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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR013972 | 13,972 | YcbB domain | YcbB | Domain | 1,512 | false | false | YcbB is a DNA-binding protein [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08664"
] | [
"YcbB"
] | [
1512
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00033342"
] | [
"15995196"
] | [
"Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
1508,
4
] | 2 | [] | [] | 0 | true | Domain | YcbB domain | YcbB domain | YcbB | 3 |
IPR013974 | 13,974 | SAF domain | SAF | Domain | 48,584 | false | false | This entry includes a range of different proteins, such as antifreeze proteins, flagellar FlgA proteins, and CpaB pilus proteins [ ]. This domain adopts a β-clip fold [ , ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08666",
"SM00858"
] | [
"SAF",
"SAF"
] | [
35989,
46096
] | 2 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1636",
"GenProp1737",
"R-DME-4085001",
"R-HSA-4085001",
"R-MMU-4085001"
] | [
"GP:GenProp1636",
"GP:GenProp1737",
"REACTOME:R-DME-4085001",
"REACTOME:R-HSA-4085001",
"REACTOME:R-MMU-4085001"
] | 5 | [
"1c89",
"1c8a",
"1ops",
"1ucs",
"1vli",
"1wvo",
"1xuu",
"1xuz",
"2wqp",
"3frn",
"3g8r",
"3k3s",
"3laz",
"3nla",
"3rdn",
"3tee",
"3upl",
"3upy",
"3vjp",
"3vki",
"4ipi",
"4ipj",
"4ur6",
"5xqn",
"5xqp",
"5xqr",
"5xqu",
"5xqv",
"5xr0",
"6ppw",
"6ppx",
"6ppy"... | 37 | [
"PUB00017194",
"PUB00089354",
"PUB00095186"
] | [
"15146494",
"27273476",
"31811683"
] | [
"The emergence of catalytic and structural diversity within the beta-clip fold.",
"Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.",
"Structure of galactarate dehydratase, a new fold in an enolase involved in bacterial fitness after antibiotic... | [
2004,
2016,
2020
] | 3 | [] | [
"IPR006190",
"IPR017585",
"IPR044144"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
314,
46059,
1434,
2,
775
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
3,
2,
1,
4
] | 6 | true | Domain | SAF domain | SAF domain | SAF | 8 |
IPR013975 | 13,975 | Transcription regulator BetR, N-terminal | Tscrpt_reg_BetR_N | Domain | 1,253 | false | false | CheY-like phosphoacceptor (or receiver [REC]) domain is a common module in a variety of response regulators of the bacterial signal transduction systems. BetR is one of the many response regulators and is encoded mainly in Burkholderia spp. It is a N-terminal helix-turn-helix domain (HTH) and has been shown to be relat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08667"
] | [
"BetR"
] | [
1253
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053583"
] | [
"16740923"
] | [
"Structural classification of bacterial response regulators: diversity of output domains and domain combinations."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
1201,
45,
4,
3
] | 4 | [] | [] | 0 | true | Domain | Transcription regulator BetR, N-terminal | Transcription regulator BetR, N-terminal | Tscrpt_reg_BetR_N | 5 |
IPR013978 | 13,978 | MEKHLA | MEKHLA | Domain | 5,214 | false | false | The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08670"
] | [
"MEKHLA"
] | [
5214
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanoperedens nitratireducens",
"Eukaryota",
"metagenomes"
] | [
1231,
1,
3971,
11
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
25,
15,
66
] | 3 | true | Domain | MEKHLA | MEKHLA | MEKHLA | 1 |
IPR013979 | 13,979 | Translation initiation factor, beta propellor-like domain | TIF_beta_prop-like | Domain | 12,790 | false | false | This entry contains β-propeller domains found in eukaryotic translation initiation factors and WD domain-containing proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08662"
] | [
"eIF2A"
] | [
12790
] | 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-72649",
"R-BTA-72689",
"R-BTA-72695",
"R-BTA-72702",
