-KhpB complex stimulates or control... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PANTHER",
"CDD"
] | [
"MF_00088",
"PTHR34654",
"cd22533"
] | [
"KhpA",
"",
"KH-II_YlqC-like"
] | [
10451,
11353,
10858
] | 3 | [] | [] | [] | 0 | [
"7xqc"
] | 1 | [
"PUB00100213",
"PUB00100215"
] | [
"28941257",
"30842445"
] | [
"Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses the requirement for PBP2b by overproduction of FtsA in Streptococcus pneumoniae D39.",
"Prevention of EloR/KhpA heterodimerization by introduction of site-specific amino acid substitutions renders the essential elongasome protein PBP2b redun... | [
2017,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"metagenomes"
] | [
11271,
8,
1,
283
] | 4 | [] | [] | 0 | true | Family | RNA-binding protein KhpA | RNA-binding protein KhpA | KhpA | 5 |
IPR020628 | 20,628 | Formate-tetrahydrofolate ligase, FTHFS, conserved site | Formate_THF_ligase_CS | Conserved_site | 18,215 | false | false | Formate--tetrahydrofolate ligase ( ) (formyltetrahydrofolate synthetase) (FTHFS) is one of the enzymes participating in the transfer of one-carbon units, an essential element of various biosynthetic pathways. FTHFS catalyzes the ATP-dependent activation of formate ion via its addition to the N10 position of tetrahydrof... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00721",
"PS00722"
] | [
"FTHFS_1",
"FTHFS_2"
] | [
16186,
15428
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4.3",
"PWY-1722",
"PWY-2161",
"PWY-2201",
"PWY-3841",
"PWY-8303",
"R-BTA-196757",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:6.3.4.3",
"METACYC:PWY-1722",
"METACYC:PWY-2161",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-8303",
"REACTOME:R-BTA-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-196757",
"REACTOME:R-SCE-196757",
"REACTOME:R-SPO-196757"
] | 13 | [
"1eg7",
"1fp7",
"1fpm",
"3do6",
"3qus",
"4ioj",
"4iok",
"4iol",
"4iom",
"4jim",
"4jjk",
"4jjz",
"4jki",
"5a4j",
"5a5g",
"7c11",
"7xzn",
"7xzo",
"7xzp"
] | 19 | [
"PUB00000324",
"PUB00002486",
"PUB00006525",
"PUB00021607"
] | [
"2200509",
"2836393",
"10747779",
"11087401"
] | [
"Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum.",
"Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase.",
"The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moor... | [
1990,
1988,
2000,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
169,
10759,
6863,
424
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
3,
4,
15,
6,
2,
4,
15,
2,
2,
4
] | 12 | true | Conserved_site | Formate-tetrahydrofolate ligase, FTHFS, conserved site | Formate-tetrahydrofolate ligase, FTHFS, conserved site | Formate_THF_ligase_CS | 9 |
IPR020629 | 20,629 | Formamidopyrimidine-DNA glycosylase | FPG_Glyclase | Family | 21,177 | false | false | This entry represents formamidopyrimidine-DNA glycosylase proteins mostly found in bacteria. Formamidopyrimidine-DNA glycosylases (Fpg, MutM) are trifunctional DNA base excision repair enzymes that remove a wide range of oxidation-damaged bases (N-glycosylase activity; ) and cleave both the 3'- and 5'-phosphodiester bo... | [
"GO:0003906",
"GO:0008270",
"GO:0008534",
"GO:0006281"
] | [
"DNA-(apurinic or apyrimidinic site) endonuclease activity",
"zinc ion binding",
"oxidized purine nucleobase lesion DNA N-glycosylase activity",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM"
] | [
"MF_00103",
"NF002211",
"TIGR00577"
] | [
"Fapy_DNA_glycosyl",
"PRK01103.1",
"fpg"
] | [
17540,
20338,
20672
] | 3 | [
"EC",
"EC",
"GP"
] | [
"3.2.2.23",
"4.2.99.18",
"GenProp1099"
] | [
"EC:3.2.2.23",
"EC:4.2.99.18",
"GP:GenProp1099"
] | 3 | [
"1ee8",
"1k82",
"1kfv",
"1l1t",
"1l1z",
"1l2b",
"1l2c",
"1l2d",
"1nnj",
"1pji",
"1pjj",
"1pm5",
"1r2y",
"1r2z",
"1tdz",
"1xc8",
"2f5n",
"2f5o",
"2f5p",
"2f5q",
"2f5s",
"2xzf",
"2xzu",
"3c58",
"3go8",
"3gp1",
"3gpp",
"3gpu",
"3gpx",
"3gpy",
"3gq3",
"3gq4"... | 74 | [
"PUB00002832",
"PUB00003593",
"PUB00012853",
"PUB00014010",
"PUB00018047",
"PUB00031419"
] | [
"8473347",
"7704272",
"11912217",
"10921868",
"12055620",
"15232006"
] | [
"Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role.",
"Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein.",
"Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA.",
"Cryst... | [
1993,
1995,
2002,
2000,
2002,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacillus phage G",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
22,
1,
20187,
616,
351
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
1,
7,
4
] | 4 | true | Family | Formamidopyrimidine-DNA glycosylase | Formamidopyrimidine-DNA glycosylase | FPG_Glyclase | 7 |
IPR020630 | 20,630 | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain | THF_DH/CycHdrlase_cat_dom | Domain | 43,269 | false | false | This entry represents the N-terminal catalytic domain of enzymes that belong to the tetrahydrofolate dehydrogenase/cyclohydrolase family, which are mainly found in bacteria but also in archaeal and eukaryotic organisms. Enzymes that participate in the transfer of one-carbon units require the coenzyme tetrahydrofolate (... | [
"GO:0004488"
] | [
"methylenetetrahydrofolate dehydrogenase (NADP+) activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00763"
] | [
"THF_DHG_CYH"
] | [
43269
] | 1 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.5",
"3.5.4.9",
"GenProp1356",
"PWY-1722",
"PWY-2201",
"PWY-3841",
"PWY-5030",
"PWY-5497",
"PWY-6613",
"PWY-7909",
"PWY-8303",
"R-BTA-196757",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.5",
"EC:3.5.4.9",
"GP:GenProp1356",
"METACYC:PWY-1722",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"METACYC:PWY-6613",
"METACYC:PWY-7909",
"METACYC:PWY-8303",
"REACTOME:R-BTA-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"REACTO... | 18 | [
"1a4i",
"1b0a",
"1dia",
"1dib",
"1dig",
"1edz",
"1ee9",
"2c2x",
"2c2y",
"3l07",
"3ngl",
"3ngx",
"3p2o",
"4a26",
"4a5o",
"4b4u",
"4b4v",
"4b4w",
"4cjx",
"5nhs",
"5o22",
"5o28",
"5o2a",
"5tc4",
"5zf1",
"6ape",
"6de8",
"6deb",
"6ecp",
"6ecq",
"6ecr",
"6jib"... | 54 | [
"PUB00000304",
"PUB00000651"
] | [
"2541774",
"8485162"
] | [
"Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme.",
"The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
] | [
1989,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
679,
28645,
13253,
17,
675
] | 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,
1,
26,
7,
1,
27,
11,
3,
11,
20,
3,
3,
17
] | 13 | true | Domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain | THF_DH/CycHdrlase_cat_dom | 7 |
IPR020631 | 20,631 | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain | THF_DH/CycHdrlase_NAD-bd_dom | Domain | 43,548 | false | false | This entry represents the NAD(P)-binding domain found in enzymes that belong to the tetrahydrofolate dehydrogenase/cyclohydrolase family, which are mainly found in bacteria but also in archaeal and eukaryotic organisms. Enzymes that participate in the transfer of one-carbon units require the coenzyme tetrahydrofolate (... | [
"GO:0004488"
] | [
"methylenetetrahydrofolate dehydrogenase (NADP+) activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"CDD"
] | [
"PF02882",
"cd01080"
] | [
"THF_DHG_CYH_C",
"NAD_bind_m-THF_DH_Cyclohyd"
] | [
43542,
38232
] | 2 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.5",
"3.5.4.9",
"GenProp1356",
"PWY-1722",
"PWY-2201",
"PWY-3841",
"PWY-5030",
"PWY-5497",
"PWY-6613",
"PWY-7909",
"PWY-8303",
"R-BTA-196757",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.5",
"EC:3.5.4.9",
"GP:GenProp1356",
"METACYC:PWY-1722",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"METACYC:PWY-6613",
"METACYC:PWY-7909",
"METACYC:PWY-8303",
"REACTOME:R-BTA-196757",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"REACTO... | 18 | [
"1a4i",
"1b0a",
"1dia",
"1dib",
"1dig",
"1edz",
"1ee9",
"2c2x",
"2c2y",
"3l07",
"3ngl",
"3ngx",
"3p2o",
"4a26",
"4a5o",
"4b4u",
"4b4v",
"4b4w",
"4cjx",
"5nhs",
"5o22",
"5o28",
"5o2a",
"5tc4",
"5zf1",
"6ape",
"6de8",
"6deb",
"6ecp",
"6ecq",
"6ecr",
"6jib"... | 54 | [
"PUB00000304",
"PUB00000651"
] | [
"2541774",
"8485162"
] | [
"Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme.",
"The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
] | [
1989,
1993
] | 2 | [] | [
"IPR035812"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
689,
28873,
13230,
23,
733
] | 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,
1,
26,
7,
1,
26,
10,
2,
11,
20,
3,
3,
19
] | 13 | true | Domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain | THF_DH/CycHdrlase_NAD-bd_dom | 6 |
IPR020633 | 20,633 | Thymidine kinase, conserved site | Thymidine_kinase_CS | Conserved_site | 12,227 | false | false | Thymidine kinase (TK) ( ) is an ubiquitous enzyme that catalyzes the ATP-dependent phosphorylation of thymidine. This entry represents a conserved site of thymidine kinase. | [
"GO:0004797",
"GO:0005524"
] | [
"thymidine kinase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00603"
] | [
"TK_CELLULAR_TYPE"
] | [
12227
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.21",
"PWY-7199",
"R-DDI-73614",
"R-GGA-73614",
"R-HSA-69205",
"R-HSA-73614",
"R-MMU-73614"
] | [
"EC:2.7.1.21",
"METACYC:PWY-7199",
"REACTOME:R-DDI-73614",
"REACTOME:R-GGA-73614",
"REACTOME:R-HSA-69205",
"REACTOME:R-HSA-73614",
"REACTOME:R-MMU-73614"
] | 7 | [
"1w4r",
"1xbt",
"1xx6",
"2b8t",
"2j87",
"2j9r",
"2ja1",
"2orv",
"2orw",
"2qpo",
"2qq0",
"2qqe",
"2uz3",
"2wvj",
"3e2i",
"4uxh",
"4uxi",
"4uxj",
"5fuv",
"5fuw",
"5fux",
"5fuy",
"8y7w",
"9k6k"
] | 24 | [
"PUB00005563",
"PUB00005572"
] | [
"3027984",
"2389555"
] | [
"Fowlpox virus thymidine kinase: nucleotide sequence and relationships to other thymidine kinases.",
"Sequence and evolutionary relationships of African swine fever virus thymidine kinase."
] | [
1987,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
218,
8804,
2429,
585,
191
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
7,
2,
1,
1,
5,
2,
5,
5,
4
] | 9 | true | Conserved_site | Thymidine kinase, conserved site | Thymidine kinase, conserved site | Thymidine_kinase_CS | 3 |
IPR020635 | 20,635 | Tyrosine-protein kinase, catalytic domain | Tyr_kinase_cat_dom | Domain | 161,148 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004713",
"GO:0006468"
] | [
"protein tyrosine kinase activity",
"protein phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"SMART"
] | [
"SM00219"
] | [
"TyrKc"
] | [
161148
] | 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... | [
"2.7.10",
"2.7.10.1",
"R-BTA-114604",
"R-BTA-1227986",
"R-BTA-1257604",
"R-BTA-1433557",
"R-BTA-1433559",
"R-BTA-180292",
"R-BTA-202427",
"R-BTA-202733",
"R-BTA-2029481",
"R-BTA-210990",
"R-BTA-210993",
"R-BTA-2424491",
"R-BTA-354192",
"R-BTA-373753",
"R-BTA-375165",
"R-BTA-389356"... | [
"EC:2.7.10",
"EC:2.7.10.1",
"REACTOME:R-BTA-114604",
"REACTOME:R-BTA-1227986",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1433557",
"REACTOME:R-BTA-1433559",
"REACTOME:R-BTA-180292",
"REACTOME:R-BTA-202427",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2029481",
"REACTOME:R-BTA-210990",
"REACTOME... | 1,314 | [
"1ad5",
"1agw",
"1byg",
"1fgi",
"1fgk",
"1fmk",
"1fpu",
"1fvr",
"1gag",
"1gjo",
"1i44",
"1iep",
"1ir3",
"1irk",
"1jpa",
"1jqh",
"1k2p",
"1k3a",
"1k9a",
"1ksw",
"1luf",
"1m14",
"1m17",
"1m52",
"1m7n",
"1mp8",
"1mqb",
"1oec",
"1opj",
"1p4o",
"1pkg",
"1qcf"... | 1,990 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005
] | 8 | [
"IPR001245"
] | [
"IPR028174",
"IPR035588",
"IPR035589",
"IPR042785"
] | 1 | 4 | 0 | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
1600,
159485,
51,
12
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
77,
101,
536,
313,
462,
298,
54,
376,
124
] | 9 | true | Domain | Tyrosine-protein kinase, catalytic domain | Tyrosine-protein kinase, catalytic domain | Tyr_kinase_cat_dom | 8 |
IPR020653 | 20,653 | Tryptophan-tRNA ligase, archaea | Tryptophan-tRNA-ligase_arc | Family | 762 | false | false | Tryptophan-tRNA ligases (also known as Tryptophanyl-tRNA synthetases) are widely distributed, being found in archaea, bacteria and eukaryotes. This entry represents an archaeal subgroup of the enzymes. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cogn... | [
"GO:0004830",
"GO:0005524",
"GO:0006436",
"GO:0005737"
] | [
"tryptophan-tRNA ligase activity",
"ATP binding",
"tryptophanyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP"
] | [
"MF_00140_A"
] | [
"Trp_tRNA_synth_A"
] | [
762
] | 1 | [
"EC"
] | [
"6.1.1.2"
] | [
"EC:6.1.1.2"
] | 1 | [
"3a04",
"3a05",
"3jxe"
] | 3 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00055442",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"11590011",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2001,
2000,
2002
] | 10 | [
"IPR002306"
] | [] | 1 | 0 | 1 | [
"Archaea",
"unclassified sequences"
] | [
759,
3
] | 2 | [] | [] | 0 | true | Family | Tryptophan-tRNA ligase, archaea | Tryptophan-tRNA ligase, archaea | Tryptophan-tRNA-ligase_arc | 7 |
IPR020667 | 20,667 | DNA mismatch repair protein, MutL | DNA_mismatch_repair_MutL | Family | 20,421 | false | false | Mismatch repair is one of five major DNA repair pathways, the others being homologous recombination repair, non-homologous end joining, nucleotide excision repair, and base excision repair. The mismatch repair system recognises and repairs mispaired or unpaired nucleotides that result from errors in DNA replication. Ma... | [
"GO:0006298"
] | [
"mismatch repair"
] | [
"biological_process"
] | 1 | [
"HAMAP"
] | [
"MF_00149"
] | [
"DNA_mis_repair"
] | [
20421
] | 1 | [] | [] | [] | 0 | [
"7p8v"
] | 1 | [
"PUB00014543",
"PUB00014545"
] | [
"12052432",
"12222686"
] | [
"DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: fail-safe protection against carcinogenesis.",
"DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers."
] | [
2002,
2002
] | 2 | [
"IPR002099"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
620,
19603,
31,
167
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | DNA mismatch repair protein, MutL | DNA mismatch repair protein, MutL | DNA_mismatch_repair_MutL | 3 |
IPR020672 | 20,672 | Ribose-5-phosphate isomerase, type A, subgroup | Ribose5P_isomerase_typA_subgr | Family | 16,178 | false | false | Ribose 5-phosphate isomerase, also known as phosphoriboisomerase, catalyses the reversible conversion of D-ribose 5-phosphate to D-ribulose 5-phosphate, the first step in the non-oxidative branch of the pentose phosphate pathway [ ]. This reaction enables ribose to be synthesized from sugars, as well as the recycling o... | [
"GO:0004751",
"GO:0009052"
] | [
"ribose-5-phosphate isomerase activity",
"pentose-phosphate shunt, non-oxidative branch"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00170"
] | [
"Rib_5P_isom_A"
] | [
16178
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.3.1.6",
"PWY-1861",
"PWY-5723",
"PWY-8178",
"R-DDI-71336",
"R-HSA-5659996",
"R-HSA-6791461",
"R-HSA-71336",
"R-MMU-71336"
] | [
"EC:5.3.1.6",
"METACYC:PWY-1861",
"METACYC:PWY-5723",
"METACYC:PWY-8178",
"REACTOME:R-DDI-71336",
"REACTOME:R-HSA-5659996",
"REACTOME:R-HSA-6791461",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-71336"
] | 9 | [
"1ks2",
"1lk5",
"1lk7",
"1lkz",
"1m0s",
"1o8b",
"1uj4",
"1uj5",
"1uj6",
"3enq",
"3env",
"3enw",
"3hhe",
"3ixq",
"3kwm",
"3l7o",
"3u7j",
"3uw1",
"4gmk",
"4io1",
"4m8l",
"4nml",
"4x84",
"5uf2",
"6eep",
"6j1k",
"6mc0",
"6zxt",
"7lda"
] | 29 | [
"PUB00020248",
"PUB00028856"
] | [
"12211039",
"12517338"
] | [
"Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli.",
"Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle."
] | [
2002,
2003
] | 2 | [
"IPR004788"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
685,
12718,
2633,
142
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
11,
1,
1,
1,
1,
6,
2,
9
] | 8 | true | Family | Ribose-5-phosphate isomerase, type A, subgroup | Ribose-5-phosphate isomerase, type A, subgroup | Ribose5P_isomerase_typA_subgr | 6 |
IPR020683 | 20,683 | Domain of unknown function DUF3447 | DUF3447 | Domain | 1,473 | false | false | This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is about 80 amino acids in length. This domain is found associated with [ ]. This domain has a conserved SHN sequence motif. It seems likely that this region represents divergent Ankyrin repeats. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF11929"
] | [
"DUF3447"
] | [
1473
] | 1 | [
"GP",
"GP"
] | [
"GenProp1352",
"GenProp1575"
] | [
"GP:GenProp1352",
"GP:GenProp1575"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Harvfovirus sp.",
"Parabasalia"
] | [
1,
1472
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF3447 | Domain of unknown function DUF3447 | DUF3447 | 6 |
IPR020684 | 20,684 | Rho-associated protein kinase 1/2 | ROCK1/ROCK2 | Family | 1,885 | false | false | Eukaryotic protein kinases [ , , , ] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. Rho kinases are serine/threonine kinases that are important in cell migration, cell proliferation and cell survival. ... | [
"GO:0004674",
"GO:0030036"
] | [
"protein serine/threonine kinase activity",
"actin cytoskeleton organization"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF037568"
] | [
"Rho_kinase"
] | [
1885
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.39",
"R-HSA-111465",
"R-HSA-3928662",
"R-HSA-3928663",
"R-HSA-416482",
"R-HSA-416572",
"R-HSA-4420097",
"R-HSA-5627117",
"R-HSA-6798695",
"R-HSA-8980692",
"R-HSA-9013026",
"R-HSA-9013106",
"R-HSA-9013407",
"R-HSA-9013422",
"R-HSA-9679191",
"R-HSA-9696264",
"R-MMU-111465",
"... | [
"EC:2.7.11.39",
"REACTOME:R-HSA-111465",
"REACTOME:R-HSA-3928662",
"REACTOME:R-HSA-3928663",
"REACTOME:R-HSA-416482",
"REACTOME:R-HSA-416572",
"REACTOME:R-HSA-4420097",
"REACTOME:R-HSA-5627117",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013026",
"REACTOME:R-HSA-90131... | 51 | [] | 0 | [
"PUB00001530",
"PUB00003568",
"PUB00003569",
"PUB00005115",
"PUB00035008",
"PUB00035531",
"PUB00035532"
] | [
"7768349",
"1835513",
"1956325",
"3291115",
"15864268",
"8772201",
"12832488"
] | [
"Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.",
"Protein kinase classification.",
"Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.",
"The ... | [
1995,
1991,
1991,
1988,
2005,
1996,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1885
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
3,
4,
3,
6
] | 5 | true | Family | Rho-associated protein kinase 1/2 | Rho-associated protein kinase 1/2 | ROCK1/ROCK2 | 9 |
IPR020708 | 20,708 | DNA-directed RNA polymerase, 14-18kDa subunit, conserved site | DNA-dir_RNA_polK_14-18kDa_CS | Conserved_site | 5,305 | false | false | DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase... | [
"GO:0003677",
"GO:0003899",
"GO:0006351"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS01111"
] | [
"RNA_POL_K_14KD"
] | [
5305
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-5250924",
"R-CEL-5578749",
"R-CEL-674695",
"R-CEL-6781823",
"R-CEL-6782135",
"R-CEL-6782210",
"R-CEL-6796648",
"R-CEL-6803529",
"R-CEL-6807505",
"R-CEL-72086",
"R-CEL-72163",
"R-CEL-72165",
"R-CEL-72203",
"R-CEL-73762",
"R-CEL-73772... | [
"EC:2.7.7.6",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-5578749",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6781823",
"REACTOME:R-CEL-6782135",
"REACTOME:R-CEL-6782210",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-6803529",
"REACTOME:R-CEL-6807505... | 216 | [
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1qkl",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 550 | [
"PUB00000061",
"PUB00002250",
"PUB00004425",
"PUB00033173"
] | [
"3052291",
"8045907",
"8332503",
"10499798"
] | [
"Structure and function of bacterial sigma factors.",
"Halobacterial S9 operon contains two genes encoding proteins homologous to subunits shared by eukaryotic RNA polymerases I, II, and III.",
"An African swine fever virus gene with a similarity to eukaryotic RNA polymerase subunit 6.",
"Crystal structure of... | [
1988,
1994,
1993,
1999
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Nucleocytoviricota",
"metagenomes"
] | [
566,
3,
4601,
17,
118
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
1,
2,
8,
4,
1,
8,
2,
1,
1,
7
] | 12 | true | Conserved_site | DNA-directed RNA polymerase, 14-18kDa subunit, conserved site | DNA-directed RNA polymerase, 14-18kDa subunit, conserved site | DNA-dir_RNA_polK_14-18kDa_CS | 4 |
IPR020717 | 20,717 | Apoptosis regulator, Bcl-2, BH1 motif, conserved site | Bcl2_BH1_motif_CS | Conserved_site | 3,928 | false | false | Active cell suicide (apoptosis) is induced by events such as growth factor withdrawal and toxins. It is controlled by regulators, which have either an inhibitory effect on programmed cell death (anti-apoptotic) or block the protective effect of inhibitors (pro-apoptotic) [ , ]. Many viruses have found a way of counteri... | [
"GO:0042981"
] | [
"regulation of apoptotic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01080"
] | [
"BH1"
] | [
3928
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111457",
"R-BTA-114294",
"R-BTA-5620971",
"R-BTA-6804114",
"R-CEL-111453",
"R-CEL-9648002",
"R-GGA-111453",
"R-GGA-844455",
"R-GGA-9648002",
"R-HSA-111447",
"R-HSA-111452",
"R-HSA-111453",
"R-HSA-111457",
"R-HSA-114294",
"R-HSA-5620971",
"R-HSA-6785807",
"R-HSA-6803204",
"R-... | [
"REACTOME:R-BTA-111457",
"REACTOME:R-BTA-114294",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-6804114",
"REACTOME:R-CEL-111453",
"REACTOME:R-CEL-9648002",
"REACTOME:R-GGA-111453",
"REACTOME:R-GGA-844455",
"REACTOME:R-GGA-9648002",
"REACTOME:R-HSA-111447",
"REACTOME:R-HSA-111452",
"REACTOME:R-HSA... | 46 | [
"1af3",
"1bxl",
"1f16",
"1g5j",
"1g5m",
"1gjh",
"1lxl",
"1maz",
"1mk3",
"1o0l",
"1pq0",
"1pq1",
"1r2d",
"1r2e",
"1r2g",
"1ty4",
"1wsx",
"1ysg",
"1ysi",
"1ysn",
"1ysw",
"1zy3",
"2b48",
"2bzw",
"2ims",
"2imt",
"2jcn",
"2jm6",
"2k7w",
"2kbw",
"2lp8",
"2lpc"... | 424 | [
"PUB00000008",
"PUB00001030",
"PUB00052462"
] | [
"8910675",
"15335822",
"8557188"
] | [
"Structure-function analysis of Bcl-2 family proteins. Regulators of programmed cell death.",
"A boom time for necrobiology.",
"Life, death, and the pursuit of apoptosis."
] | [
1996,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Metazoa",
"Viruses",
"bird metagenome"
] | [
3906,
21,
1
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
48,
34,
36
] | 5 | true | Conserved_site | Apoptosis regulator, Bcl-2, BH1 motif, conserved site | Apoptosis regulator, Bcl-2, BH1 motif, conserved site | Bcl2_BH1_motif_CS | 8 |
IPR020719 | 20,719 | RNA 3'-terminal phosphate cyclase-like, conserved site | RNA3'_term_phos_cycl-like_CS | Conserved_site | 6,196 | false | false | RNA cyclases are a family of RNA-modifying enzymes that are conserved in eukaryotes, bacteria and archaea. Type 1 RNA 3'-terminal phosphate cyclases ( ) [ , ] catalyse the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA: ATP + RNA 3'-terminal-phosphate = AMP + diphosphate + RNA terminal-2'... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01287"
] | [
"RTC"
] | [
6196
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.5.1.4",
"R-BTA-6791226",
"R-CEL-6791226",
"R-DDI-6791226",
"R-DME-6791226",
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"EC:6.5.1.4",
"REACTOME:R-BTA-6791226",
"REACTOME:R-CEL-6791226",
"REACTOME:R-DDI-6791226",
"REACTOME:R-DME-6791226",
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 10 | [
"1qmh",
"1qmi",
"3kgd",
"3pqv",
"3tut",
"3tux",
"3tv1",
"3tw3",
"4clq",
"4o89",
"4o8j",
"5jpq",
"5tzs",
"5wlc",
"5wyj",
"5wyk",
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6zqa",
"6zqb",
"6zqc",
"6zqd",
"6zqe",
"6zqf",
"6zqg",
"7ajt"... | 58 | [
"PUB00001300",
"PUB00003565",
"PUB00042947"
] | [
"9184239",
"2199762",
"10790377"
] | [
"The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea.",
"RNA 3'-terminal phosphate cyclase from HeLa cells.",
"Rcl1p, the yeast protein similar to the RNA 3'-phosphate cyclase, associates with U3 snoRNP and is required for 18S rRNA bioge... | [
1997,
1990,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
447,
724,
5014,
11
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (s... | [
5,
1,
2,
1,
1,
3,
10,
7,
7,
1,
1,
5
] | 12 | true | Conserved_site | RNA 3'-terminal phosphate cyclase-like, conserved site | RNA 3'-terminal phosphate cyclase-like, conserved site | RNA3'_term_phos_cycl-like_CS | 2 |
IPR020726 | 20,726 | Apoptosis regulator, Bcl-2, BH2 motif, conserved site | Bcl2_BH2_motif_CS | Conserved_site | 4,509 | false | false | Active cell suicide (apoptosis) is induced by events such as growth factor withdrawal and toxins. It is controlled by regulators, which have either an inhibitory effect on programmed cell death (anti-apoptotic) or block the protective effect of inhibitors (pro-apoptotic) [ , ]. Many viruses have found a way of counteri... | [
"GO:0042981"
] | [
"regulation of apoptotic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01258"
] | [
"BH2"
] | [
4509
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111457",
"R-BTA-114294",
"R-BTA-5620971",
"R-BTA-6804114",
"R-GGA-111453",
"R-GGA-844455",
"R-GGA-9648002",
"R-HSA-111447",
"R-HSA-111452",
"R-HSA-111453",
"R-HSA-111457",
"R-HSA-114294",
"R-HSA-5620971",
"R-HSA-6785807",
"R-HSA-6803204",
"R-HSA-6804114",
"R-HSA-844455",
"R-... | [
"REACTOME:R-BTA-111457",
"REACTOME:R-BTA-114294",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-6804114",
"REACTOME:R-GGA-111453",
"REACTOME:R-GGA-844455",
"REACTOME:R-GGA-9648002",
"REACTOME:R-HSA-111447",
"REACTOME:R-HSA-111452",
"REACTOME:R-HSA-111453",
"REACTOME:R-HSA-111457",
"REACTOME:R-HSA-... | 44 | [
"1af3",
"1bxl",
"1f16",
"1g5j",
"1g5m",
"1gjh",
"1lxl",
"1maz",
"1mk3",
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"1pq0",
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"1r2e",
"1r2g",
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"1ysw",
"1zy3",
"2b48",
"2bzw",
"2ims",
"2imt",
"2jcn",
"2jm6",
"2k7w",
"2kbw"... | 421 | [
"PUB00000008",
"PUB00001030",
"PUB00052462"
] | [
"8910675",
"15335822",
"8557188"
] | [
"Structure-function analysis of Bcl-2 family proteins. Regulators of programmed cell death.",
"A boom time for necrobiology.",
"Life, death, and the pursuit of apoptosis."
] | [
1996,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"Viruses",
"bioreactor metagenome"
] | [
180,
4250,
3,
74,
2
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
28,
22,
26
] | 4 | true | Conserved_site | Apoptosis regulator, Bcl-2, BH2 motif, conserved site | Apoptosis regulator, Bcl-2, BH2 motif, conserved site | Bcl2_BH2_motif_CS | 2 |
IPR020728 | 20,728 | Apoptosis regulator, Bcl-2, BH3 motif, conserved site | Bcl2_BH3_motif_CS | Conserved_site | 2,665 | false | false | Active cell suicide (apoptosis) is induced by events such as growth factor withdrawal and toxins. It is controlled by regulators, which have either an inhibitory effect on programmed cell death (anti-apoptotic) or block the protective effect of inhibitors (pro-apoptotic) [ , ]. Many viruses have found a way of counteri... | [
"GO:0042981"
] | [
"regulation of apoptotic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01259"
] | [
"BH3"
] | [
2665
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111457",
"R-BTA-114294",
"R-BTA-5620971",
"R-BTA-6804114",
"R-GGA-111453",
"R-GGA-844455",
"R-GGA-9648002",
"R-HSA-111447",
"R-HSA-111452",
"R-HSA-111453",
"R-HSA-111457",
"R-HSA-114294",
"R-HSA-5620971",
"R-HSA-6785807",
"R-HSA-6803204",
"R-HSA-6804114",
"R-HSA-75108",
"R-H... | [
"REACTOME:R-BTA-111457",
"REACTOME:R-BTA-114294",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-6804114",
"REACTOME:R-GGA-111453",
"REACTOME:R-GGA-844455",
"REACTOME:R-GGA-9648002",
"REACTOME:R-HSA-111447",
"REACTOME:R-HSA-111452",
"REACTOME:R-HSA-111453",
"REACTOME:R-HSA-111457",
"REACTOME:R-HSA-... | 47 | [
"1af3",
"1bxl",
"1ddb",
"1f16",
"1g5j",
"1g5m",
"1gjh",
"1lxl",
"1maz",
"1pq0",
"1pq1",
"1r2d",
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"2b48",
"2bid",
"2bzw",
"2ims",
"2imt",
"2jby",
"2jcn",
"2jm6",
"2k7w",
"2kbw",
"2l58",
"2lp8"... | 397 | [
"PUB00000008",
"PUB00001030",
"PUB00052462"
] | [
"8910675",
"15335822",
"8557188"
] | [
"Structure-function analysis of Bcl-2 family proteins. Regulators of programmed cell death.",
"A boom time for necrobiology.",
"Life, death, and the pursuit of apoptosis."
] | [
1996,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria",
"Podoviridae sp. ctzXp5"
] | [
6,
2658,
1
] | 3 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
44,
26,
30
] | 3 | true | Conserved_site | Apoptosis regulator, Bcl-2, BH3 motif, conserved site | Apoptosis regulator, Bcl-2, BH3 motif, conserved site | Bcl2_BH3_motif_CS | 1 |
IPR020731 | 20,731 | Apoptosis regulator, Bcl-2, BH4 motif, conserved site | Bcl2_BH4_motif_CS | Conserved_site | 1,365 | false | false | Active cell suicide (apoptosis) is induced by events such as growth factor withdrawal and toxins. It is controlled by regulators, which have either an inhibitory effect on programmed cell death (anti-apoptotic) or block the protective effect of inhibitors (pro-apoptotic) [ , ]. Many viruses have found a way of counteri... | [
"GO:0042981"
] | [
"regulation of apoptotic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS01260"
] | [
"BH4_1"
] | [
1365
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-111453",
"R-GGA-844455",
"R-GGA-9648002",
"R-HSA-111447",
"R-HSA-111453",
"R-HSA-6785807",
"R-HSA-844455",
"R-HSA-9018519",
"R-HSA-9634638",
"R-HSA-9648002",
"R-HSA-9692913",
"R-HSA-9702518",
"R-HSA-9818030",
"R-HSA-9824594",
"R-MMU-111447",
"R-MMU-111453",
"R-MMU-844455",
"... | [
"REACTOME:R-GGA-111453",
"REACTOME:R-GGA-844455",
"REACTOME:R-GGA-9648002",
"REACTOME:R-HSA-111447",
"REACTOME:R-HSA-111453",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-844455",
"REACTOME:R-HSA-9018519",
"REACTOME:R-HSA-9634638",
"REACTOME:R-HSA-9648002",
"REACTOME:R-HSA-9692913",
"REACTOME:R-H... | 21 | [
"1af3",
"1bxl",
"1g5j",
"1g5m",
"1gjh",
"1lxl",
"1maz",
"1mk3",
"1o0l",
"1pq0",
"1pq1",
"1r2d",
"1r2e",
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"1ysg",
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"1ysn",
"1ysw",
"1zy3",
"2b48",
"2bzw",
"2lp8",
"2lpc",
"2m03",
"2m04",
"2me8",
"2me9",
"2mej",
"2o1y",
"2o21"... | 168 | [
"PUB00000008",
"PUB00001030",
"PUB00052462"
] | [
"8910675",
"15335822",
"8557188"
] | [
"Structure-function analysis of Bcl-2 family proteins. Regulators of programmed cell death.",
"A boom time for necrobiology.",
"Life, death, and the pursuit of apoptosis."
] | [
1996,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Amniota"
] | [
1365
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
23,
14,
23
] | 3 | true | Conserved_site | Apoptosis regulator, Bcl-2, BH4 motif, conserved site | Apoptosis regulator, Bcl-2, BH4 motif, conserved site | Bcl2_BH4_motif_CS | 7 |
IPR020751 | 20,751 | Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2 | aa-tRNA-synth_I_codon-bd_sub2 | Homologous_superfamily | 39,525 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.10.350"
] | [
""
] | [
39525
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME"
] | [
"6.1.1",
"6.1.1.17",
"PWY-5188",
"R-HSA-379726"
] | [
"EC:6.1.1",
"EC:6.1.1.17",
"METACYC:PWY-5188",
"REACTOME:R-HSA-379726"
] | 4 | [
"1g59",
"1gln",
"1irx",
"1j09",
"1n75",
"1n77",
"1n78",
"2cfo",
"2cuz",
"2cv0",
"2cv1",
"2cv2",
"2dxi",
"2ja2",
"2o5r",
"3afh",
"3akz",
"3al0",
"3pnv",
"3pny",
"4g6z",
"4gri",
"5h4v",
"5tgt",
"6b1p",
"6b1z",
"6brl",
"7k86",
"8i9i",
"8jpv",
"8vc5",
"9y81"... | 33 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873",
"PUB00098804"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790",
"29305884"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002,
2018
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
816,
34322,
3671,
2,
714
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
4,
1,
6,
3,
1,
1,
1,
1,
2,
3,
1,
1,
12
] | 13 | true | Homologous_superfamily | Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2 | Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2 | aa-tRNA-synth_I_codon-bd_sub2 | 5 |
IPR020752 | 20,752 | Glutamate-tRNA synthetase, class I, anticodon-binding domain, subdomain 1 | Glu-tRNA-synth_I_codon-bd_sub1 | Homologous_superfamily | 6,515 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000049"
] | [
"tRNA binding"
] | [
"molecular_function"
] | 1 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.8.70"
] | [
""
] | [
6515
] | 1 | [
"EC",
"METACYC"
] | [
"6.1.1.17",
"PWY-5188"
] | [
"EC:6.1.1.17",
"METACYC:PWY-5188"
] | 2 | [
"1g59",
"1gln",
"1j09",
"1n75",
"1n77",
"1n78",
"2cfo",
"2cuz",
"2cv0",
"2cv1",
"2cv2",
"2dxi",
"2ja2",
"2o5r",
"3afh",
"3akz",
"3al0",
"3pnv",
"3pny",
"4gri"
] | 20 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873",
"PUB00098804"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790",
"29305884"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002,
2018
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
6304,
13,
198
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Glutamate-tRNA synthetase, class I, anticodon-binding domain, subdomain 1 | Glutamate-tRNA synthetase, class I, anticodon-binding domain, subdomain 1 | Glu-tRNA-synth_I_codon-bd_sub1 | 1 |
IPR020761 | 20,761 | Uncharacterised protein family UPF0114, bacteria | UPF0114_bac | Family | 5,717 | false | false | This conserved hypothetical protein family with four predicted transmembrane regions is found in Escherichia coli, Haemophilus influenzae, and Helicobacter pylori 26695, among completed genomes. This entry represents a group of uncharacterised proteins. | [] | [] | [] | 0 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00143",
"PTHR38596",
"TIGR00645"
] | [
"UPF0114",
"",
"HI0507"
] | [
5674,
5714,
5233
] | 3 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR005134"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Methanobrevibacter",
"unclassified sequences"
] | [
5589,
3,
9,
2,
114
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Uncharacterised protein family UPF0114, bacteria | Uncharacterised protein family UPF0114, bacteria | UPF0114_bac | 5 |
IPR020775 | 20,775 | Tyrosine-protein kinase, non-receptor Jak3 | Tyr_kinase_non-rcpt_Jak3 | Family | 350 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004715",
"GO:0005524",
"GO:0006468",
"GO:0035556",
"GO:0016020"
] | [
"non-membrane spanning protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"intracellular signal transduction",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR01826"
] | [
"JANUSKINASE3"
] | [
350
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.2",
"R-HSA-1266695",
"R-HSA-201556",
"R-HSA-5673001",
"R-HSA-6785807",
"R-HSA-8854691",
"R-HSA-8983432",
"R-HSA-8985947",
"R-HSA-9020558",
"R-HSA-9020958",
"R-HSA-912526",
"R-HSA-9679191",
"R-MMU-1266695",
"R-MMU-201556",
"R-MMU-5673001",
"R-MMU-6785807",
"R-MMU-8854691",
"... | [
"EC:2.7.10.2",
"REACTOME:R-HSA-1266695",
"REACTOME:R-HSA-201556",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-8854691",
"REACTOME:R-HSA-8983432",
"REACTOME:R-HSA-8985947",
"REACTOME:R-HSA-9020558",
"REACTOME:R-HSA-9020958",
"REACTOME:R-HSA-912526",
"REACTOME:R-HSA-96791... | 32 | [] | 0 | [
"PUB00005115",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052425",
"PUB00052556"
] | [
"3291115",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350",
"19290934",
"18045056"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein kinase complement of the human genome.",
"High-throughput structural biology in drug discovery: protein kinases.",
"Creating chemical dive... | [
1988,
2002,
2002,
2004,
2004,
2009,
2006,
2005,
2009,
2007
] | 10 | [
"IPR016251"
] | [] | 1 | 0 | 1 | [
"Amniota"
] | [
350
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
3,
2
] | 3 | true | Family | Tyrosine-protein kinase, non-receptor Jak3 | Tyrosine-protein kinase, non-receptor Jak3 | Tyr_kinase_non-rcpt_Jak3 | 6 |
IPR020776 | 20,776 | Tyrosine-protein kinase, non-receptor Jak1 | Tyr_kinase_non-rcpt_Jak1 | Family | 1,484 | false | false | Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra... | [
"GO:0004715",
"GO:0005524",
"GO:0006468",
"GO:0035556",
"GO:0016020"
] | [
"non-membrane spanning protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"intracellular signal transduction",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR01824"
] | [
"JANUSKINASE1"
] | [
1484
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.2",
"R-DRE-1059683",
"R-DRE-110056",
"R-DRE-112411",
"R-DRE-6783783",
"R-DRE-6788467",
"R-DRE-877300",
"R-DRE-877312",
"R-DRE-8854691",
"R-DRE-8985947",
"R-DRE-9020958",
"R-HSA-1059683",
"R-HSA-110056",
"R-HSA-112411",
"R-HSA-1169408",
"R-HSA-1266695",
"R-HSA-449836",
"R-HS... | [
"EC:2.7.10.2",
"REACTOME:R-DRE-1059683",
"REACTOME:R-DRE-110056",
"REACTOME:R-DRE-112411",
"REACTOME:R-DRE-6783783",
"REACTOME:R-DRE-6788467",
"REACTOME:R-DRE-877300",
"REACTOME:R-DRE-877312",
"REACTOME:R-DRE-8854691",
"REACTOME:R-DRE-8985947",
"REACTOME:R-DRE-9020958",
"REACTOME:R-HSA-1059683... | 65 | [
"5ixd",
"5ixi",
"5l04",
"7t6f",
"8ewy"
] | 5 | [
"PUB00005115",
"PUB00013869",
"PUB00015362",
"PUB00020114",
"PUB00034898",
"PUB00034899",
"PUB00052410",
"PUB00052411",
"PUB00052412",
"PUB00052425",
"PUB00100478",
"PUB00100479",
"PUB00100480",
"PUB00100481"
] | [
"3291115",
"1848670",
"12368087",
"12471243",
"15078142",
"15320712",
"19275641",
"16700535",
"15845350",
"19290934",
"12133952",
"11909529",
"32750333",
"16239216"
] | [
"The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase.",
"Evolution of protein kinase signaling from yeast to man.",
"The protein... | [
1988,
1991,
2002,
2002,
2004,
2004,
2009,
2006,
2005,
2009,
2002,
2002,
2020,
2005
] | 14 | [
"IPR016251"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1484
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
9,
4,
3
] | 4 | true | Family | Tyrosine-protein kinase, non-receptor Jak1 | Tyrosine-protein kinase, non-receptor Jak1 | Tyr_kinase_non-rcpt_Jak1 | 4 |
IPR020777 | 20,777 | Growth factor receptor NTRK | NTRK | Family | 4,070 | false | false | Neurotrophins are a family of secreted proteins that regulate development, maintenance and function of vertebrate nervous systems. They act via two different classes of receptor: p75NTR (a member of the TNF receptor superfamily), and neurotrophic tyrosine kinase receptors (NTRKs) - also known as tropomyosin-related kin... | [
"GO:0004714",
"GO:0005524",
"GO:0006468",
"GO:0007169",
"GO:0005886"
] | [
"transmembrane receptor protein tyrosine kinase activity",
"ATP binding",
"protein phosphorylation",
"cell surface receptor protein tyrosine kinase signaling pathway",
"plasma membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR01939"
] | [
"NTKRECEPTOR"
] | [
4070
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.10.1",
"R-GGA-1257604",
"R-GGA-388844",
"R-GGA-6811558",
"R-GGA-9026527",
"R-GGA-9028731",
"R-GGA-9032759",
"R-GGA-9034013",
"R-GGA-9034793",
"R-GGA-9603381",
"R-HSA-1257604",
"R-HSA-167021",
"R-HSA-167044",
"R-HSA-170968",
"R-HSA-170984",
"R-HSA-177504",
"R-HSA-187024",
"R-HS... | [
"EC:2.7.10.1",
"REACTOME:R-GGA-1257604",
"REACTOME:R-GGA-388844",
"REACTOME:R-GGA-6811558",
"REACTOME:R-GGA-9026527",
"REACTOME:R-GGA-9028731",
"REACTOME:R-GGA-9032759",
"REACTOME:R-GGA-9034013",
"REACTOME:R-GGA-9034793",
"REACTOME:R-GGA-9603381",
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-1670... | 68 | [
"2ifg",
"4pbv",
"4pbw",
"7n3t"
] | 4 | [
"PUB00046048",
"PUB00046049"
] | [
"7605062",
"11520916"
] | [
"Functional interactions of neurotrophins and neurotrophin receptors.",
"Neurotrophins: roles in neuronal development and function."
] | [
1995,
2001
] | 2 | [] | [
"IPR020446",
"IPR020455",
"IPR020461"
] | 0 | 3 | 0 | [
"Bilateria"
] | [
4070
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
29,
11,
15
] | 4 | true | Family | Growth factor receptor NTRK | Growth factor receptor NTRK | NTRK | 8 |
IPR020779 | 20,779 | dNTP triphosphohydrolase, type 1 | dNTPase_1 | Family | 1,976 | false | false | This entry represents a subgroup of dNTP triphosphohydrolases mostly from gamma-proteobacteria. Proteins in this entry include dGTPase from E. coli and PA1124 ( ) from Pseudomonas aeruginosa. They are triphosphohydrolases that have a preference for dGTP [ ]. | [
"GO:0000287",
"GO:0008832",
"GO:0006203"
] | [
"magnesium ion binding",
"dGTPase activity",
"dGTP catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00030",
"NF003429"
] | [
"dGTPase_type1",
"PRK04926.1"
] | [
1646,
1975
] | 2 | [
"EC"
] | [
"3.1.5.1"
] | [
"EC:3.1.5.1"
] | 1 | [
"4x9e",
"4xds",
"6oi7",
"6oiv",
"6oiw",
"6oix",
"6oiy",
"7u65",
"7u66",
"7u67",
"7w1f"
] | 11 | [
"PUB00083218",
"PUB00083224"
] | [
"19438719",
"25694425"
] | [
"Two dNTP triphosphohydrolases from Pseudomonas aeruginosa possess diverse substrate specificities.",
"Structure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules."
] | [
2009,
2015
] | 2 | [
"IPR006261"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Bracon brevicornis",
"metagenomes"
] | [
1971,
1,
4
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | dNTP triphosphohydrolase, type 1 | dNTP triphosphohydrolase, type 1 | dNTPase_1 | 5 |
IPR020783 | 20,783 | Large ribosomal subunit protein uL11, C-terminal | Ribosomal_uL11_C | Domain | 36,172 | false | false | This entry represents the C-terminal domain of uL11. The domain consists of a three-helical bundle and a short parallel two-stranded β-ribbon, with an overall α3-β4-α4-α5-β5 topology. All five secondary structure elements contribute to a conserved hydrophobic core. The domain is characterised by two extended loops that... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00298"
] | [
"Ribosomal_L11"
] | [
36172
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-BTA-9937383",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-5389840",
"R-CEL-5419276",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-BTA-9937383",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-... | 84 | [
"1aci",
"1c04",
"1eg0",
"1fow",
"1fox",
"1foy",
"1hc8",
"1jqm",
"1jqs",
"1jqt",
"1mj1",
"1ml5",
"1mms",
"1mvr",
"1nkw",
"1nwx",
"1nwy",
"1oln",
"1pn7",
"1pn8",
"1qa6",
"1r2w",
"1r2x",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk"... | 894 | [
"PUB00000269",
"PUB00004378",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00022183",
"PUB00042066",
"PUB00050356",
"PUB00051026"
] | [
"2483975",
"2167467",
"11297922",
"11290319",
"11114498",
"10338213",
"17215866",
"18406324",
"18611379"
] | [
"Structural properties of ribosomal protein L11 from Escherichia coli.",
"The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end ... | [
1989,
1990,
2001,
2001,
2000,
1999,
2007,
2008,
2008
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
912,
23511,
11261,
488
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
16,
2,
4,
3,
1,
6,
7,
2,
10,
11,
3,
3,
26
] | 13 | true | Domain | Large ribosomal subunit protein uL11, C-terminal | Large ribosomal subunit protein uL11, C-terminal | Ribosomal_uL11_C | 9 |
IPR020785 | 20,785 | Large ribosomal subunit protein uL11, conserved site | Ribosomal_uL11_CS | Conserved_site | 23,496 | false | false | This entry identifies a conserved region located in the C-terminal section of these proteins. Ribosomal protein uL11 (also known as L12 in mammals and yeast) is one of the proteins from the large ribosomal subunit. In Escherichia coli, uL11 is known to bind directly to the 23S rRNA and plays a significant role during i... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE"
] | [
"PS00359"
] | [
"RIBOSOMAL_L11"
] | [
23496
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CFA-156827",
"R-CFA-1799339",
"R-CFA-6791226",
"R-CFA-72689",
"R-CFA-727... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 59 | [
"1aci",
"1fow",
"1fox",
"1foy",
"1hc8",
"1mj1",
"1ml5",
"1mms",
"1mvr",
"1nkw",
"1nwx",
"1nwy",
"1oln",
"1r2w",
"1r2x",
"1s72",
"1sm1",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1xbp",
"1y39",
"1yhq"... | 754 | [
"PUB00000269",
"PUB00004378",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00022183",
"PUB00042066",
"PUB00050356",
"PUB00051026"
] | [
"2483975",
"2167467",
"11297922",
"11290319",
"11114498",
"10338213",
"17215866",
"18406324",
"18611379"
] | [
"Structural properties of ribosomal protein L11 from Escherichia coli.",
"The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end ... | [
1989,
1990,
2001,
2001,
2000,
1999,
2007,
2008,
2008
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
672,
16417,
6178,
229
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (s... | [
13,
1,
4,
2,
1,
3,
4,
8,
8,
2,
2,
25
] | 12 | true | Conserved_site | Large ribosomal subunit protein uL11, conserved site | Large ribosomal subunit protein uL11, conserved site | Ribosomal_uL11_CS | 5 |
IPR020787 | 20,787 | Ribonuclease HII, archaea | RNase_HII_arc | Family | 731 | false | false | Ribonuclease HII is an endonuclease that specifically degrades the RNA of RNA-DNA hybrids via cleavage of the 5'-phosphomonoester. This entry contains proteins restricted to the archaea. | [
"GO:0004523",
"GO:0030145",
"GO:0006401",
"GO:0005737"
] | [
"RNA-DNA hybrid ribonuclease activity",
"manganese ion binding",
"RNA catabolic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP"
] | [
"MF_00052_A"
] | [
"RNase_HII_A"
] | [
731
] | 1 | [
"EC"
] | [
"3.1.26.4"
] | [
"EC:3.1.26.4"
] | 1 | [
"1eke",
"1i39",
"1i3a",
"1io2",
"1uax",
"1x1p",
"2dfe",
"2dff",
"2dfh",
"3p83"
] | 10 | [] | [] | [] | [] | 0 | [
"IPR004649"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
711,
8,
12
] | 3 | [] | [] | 0 | true | Family | Ribonuclease HII, archaea | Ribonuclease HII, archaea | RNase_HII_arc | 9 |
IPR020789 | 20,789 | RNA polymerases, subunit N, zinc binding site | RNA_pol_suN_Zn-BS | Binding_site | 4,382 | false | false | In eukaryotes, there are three different forms of DNA-dependent RNA polymerases ( ) transcribing different sets of genes. Each class of RNA polymerase is an assemblage of ten to twelve different polypeptides. In archaebacteria, there is generally a single form of RNA polymerase which also consists of an oligomeric asse... | [
"GO:0003677",
"GO:0003899",
"GO:0008270",
"GO:0006351"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"zinc ion binding",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PROSITE"
] | [
"PS01112"
] | [
"RNA_POL_N_8KD"
] | [
4382
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.6",
"R-BTA-112382",
"R-BTA-113418",
"R-BTA-5250924",
"R-BTA-5578749",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6803529",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-72165",
"R-BTA-72203",
"R-BTA-73762",
"R-BTA-73772... | [
"EC:2.7.7.6",
"REACTOME:R-BTA-112382",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-5578749",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-6803529",
"REACTOME:R-BTA-6807505... | 216 | [
"1ef4",
"1i3q",
"1i50",
"1i6h",
"1k83",
"1nik",
"1nt9",
"1pqv",
"1r5u",
"1r9s",
"1r9t",
"1sfo",
"1twa",
"1twc",
"1twf",
"1twg",
"1twh",
"1wcm",
"1y1v",
"1y1w",
"1y1y",
"1y77",
"2b63",
"2b8k",
"2e2h",
"2e2i",
"2e2j",
"2ja5",
"2ja6",
"2ja7",
"2ja8",
"2nvq"... | 546 | [
"PUB00002250",
"PUB00004866",
"PUB00015096",
"PUB00015097"
] | [
"8045907",
"7597027",
"10841539",
"11831707"
] | [
"Halobacterial S9 operon contains two genes encoding proteins homologous to subunits shared by eukaryotic RNA polymerases I, II, and III.",
"Transcription in archaea: similarity to that in eucarya.",
"Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum."... | [
1994,
1995,
2000,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
795,
11,
3393,
30,
153
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
1,
2,
1,
1,
1,
5,
4,
1,
1,
10
] | 12 | true | Binding_site | RNA polymerases, subunit N, zinc binding site | RNA polymerases, subunit N, zinc binding site | RNA_pol_suN_Zn-BS | 1 |
IPR020791 | 20,791 | Leucine-tRNA ligase, archaeal | Leu-tRNA-lgase_arc | Family | 672 | false | false | Leucine tRNA ligase ( ) is an alpha monomer that belongs to class Ia. This entry represents a group of leucine tRNA ligases found only in Archaea. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific tw... | [
"GO:0000166",
"GO:0004823",
"GO:0005524",
"GO:0006429",
"GO:0005737"
] | [
"nucleotide binding",
"leucine-tRNA ligase activity",
"ATP binding",
"leucyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"HAMAP"
] | [
"MF_00049_A"
] | [
"Leu_tRNA_synth_A"
] | [
672
] | 1 | [
"EC"
] | [
"6.1.1.4"
] | [
"EC:6.1.1.4"
] | 1 | [
"1wkb",
"1wz2"
] | 2 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [
"IPR004493"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Candidatus Rhodobacter oscarellae",
"Geodia barretti",
"ecological metagenomes"
] | [
663,
1,
1,
7
] | 4 | [] | [] | 0 | true | Family | Leucine-tRNA ligase, archaeal | Leucine-tRNA ligase, archaeal | Leu-tRNA-lgase_arc | 6 |
IPR020792 | 20,792 | Sulphate adenylyltransferase, prokaryotic-type | SO4_adenylyltransferase_pro | Family | 2,835 | false | false | ATP-sulfurylase catalyses a key reaction in the global sulfur cycle by reversibly converting inorganic sulfate with ATP to adenosine 5'-phosphosulfate (APS) and pyrophosphate (PPi) [ ]. This entry consists of sulphate adenylyltransferase or ATP-sulfurylase ( ), mainly from prokaryotes. It also includes ATP-sulfurylase ... | [
"GO:0004781",
"GO:0000103"
] | [
"sulfate adenylyltransferase (ATP) activity",
"sulfate assimilation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00066"
] | [
"Sulf_adenylyltr"
] | [
2835
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.4",
"PWY-5278",
"PWY-5340",
"PWY-6683",
"PWY-6932"
] | [
"EC:2.7.7.4",
"METACYC:PWY-5278",
"METACYC:PWY-5340",
"METACYC:PWY-6683",
"METACYC:PWY-6932"
] | 5 | [
"1jhd",
"2gks",
"4dnx",
"8a8d",
"8a8g"
] | 5 | [
"PUB00072996",
"PUB00072997"
] | [
"9920405",
"24073218"
] | [
"Cloning and bacterial expression of adenosine-5'-triphosphate sulfurylase from the enteric protozoan parasite Entamoeba histolytica.",
"Structural, biochemical and genetic characterization of dissimilatory ATP sulfurylase from Allochromatium vinosum."
] | [
1998,
2013
] | 2 | [
"IPR002650"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
145,
2618,
15,
57
] | 4 | [] | [] | 0 | true | Family | Sulphate adenylyltransferase, prokaryotic-type | Sulphate adenylyltransferase, prokaryotic-type | SO4_adenylyltransferase_pro | 5 |
IPR020795 | 20,795 | Origin recognition complex, subunit 3 | ORC3 | Family | 4,764 | false | false | The Origin Recognition Complex (ORC) is a six-subunit ATP-dependent DNA-binding complex encoded by ORC1-6 [ ]. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle [ ]. ORC directs DNA replication throughout the genome and is required for its in... | [
"GO:0003677",
"GO:0006260",
"GO:0005664"
] | [
"DNA binding",
"DNA replication",
"nuclear origin of replication recognition complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER"
] | [
"PTHR12748"
] | [
""
] | [
4764
] | 1 | [
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"R-MMU-68949",
"R-MMU-68962",
"R-RNO-176187",
"R-RNO-68616",
"R-RNO-68689",
"R-RNO... | [
"REACTOME:R-DDI-68616",
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"REACTOME:R-HSA-113507",
"REACTOME:R-HSA-176187",
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"REACTOME:R-HSA-68867",
"REACTOME:R-HSA-68949",
"REACTOME:R-HSA-68962",
"REACTOME:R-MMU-176187",
"REACTOME:R-MMU-68616",
"... | 29 | [
"4xgc",
"5uj8",
"5ujm",
"5v8f",
"5zr1",
"6rqc",
"6wgc",
"6wgg",
"6wgi",
"7cte",
"7ctf",
"7ctg",
"7jgr",
"7jgs",
"7jk2",
"7jk3",
"7jk4",
"7jk5",
"7jk6",
"7jpo",
"7jpp",
"7jpq",
"7jpr",
"7jps",
"7mca",
"7tjf",
"7tjh",
"7tji",
"7tjj",
"7tjk",
"8rwv",
"8s0c"... | 43 | [
"PUB00052559",
"PUB00052560",
"PUB00052561",
"PUB00052562",
"PUB00052563",
"PUB00052564",
"PUB00052565",
"PUB00052566",
"PUB00052567",
"PUB00052568",
"PUB00052569",
"PUB00052570",
"PUB00052571",
"PUB00052572",
"PUB00052573",
"PUB00052574",
"PUB00052575",
"PUB00052576",
"PUB000525... | [
"17241905",
"17825065",
"1579162",
"7585959",
"16716188",
"7892251",
"7781615",
"16228006",
"10966477",
"12045100",
"15680967",
"11572976",
"11429609",
"16024805",
"8622770",
"9171055",
"9038340",
"11459976",
"15610739",
"16387651",
"17053779",
"9442876",
"31160578",
"3... | [
"Multiple functions of the origin recognition complex.",
"Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.",
"ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex.... | [
2007,
2007,
1992,
1995,
2006,
1995,
1995,
2005,
2000,
2002,
2005,
2001,
2001,
2005,
1996,
1997,
1997,
2001,
2004,
2006,
2006,
1997,
2019,
2020
] | 24 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4764
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
3,
1,
3,
7,
3,
1,
1,
6,
1,
1,
4
] | 11 | true | Family | Origin recognition complex, subunit 3 | Origin recognition complex, subunit 3 | ORC3 | 9 |
IPR020796 | 20,796 | Origin recognition complex, subunit 5 | ORC5 | Family | 4,586 | false | false | The Origin Recognition Complex (ORC) is a six-subunit ATP-dependent DNA-binding complex encoded by ORC1-6 [ ]. ORC is a central component for eukaryotic DNA replication, and binds chromatin at replication origins throughout the cell cycle [ ]. ORC directs DNA replication throughout the genome and is required for its in... | [
"GO:0006260",
"GO:0000808",
"GO:0005634"
] | [
"DNA replication",
"origin recognition complex",
"nucleus"
] | [
"biological_process",
"cellular_component",
"cellular_component"
] | 3 | [
"PANTHER"
] | [
"PTHR12705"
] | [
""
] | [
4586
] | 1 | [
"REACTOME",
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"R-HSA-68949",
"R-HSA-68962",
"R-MMU-176187",
"R-MMU-68616",
"R-MMU-68689",
"R-MMU... | [
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"REACTOME:R-DDI-68962",
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"REACTOME:R-DME-68616",
"REACTOME:R-DME-68689",
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"REACTOME:R-HSA-113507",
"REACTOME:R-HSA-176187",
"REACTOME:R-HSA-68616",
"REACTOME:R-HSA-68689",
"... | 29 | [
"4xgc",
"5uj7",
"5ujm",
"5v8f",
"5zr1",
"6rqc",
"6wgc",
"6wgg",
"6wgi",
"7cte",
"7ctf",
"7ctg",
"7jgr",
"7jgs",
"7jk2",
"7jk3",
"7jk4",
"7jk5",
"7jk6",
"7jpo",
"7jpp",
"7jpq",
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"7jps",
"7mca",
"7tjf",
"7tjh",
"7tji",
"7tjj",
"7tjk",
"8rwv",
"8s0c"... | 43 | [
"PUB00052559",
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"PUB00052574",
"PUB00052575",
"PUB00052576",
"PUB000525... | [
"17241905",
"17825065",
"1579162",
"7585959",
"16716188",
"7892251",
"7781615",
"16228006",
"10966477",
"12045100",
"15680967",
"11572976",
"11429609",
"16024805",
"8622770",
"9171055",
"9038340",
"11459976",
"15610739",
"16387651",
"17053779",
"9442876",
"31160578",
"3... | [
"Multiple functions of the origin recognition complex.",
"Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.",
"ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex.... | [
2007,
2007,
1992,
1995,
2006,
1995,
1995,
2005,
2000,
2002,
2005,
2001,
2001,
2005,
1996,
1997,
1997,
2001,
2004,
2006,
2006,
1997,
2019,
2020
] | 24 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1)"
] | [
4585,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
13,
1,
8,
2,
1,
1,
4,
1,
1,
7
] | 12 | true | Family | Origin recognition complex, subunit 5 | Origin recognition complex, subunit 5 | ORC5 | 9 |
IPR020797 | 20,797 | Cytidine deaminase, bacteria | Cytidine_deaminase_bacteria | Family | 2,006 | false | false | This family represents the homodimeric form of cytidine deaminase, a zinc metalloprotein. Cytidine deaminase scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. This entry contains predominantly bacterial proteins. | [
"GO:0004126",
"GO:0008270"
] | [
"cytidine deaminase activity",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP"
] | [
"MF_01558"
] | [
"Cyt_deam"
] | [
2006
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.5.4.5",
"PWY-6556",
"PWY-7181",
"PWY-7193",
"PWY-7199"
] | [
"EC:3.5.4.5",
"METACYC:PWY-6556",
"METACYC:PWY-7181",
"METACYC:PWY-7193",
"METACYC:PWY-7199"
] | 5 | [
"1af2",
"1aln",
"1ctt",
"1ctu",
"4eg2",
"6k63"
] | 6 | [] | [] | [] | [] | 0 | [
"IPR006263"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
2003,
3
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Cytidine deaminase, bacteria | Cytidine deaminase, bacteria | Cytidine_deaminase_bacteria | 6 |
IPR020798 | 20,798 | Large ribosomal subunit protein uL16, conserved site | Ribosomal_uL16_CS | Conserved_site | 40,595 | false | false | Ribosomal protein uL16 is one of the proteins from the large ribosomal subunit from bacteria and its homologues from chloroplast and mitochondria. In Escherichia coli, uL16 is known to bind directly the 23S rRNA and to be located at the A site of the peptidyltransferase centre. uL16 is a protein of 133 to 185 amino-aci... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00586",
"PS00701"
] | [
"RIBOSOMAL_L16_1",
"RIBOSOMAL_L16_2"
] | [
35081,
37272
] | 2 | [] | [] | [] | 0 | [
"1njm",
"1njp",
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1xbp",
"1y69",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3j5l",
"3j6b",
"3j7z",
"3j8g",
"3j9w",
"3j9y",
"3j9z",
"3ja1",
"3jbu",
"3jbv",
"3jcd",
"3jce",
"3jcj",
"3jcn",
"3pio",
"3pip"... | 811 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
22428,
17776,
391
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
13,
1,
1,
7,
1,
1,
5
] | 7 | true | Conserved_site | Large ribosomal subunit protein uL16, conserved site | Large ribosomal subunit protein uL16, conserved site | Ribosomal_uL16_CS | 3 |
IPR020799 | 20,799 | A-kinase anchor 110kDa | AKAP_110 | Family | 656 | false | false | This family consists of several mammalian protein kinase A anchoring protein 3 (PRKA3) or A-kinase anchor protein 110kDa (AKAP 110) sequences. Agents that increase intracellular cAMP are potent stimulators of sperm motility. Anchoring inhibitor peptides, designed to disrupt the interaction of the cAMP-dependent protein... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00807"
] | [
"AKAP_110"
] | [
656
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00011239"
] | [
"10319321"
] | [
"Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein."
] | [
1999
] | 1 | [
"IPR008382"
] | [] | 1 | 0 | 1 | [
"Amniota"
] | [
656
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
6
] | 3 | true | Family | A-kinase anchor 110kDa | A-kinase anchor 110kDa | AKAP_110 | 6 |
IPR020802 | 20,802 | Thioesterase TesA-like | TesA-like | Domain | 21,257 | false | false | Thioesterase domains often occur integrated in or associated with peptide synthetases which are involved in the non-ribosomal synthesis of peptide antibiotics [ ]. Thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Next to the operons encod... | [
"GO:0009058"
] | [
"biosynthetic process"
] | [
"biological_process"
] | 1 | [
"SMART"
] | [
"SM00824"
] | [
"PKS_TE"
] | [
21257
] | 1 | [] | [] | [] | 0 | [
"1kez",
"1mn6",
"1mna",
"1mnq",
"1mo2",
"2h7x",
"2h7y",
"2hfj",
"2hfk",
"2roq",
"3fla",
"3lcr",
"3qmv",
"3qmw",
"3tej",
"4zxh",
"4zxi",
"5d3k",
"5d3z",
"5ja1",
"5ja2",
"5t3d",
"6ecb",
"6ecc",
"6ecd",
"6ece",
"6ecf",
"6fvj",
"6fw5",
"6mlk",
"6n8e",
"6vap"... | 52 | [
"PUB00000169"
] | [
"9560421"
] | [
"Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis."
] | [
1998
] | 1 | [
"IPR001031"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE)",
"unclassified sequences"
] | [
20458,
759,
1,
39
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Thioesterase TesA-like | Thioesterase TesA-like | TesA-like | 2 |
IPR020803 | 20,803 | Polyketide synthase-like, methyltransferase domain | MeTfrase_dom | Domain | 3,265 | false | false | Methyl transfer from the ubiquitous donor S-adenosyl-L-methionine (SAM) to either nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms ranging from bacteria to plants and mammals. The reaction is catalyzed by methyltransferases (Mtases) and modifies DNA, RNA, proteins and small molecules, such a... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00828"
] | [
"PKS_MT"
] | [
3265
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.1.1.-",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601",
"PWY-6045"... | [
"EC:2.1.1.-",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",
"METACYC:PWY-5... | 146 | [
"3bus",
"6ect",
"6ecu",
"6ecv",
"6ecw",
"6ecx",
"6hp1",
"6hp2",
"6uv6",
"6uvq",
"6uwd",
"8zc7",
"8zc8"
] | 13 | [
"PUB00158926",
"PUB00158927",
"PUB00158928"
] | [
"26630077",
"29914944",
"39105744"
] | [
"Parallel Post-Polyketide Synthase Modification Mechanism Involved in FD-891 Biosynthesis in Streptomyces graminofaciens A-8890.",
"Thailandamide, a Fatty Acid Synthesis Antibiotic That Is Coexpressed with a Resistant Target Gene.",
"Discovery of a Hybrid Molecule with Phytotoxic Activity by Genome Mining, Hete... | [
2016,
2018,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"unclassified sequences"
] | [
3067,
163,
12,
23
] | 4 | [
"Caenorhabditis elegans"
] | [
1
] | 1 | true | Domain | Polyketide synthase-like, methyltransferase domain | Polyketide synthase-like, methyltransferase domain | MeTfrase_dom | 3 |
IPR020806 | 20,806 | Polyketide synthase-like, phosphopantetheine-binding domain | PKS_PP-bd | Domain | 145,566 | false | false | This entry represents the phosphopantetheine-binding domain from polyketide synthases and related synthase proteins. Polyketide synthases are large multidomain proteins involved in the synthesis of secondary metabolites [ ]. Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier protei... | [
"GO:0031177"
] | [
"phosphopantetheine binding"
] | [
"molecular_function"
] | 1 | [
"SMART"
] | [
"SM00823"
] | [
"PKS_PP"
] | [
145566
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-163765",
"R-HSA-199220",
"R-HSA-2426168",
"R-HSA-75105",
"R-HSA-9029558",
"R-MMU-199220",
"R-MMU-75105",
"R-MTU-9635470",
"R-RNO-199220",
"R-RNO-75105"
] | [
"REACTOME:R-HSA-163765",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-2426168",
"REACTOME:R-HSA-75105",
"REACTOME:R-HSA-9029558",
"REACTOME:R-MMU-199220",
"REACTOME:R-MMU-75105",
"REACTOME:R-MTU-9635470",
"REACTOME:R-RNO-199220",
"REACTOME:R-RNO-75105"
] | 10 | [
"1dny",
"2afd",
"2afe",
"2ava",
"2cg5",
"2ehs",
"2eht",
"2fva",
"2fve",
"2fvf",
"2gdw",
"2gdx",
"2gdy",
"2jgp",
"2ju1",
"2ju2",
"2kr5",
"2l22",
"2liu",
"2liw",
"2md9",
"2mf4",
"2mr7",
"2mr8",
"2n57",
"2n98",
"2png",
"2vsq",
"2vz8",
"2vz9",
"2xz0",
"2xz1"... | 189 | [
"PUB00002372",
"PUB00007945",
"PUB00057835"
] | [
"5321311",
"11825906",
"15958783"
] | [
"Studies on the mechanism of fatty acid synthesis. XIV. The prosthetic group of acyl carrier protein and the mode of its attachment to the protein.",
"The solution structure of acyl carrier protein from Mycobacterium tuberculosis.",
"Evolutionary implications of bacterial polyketide synthases."
] | [
1965,
2002,
2005
] | 3 | [
"IPR009081"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Brevundimonas phage vB_BgoS-Bajun",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
106334,
1,
38966,
5,
260
] | 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,
4,
5,
10,
1,
2,
4,
10,
7,
3,
1,
2,
11
] | 13 | true | Domain | Polyketide synthase-like, phosphopantetheine-binding domain | Polyketide synthase-like, phosphopantetheine-binding domain | PKS_PP-bd | 7 |
IPR020807 | 20,807 | Polyketide/metazoan fatty acid synthase-like, dehydratase domain | PKS_DH | Domain | 40,973 | false | false | This entry represents the dehydratase domain (DH) found in polyketide synthases, fatty acid synthase and some nodulation proteins. The fundamental polymers of biology proteins, DNA, and RNA are products of repetitive condensation of simple amino acid or nucleotide building blocks and are comparatively easy to assemble.... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00826"
] | [
"PKS_DH"
] | [
40973
] | 1 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METAC... | [
"2.3.1",
"2.3.1.-",
"GenProp1220",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679"... | [
"EC:2.3.1",
"EC:2.3.1.-",
"GP:GenProp1220",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"ME... | 231 | [
"2vz8",
"2vz9",
"3el6",
"3kg6",
"3kg7",
"3kg8",
"3kg9",
"4ln9",
"4ooc",
"5bp2",
"5bp3",
"5bp4",
"5hqw",
"5hst",
"5hu7",
"5i0k",
"5il6",
"5j6o",
"5l84",
"5nji",
"5o15",
"5o16",
"5tz5",
"5tz6",
"5tz7",
"6b2v",
"6fn6",
"6k97",
"6mbf",
"6mbg",
"6mbh",
"6obt"... | 77 | [
"PUB00051727",
"PUB00055224",
"PUB00153277",
"PUB00153278",
"PUB00153279",
"PUB00160320",
"PUB00160321",
"PUB00160322"
] | [
"18952099",
"20152156",
"18772425",
"30137093",
"35618872",
"1595878",
"18663394",
"26689670"
] | [
"Crystal structure of the erythromycin polyketide synthase dehydratase.",
"Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway.",
"An enzyme assembly line",
"The architectures of iterative type I PKS and FAS.",
"The Streptomyces viridochromogenes product template domai... | [
2008,
2010,
2008,
2018,
2022,
1992,
2008,
2016
] | 8 | [] | [
"IPR049900"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
23262,
17678,
33
] | 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"
] | [
1,
8,
5,
2,
4,
6,
2
] | 7 | true | Domain | Polyketide/metazoan fatty acid synthase-like, dehydratase domain | Polyketide/metazoan fatty acid synthase-like, dehydratase domain | PKS_DH | 1 |
IPR020808 | 20,808 | Bacterial microcompartments protein, conserved site | Bact_microcomp_CS | Conserved_site | 6,628 | false | false | Bacterial microcompartments (BMCs) are large proteinaceous structures comprised of a roughly icosahedral shell and a series of encapsulated enzymes. The shells of BMCs are made primarily of a family of proteins whose structural core is the BMC domain, and variations upon this core provide functional diversity. This dom... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS01139"
] | [
"BMC_1"
] | [
6628
] | 1 | [] | [] | [] | 0 | [
"2a10",
"2a18",
"2a1b",
"2ewh",
"2g13",
"3bn4",
"3cim",
"3dn9",
"3dnc",
"3gv2",
"3h8y",
"3i6p",
"3mpw",
"3mpy",
"3ngk",
"3ssq",
"3ssr",
"3sss",
"4axj",
"4liw",
"4ox6",
"4ox7",
"4ox8",
"4qiv",
"5djb",
"5v74",
"6mzu",
"6mzv",
"6mzx",
"6mzy",
"6n06",
"6n07"... | 56 | [
"PUB00002263",
"PUB00009955",
"PUB00011184",
"PUB00013595",
"PUB00014337",
"PUB00014338",
"PUB00015063",
"PUB00015068",
"PUB00050993",
"PUB00051867",
"PUB00065414",
"PUB00096711",
"PUB00097502",
"PUB00097503",
"PUB00097504"
] | [
"7868611",
"10464203",
"10498708",
"11844753",
"15012219",
"9891798",
"11722879",
"14729686",
"18786396",
"19328811",
"20870711",
"33116131",
"30389783",
"25455419",
"30901520"
] | [
"Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster.",
"The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins.",
"The propanediol ut... | [
1995,
1999,
1999,
2002,
1999,
1998,
2001,
2004,
2008,
2009,
2010,
2020,
2019,
2015,
2019
] | 15 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6549,
11,
68
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Conserved_site | Bacterial microcompartments protein, conserved site | Bacterial microcompartments protein, conserved site | Bact_microcomp_CS | 8 |
IPR020809 | 20,809 | Enolase, conserved site | Enolase_CS | Conserved_site | 39,219 | false | false | This entry represents a conserved region located in the C-terminal third of the sequence. Enolase (2-phospho-D-glycerate hydrolase) is an essential glycolytic enzyme that catalyses the interconversion of 2-phosphoglycerate and phosphoenolpyruvate [ , ]. In vertebrates, there are 3 different, tissue-specific isoenzymes,... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00164"
] | [
"ENOLASE"
] | [
39219
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
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"METACYC",
"METACYC",
"METACYC",
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... | [
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"... | [
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"METACYC:PWY-7003",
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"METACYC:PWY-7218",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-B... | 37 | [
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"2pu0",
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"2xgz",
"2xh0",
"2xh2"... | 112 | [
"PUB00000466",
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"Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence.",
"Molecular structure of the human muscle-specific enolase gene (ENO3).",
"Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli.",
"Recruitment of enzymes... | [
1988,
1991,
1991,
1987
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
845,
25581,
12207,
1,
585
] | 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,
1,
8,
2,
1,
12,
12,
2,
19,
23,
5,
2,
33
] | 13 | true | Conserved_site | Enolase, conserved site | Enolase, conserved site | Enolase_CS | 3 |
IPR020810 | 20,810 | Enolase, C-terminal TIM barrel domain | Enolase_C | Domain | 49,561 | false | false | Enolase (2-phospho-D-glycerate hydrolase) is an essential, homodimeric enzyme that catalyses the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways [ , ]. The reaction is facilitated by the presence of metal ions [ ]. In vertebrates, there are 3... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00113",
"SM01192"
] | [
"Enolase_C",
"Enolase_C"
] | [
49505,
47546
] | 2 | [
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"METACYC",
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"REACTOME",
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... | [
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"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"... | [
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"METACYC:PWY-1042",
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"METACYC:PWY-2221",
"METACYC:PWY-5484",
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"METACYC:PWY-6142",
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"METACYC:PWY-7003",
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"METACYC:PWY-7218",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-B... | 41 | [
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"2xh2"... | 112 | [
"PUB00000466",
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"Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence.",
"Molecular structure of the human muscle-specific enolase gene (ENO3).",
"Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli.",
"Recruitment of enzymes... | [
1988,
1991,
1991,
1987,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
1038,
27395,
20327,
1,
800
] | 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,
1,
13,
2,
1,
23,
20,
2,
20,
33,
5,
2,
51
] | 13 | true | Domain | Enolase, C-terminal TIM barrel domain | Enolase, C-terminal TIM barrel domain | Enolase_C | 5 |
IPR020811 | 20,811 | Enolase, N-terminal | Enolase_N | Domain | 44,766 | false | false | Enolase (2-phospho-D-glycerate hydrolase) is an essential, homodimeric enzyme that catalyses the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways [ , ]. The reaction is facilitated by the presence of metal ions [ ]. In vertebrates, there are 3... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF03952",
"SM01193"
] | [
"Enolase_N",
"Enolase_N"
] | [
43460,
44375
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
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"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
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"PWY-1622",
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"PWY-5484",
"PWY-5723",
"PWY-6142",
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"PWY-6901",
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"PWY-7124",
"PWY-7218",
"PWY-8004",
"PWY-8404",
"R-BTA-70171",
"R-BTA-70263",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"... | [
"EC:4.2.1.11",
"METACYC:PWY-1042",
"METACYC:PWY-1622",
"METACYC:PWY-2221",
"METACYC:PWY-5484",
"METACYC:PWY-5723",
"METACYC:PWY-6142",
"METACYC:PWY-6886",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-7124",
"METACYC:PWY-7218",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-B... | 41 | [
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"1ebg",
"1ebh",
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"2pu0",
"2pu1",
"2xgz",
"2xh0",
"2xh2"... | 112 | [
"PUB00000466",
"PUB00000496",
"PUB00004545",
"PUB00005102",
"PUB00029502"
] | [
"3390159",
"1840492",
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"Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence.",
"Molecular structure of the human muscle-specific enolase gene (ENO3).",
"Characterization of a maize cDNA that complements an enolase-deficient mutant of Escherichia coli.",
"Recruitment of enzymes... | [
1988,
1991,
1991,
1987,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Streptococcus phage 20617",
"unclassified sequences"
] | [
1051,
26955,
16121,
1,
638
] | 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,
1,
13,
2,
1,
26,
24,
2,
16,
30,
5,
2,
36
] | 13 | true | Domain | Enolase, N-terminal | Enolase, N-terminal | Enolase_N | 2 |
IPR020814 | 20,814 | Small ribosomal subunit protein bS6, plastid/chloroplast | Ribosomal_S6_plastid/chlpt | Family | 25,588 | false | false | This entry represents the small ribosomal subunit protein bS6 family. The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). Ribosomal protein bS6 is one of the proteins from the small ribosomal subunit. [ ].... | [
"GO:0003735",
"GO:0019843",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"rRNA binding",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"CDD"
] | [
"MF_00360",
"cd00473"
] | [
"Ribosomal_bS6",
"bS6"
] | [
25308,
24119
] | 2 | [] | [] | [] | 0 | [
"1cqm",
"1cqn",
"1eg0",
"1fjg",
"1fka",
"1g1x",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
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"1i95",
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"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1lou",
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"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1qjh",
"1ris",
"1vmb",
"1vvj"... | 1,204 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00101116"
] | [
"11297922",
"11290319",
"11114498",
"18042701"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins."
] | [
2001,
2001,
2000,
2007
] | 4 | [
"IPR000529"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
23373,
1759,
1,
455
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
1,
7,
1,
5
] | 5 | true | Family | Small ribosomal subunit protein bS6, plastid/chloroplast | Small ribosomal subunit protein bS6, plastid/chloroplast | Ribosomal_S6_plastid/chlpt | 1 |
IPR020815 | 20,815 | Small ribosomal subunit protein bS6, conserved site | Ribosomal_bS6_CS | Conserved_site | 8,893 | false | false | This entry represents a conserved region located in the N-terminal section of the small ribosomal subunit protein bS6 family. The small subunits of bacterial and eukaryotic ribosomes have the same overall shapes (with structural elements described as head, body, platform, beak and shoulder). Ribosomal protein bS6 is on... | [
"GO:0003735",
"GO:0019843",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"rRNA binding",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PROSITE"
] | [
"PS01048"
] | [
"RIBOSOMAL_S6"
] | [
8893
] | 1 | [] | [] | [] | 0 | [
"1cqm",
"1cqn",
"1eg0",
"1fjg",
"1fka",
"1g1x",
"1hnw",
"1hnx",
"1hnz",
"1hr0",
"1i94",
"1i95",
"1i96",
"1i97",
"1ibk",
"1ibl",
"1ibm",
"1j5e",
"1jgo",
"1jgp",
"1jgq",
"1lou",
"1ml5",
"1n32",
"1n33",
"1n34",
"1n36",
"1qd7",
"1ris",
"1vvj",
"1vy4",
"1vy5"... | 1,170 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00101116"
] | [
"11297922",
"11290319",
"11114498",
"18042701"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins."
] | [
2001,
2001,
2000,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8354,
429,
110
] | 3 | [
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
1,
4,
3
] | 3 | true | Conserved_site | Small ribosomal subunit protein bS6, conserved site | Small ribosomal subunit protein bS6, conserved site | Ribosomal_bS6_CS | 5 |
IPR020816 | 20,816 | Histone-like DNA-binding protein, conserved site | Histone-like_DNA-bd_CS | Conserved_site | 40,712 | false | false | This entry represents a twenty residue sequence which includes three perfectly conserved positions. According to the tertiary structure of one of these proteins [ ], this pattern spans exactly the first half of the flexible DNA-binding arm. Bacteria synthesise a set of small, usually basic proteins of about 90 residues... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS00045"
] | [
"HISTONE_LIKE"
] | [
40712
] | 1 | [] | [] | [] | 0 | [
"1b8z",
"1exe",
"1hue",
"1huu",
"1ihf",
"1mul",
"1ouz",
"1owf",
"1owg",
"1p51",
"1p71",
"1p78",
"1riy",
"1wtu",
"2ht0",
"2iie",
"2iif",
"2np2",
"2o97",
"3rhi",
"4dky",
"4p3v",
"4pt4",
"4qjn",
"4qju",
"4yew",
"4yex",
"4yey",
"4yf0",
"4yfh",
"4yft",
"5eka"... | 53 | [
"PUB00000820",
"PUB00002462",
"PUB00003604",
"PUB00003987",
"PUB00004416",
"PUB00004725"
] | [
"2972385",
"3047111",
"3118156",
"6540370",
"8464748",
"1961745"
] | [
"Integration host factor: a protein for all reasons.",
"Histone-like proteins and bacterial chromosome structure.",
"Histonelike proteins of bacteria.",
"3-A resolution structure of a protein with histone-like properties in prokaryotes.",
"An African swine fever virus gene with similarity to bacterial DNA b... | [
1988,
1988,
1987,
1984,
1993,
1991
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
29,
39798,
165,
134,
586
] | 5 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Conserved_site | Histone-like DNA-binding protein, conserved site | Histone-like DNA-binding protein, conserved site | Histone-like_DNA-bd_CS | 2 |
IPR020818 | 20,818 | GroES chaperonin family | Chaperonin_GroES | Family | 40,471 | false | false | The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins [ ]. These are required for normal cell growth [ ], and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitocho... | [
"GO:0005524",
"GO:0044183",
"GO:0006457"
] | [
"ATP binding",
"protein folding chaperone",
"protein folding"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER",
"SMART",
"CDD"
] | [
"MF_00580",
"PF00166",
"PR00297",
"PTHR10772",
"SM00883",
"cd00320"
] | [
"CH10",
"Cpn10",
"CHAPERONIN10",
"",
"Cpn10",
"cpn10"
] | [
31724,
40406,
37262,
37054,
39510,
40210
] | 6 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0245",
"GenProp1181",
"R-BTA-9013408",
"R-HSA-9013408",
"R-HSA-9841251",
"R-MMU-9013408",
"R-RNO-9013408"
] | [
"GP:GenProp0245",
"GP:GenProp1181",
"REACTOME:R-BTA-9013408",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9841251",
"REACTOME:R-MMU-9013408",
"REACTOME:R-RNO-9013408"
] | 7 | [
"1aon",
"1g31",
"1gru",
"1hx5",
"1lep",
"1p3h",
"1pcq",
"1pf9",
"1svt",
"1sx4",
"1wnr",
"2c7c",
"2c7d",
"2cgt",
"3nx6",
"3wvl",
"3zpz",
"3zq0",
"3zq1",
"4pj1",
"4pkn",
"4pko",
"4v4o",
"5opx",
"6ht7",
"6mrc",
"6mrd",
"7ekq",
"7pbj",
"7pbx",
"7vwx",
"8ba9"... | 58 | [
"PUB00002183",
"PUB00004022",
"PUB00004159",
"PUB00004550",
"PUB00009990"
] | [
"1350777",
"2897629",
"7901771",
"1349837",
"12354603"
] | [
"Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis.",
"Homologous plant and bacterial proteins chaperone oligomeric protein assembly.",
"Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.",
"cDNA clones encoding Arabido... | [
1992,
1988,
1993,
1992,
2002
] | 5 | [] | [
"IPR016416",
"IPR017416"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
77,
29446,
8957,
1238,
753
] | 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,
1,
2,
2,
1,
6,
3,
1,
26,
6,
1,
1,
48
] | 13 | true | Family | GroES chaperonin family | GroES chaperonin family | Chaperonin_GroES | 7 |
IPR020821 | 20,821 | ENPP1-3/EXOG-like, endonuclease/phosphodiesterase domain | ENPP1-3/EXOG-like_nuc-like | Domain | 23,263 | false | false | A family of bacterial and eukaryotic endonucleases share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. A histidine has been shown [ ] to be essential for the activity of the Serratia ... | [
"GO:0003676",
"GO:0016787",
"GO:0046872"
] | [
"nucleic acid binding",
"hydrolase activity",
"metal ion binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"SMART"
] | [
"SM00477"
] | [
"NUC"
] | [
23263
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-114608",
"R-HSA-196843",
"R-HSA-199220",
"R-HSA-9913635",
"R-MMU-114608",
"R-MMU-196843",
"R-RNO-196843"
] | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-196843",
"REACTOME:R-HSA-199220",
"REACTOME:R-HSA-9913635",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-196843",
"REACTOME:R-RNO-196843"
] | 7 | [
"1g8t",
"1qae",
"1ql0",
"1smn",
"1zm8",
"2o3b",
"2xr9",
"2xrg",
"3ism",
"3nkm",
"3nkn",
"3nko",
"3nkp",
"3nkq",
"3nkr",
"3s5b",
"3wav",
"3waw",
"3wax",
"3way",
"4a1n",
"4b56",
"4e3y",
"4gtw",
"4gtx",
"4gty",
"4gtz",
"4qn0",
"4zg6",
"4zg7",
"4zg9",
"4zga"... | 316 | [
"PUB00004455",
"PUB00091392",
"PUB00097865",
"PUB00154559",
"PUB00154562",
"PUB00154563",
"PUB00154564",
"PUB00154578",
"PUB00154579",
"PUB00154580",
"PUB00154581"
] | [
"8078761",
"18187503",
"29717535",
"25355512",
"25344812",
"28011303",
"35147247",
"11004006",
"26371182",
"27467858",
"27754931"
] | [
"Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis.",
"EXOG, a novel paralog of Endonuclease G in higher eukaryotes.",
"Structural basis for nucleotide recognition by the ectoenzyme CD203c.",
"Endonuclease G preferentiall... | [
1994,
2008,
2018,
2014,
2014,
2017,
2022,
2000,
2015,
2016,
2017
] | 11 | [
"IPR001604"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
15,
8359,
14761,
43,
85
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
1,
46,
12,
16,
14,
1,
30,
1,
1
] | 9 | true | Domain | ENPP1-3/EXOG-like, endonuclease/phosphodiesterase domain | ENPP1-3/EXOG-like, endonuclease/phosphodiesterase domain | ENPP1-3/EXOG-like_nuc-like | 6 |
IPR020823 | 20,823 | Cell division protein FtsA | Cell_div_FtsA | Family | 18,163 | false | false | FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains [ ]. | [] | [] | [] | 0 | [
"HAMAP",
"PIRSF",
"NCBIFAM",
"CDD"
] | [
"MF_02033",
"PIRSF003101",
"TIGR01174",
"cd24048"
] | [
"FtsA",
"FtsA",
"ftsA",
"ASKHA_NBD_FtsA"
] | [
17567,
17427,
18055,
17158
] | 4 | [] | [] | [] | 0 | [
"1e4f",
"1e4g",
"3wqt",
"3wqu",
"3wt0",
"4a2a",
"4a2b",
"7q6d",
"7q6f",
"7q6g",
"7q6i"
] | 11 | [
"PUB00009447",
"PUB00024420",
"PUB00158650",
"PUB00158651",
"PUB00158652",
"PUB00158653",
"PUB00158654",
"PUB00158655",
"PUB00158656",
"PUB00158657",
"PUB00158658",
"PUB00158659",
"PUB00158660",
"PUB00158661",
"PUB00158662",
"PUB00158663",
"PUB00158664"
] | [
"9352931",
"11032797",
"9287029",
"10753635",
"16159787",
"11298280",
"3139638",
"1624452",
"1569582",
"2995680",
"2846985",
"2228979",
"6094474",
"3000876",
"2203741",
"8955398",
"8917533"
] | [
"Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring.",
"Crystal structure of the cell division protein FtsA from Thermotoga maritima.",
"Identification and characterization of cell wall-cell division gene clusters in pathogenic gram-positive cocci.",
"A conserved residue at the extreme ... | [
1997,
2000,
1997,
2000,
2005,
2001,
1988,
1992,
1992,
1985,
1988,
1990,
1984,
1985,
1990,
1996,
1996
] | 17 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine group II/III euryarchaeote AD1000_29_E08"
] | [
17818,
42,
302,
1
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Cell division protein FtsA | Cell division protein FtsA | Cell_div_FtsA | 8 |
IPR020825 | 20,825 | Phenylalanyl-tRNA synthetase-like, B3/B4 | Phe-tRNA_synthase-like_B3/B4 | Homologous_superfamily | 42,380 | false | false | This entry represents the B3/B4 domain found in tRNA synthetase beta subunits as well as in some non-tRNA synthetase proteins. This domain has a 3-layer structure, and contains a β-sandwich fold of unusual topology, and contains a putative tRNA-binding structural motif [ ]. In Thermus thermophilus, both the catalytic a... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:3.50.40.10"
] | [
""
] | [
42380
] | 1 | [
"EC",
"REACTOME"
] | [
"6.1.1.20",
"R-HSA-379716"
] | [
"EC:6.1.1.20",
"REACTOME:R-HSA-379716"
] | 2 | [
"1b70",
"1b7y",
"1eiy",
"1jjc",
"1pys",
"2akw",
"2aly",
"2amc",
"2cxi",
"2iy5",
"2rhq",
"2rhs",
"3hfz",
"3l4g",
"3pco",
"3teh",
"4p71",
"4p72",
"4p73",
"4p74",
"4p75",
"4tva",
"6oz5",
"6p24",
"6p26",
"6p8t",
"6zxd",
"6zxe",
"6zxf",
"6zxg",
"7by6",
"7daw"... | 49 | [
"PUB00020104",
"PUB00042628"
] | [
"7664121",
"15526031"
] | [
"Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.",
"Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase."
] | [
1995,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Myoviridae sp. ctBoB21",
"unclassified sequences"
] | [
1145,
33188,
7336,
1,
710
] | 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,
2,
4,
1,
1,
5,
13,
1,
3,
6,
1,
1,
9
] | 13 | true | Homologous_superfamily | Phenylalanyl-tRNA synthetase-like, B3/B4 | Phenylalanyl-tRNA synthetase-like, B3/B4 | Phe-tRNA_synthase-like_B3/B4 | 2 |
IPR020826 | 20,826 | Transketolase binding site | Transketolase_BS | Binding_site | 56,546 | false | false | This entry represents a short region of conserved acidic residues that are located in the central section of a group of transketolase proteins widespread among all cellular organisms. This region may participate in substrate-binding [ ]. Transketolase (TK) catalyses the reversible transfer of a two-carbon ketol unit fr... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00802"
] | [
"TRANSKETOLASE_2"
] | [
56546
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.2.1.7",
"PWY-6891",
"PWY-6892",
"PWY-7560",
"R-HSA-163754",
"R-HSA-71336",
"R-HSA-9818028",
"R-MMU-163754",
"R-MMU-71336",
"R-RNO-163754",
"R-RNO-71336"
] | [
"EC:2.2.1.7",
"METACYC:PWY-6891",
"METACYC:PWY-6892",
"METACYC:PWY-7560",
"REACTOME:R-HSA-163754",
"REACTOME:R-HSA-71336",
"REACTOME:R-HSA-9818028",
"REACTOME:R-MMU-163754",
"REACTOME:R-MMU-71336",
"REACTOME:R-RNO-163754",
"REACTOME:R-RNO-71336"
] | 11 | [
"1ay0",
"1gpu",
"1ngs",
"1qgd",
"1r9j",
"1tka",
"1tkb",
"1tkc",
"1trk",
"2o1s",
"2o1x",
"2r5n",
"2r8o",
"2r8p",
"3hyl",
"3kom",
"3l84",
"3m34",
"3m49",
"3m6l",
"3m7i",
"3mos",
"3ooy",
"3rim",
"4kxu",
"4kxv",
"4kxw",
"4kxx",
"4kxy",
"4xeu",
"5hgx",
"5hje"... | 95 | [
"PUB00000209",
"PUB00000362",
"PUB00001222",
"PUB00004906"
] | [
"1567394",
"1737042",
"1628611",
"9371765"
] | [
"Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase.",
"DNA sequence of the yeast transketolase gene.",
"Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.",
"Identification of a thiamin-dependent synthase ... | [
1992,
1992,
1992,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
20,
46260,
9441,
825
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
23,
1,
2,
5,
3,
14,
4,
1,
2,
10,
2,
1,
14
] | 13 | true | Binding_site | Transketolase binding site | Transketolase binding site | Transketolase_BS | 4 |
IPR020827 | 20,827 | Asparaginase/glutaminase, active site 1 | Asparaginase/glutaminase_AS1 | Active_site | 19,744 | false | false | Asparaginase, which is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma [ ]. The enzyme is effective in the treatment of human malignant lymphomas, which have a dimini... | [
"GO:0006520"
] | [
"amino acid metabolic process"
] | [
"biological_process"
] | 1 | [
"PROSITE"
] | [
"PS00144"
] | [
"ASN_GLN_ASE_1"
] | [
19744
] | 1 | [] | [] | [] | 0 | [
"1agx",
"1djo",
"1djp",
"1hfj",
"1hfk",
"1hfw",
"1hg0",
"1hg1",
"1ho3",
"1ihd",
"1jaz",
"1jja",
"1jsl",
"1jsr",
"1nns",
"1o7j",
"1wsa",
"1zcf",
"1zq1",
"2d6f",
"2gvn",
"2him",
"2hln",
"2jk0",
"2ocd",
"2p2d",
"2p2n",
"2wlt",
"2wt4",
"3eca",
"3ntx",
"3nxk"... | 108 | [
"PUB00001616",
"PUB00001663",
"PUB00001757",
"PUB00002099",
"PUB00002487"
] | [
"1906013",
"8348975",
"3026924",
"2407723",
"3379033"
] | [
"A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis.",
"A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate.",
"Nucleotide sequence of the Erwinia chrysanthemi NCPPB 10... | [
1991,
1993,
1986,
1990,
1988
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
917,
16910,
30,
1777,
110
] | 5 | [
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
1,
2,
5,
1
] | 4 | true | Active_site | Asparaginase/glutaminase, active site 1 | Asparaginase/glutaminase, active site 1 | Asparaginase/glutaminase_AS1 | 8 |
IPR020828 | 20,828 | Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain | GlycerAld_3-P_DH_NAD(P)-bd | Domain | 73,233 | false | false | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis [ ] by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. The enzyme exists as a tetramer of identical subunits, each containing 2 conserved functio... | [
"GO:0051287"
] | [
"NAD binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00044",
"SM00846"
] | [
"Gp_dh_N",
"Gp_dh_N"
] | [
65905,
73002
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.2.1",
"R-BTA-70171",
"R-BTA-70263",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",
"R-DRE-70171",
"R-DRE-70263",
"R-GGA-352875",
"R-GGA-352882",
"R-GGA-70171",
"R-GGA-70263",
"R-HSA-390471",
"R-HSA-70171",
"R-HSA-70263",
"R-MMU-70171"... | [
"EC:1.2.1",
"REACTOME:R-BTA-70171",
"REACTOME:R-BTA-70263",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-70263",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70263",
"REACTOME:R-DME-70171",
"REACTOME:R-DME-70263",
"REACTOME:R-DRE-70171",
"REACTOME:R-DRE-70263",
"REACTOME:R-GGA-352875",
"REACTOME:R-GGA... | 28 | [
"1a7k",
"1b7g",
"1cer",
"1cf2",
"1crw",
"1dbv",
"1dc3",
"1dc4",
"1dc5",
"1dc6",
"1dss",
"1gad",
"1gae",
"1gd1",
"1gpd",
"1gyp",
"1gyq",
"1hdg",
"1i32",
"1i33",
"1ihx",
"1ihy",
"1j0x",
"1jn0",
"1k3t",
"1ml3",
"1nbo",
"1npt",
"1nq5",
"1nqa",
"1nqo",
"1obf"... | 251 | [
"PUB00000277",
"PUB00003246",
"PUB00014241",
"PUB00014242"
] | [
"6303388",
"2716055",
"12721812",
"10740219"
] | [
"Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle.",
"Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans.",
"Neuroprotection by deprenyl and other pro... | [
1983,
1989,
2003,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1105,
45619,
25760,
2,
747
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
30,
4,
3,
4,
2,
11,
17,
1,
19,
34,
3,
2,
87
] | 13 | true | Domain | Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain | Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain | GlycerAld_3-P_DH_NAD(P)-bd | 1 |
IPR020829 | 20,829 | Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain | GlycerAld_3-P_DH_cat | Domain | 80,638 | false | false | This entry represents the C-terminal domain which is a mixed α/antiparallel-β-fold. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis [ ] by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. The en... | [
"GO:0016620"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF02800"
] | [
"Gp_dh_C"
] | [
80638
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.2.1",
"R-BTA-70171",
"R-BTA-70263",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",
"R-DRE-70171",
"R-DRE-70263",
"R-GGA-352875",
"R-GGA-352882",
"R-GGA-70171",
"R-GGA-70263",
"R-HSA-390471",
"R-HSA-70171",
"R-HSA-70263",
"R-MMU-70171"... | [
"EC:1.2.1",
"REACTOME:R-BTA-70171",
"REACTOME:R-BTA-70263",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-70263",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70263",
"REACTOME:R-DME-70171",
"REACTOME:R-DME-70263",
"REACTOME:R-DRE-70171",
"REACTOME:R-DRE-70263",
"REACTOME:R-GGA-352875",
"REACTOME:R-GGA... | 28 | [
"1a7k",
"1b7g",
"1cer",
"1cf2",
"1crw",
"1dbv",
"1dc3",
"1dc4",
"1dc5",
"1dc6",
"1dss",
"1gad",
"1gae",
"1gd1",
"1gpd",
"1gyp",
"1gyq",
"1hdg",
"1i32",
"1i33",
"1ihx",
"1ihy",
"1j0x",
"1jn0",
"1k3t",
"1ml3",
"1nbo",
"1npt",
"1nq5",
"1nqa",
"1nqo",
"1obf"... | 255 | [
"PUB00000277",
"PUB00003246",
"PUB00014241",
"PUB00014242"
] | [
"6303388",
"2716055",
"12721812",
"10740219"
] | [
"Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle.",
"Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans.",
"Neuroprotection by deprenyl and other pro... | [
1983,
1989,
2003,
2000
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1109,
46442,
32296,
2,
789
] | 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",... | [
34,
4,
3,
4,
2,
11,
15,
1,
22,
37,
3,
2,
73
] | 13 | true | Domain | Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain | Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain | GlycerAld_3-P_DH_cat | 8 |
IPR020831 | 20,831 | Glyceraldehyde/Erythrose phosphate dehydrogenase family | GlycerAld/Erythrose_P_DH | Family | 84,714 | false | false | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis [ ] by reversibly catalysing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. The enzyme exists as a tetramer of identical subunits, each containing 2 conserved functio... | [
"GO:0016620"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor"
] | [
"molecular_function"
] | 1 | [
"PIRSF",
"PRINTS",
"PANTHER",
"PANTHER"
] | [
"PIRSF000149",
"PR00078",
"PTHR10836",
"PTHR43148"
] | [
"GAP_DH",
"G3PDHDRGNASE",
"",
""
] | [
50844,
78113,
41087,
34539
] | 4 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.2.1",
"1.2.1.12",
"PWY-1042",
"PWY-5484",
"PWY-6901",
"PWY-7003",
"PWY-8004",
"PWY-8404",
"R-BTA-70171",
"R-BTA-70263",
"R-CEL-70171",
"R-CEL-70263",
"R-DDI-70171",
"R-DDI-70263",
"R-DME-70171",
"R-DME-70263",
"R-DRE-70171",
"R-DRE-70263",
"R-GGA-352875",
"R-GGA-352882",
"... | [
"EC:1.2.1",
"EC:1.2.1.12",
"METACYC:PWY-1042",
"METACYC:PWY-5484",
"METACYC:PWY-6901",
"METACYC:PWY-7003",
"METACYC:PWY-8004",
"METACYC:PWY-8404",
"REACTOME:R-BTA-70171",
"REACTOME:R-BTA-70263",
"REACTOME:R-CEL-70171",
"REACTOME:R-CEL-70263",
"REACTOME:R-DDI-70171",
"REACTOME:R-DDI-70263",... | 35 | [
"1a7k",
"1b7g",
"1cer",
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"1dbv",
"1dc3",
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"1k3t",
"1ml3",
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"1npt",
"1nq5",
"1nqa",
"1nqo",
"1obf"... | 251 | [
"PUB00000277",
"PUB00002270",
"PUB00003246",
"PUB00014241",
"PUB00014242"
] | [
"6303388",
"7751290",
"2716055",
"12721812",
"10740219"
] | [
"Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle.",
"Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate ... | [
1983,
1995,
1989,
2003,
2000
] | 5 | [] | [
"IPR006422",
"IPR006424",
"IPR006436"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1139,
46649,
36072,
2,
852
] | 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",... | [
34,
4,
3,
4,
2,
14,
20,
1,
23,
45,
3,
2,
87
] | 13 | true | Family | Glyceraldehyde/Erythrose phosphate dehydrogenase family | Glyceraldehyde/Erythrose phosphate dehydrogenase family | GlycerAld/Erythrose_P_DH | 1 |
IPR020833 | 20,833 | Lipoxygenase, iron binding site | LipOase_Fe_BS | Binding_site | 10,198 | false | false | Lipoxygenases ([ec:1.13.11.-]) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resist... | [
"GO:0016702",
"GO:0046872"
] | [
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00711"
] | [
"LIPOXYGENASE_1"
] | [
10198
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.13.11",
"R-BTA-2142691",
"R-BTA-2142712",
"R-BTA-2142770",
"R-BTA-9018677",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9023661",
"R-BTA-9025106",
"R-BTA-9026286",
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"R-HSA-2142691",
"R-HSA-2142696",
"R-HSA-2142700",
"R-HSA-2142712",
"R-HSA-2142770",
"R-HSA-6785807",
... | [
"EC:1.13.11",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-2142770",
"REACTOME:R-BTA-9018677",
"REACTOME:R-BTA-9018681",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9023661",
"REACTOME:R-BTA-9025106",
"REACTOME:R-BTA-9026286",
"REACTOME:R-HSA-2142688",
"REACTOME:R-HSA-2142... | 78 | [
"1f8n",
"1fgm",
"1fgq",
"1fgr",
"1fgt",
"1hu9",
"1ik3",
"1jnq",
"1lnh",
"1lox",
"1n8q",
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"1rrl",
"1y4k",
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"2fnq",
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"3bnb",
"3bnc",
"3bnd",
"3bne",
"3d3l",
"3dy5",
"3fg1",
"3fg3",
"3fg4",
"3o8y"... | 73 | [
"PUB00000045",
"PUB00000363",
"PUB00002887",
"PUB00005162"
] | [
"3017195",
"1567851",
"7508918",
"8502991"
] | [
"Arachidonic acid metabolism.",
"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.",
"A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus.",
"The three-dimensional structure of an arachid... | [
1986,
1992,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
52,
10145,
1
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
28,
37,
22,
22,
41,
30,
93
] | 7 | true | Binding_site | Lipoxygenase, iron binding site | Lipoxygenase, iron binding site | LipOase_Fe_BS | 7 |
IPR020834 | 20,834 | Lipoxygenase, conserved site | LipOase_CS | Conserved_site | 12,328 | false | false | Lipoxygenases ([ec:1.13.11.-]) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resist... | [
"GO:0016702",
"GO:0046872"
] | [
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS00081"
] | [
"LIPOXYGENASE_2"
] | [
12328
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.13.11",
"R-BTA-2142691",
"R-BTA-2142712",
"R-BTA-2142770",
"R-BTA-9018677",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9023661",
"R-BTA-9025106",
"R-BTA-9026286",
"R-HSA-2142688",
"R-HSA-2142691",
"R-HSA-2142696",
"R-HSA-2142700",
"R-HSA-2142712",
"R-HSA-2142770",
"R-HSA-6785807",
... | [
"EC:1.13.11",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-2142712",
"REACTOME:R-BTA-2142770",
"REACTOME:R-BTA-9018677",
"REACTOME:R-BTA-9018681",
"REACTOME:R-BTA-9018896",
"REACTOME:R-BTA-9023661",
"REACTOME:R-BTA-9025106",
"REACTOME:R-BTA-9026286",
"REACTOME:R-HSA-2142688",
"REACTOME:R-HSA-2142... | 78 | [
"1f8n",
"1fgm",
"1fgo",
"1fgq",
"1fgr",
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"1hu9",
"1ik3",
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"3bnb",
"3bnc",
"3bnd",
"3bne",
"3d3l",
"3dy5",
"3fg1",
"3fg3",
"3fg4"... | 71 | [
"PUB00000045",
"PUB00000363",
"PUB00002887",
"PUB00005162"
] | [
"3017195",
"1567851",
"7508918",
"8502991"
] | [
"Arachidonic acid metabolism.",
"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement.",
"A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus.",
"The three-dimensional structure of an arachid... | [
1986,
1992,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
107,
12221
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
28,
43,
22,
20,
45,
28,
97
] | 7 | true | Conserved_site | Lipoxygenase, conserved site | Lipoxygenase, conserved site | LipOase_CS | 9 |
IPR020835 | 20,835 | Catalase superfamily | Catalase_sf | Homologous_superfamily | 49,192 | false | false | This entry represents a fold found in the mono-functional, haem-containing catalases and also in haem peroxidases such as allene oxide synthase [ , , ]. In catalases, this entry covers the core forming domain and, if present, the immune-responsive C-terminal domain. | [
"GO:0020037"
] | [
"heme binding"
] | [
"molecular_function"
] | 1 | [
"SSF"
] | [
"SSF56634"
] | [
""
] | [
49192
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.11.1.6",
"R-BTA-3299685",
"R-BTA-6798695",
"R-BTA-9033241",
"R-CFA-3299685",
"R-CFA-6798695",
"R-CFA-9033241",
"R-DDI-3299685",
"R-DDI-6798695",
"R-DDI-9033241",
"R-DME-3299685",
"R-DME-6798695",
"R-DME-9033241",
"R-DRE-3299685",
"R-DRE-6798695",
"R-HSA-3299685",
"R-HSA-6798695",
... | [
"EC:1.11.1.6",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9033241",
"REACTOME:R-CFA-3299685",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-9033241",
"REACTOME:R-DDI-3299685",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-9033241",
"REACTOME:R-DME-3299685",
"REACTOME:R-DME-679... | 32 | [
"1a4e",
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"1dgb",
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"1dgg",
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"1e93",
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"1nm0",
"1p7y",
"1p7z",
"1p80",
"1p81",
"1qf7",
"1qqw",
"1qwl"... | 164 | [
"PUB00027249",
"PUB00030416",
"PUB00037840"
] | [
"12557185",
"15023060",
"15625113"
] | [
"Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution.",
"Structure of Helicobacter pylori catalase, with and without formic acid bound, at 1.6 A resolution.",
"The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide."
... | [
2003,
2004,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Tupanvirus",
"unclassified sequences"
] | [
194,
32772,
16061,
4,
161
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
26,
4,
2,
6,
1,
5,
8,
3,
11,
4,
2,
1,
18
] | 13 | true | Homologous_superfamily | Catalase superfamily | Catalase superfamily | Catalase_sf | 8 |
IPR020837 | 20,837 | Fibrinogen, conserved site | Fibrinogen_CS | Conserved_site | 24,668 | false | false | Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation, the conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin, resulting in the polymerisation of fibrin, which forms a soft clot; this is then converted to a hard clot by factor XIIIA, which cro... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00514"
] | [
"FIBRINOGEN_C_1"
] | [
24668
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
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"REACTOME",
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"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-166662",
"R-BTA-166663",
"R-BTA-210993",
"R-BTA-2855086",
"R-BTA-5673001",
"R-BTA-6798695",
"R-BTA-8963889",
"R-BTA-9762292",
"R-CFA-210993",
"R-HSA-114608",
"R-HSA-1236974",
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"R-HSA-166058",
"R-HSA-166662",
"R-HSA-166663",
"R-HSA-1989781",
"R-HSA-210993",
"R-... | [
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"REACTOME:R-BTA-166663",
"REACTOME:R-BTA-210993",
"REACTOME:R-BTA-2855086",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8963889",
"REACTOME:R-BTA-9762292",
"REACTOME:R-CFA-210993",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-1236974",
"REACTOME:R-H... | 81 | [
"1deq",
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"1fib",
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"1re3",
"1re4",
"1rf0",
"1rf1",
"1z3s",
"1z3u",
"2d39",
"2ffd",
"2fib",
"2gy7",
"2h43",
"2hlo"... | 94 | [
"PUB00016231",
"PUB00016232",
"PUB00016233",
"PUB00016234",
"PUB00017188"
] | [
"12799374",
"11460466",
"11593005",
"12396010",
"15837518"
] | [
"Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen.",
"The structure and biological features of fibrinogen and fibrin.",
"Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution... | [
2003,
2001,
2001,
2002,
2005
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
10,
24658
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
69,
12,
57,
43,
61
] | 6 | true | Conserved_site | Fibrinogen, conserved site | Fibrinogen, conserved site | Fibrinogen_CS | 7 |
IPR020838 | 20,838 | DBINO domain | DBINO | Domain | 4,258 | false | false | Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodelling complexes that are implicated in epigenetic control of gene expression. Members of the SNF2 family of proteins have been identified in organisms ranging from Escherichia coli to Homo sapiens (Human). All of... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF13892",
"PS51413"
] | [
"DBINO",
"DBINO"
] | [
4202,
4220
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.4.-",
"PWY-7250",
"R-DME-5689603",
"R-DME-5696394",
"R-HSA-5689603",
"R-HSA-5696394",
"R-MMU-5689603",
"R-MMU-5696394"
] | [
"EC:3.6.4.-",
"METACYC:PWY-7250",
"REACTOME:R-DME-5689603",
"REACTOME:R-DME-5696394",
"REACTOME:R-HSA-5689603",
"REACTOME:R-HSA-5696394",
"REACTOME:R-MMU-5689603",
"REACTOME:R-MMU-5696394"
] | 8 | [
"5nbn",
"6fhs",
"6fml",
"6hts",
"7zi4",
"8a5a",
"8a5d",
"8a5o",
"8a5p",
"8a5q",
"8atf",
"8av6",
"8euf",
"8oo7",
"8oo9",
"8ooc",
"8oop",
"8oor",
"8oos",
"9c9g",
"9c9s",
"9c9t",
"9c9z",
"9can",
"9cat",
"9cb7",
"9ccd",
"9gcg",
"9gev",
"9gfb"
] | 30 | [
"PUB00052592",
"PUB00052593",
"PUB00062156"
] | [
"15207721",
"16298340",
"21303910"
] | [
"In silico characterization of the INO80 subfamily of SWI2/SNF2 chromatin remodeling proteins.",
"Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity.",
"Subunit organization of the human INO80 chromatin remodeling complex: an evolutionarily conserved c... | [
2004,
2006,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Streptomyces"
] | [
4255,
3
] | 2 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
5,
7,
2,
4,
2,
2,
3,
1,
1,
1,
18
] | 11 | true | Domain | DBINO domain | DBINO domain | DBINO | 1 |
IPR020839 | 20,839 | Stromalin conservative domain | SCD | Domain | 9,518 | false | false | The stromal antigens or stromalins are a group of highly conserved nuclear proteins, originally identified from a murine bone marrows stromal cell line. Stromalins are represented in several organisms from yeast to humans and are characterised by the stromalin conservative domain (SCD), an 86 amino acid motif found in ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF21581",
"PS51425"
] | [
"SCD",
"SCD"
] | [
9410,
9443
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-2468052",
"R-CEL-2470946",
"R-CEL-2500257",
"R-CEL-3108214",
"R-HSA-1221632",
"R-HSA-2467813",
"R-HSA-2468052",
"R-HSA-2470946",
"R-HSA-2500257",
"R-HSA-3108214",
"R-HSA-9018519",
"R-MMU-2467813",
"R-MMU-2468052",
"R-MMU-2470946",
"R-MMU-2500257",
"R-MMU-3108214",
"R-SCE-24680... | [
"REACTOME:R-CEL-2468052",
"REACTOME:R-CEL-2470946",
"REACTOME:R-CEL-2500257",
"REACTOME:R-CEL-3108214",
"REACTOME:R-HSA-1221632",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2468052",
"REACTOME:R-HSA-2470946",
"REACTOME:R-HSA-2500257",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-9018519",
"REACTOM... | 22 | [
"4pju",
"4pjw",
"4pk7",
"4uvk",
"5qst",
"5qsu",
"5qsv",
"5qsw",
"5qsx",
"6h8q",
"6qb5",
"6qnx",
"6rrc",
"6wg3",
"7w1m",
"7zjs",
"8k4d",
"9ep3",
"9hms",
"9hmv",
"9j0a"
] | 21 | [
"PUB00052629"
] | [
"10698974"
] | [
"STAG3, a novel gene encoding a protein involved in meiotic chromosome pairing and location of STAG3-related genes flanking the Williams-Beuren syndrome deletion."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
9516,
2
] | 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... | [
2,
1,
20,
4,
23,
10,
1,
5,
14,
1,
2,
6
] | 12 | true | Domain | Stromalin conservative domain | Stromalin conservative domain | SCD | 4 |
IPR020840 | 20,840 | Extracellular matrix-binding protein ebh, GA module | Extracell_matrix-bd_GA | Domain | 964 | false | false | This entry represents the GA module from the extracellular matrix-binding protein ebhB. Protein G-related albumin-binding (GA) modules occur on the surface of numerous Gram-positive bacterial pathogens. Protein G of group C and G Streptococci interacts with the constant region of IgG and with human serum albumin. The G... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00844"
] | [
"GA"
] | [
964
] | 1 | [] | [] | [] | 0 | [
"2dgj",
"4kjm",
"6gv5"
] | 3 | [
"PUB00003376",
"PUB00031434",
"PUB00035975",
"PUB00035976"
] | [
"9086265",
"15269208",
"16906768",
"7589548"
] | [
"Solution structure of the albumin-binding GA module: a versatile bacterial protein domain.",
"Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin.",
"Structure, dynamics, and stability variation in bacterial albumin binding modules: implicatio... | [
1997,
2004,
2006,
1995
] | 4 | [
"IPR002988"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)",
"human gut metagenome"
] | [
961,
1,
2
] | 3 | [] | [] | 0 | true | Domain | Extracellular matrix-binding protein ebh, GA module | Extracellular matrix-binding protein ebh, GA module | Extracell_matrix-bd_GA | 1 |
IPR020841 | 20,841 | Polyketide synthase, beta-ketoacyl synthase domain | PKS_Beta-ketoAc_synthase_dom | Domain | 158,850 | false | false | This entry represents the beta-ketoacyl synthase region from a number of polyketide synthases including erythronolide synthase and the lovastatin nonaketide chain synthase. Beta-ketoacyl-ACP synthase (KAS) [ ] is the enzyme that catalyses the condensation of malonyl-ACP with the growing fatty acid chain. It is found as... | [] | [] | [] | 0 | [
"PROFILE",
"SMART"
] | [
"PS52004",
"SM00825"
] | [
"KS3_2",
"PKS_KS"
] | [
158272,
151350
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"2.3.1",
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
... | [
"EC:2.3.1",
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"... | 236 | [
"1b3n",
"1dd8",
"1e5m",
"1ek4",
"1f91",
"1fj4",
"1fj8",
"1g5x",
"1h4f",
"1j3n",
"1kas",
"1ox0",
"1oxh",
"1tqy",
"1w0i",
"2alm",
"2aq7",
"2aqb",
"2buh",
"2bui",
"2byw",
"2byx",
"2byy",
"2byz",
"2bz3",
"2bz4",
"2c9h",
"2cdh",
"2cf2",
"2gfv",
"2gfw",
"2gfx"... | 356 | [
"PUB00000791",
"PUB00001385"
] | [
"3076376",
"2209605"
] | [
"beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue.",
"The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases."
] | [
1988,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
29,
114805,
42673,
8,
1335
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
5,
11,
9,
2,
5,
6,
9,
16,
5,
2,
2,
42
] | 13 | true | Domain | Polyketide synthase, beta-ketoacyl synthase domain | Polyketide synthase, beta-ketoacyl synthase domain | PKS_Beta-ketoAc_synthase_dom | 1 |
IPR020844 | 20,844 | Circadian clock protein KaiA, N-terminal | Circadian_clock_KaiA_N | Domain | 338 | false | false | This entry represents the N-terminal domain of KaiA. Cyanobacteria are the most primitive organisms known to exhibit circadian rhythms. KaiA, kaiB and kaiC constitute the circadian clock machinery in cyanobacteria, and kaiA activates kaiBC expression whereas kaiC represses it [ , ]. Apparent homologues of kaiB and kaiC... | [
"GO:0007623"
] | [
"circadian rhythm"
] | [
"biological_process"
] | 1 | [
"PROFILE"
] | [
"PS51430"
] | [
"KAIA_N"
] | [
338
] | 1 | [] | [] | [] | 0 | [
"1m2e",
"1m2f",
"1r8j",
"4g86",
"5c5e",
"5jwr",
"5n8y"
] | 7 | [
"PUB00014089",
"PUB00030142",
"PUB00030572",
"PUB00031213",
"PUB00031979",
"PUB00103685",
"PUB00103686",
"PUB00103687"
] | [
"12438647",
"14749515",
"15007067",
"15256595",
"15170179",
"28302852",
"17717528",
"17916691"
] | [
"Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.",
"NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction.",
"Crystal structure of circadian clock protein KaiA... | [
2002,
2004,
2004,
2004,
2004,
2017,
2007,
2007
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
295,
43
] | 2 | [] | [] | 0 | true | Domain | Circadian clock protein KaiA, N-terminal | Circadian clock protein KaiA, N-terminal | Circadian_clock_KaiA_N | 8 |
IPR020845 | 20,845 | AMP-binding, conserved site | AMP-binding_CS | Conserved_site | 455,038 | false | false | It has been shown that a number of prokaryotic and eukaryotic enzymes which all probably act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ , , , ]. These enzymes are: Insects luciferase (luciferin 4-monooxygenase) ( ). Luciferase produces light by catalysing th... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00455"
] | [
"AMP_BINDING"
] | [
455038
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"6.2.1",
"R-BTA-75876",
"R-BTA-77111",
"R-BTA-77289",
"R-CEL-77111",
"R-DDI-2046105",
"R-DDI-2046106",
"R-DDI-2151201",
"R-DDI-71384",
"R-DDI-75876",
"R-DDI-77111",
"R-DME-71384",
"R-DRE-77111",
"R-DRE-77289",
"R-HSA-159418",
"R-HSA-177128",
"R-HSA-177135",
"R-HSA-177162",
"R-HSA... | [
"EC:6.2.1",
"REACTOME:R-BTA-75876",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-77289",
"REACTOME:R-CEL-77111",
"REACTOME:R-DDI-2046105",
"REACTOME:R-DDI-2046106",
"REACTOME:R-DDI-2151201",
"REACTOME:R-DDI-71384",
"REACTOME:R-DDI-75876",
"REACTOME:R-DDI-77111",
"REACTOME:R-DME-71384",
"REACTOME:... | 98 | [
"1amu",
"1ba3",
"1lci",
"1md9",
"1mdb",
"1mdf",
"1pg3",
"1pg4",
"1ry2",
"1t5d",
"1t5h",
"1ult",
"1v25",
"1v26",
"2d1q",
"2d1r",
"2d1s",
"2d1t",
"2p20",
"2p2b",
"2p2f",
"2p2j",
"2p2m",
"2p2q",
"2qvx",
"2qvy",
"2qvz",
"2qw0",
"2vsq",
"2vze",
"2wd9",
"3a9u"... | 334 | [
"PUB00000365",
"PUB00001189",
"PUB00001787",
"PUB00002167",
"PUB00002193",
"PUB00003833",
"PUB00005067"
] | [
"1351742",
"2118102",
"2311935",
"1551828",
"1629163",
"1560782",
"1946328"
] | [
"Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases.",
"The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum i... | [
1992,
1990,
1990,
1992,
1992,
1992,
1991
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
5446,
308761,
137125,
1,
13,
3692
] | 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",... | [
201,
31,
66,
54,
9,
110,
75,
21,
113,
113,
9,
7,
240
] | 13 | true | Conserved_site | AMP-binding, conserved site | AMP-binding, conserved site | AMP-binding_CS | 7 |
IPR020846 | 20,846 | Major facilitator superfamily domain | MFS_dom | Domain | 1,553,932 | false | false | This entry represents the MFS superfamily domain, which consists of twelve transmembrane helices. This domain can be found in glycerol-3-phosphate transporter from Escherichia coli, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm [ ]. The E. coli proton/sugar transpor... | [
"GO:0022857"
] | [
"transmembrane transporter activity"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS50850"
] | [
"MFS"
] | [
1553932
] | 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-112311",
"R-BTA-181430",
"R-BTA-189200",
"R-BTA-196757",
"R-BTA-196836",
"R-BTA-210500",
"R-BTA-210991",
"R-BTA-2161517",
"R-BTA-422356",
"R-BTA-428643",
"R-BTA-433692",
"R-BTA-442660",
"R-BTA-549127",
"R-BTA-5653890",
"R-BTA-6798695",
"R-BTA-8981373",
"R-BTA-917937",
"R-BTA... | [
"REACTOME:R-BTA-112311",
"REACTOME:R-BTA-181430",
"REACTOME:R-BTA-189200",
"REACTOME:R-BTA-196757",
"REACTOME:R-BTA-196836",
"REACTOME:R-BTA-210500",
"REACTOME:R-BTA-210991",
"REACTOME:R-BTA-2161517",
"REACTOME:R-BTA-422356",
"REACTOME:R-BTA-428643",
"REACTOME:R-BTA-433692",
"REACTOME:R-BTA-44... | 257 | [
"1pv6",
"1pv7",
"1pw4",
"2cfp",
"2cfq",
"2gfp",
"2v8n",
"2y5y",
"3o7p",
"3o7q",
"3wdo",
"4aps",
"4d2b",
"4d2c",
"4d2d",
"4gby",
"4gbz",
"4gc0",
"4ikv",
"4ikw",
"4ikx",
"4iky",
"4ikz",
"4ja3",
"4ja4",
"4lds",
"4oaa",
"4pyp",
"4q65",
"4qiq",
"4w6v",
"4xni"... | 404 | [
"PUB00007278",
"PUB00007279",
"PUB00018323",
"PUB00029988",
"PUB00030004",
"PUB00040002",
"PUB00052599"
] | [
"9529885",
"9868370",
"7961399",
"12893935",
"12893936",
"16525509",
"1157130"
] | [
"Major facilitator superfamily.",
"Sugar transporters from bacteria, parasites and mammals: structure-activity relationships.",
"Identification of the pcaRKF gene cluster from Pseudomonas putida: involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate.",
"Structure and mechanism of the l... | [
1998,
1998,
1994,
2003,
2003,
2006,
1975
] | 7 | [] | [
"IPR047969"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
13299,
913895,
618065,
19,
6,
8648
] | 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",... | [
460,
165,
333,
224,
73,
332,
225,
129,
352,
345,
63,
55,
646
] | 13 | true | Domain | Major facilitator superfamily domain | Major facilitator superfamily domain | MFS_dom | 1 |
IPR020847 | 20,847 | AP endonuclease 1, binding site | AP_endonuclease_F1_BS | Binding_site | 26,447 | false | false | DNA damaging agents such as the anti-tumour drugs bleomycin and neocarzinostatin or those that generate oxygen radicals produce a variety of lesions in DNA. Amongst these is base-loss which forms apurinic/apyrimidinic (AP) sites or strand breaks with atypical 3' termini. DNA repair at the AP sites is initiated by speci... | [
"GO:0003677",
"GO:0004519",
"GO:0006281"
] | [
"DNA binding",
"endonuclease activity",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00726"
] | [
"AP_NUCLEASE_F1_1"
] | [
26447
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.11.2",
"R-DDI-110357",
"R-DDI-110362",
"R-DDI-110373",
"R-DDI-5651801",
"R-DDI-73930",
"R-DDI-73933",
"R-DME-110357",
"R-DME-110373",
"R-DME-5651801",
"R-DME-73933",
"R-DRE-110357",
"R-DRE-110362",
"R-DRE-110373",
"R-DRE-73930",
"R-DRE-73933",
"R-HSA-110357",
"R-HSA-110362",
... | [
"EC:3.1.11.2",
"REACTOME:R-DDI-110357",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110373",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DDI-73930",
"REACTOME:R-DDI-73933",
"REACTOME:R-DME-110357",
"REACTOME:R-DME-110373",
"REACTOME:R-DME-5651801",
"REACTOME:R-DME-73933",
"REACTOME:R-DRE-110357",
"RE... | 34 | [
"1ako",
"1bix",
"1de8",
"1de9",
"1dew",
"1e9n",
"1hd7",
"2isi",
"2j63",
"2jc4",
"2jc5",
"2o3c",
"2o3h",
"2voa",
"3fzi",
"3g00",
"3g0a",
"3g0r",
"3g1k",
"3g2c",
"3g2d",
"3g38",
"3g3c",
"3g3y",
"3g4t",
"3g8v",
"3g91",
"3ga6",
"3u8u",
"3w2x",
"3w2y",
"4b5f"... | 96 | [
"PUB00004207"
] | [
"7885481"
] | [
"Structure and function of the multifunctional DNA-repair enzyme exonuclease III."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Nucleocytoviricota",
"unclassified sequences"
] | [
152,
20911,
5067,
7,
310
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pomb... | [
9,
6,
3,
1,
14,
10,
2,
2,
11,
1,
8
] | 11 | true | Binding_site | AP endonuclease 1, binding site | AP endonuclease 1, binding site | AP_endonuclease_F1_BS | 7 |
IPR020848 | 20,848 | AP endonuclease 1, conserved site | AP_endonuclease_F1_CS | Conserved_site | 16,553 | false | false | DNA damaging agents such as the anti-tumour drugs bleomycin and neocarzinostatin or those that generate oxygen radicals produce a variety of lesions in DNA. Amongst these is base-loss which forms apurinic/apyrimidinic (AP) sites or strand breaks with atypical 3' termini. DNA repair at the AP sites is initiated by speci... | [
"GO:0003677",
"GO:0004519",
"GO:0006281"
] | [
"DNA binding",
"endonuclease activity",
"DNA repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE",
"PROSITE"
] | [
"PS00727",
"PS00728"
] | [
"AP_NUCLEASE_F1_2",
"AP_NUCLEASE_F1_3"
] | [
6653,
13382
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.11.2",
"R-DDI-110357",
"R-DDI-110362",
"R-DDI-110373",
"R-DDI-5651801",
"R-DDI-73930",
"R-DDI-73933",
"R-DME-110357",
"R-DME-110373",
"R-DME-5651801",
"R-DME-73933",
"R-DRE-110357",
"R-DRE-110362",
"R-DRE-110373",
"R-DRE-73930",
"R-DRE-73933",
"R-HSA-110357",
"R-HSA-110362",
... | [
"EC:3.1.11.2",
"REACTOME:R-DDI-110357",
"REACTOME:R-DDI-110362",
"REACTOME:R-DDI-110373",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DDI-73930",
"REACTOME:R-DDI-73933",
"REACTOME:R-DME-110357",
"REACTOME:R-DME-110373",
"REACTOME:R-DME-5651801",
"REACTOME:R-DME-73933",
"REACTOME:R-DRE-110357",
"RE... | 34 | [
"1ako",
"1bix",
"1de8",
"1de9",
"1dew",
"1e9n",
"1hd7",
"2isi",
"2j63",
"2o3c",
"2o3h",
"3u8u",
"4iem",
"4lnd",
"4qh9",
"4qhd",
"4qhe",
"5cfe",
"5cfg",
"5dff",
"5dfh",
"5dfi",
"5dfj",
"5dg0",
"5wn0",
"5wn1",
"5wn2",
"5wn3",
"5wn4",
"5wn5",
"6boq",
"6bor"... | 76 | [
"PUB00004207"
] | [
"7885481"
] | [
"Structure and function of the multifunctional DNA-repair enzyme exonuclease III."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Imitervirales",
"unclassified sequences"
] | [
53,
12398,
3940,
3,
159
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae... | [
8,
5,
2,
1,
3,
3,
2,
9,
6,
1,
1,
18
] | 12 | true | Conserved_site | AP endonuclease 1, conserved site | AP endonuclease 1, conserved site | AP_endonuclease_F1_CS | 7 |
IPR020849 | 20,849 | Small GTPase, Ras-type | Small_GTPase_Ras-type | Family | 39,124 | false | false | Ras proteins are small GTPases that regulate cell growth, proliferation and differentiation. The different Ras isoforms: H-ras, N-ras and K-ras, generate distinct signal outputs, despite interacting with a common set of activators and effectors. Ras is activated by guanine nucleotide exchange factors (GEFs) that releas... | [
"GO:0005525",
"GO:0007165",
"GO:0016020"
] | [
"GTP binding",
"signal transduction",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER"
] | [
"PTHR24070"
] | [
""
] | [
39124
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.5.2",
"R-BTA-170968",
"R-BTA-170984",
"R-BTA-354192",
"R-BTA-354194",
"R-BTA-372708",
"R-BTA-381676",
"R-BTA-392517",
"R-BTA-5674135",
"R-BTA-6798695",
"R-BTA-8875555",
"R-CEL-1169092",
"R-CEL-1433557",
"R-CEL-1632852",
"R-CEL-165159",
"R-CEL-166208",
"R-CEL-170968",
"R-CEL-17... | [
"EC:3.6.5.2",
"REACTOME:R-BTA-170968",
"REACTOME:R-BTA-170984",
"REACTOME:R-BTA-354192",
"REACTOME:R-BTA-354194",
"REACTOME:R-BTA-372708",
"REACTOME:R-BTA-381676",
"REACTOME:R-BTA-392517",
"REACTOME:R-BTA-5674135",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8875555",
"REACTOME:R-CEL-1169092",
... | 426 | [
"121p",
"1aa9",
"1agp",
"1bkd",
"1c1y",
"1clu",
"1crp",
"1crq",
"1crr",
"1ctq",
"1gnp",
"1gnq",
"1gnr",
"1gua",
"1he8",
"1iaq",
"1ioz",
"1jah",
"1jai",
"1k8r",
"1kao",
"1lf0",
"1lf5",
"1lfd",
"1nvu",
"1nvv",
"1nvw",
"1nvx",
"1p2s",
"1p2t",
"1p2u",
"1p2v"... | 788 | [
"PUB00000348",
"PUB00004087",
"PUB00011127",
"PUB00015117",
"PUB00023196",
"PUB00052600"
] | [
"2029511",
"1898771",
"12728271",
"11995995",
"2196171",
"2122258"
] | [
"The ras protein family: evolutionary tree and role of conserved amino acids.",
"The GTPase superfamily: conserved structure and molecular mechanism.",
"Ras proteins: different signals from different locations.",
"Structure of small G proteins and their regulators.",
"Refined crystal structure of the tripho... | [
1991,
1991,
2003,
2001,
1990,
1990
] | 6 | [
"IPR001806"
] | [
"IPR038851",
"IPR041840",
"IPR041841"
] | 1 | 3 | 0 | [
"Eukaryota",
"Legionella drozanskii LLAP-1",
"Viruses",
"metagenomes"
] | [
39108,
1,
11,
4
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
14,
48,
15,
98,
74,
5,
80,
4,
2
] | 9 | true | Family | Small GTPase, Ras-type | Small GTPase, Ras-type | Small_GTPase_Ras-type | 1 |
IPR020852 | 20,852 | Ribonucleotide reductase, class Ib, NrdI, bacterial | RNR_Ib_NrdI_bac | Family | 4,995 | false | false | Ribonucleotide reductases (RNRs) are enzymes that catalyse the conversion of ribonucleotides to the corresponding deoxyribonucleotides to provide the precursors of DNA synthesis. There are three classes (I-III) of RNRs and four known subclasses within class I RNRs (Ia-Id) [ ], which differ by their metal cofactor, thei... | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_00128"
] | [
"NrdI"
] | [
4995
] | 1 | [] | [] | [] | 0 | [
"1rlj",
"2x2o",
"2x2p",
"2xod",
"2xoe",
"3n39",
"3n3a",
"3n3b",
"4bmo",
"4bmp",
"6ebq",
"7mmp",
"7mmq",
"7mmr",
"7mms",
"7z3d",
"7z3e",
"8j4v",
"8j4w",
"8j4x",
"8j4y"
] | 21 | [
"PUB00017193",
"PUB00100955",
"PUB00100956"
] | [
"12686643",
"24295378",
"30224458"
] | [
"Corynebacterium ammoniagenes class Ib ribonucleotide reductase: transcriptional regulation of an atypical genomic organization in the nrd cluster.",
"Crystal structure of Bacillus cereus class Ib ribonucleotide reductase di-iron NrdF in complex with NrdI.",
"Metal-free class Ie ribonucleotide reductase from pa... | [
2003,
2014,
2018
] | 3 | [
"IPR004465"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Caudoviricetes",
"Rhynchospora breviuscula",
"ecological metagenomes"
] | [
4966,
17,
1,
11
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonucleotide reductase, class Ib, NrdI, bacterial | Ribonucleotide reductase, class Ib, NrdI, bacterial | RNR_Ib_NrdI_bac | 1 |
IPR020855 | 20,855 | Ureohydrolase, manganese-binding site | Ureohydrolase_Mn_BS | Binding_site | 33,328 | false | false | This entry represents a conserved region that contain charged residues which are involved in the binding of the two manganese ions in the active site. It is located in a loop segment of the central β-sheet [ , , , ]. The ureohydrolase superfamily includes arginase ( ), agmatinase ( ), formiminoglutamase ( ) and proclav... | [
"GO:0016813",
"GO:0046872"
] | [
"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines",
"metal ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROSITE"
] | [
"PS01053"
] | [
"ARGINASE_1"
] | [
33328
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.3",
"R-BTA-6798695",
"R-BTA-70635",
"R-HSA-351143",
"R-HSA-6798695",
"R-HSA-70635",
"R-HSA-9837999",
"R-MMU-6798695",
"R-MMU-70635",
"R-MMU-9837999",
"R-RNO-6798695",
"R-RNO-70635",
"R-RNO-9837999",
"R-SCE-6798695",
"R-SCE-70635",
"R-SCE-9837999",
"R-SPO-6798695",
"R-SPO-70635... | [
"EC:3.5.3",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70635",
"REACTOME:R-HSA-351143",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70635",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-70635",
"REACTOME:R-MMU-9837999",
"REACTOME:R-RNO-6798695",
"REACTOME:R-RNO-70635",
"RE... | 21 | [
"1cev",
"1d3v",
"1gq6",
"1gq7",
"1hq5",
"1hqf",
"1hqg",
"1hqh",
"1hqx",
"1p8m",
"1p8o",
"1p8p",
"1p8r",
"1pq3",
"1r1o",
"1rla",
"1t4p",
"1t4r",
"1t4s",
"1t4t",
"1t5f",
"1t5g",
"1ta1",
"1tbh",
"1tbj",
"1tbl",
"1wog",
"1woh",
"1woi",
"1wva",
"1wvb",
"1xfk"... | 157 | [
"PUB00001437",
"PUB00004245",
"PUB00025337",
"PUB00028086",
"PUB00028087",
"PUB00052609"
] | [
"7916684",
"8849731",
"12020346",
"15355972",
"16141327",
"18360740"
] | [
"Developmental and hormonal regulation of the Xenopus liver-type arginase gene.",
"Structure of a unique binuclear manganese cluster in arginase.",
"Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis.",
"Crystal structure of agmatinas... | [
1993,
1996,
2002,
2004,
2005,
2008
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1409,
22565,
8941,
3,
410
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)... | [
2,
3,
2,
5,
3,
5,
2,
9,
1,
5,
4
] | 11 | true | Binding_site | Ureohydrolase, manganese-binding site | Ureohydrolase, manganese-binding site | Ureohydrolase_Mn_BS | 9 |
IPR020856 | 20,856 | Circadian clock oscillator protein KaiA, C-terminal | Circadian_clock_protein_KaiA_C | Domain | 422 | false | false | This entry represents the C-terminal domain of Circadian clock protein KaiA. Cyanobacteria are the most primitive organisms known to exhibit circadian rhythms. KaiA, kaiB and kaiC constitute the circadian clock machinery in cyanobacteria, and kaiA activates kaiBC expression whereas kaiC represses it [ , ]. Apparent hom... | [
"GO:0006468",
"GO:0007623"
] | [
"protein phosphorylation",
"circadian rhythm"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF07688",
"PS51431"
] | [
"KaiA",
"KAIA_C"
] | [
366,
421
] | 2 | [
"GP"
] | [
"GenProp0465"
] | [
"GP:GenProp0465"
] | 1 | [
"1q6a",
"1q6b",
"1r5q",
"1r8j",
"1suy",
"1sv1",
"1v2z",
"4g86",
"5c5e",
"5jwr",
"5n8y"
] | 11 | [
"PUB00014089",
"PUB00030142",
"PUB00030572",
"PUB00031213",
"PUB00031979",
"PUB00103685",
"PUB00103686",
"PUB00103687"
] | [
"12438647",
"14749515",
"15007067",
"15256595",
"15170179",
"28302852",
"17717528",
"17916691"
] | [
"Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.",
"NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction.",
"Crystal structure of circadian clock protein KaiA... | [
2002,
2004,
2004,
2004,
2004,
2017,
2007,
2007
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methermicoccus shengliensis",
"ecological metagenomes"
] | [
402,
16,
1,
3
] | 4 | [] | [] | 0 | true | Domain | Circadian clock oscillator protein KaiA, C-terminal | Circadian clock oscillator protein KaiA, C-terminal | Circadian_clock_protein_KaiA_C | 3 |
IPR020857 | 20,857 | Serum albumin, conserved site | Serum_albumin_CS | Conserved_site | 2,197 | false | false | A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [ , , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs - its main function ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00212"
] | [
"ALBUMIN_1"
] | [
2197
] | 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-381426",
"R-BTA-8957275",
"R-HSA-114608",
"R-HSA-159418",
"R-HSA-189451",
"R-HSA-189483",
"R-HSA-196791",
"R-HSA-2168880",
"R-HSA-381426",
"R-HSA-8957275",
"R-HSA-8964058",
"R-HSA-9707564",
"R-HSA-9749641",
"R-HSA-9757110",
"R-HSA-9793528",
"R-MMU-114608",
"R-MMU-159418",
"R... | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-159418",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-2168880",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8964058",
"REACTOME:R-HSA... | 43 | [
"1ao6",
"1bj5",
"1bke",
"1bm0",
"1e78",
"1e7a",
"1e7b",
"1e7c",
"1e7e",
"1e7f",
"1e7g",
"1e7h",
"1e7i",
"1gni",
"1gnj",
"1h9z",
"1ha2",
"1hk1",
"1hk2",
"1hk3",
"1hk4",
"1hk5",
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9",
"1n5u",
"1o9x",
"1tf0",
"1uor"... | 242 | [
"PUB00000582",
"PUB00002857",
"PUB00003407",
"PUB00004128"
] | [
"2423133",
"7517938",
"2481749",
"1630489"
] | [
"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.",
"Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.",
"Amphibian albumins as memb... | [
1986,
1994,
1989,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
4,
2193
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
21,
10,
27
] | 3 | true | Conserved_site | Serum albumin, conserved site | Serum albumin, conserved site | Serum_albumin_CS | 3 |
IPR020858 | 20,858 | Serum albumin-like | Serum_albumin-like | Homologous_superfamily | 3,950 | false | false | A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [ , , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca 2+ , Na + and K + ), fatty acids, hormones, bilirubin and drugs - its main function ... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"SSF"
] | [
"SSF48552"
] | [
""
] | [
3950
] | 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-381426",
"R-BTA-8957275",
"R-HSA-114608",
"R-HSA-159418",
"R-HSA-189451",
"R-HSA-189483",
"R-HSA-196791",
"R-HSA-2168880",
"R-HSA-381426",
"R-HSA-8957275",
"R-HSA-8964058",
"R-HSA-9707564",
"R-HSA-9749641",
"R-HSA-9757110",
"R-HSA-9793528",
"R-MMU-114608",
"R-MMU-159418",
"R... | [
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-159418",
"REACTOME:R-HSA-189451",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-196791",
"REACTOME:R-HSA-2168880",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-8964058",
"REACTOME:R-HSA... | 43 | [
"1ao6",
"1bj5",
"1bke",
"1bm0",
"1e78",
"1e7a",
"1e7b",
"1e7c",
"1e7e",
"1e7f",
"1e7g",
"1e7h",
"1e7i",
"1gni",
"1gnj",
"1h9z",
"1ha2",
"1hk1",
"1hk2",
"1hk3",
"1hk4",
"1hk5",
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9",
"1n5u",
"1o9x",
"1tf0",
"1uor"... | 242 | [
"PUB00000582",
"PUB00002857",
"PUB00003407",
"PUB00004128"
] | [
"2423133",
"7517938",
"2481749",
"1630489"
] | [
"Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.",
"Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.",
"Amphibian albumins as memb... | [
1986,
1994,
1989,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
6,
3944
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
30,
21,
33
] | 4 | true | Homologous_superfamily | Serum albumin-like | Serum albumin-like | Serum_albumin-like | 5 |
IPR020859 | 20,859 | Roc domain | ROC | Domain | 7,975 | false | false | This entry represents the Roc domain found in small GTPase. Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [ , ]. Sequ... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51424"
] | [
"ROC"
] | [
7975
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.11.1",
"R-DDI-1483248",
"R-DDI-1632852",
"R-DDI-1660499",
"R-DDI-1660516",
"R-DDI-1660517",
"R-DDI-5675482",
"R-DDI-8876198",
"R-HSA-418889",
"R-HSA-8857538",
"R-MMU-8857538"
] | [
"EC:2.7.11.1",
"REACTOME:R-DDI-1483248",
"REACTOME:R-DDI-1632852",
"REACTOME:R-DDI-1660499",
"REACTOME:R-DDI-1660516",
"REACTOME:R-DDI-1660517",
"REACTOME:R-DDI-5675482",
"REACTOME:R-DDI-8876198",
"REACTOME:R-HSA-418889",
"REACTOME:R-HSA-8857538",
"REACTOME:R-MMU-8857538"
] | 11 | [
"2zej",
"3d6t",
"3dpu",
"4wnr",
"6hlu",
"6oje",
"6ojf",
"6vno",
"6vp6",
"6vp7",
"6vp8",
"6xaf",
"6xr4",
"7lht",
"7lhw",
"7li3",
"7li4",
"7thy",
"7thz",
"8e04",
"8e05",
"8e06",
"8fac",
"8fo2",
"8fo7",
"8fo8",
"8fo9",
"8r4b",
"8r4c",
"8r4d",
"8smc",
"8txz"... | 50 | [
"PUB00000348",
"PUB00004087",
"PUB00015117",
"PUB00023196",
"PUB00052600"
] | [
"2029511",
"1898771",
"11995995",
"2196171",
"2122258"
] | [
"The ras protein family: evolutionary tree and role of conserved amino acids.",
"The GTPase superfamily: conserved structure and molecular mechanism.",
"Structure of small G proteins and their regulators.",
"Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implicat... | [
1991,
1991,
2001,
1990,
1990
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
29,
561,
7378,
7
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
20,
3,
10,
6,
14
] | 6 | true | Domain | Roc domain | Roc domain | ROC | 6 |
IPR020860 | 20,860 | MIRO domain | MIRO_dom | Domain | 8,237 | false | false | Mitochondrial Rho (Miro) proteins are aberrant members of the small GTPase superfamily found in most eukaryotes. Miro contains a transmembrane region located at the C terminus anchors the protein to the outer membrane of mitochondria, the GTPase domains and EF-hands located in the cytoplasm. Miro and its cytoplasmic bi... | [
"GO:0003924",
"GO:0005525"
] | [
"GTPase activity",
"GTP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PROFILE"
] | [
"PS51423"
] | [
"MIRO"
] | [
8237
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.5.-",
"R-BTA-5689880",
"R-BTA-9013419",
"R-BTA-9013425",
"R-CEL-5689880",
"R-CEL-9013419",
"R-CEL-9013425",
"R-DDI-9013419",
"R-DDI-9013425",
"R-DME-5689880",
"R-DME-9013419",
"R-DME-9013425",
"R-DRE-5689880",
"R-DRE-9013419",
"R-DRE-9013425",
"R-HSA-5689880",
"R-HSA-9013419",
... | [
"EC:3.6.5.-",
"REACTOME:R-BTA-5689880",
"REACTOME:R-BTA-9013419",
"REACTOME:R-BTA-9013425",
"REACTOME:R-CEL-5689880",
"REACTOME:R-CEL-9013419",
"REACTOME:R-CEL-9013425",
"REACTOME:R-DDI-9013419",
"REACTOME:R-DDI-9013425",
"REACTOME:R-DME-5689880",
"REACTOME:R-DME-9013419",
"REACTOME:R-DME-9013... | 28 | [
"4c0j",
"4c0k",
"4c0l",
"5kso",
"5ksp",
"5ksy",
"5ksz",
"5kty",
"5ku1",
"5kut",
"6d71",
"9e2p"
] | 12 | [
"PUB00085980",
"PUB00085981",
"PUB00085982",
"PUB00085983",
"PUB00085984"
] | [
"27064409",
"24711517",
"27386195",
"21825164",
"28122638"
] | [
"C. elegans miro-1 Mutation Reduces the Amount of Mitochondria and Extends Life Span.",
"Miro1: new wheels for transferring mitochondria.",
"Regulation of mitochondrial trafficking, function and quality control by the mitochondrial GTPases Miro1 and Miro2.",
"The conserved GTPase Gem1 regulates endoplasmic re... | [
2016,
2014,
2015,
2011,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8237
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
15,
1,
12,
4,
11,
8,
1,
8,
13,
1,
1,
30
] | 12 | true | Domain | MIRO domain | MIRO domain | MIRO_dom | 4 |
IPR020863 | 20,863 | Membrane attack complex component/perforin domain, conserved site | MACPF_CS | Conserved_site | 7,917 | false | false | The membrane attack complex/perforin (MACPF) domain is conserved in bacteria, fungi, mammals and plants. It was originally identified and named as being common to five complement components (C6, C7, C8-alpha, C8-beta, and C9) and perforin. These molecules perform critical functions in innate and adaptive immunity. The ... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00279"
] | [
"MACPF_1"
] | [
7917
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-166665",
"R-BTA-977606",
"R-HSA-166665",
"R-HSA-9725371",
"R-HSA-977606",
"R-MMU-166665",
"R-MMU-977606",
"R-RNO-166665",
"R-RNO-977606"
] | [
"REACTOME:R-BTA-166665",
"REACTOME:R-BTA-977606",
"REACTOME:R-HSA-166665",
"REACTOME:R-HSA-9725371",
"REACTOME:R-HSA-977606",
"REACTOME:R-MMU-166665",
"REACTOME:R-MMU-977606",
"REACTOME:R-RNO-166665",
"REACTOME:R-RNO-977606"
] | 9 | [
"2qqh",
"2rd7",
"3nsj",
"3ojy",
"3t5o",
"4a5w",
"4e0s",
"5fmw",
"6cxo",
"6dlw",
"6h03",
"6h04",
"7nyc",
"7nyd",
"7pag",
"8b0f",
"8b0g",
"8b0h",
"8de6"
] | 19 | [
"PUB00045017",
"PUB00045018",
"PUB00052622",
"PUB00052623",
"PUB00052624",
"PUB00052625",
"PUB00052626",
"PUB00052627"
] | [
"17717151",
"17872444",
"16900325",
"18440555",
"15659064",
"17368498",
"15799997",
"10608922"
] | [
"A common fold mediates vertebrate defense and bacterial attack.",
"Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense.",
"Loss of Necrotic Spotted Lesions 1 associates with cell death and defense responses in Arabidopsis thaliana.",
"Crystal structure of the MACPF do... | [
2007,
2007,
2006,
2008,
2005,
2007,
2005,
1999
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
89,
7828
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
32,
27,
10,
22
] | 4 | true | Conserved_site | Membrane attack complex component/perforin domain, conserved site | Membrane attack complex component/perforin domain, conserved site | MACPF_CS | 7 |
IPR020867 | 20,867 | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site | THF_DH/CycHdrlase_CS | Conserved_site | 29,088 | false | false | Enzymes that participate in the transfer of one-carbon units require the coenzyme tetrahydrofolate (THF). Various reactions generate one-carbon derivatives of THF, which can be interconverted between different oxidation states by methylene-THF dehydrogenase ( ), methenyl-THF cyclohydrolase ( ) and formyl-THF synthetase... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00766",
"PS00767"
] | [
"THF_DHG_CYH_1",
"THF_DHG_CYH_2"
] | [
16981,
26720
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.5.1.5",
"3.5.4.9",
"PWY-1722",
"PWY-2201",
"PWY-3841",
"PWY-5030",
"PWY-5497",
"PWY-6613",
"PWY-7909",
"PWY-8303",
"R-DME-196757",
"R-HSA-196757",
"R-MMU-196757",
"R-RNO-196757",
"R-SCE-196757",
"R-SPO-196757"
] | [
"EC:1.5.1.5",
"EC:3.5.4.9",
"METACYC:PWY-1722",
"METACYC:PWY-2201",
"METACYC:PWY-3841",
"METACYC:PWY-5030",
"METACYC:PWY-5497",
"METACYC:PWY-6613",
"METACYC:PWY-7909",
"METACYC:PWY-8303",
"REACTOME:R-DME-196757",
"REACTOME:R-HSA-196757",
"REACTOME:R-MMU-196757",
"REACTOME:R-RNO-196757",
... | 16 | [
"1a4i",
"1b0a",
"1dia",
"1dib",
"1dig",
"3l07",
"3ngl",
"3ngx",
"3p2o",
"4a26",
"4a5o",
"4b4u",
"4b4v",
"4b4w",
"5nhs",
"5o22",
"5o28",
"5o2a",
"5tc4",
"5zf1",
"6ape",
"6de8",
"6deb",
"6ecp",
"6ecq",
"6ecr",
"6jib",
"6jid",
"6kg2",
"6s4a",
"6s4e",
"6s4f"... | 49 | [
"PUB00000304",
"PUB00000651"
] | [
"2541774",
"8485162"
] | [
"Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme.",
"The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase."
] | [
1989,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
246,
19287,
9165,
9,
381
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
14,
1,
24,
7,
1,
23,
9,
2,
8,
16,
2,
1,
13
] | 13 | true | Conserved_site | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site | THF_DH/CycHdrlase_CS | 7 |
IPR020868 | 20,868 | Bifunctional enzyme Fae/Hps | Fae/Hps | Family | 245 | false | false | This bifunctional enzyme catalyses the condensation of formaldehyde with tetrahydromethanopterin (H4MPT) to 5,10-methylenetetrahydromethanopterin and the formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. Formaldehyde activating enzyme (Fae) was first discovered in methylotrophic bacteria, ... | [
"GO:0016832",
"GO:0016840",
"GO:0016051"
] | [
"aldehyde-lyase activity",
"carbon-nitrogen lyase activity",
"carbohydrate biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01268",
"NF009833"
] | [
"Fae_Hps",
"PRK13307.1"
] | [
231,
245
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.43",
"4.2.1.147",
"PWY-1723",
"PWY-1861",
"PWY-7796"
] | [
"EC:4.1.2.43",
"EC:4.2.1.147",
"METACYC:PWY-1723",
"METACYC:PWY-1861",
"METACYC:PWY-7796"
] | 5 | [] | 0 | [
"PUB00053140"
] | [
"16075199"
] | [
"Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
230,
15
] | 2 | [] | [] | 0 | true | Family | Bifunctional enzyme Fae/Hps | Bifunctional enzyme Fae/Hps | Fae/Hps | 6 |
IPR020870 | 20,870 | Uncharacterised protein family UPF0387, membrane | UPF0387_membrane | Family | 625 | false | false | This family of membrane proteins is found in Enterobacteria. Their function is unknown. | [
"GO:0005886"
] | [
"plasma membrane"
] | [
"cellular_component"
] | 1 | [
"HAMAP",
"NCBIFAM",
"PFAM"
] | [
"MF_01362",
"NF010225",
"PF27791"
] | [
"UPF0387",
"PRK13681.1",
"UPF0387_membrane"
] | [
608,
544,
625
] | 3 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
625
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Uncharacterised protein family UPF0387, membrane | Uncharacterised protein family UPF0387, membrane | UPF0387_membrane | 4 |
IPR020871 | 20,871 | Ribulose bisphosphate carboxylase large subunit, type II | RuBisCO_lsuII | Family | 472 | false | false | Ribulose bisphosphate carboxylase (RuBisCO) [ , ] catalyses the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which th... | [
"GO:0000287",
"GO:0016984",
"GO:0015977"
] | [
"magnesium ion binding",
"ribulose-bisphosphate carboxylase activity",
"carbon fixation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"CDD"
] | [
"MF_01339",
"cd08211"
] | [
"RuBisCO_L_type2",
"RuBisCO_large_II"
] | [
297,
472
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.1.39",
"PWY-5532",
"PWY-5723"
] | [
"EC:4.1.1.39",
"METACYC:PWY-5532",
"METACYC:PWY-5723"
] | 3 | [
"1rba",
"1rus",
"2rus",
"4lf1",
"4lf2",
"5c2c",
"5c2g",
"5han",
"5hao",
"5hat",
"5hjx",
"5hjy",
"5hk4",
"5hql",
"5hqm",
"5koz",
"5mac",
"5rub",
"6ius",
"7t1c",
"7t1j",
"7vwx",
"8baa",
"9rub"
] | 24 | [
"PUB00000034",
"PUB00004038",
"PUB00015291",
"PUB00020282",
"PUB00049187",
"PUB00080670",
"PUB00080673",
"PUB00080674"
] | [
"6351728",
"12221984",
"1969412",
"9034362",
"18063718",
"18281717",
"24942737",
"18004873"
] | [
"Ribulose-1,5-bisphosphate carboxylase-oxygenase.",
"Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.",
"Examination of the intersubunit interaction between glutamate-48 and lysine-168 of ribulose-bisphosphate carboxylase/oxygenase by site-directed mutagenesis.",
"The struct... | [
1983,
2002,
1990,
1997,
2007,
2008,
2014,
2007
] | 8 | [
"IPR033966"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)",
"unclassified sequences"
] | [
294,
149,
1,
28
] | 4 | [] | [] | 0 | true | Family | Ribulose bisphosphate carboxylase large subunit, type II | Ribulose bisphosphate carboxylase large subunit, type II | RuBisCO_lsuII | 5 |
IPR020872 | 20,872 | 2-phosphoglycerate kinase | 2PKG | Family | 136 | false | false | Analysis of the metabolome of a number of methanogenic archaea revealed that they produced a number of unusual compounds of low molecular weight, one of which was cyclic 2,3-diphosphoglycerate (cDPG). This has been found to occur in several methanogens in high concentrations of up to 1 Molar. The highest intracellular ... | [
"GO:0016774"
] | [
"phosphotransferase activity, carboxyl group as acceptor"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00769",
"NF003259"
] | [
"2PGK",
"PRK04220.1"
] | [
123,
136
] | 2 | [
"EC",
"METACYC"
] | [
"2.7.2.16",
"PWY-8098"
] | [
"EC:2.7.2.16",
"METACYC:PWY-8098"
] | 2 | [] | 0 | [
"PUB00053141",
"PUB00053142"
] | [
"8159166",
"2226838"
] | [
"Cloning, sequencing and expression of the gene encoding 2-phosphoglycerate kinase from Methanothermus fervidus.",
"Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and characterization of 2-phosphoglycerate kinase and cyclic 2,3-diphosphoglycerate synthetase from Methanothermus fervidus."
] | [
1994,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"Rubrobacteraceae",
"bioreactor metagenome"
] | [
124,
11,
1
] | 3 | [] | [] | 0 | true | Family | 2-phosphoglycerate kinase | 2-phosphoglycerate kinase | 2PKG | 4 |
IPR020873 | 20,873 | 3'-5' exoribonuclease YhaM | 3'-5'_exoribonuclease_YhaM | Family | 469 | false | false | Exoribonucleases are enzymes that degrade RNA by removing terminal nucleotides from either the 5' end or 3' end of various RNA. This entry represents YhaM, which shows 3'-5' exoribonuclease activity [ , ]. | [
"GO:0000175"
] | [
"3'-5'-RNA exonuclease activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01427"
] | [
"3_5_Exoribonuc_YhaM"
] | [
469
] | 1 | [] | [] | [] | 0 | [
"9h3f"
] | 1 | [
"PUB00100527",
"PUB00100528"
] | [
"19880604",
"12399495"
] | [
"Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-III.",
"Bacillus subtilis YhaM, a member of a new family of 3'-to-5' exonucleases in gram-positive bacteria."
] | [
2010,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
469
] | 1 | [] | [] | 0 | true | Family | 3'-5' exoribonuclease YhaM | 3'-5' exoribonuclease YhaM | 3'-5'_exoribonuclease_YhaM | 3 |
IPR020874 | 20,874 | NAD(P)H-quinone oxidoreductase, subunit N | NAD(P)H-quinone_OxRdtase_su_N | Family | 921 | false | false | NAD(P)H-quinone oxidoreductase (NDH-1) shuttles electrons from an unknown electron donor, via FMN and iron-sulphur (Fe-S) centres, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. It couples the redox reaction... | [
"GO:0016655",
"GO:0016020"
] | [
"oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER"
] | [
"MF_01353",
"PF11909",
"PTHR35515"
] | [
"NDH1_NDH1N",
"NdhN",
""
] | [
375,
916,
914
] | 3 | [
"EC"
] | [
"7.1.1.-"
] | [
"EC:7.1.1.-"
] | 1 | [
"6hum",
"6khi",
"6khj",
"6l7o",
"6l7p",
"6nbq",
"6nbx",
"6nby",
"6tjv",
"7eu3",
"7f9o",
"7wfg",
"7wg5",
"9grx"
] | 14 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
374,
547
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
2,
3,
8
] | 3 | true | Family | NAD(P)H-quinone oxidoreductase, subunit N | NAD(P)H-quinone oxidoreductase, subunit N | NAD(P)H-quinone_OxRdtase_su_N | 8 |
IPR020875 | 20,875 | 3-phenylpropionate/cinnamic acid dioxygenase, alpha subunit | HcaE | Family | 158 | false | false | Phenylpropanoid compounds are widely available in natural environments, and they can originate from putrefaction of proteins in soil or as breakdown products of several constituents of plants, such as lignin, various oils, and resins. Microbial catabolism of phenylpropanoid compounds plays an important role not only in... | [
"GO:0005506",
"GO:0008695"
] | [
"iron ion binding",
"3-phenylpropionate dioxygenase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"HAMAP"
] | [
"MF_01648"
] | [
"HcaE"
] | [
158
] | 1 | [
"EC",
"METACYC"
] | [
"1.14.12.19",
"PWY-6690"
] | [
"EC:1.14.12.19",
"METACYC:PWY-6690"
] | 2 | [
"8k0a"
] | 1 | [
"PUB00053145",
"PUB00053146",
"PUB00053147",
"PUB00053148",
"PUB00053149",
"PUB00054929",
"PUB00054961"
] | [
"4348920",
"6345502",
"9324265",
"3531186",
"8399388",
"9603882",
"11729263"
] | [
"The purification and properties of the flavoprotein melilotate hydroxylase.",
"Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli.",
"A 3-(3-hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: cloning and characterization of the hpp operon.",
"Isola... | [
1973,
1983,
1997,
1986,
1993,
1998,
2001
] | 7 | [
"IPR001663"
] | [] | 1 | 0 | 1 | [
"Gammaproteobacteria"
] | [
158
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 3-phenylpropionate/cinnamic acid dioxygenase, alpha subunit | 3-phenylpropionate/cinnamic acid dioxygenase, alpha subunit | HcaE | 9 |
IPR020876 | 20,876 | Tyrosine recombinase XerD-like | Tyrosine_recombinase_XerD-like | Family | 604 | false | false | Phage integrases are enzymes that mediate unidirectional site-specific recombination between two DNA recognition sequences, the phage attachment site, attP, and the bacterial attachment site, attB [ ]. Integrases may be grouped into two major families, the tyrosine recombinases and the serine recombinases, based on the... | [
"GO:0005737"
] | [
"cytoplasm"
] | [
"cellular_component"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01817",
"NF002685"
] | [
"Recomb_XerD_like",
"PRK02436.1"
] | [
544,
604
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014061",
"PUB00014062"
] | [
"14687564",
"12560475"
] | [
"Phage integrases: biology and applications.",
"Conservation of structure and function among tyrosine recombinases: homology-based modeling of the lambda integrase core-binding domain."
] | [
2004,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
603,
1
] | 2 | [] | [] | 0 | true | Family | Tyrosine recombinase XerD-like | Tyrosine recombinase XerD-like | Tyrosine_recombinase_XerD-like | 3 |
IPR020877 | 20,877 | Interleukin-1 conserved site | IL-1_CS | Conserved_site | 1,748 | false | false | Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PROSITE"
] | [
"PS00253"
] | [
"INTERLEUKIN_1"
] | [
1748
] | 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-448706",
"R-BTA-5620971",
"R-BTA-9020702",
"R-CFA-9020702",
"R-HSA-2559582",
"R-HSA-448706",
"R-HSA-5620971",
"R-HSA-5660668",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-9014826",
"R-HSA-9020702",
"R-HSA-9660826",
"R-MMU-448706",
"R-MMU-5620971",
"R-MMU-5660668",
"R-MMU-9014826"... | [
"REACTOME:R-BTA-448706",
"REACTOME:R-BTA-5620971",
"REACTOME:R-BTA-9020702",
"REACTOME:R-CFA-9020702",
"REACTOME:R-HSA-2559582",
"REACTOME:R-HSA-448706",
"REACTOME:R-HSA-5620971",
"REACTOME:R-HSA-5660668",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-9014826",
"REACTOME:... | 26 | [
"1hib",
"1i1b",
"1ilr",
"1ilt",
"1iob",
"1ira",
"1irp",
"1itb",
"1l2h",
"1md6",
"1s0l",
"1t4q",
"1too",
"1tp0",
"1twe",
"1twm",
"21bi",
"2i1b",
"2ila",
"2irt",
"2kh2",
"2kki",
"2l5x",
"2mib",
"2nvh",
"2wry",
"31bi",
"3ltq",
"3nj5",
"3o4o",
"3pok",
"41bi"... | 85 | [
"PUB00003281",
"PUB00004697",
"PUB00007346",
"PUB00007347",
"PUB00007348",
"PUB00007349",
"PUB00007350"
] | [
"1738162",
"2602367",
"2969618",
"8702856",
"1833184",
"1826022",
"1339315"
] | [
"beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.",
"Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.",
"cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.",
... | [
1992,
1989,
1988,
1996,
1991,
1991,
1992
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1748
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
14,
7,
13,
21
] | 4 | true | Conserved_site | Interleukin-1 conserved site | Interleukin-1 conserved site | IL-1_CS | 2 |
IPR020878 | 20,878 | Ribulose bisphosphate carboxylase, large chain, active site | RuBisCo_large_chain_AS | Active_site | 122,837 | false | false | Ribulose bisphosphate carboxylase (RuBisCO) [ , ] catalyses the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It catalyzes the primary CO2 fixation step. RuBisCO consists of a large catalytic unit and a small subunit of undetermined function. In plants, the l... | [
"GO:0000287",
"GO:0016984",
"GO:0015977"
] | [
"magnesium ion binding",
"ribulose-bisphosphate carboxylase activity",
"carbon fixation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PROSITE"
] | [
"PS00157"
] | [
"RUBISCO_LARGE"
] | [
122837
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.1.39",
"PWY-5532",
"PWY-5723"
] | [
"EC:4.1.1.39",
"METACYC:PWY-5532",
"METACYC:PWY-5723"
] | 3 | [
"1aa1",
"1aus",
"1bwv",
"1bxn",
"1ej7",
"1gk8",
"1ir1",
"1ir2",
"1iwa",
"1rbl",
"1rbo",
"1rco",
"1rcx",
"1rlc",
"1rld",
"1rsc",
"1rus",
"1rxo",
"1svd",
"1upm",
"1upp",
"1uw9",
"1uwa",
"1uzd",
"1uzh",
"1wdd",
"2rus",
"2v63",
"2v67",
"2v68",
"2v69",
"2v6a"... | 120 | [
"PUB00000034",
"PUB00004038",
"PUB00015291",
"PUB00020282"
] | [
"6351728",
"12221984",
"1969412",
"9034362"
] | [
"Ribulose-1,5-bisphosphate carboxylase-oxygenase.",
"Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.",
"Examination of the intersubunit interaction between glutamate-48 and lysine-168 of ribulose-bisphosphate carboxylase/oxygenase by site-directed mutagenesis.",
"The struct... | [
1983,
2002,
1990,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sweet potato chlorotic fleck virus",
"unclassified sequences"
] | [
120,
4343,
117737,
10,
627
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
12,
8
] | 3 | true | Active_site | Ribulose bisphosphate carboxylase, large chain, active site | Ribulose bisphosphate carboxylase, large chain, active site | RuBisCo_large_chain_AS | 2 |
IPR020879 | 20,879 | N-acetylglucosamine-binding protein A | GlcNAc-bd_A | Family | 161 | false | false | This entry represents the N-acetylglucosamine-binding protein A (GbpA) of various pathogenic bacteria, including Vibrio cholerae, which is the etiologic agent of cholera in humans. GbpA binds to chitin and specifically to the chitin monomer N-acetylglucosamine (GlcNAc), a sugar residue that is also found on the surface... | [
"GO:0008061"
] | [
"chitin binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP"
] | [
"MF_01905"
] | [
"GbpA"
] | [
161
] | 1 | [] | [] | [] | 0 | [
"8gul",
"8gum"
] | 2 | [
"PUB00053150",
"PUB00056779"
] | [
"19734310",
"16341015"
] | [
"Levels of the Secreted Vibrio cholerae Attachment Factor, GbpA, are Modulated by Quorum Sensing Induced Proteolysis.",
"A colonization factor links Vibrio cholerae environmental survival and human infection."
] | [
2009,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
161
] | 1 | [] | [] | 0 | true | Family | N-acetylglucosamine-binding protein A | N-acetylglucosamine-binding protein A | GlcNAc-bd_A | 2 |
IPR020880 | 20,880 | Protein of unknown function UPF0741 | UPF0741 | Family | 634 | false | false | This entry contains bacterial proteins with no known function. | [] | [] | [] | 0 | [
"HAMAP"
] | [
"MF_01863"
] | [
"UPF0741"
] | [
634
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR009910"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"human gut metagenome"
] | [
633,
1
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function UPF0741 | Protein of unknown function UPF0741 | UPF0741 | 4 |
IPR020881 | 20,881 | Phosphoglycerol transferase I | OpgB | Family | 944 | false | false | Phosphoglycerol transferase I (OpgB) transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones for the biosynthesis of osmoregulated periplasmic glucan (OPG) [ , ]. Members of this protein family are found in Proteobacteria. | [
"GO:0008960",
"GO:0009250",
"GO:0005886"
] | [
"phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase activity",
"glucan biosynthetic process",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_01070"
] | [
"MdoB_OpgB"
] | [
944
] | 1 | [
"EC"
] | [
"2.7.8.20"
] | [
"EC:2.7.8.20"
] | 1 | [] | 0 | [
"PUB00053242",
"PUB00053243"
] | [
"6094515",
"2985566"
] | [
"Biosynthesis of membrane-derived oligosaccharides: characterization of mdoB mutants defective in phosphoglycerol transferase I activity.",
"Characterization of an Escherichia coli mdoB mutant strain unable to transfer sn-1-phosphoglycerol to membrane-derived oligosaccharides."
] | [
1984,
1985
] | 2 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
944
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphoglycerol transferase I | Phosphoglycerol transferase I | OpgB | 7 |
IPR020883 | 20,883 | Type I toxin-antitoxin system, SymE toxin | TypeI_TA_SymE | Family | 609 | false | false | SymE (SOS-induced yjiW gene with similarity to MazE) belongs to type I toxin-antitoxin systems, and it is an SOS-induced toxin. It inhibits cell growth, decreases protein synthesis and increases RNA degradation. It may play a role in the recycling of RNAs damaged under SOS response-inducing conditions. Its translation ... | [
"GO:0003723",
"GO:0004521",
"GO:0016070",
"GO:0005737"
] | [
"RNA binding",
"RNA endonuclease activity",
"RNA metabolic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01193",
"NF010128"
] | [
"Endoribonucl_SymE",
"PRK13605.1"
] | [
605,
592
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053151",
"PUB00064452"
] | [
"17462020",
"17376733"
] | [
"An antisense RNA controls synthesis of an SOS-induced toxin evolved from an antitoxin.",
"RNA antitoxins."
] | [
2007,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
609
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Type I toxin-antitoxin system, SymE toxin | Type I toxin-antitoxin system, SymE toxin | TypeI_TA_SymE | 2 |
IPR020885 | 20,885 | UPF0367 | UPF0367 | Family | 368 | false | false | This entry represents an uncharacterised family of proteins called UPF0367. The structure of these proteins is reminiscent of PH domains and like bacterial PH domains are predicted to form large homomeric ring complexes. In the case of this family they seem to form homoheptamers. | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"PFAM"
] | [
"MF_01360",
"NF010236",
"PF26132"
] | [
"UPF0367",
"PRK13683.1",
"UPF0367"
] | [
254,
359,
368
] | 3 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota",
"Paulinella"
] | [
364,
4
] | 2 | [] | [] | 0 | true | Family | UPF0367 | UPF0367 | UPF0367 | 6 |
IPR020886 | 20,886 | MTH_967-like | MTH_967-like | Family | 774 | false | false | Archaebacterial Putative HTH-type transcriptional regulatory proteins, including MTH_967 from Methanothermobacter thermautotrophicus contain a cro/C1-type HTH domain. The cro/C1-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 residues present in transcriptional regulators. The domain is n... | [
"GO:0003700",
"GO:0006355"
] | [
"DNA-binding transcription factor activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_00584"
] | [
"HTH_type_cro_C1"
] | [
774
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
763,
11
] | 2 | [] | [] | 0 | true | Family | MTH_967-like | MTH_967-like | MTH_967-like | 2 |
IPR020888 | 20,888 | Ribulose bisphosphate carboxylase large subunit, type I | RuBisCO_lsuI | Family | 66,548 | false | false | Ribulose bisphosphate carboxylase (RuBisCO) [ , ] catalyses the initial step in Calvin's reductive pentose phosphate cycle in plants as well as purple and green bacteria. It catalyzes the primary CO2 fixation step. RuBisCO consists of a large catalytic unit and a small subunit of undetermined function. In plants, the l... | [
"GO:0000287",
"GO:0016984",
"GO:0015977"
] | [
"magnesium ion binding",
"ribulose-bisphosphate carboxylase activity",
"carbon fixation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"CDD"
] | [
"MF_01338",
"cd08212"
] | [
"RuBisCO_L_type1",
"RuBisCO_large_I"
] | [
61373,
63487
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"4.1.1.39",
"PWY-5532",
"PWY-5723"
] | [
"EC:4.1.1.39",
"METACYC:PWY-5532",
"METACYC:PWY-5723"
] | 3 | [
"1aa1",
"1aus",
"1bwv",
"1bxn",
"1ej7",
"1gk8",
"1ir1",
"1ir2",
"1iwa",
"1rbl",
"1rbo",
"1rco",
"1rcx",
"1rlc",
"1rld",
"1rsc",
"1rxo",
"1svd",
"1upm",
"1upp",
"1uw9",
"1uwa",
"1uzd",
"1uzh",
"1wdd",
"2v63",
"2v67",
"2v68",
"2v69",
"2v6a",
"2vdh",
"2vdi"... | 103 | [
"PUB00000034",
"PUB00004038",
"PUB00015291",
"PUB00020282",
"PUB00049187",
"PUB00080670"
] | [
"6351728",
"12221984",
"1969412",
"9034362",
"18063718",
"18281717"
] | [
"Ribulose-1,5-bisphosphate carboxylase-oxygenase.",
"Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.",
"Examination of the intersubunit interaction between glutamate-48 and lysine-168 of ribulose-bisphosphate carboxylase/oxygenase by site-directed mutagenesis.",
"The struct... | [
1983,
2002,
1990,
1997,
2007,
2008
] | 6 | [
"IPR033966"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1895,
64609,
44
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
8,
7
] | 3 | true | Family | Ribulose bisphosphate carboxylase large subunit, type I | Ribulose bisphosphate carboxylase large subunit, type I | RuBisCO_lsuI | 1 |
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