"R-CEL-156827",
"R-CEL-72649",
"R-CEL-72689",
"R-CEL-72695",
"R-CEL-72702",
"R-DDI-156827",
"R-DDI-72689",
"R-DDI-72695",
"R-DDI-72702",
"R-DME-156827",
"R-DME-72649",
"R-DME-72689",
"R-DME-72695",
"R-DME... | [
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-72649",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72695",
"REACTOME:R-CEL-72702",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-72689",
"... | 46 | [
"3wj9",
"4nox",
"4u1f",
"4uer",
"5a5u",
"5k1h",
"6fec",
"6fyx",
"6fyy",
"6gsm",
"6gsn",
"6ybt",
"6zce",
"6zmw",
"6zon",
"6zp4",
"6zu9",
"6zvj",
"7a09",
"7qp6",
"7qp7",
"8cah",
"8cas",
"8dys",
"8oz0",
"8pj1",
"8pj2",
"8pj3",
"8pj4",
"8pj5",
"8pj6",
"8xxn"... | 34 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Moumouvirus sp. 'Monve'",
"unclassified sequences"
] | [
9,
367,
12410,
1,
3
] | 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... | [
20,
2,
3,
5,
11,
5,
2,
5,
9,
2,
2,
9
] | 12 | true | Domain | Translation initiation factor, beta propellor-like domain | Translation initiation factor, beta propellor-like domain | TIF_beta_prop-like | 7 |
IPR013980 | 13,980 | MANSC domain | MANSC_dom | Domain | 6,712 | false | false | The MANSC (motif at N terminus with seven cysteines) domain is a module with a well-conserved seven cysteine motif that is present at the N terminus of higher multicellular animal membrane and extracellular proteins. It is possible that some of the cysteine residues in the MANSC domain form structurally important disul... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE"
] | [
"PF07502",
"PF23597",
"PS50986"
] | [
"MANEC",
"KIAA0319_N",
"MANSC"
] | [
4087,
2549,
5074
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50986",
"R-HSA-6806942",
"R-HSA-8852405",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-6806942",
"R-MMU-8852405",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-8856825",
"R-RNO-8856828"
] | [
"PROSITEDOC:PDOC50986",
"REACTOME:R-HSA-6806942",
"REACTOME:R-HSA-8852405",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-6806942",
"REACTOME:R-MMU-8852405",
"REACTOME:R-MMU-8856825",
"REACTOME:R-MMU-8856828",
"REACTOME:R-RNO-8856825",
"REACTOME:R-RNO-8856828"
] | 11 | [
"2msx",
"5h7v"
] | 2 | [
"PUB00015396",
"PUB00155696",
"PUB00155697"
] | [
"15124631",
"19679544",
"26814968"
] | [
"MANSC: a seven-cysteine-containing domain present in animal membrane and extracellular proteins.",
"The effect of variation in expression of the candidate dyslexia susceptibility gene homolog Kiaa0319 on neuronal migration and dendritic morphology in the rat.",
"An essential receptor for adeno-associated virus... | [
2004,
2010,
2016
] | 3 | [] | [
"IPR011106"
] | 0 | 1 | 0 | [
"Metazoa"
] | [
6712
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
23,
3,
35,
19,
22
] | 6 | true | Domain | MANSC domain | MANSC domain | MANSC_dom | 9 |
IPR013983 | 13,983 | Aldehyde ferredoxin oxidoreductase, N-terminal | Ald_Fedxn_OxRdtase_N | Domain | 5,849 | false | false | This entry represents the N-terminal domain of these enzymes. This domain has been shown to interact with the tungsten cofactor [ ]. Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [ ] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [ ]. This... | [
"GO:0016491",
"GO:0016625",
"GO:0051536"
] | [
"oxidoreductase activity",
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF02730",
"SM00790"
] | [
"AFOR_N",
"AFOR_N"
] | [
5848,
5716
] | 2 | [] | [] | [] | 0 | [
"1aor",
"1b25",
"1b4n",
"4z3w",
"4z3x",
"4z3y",
"4z3z",
"4z40",
"6x1o",
"6x6u",
"8c0z",
"9g7j",
"9mqx"
] | 13 | [
"PUB00005196",
"PUB00007125",
"PUB00007126",
"PUB00007127",
"PUB00007128",
"PUB00007129",
"PUB00007130"
] | [
"7878465",
"9242907",
"8672295",
"2550230",
"8026480",
"7721730",
"9275170"
] | [
"Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase.",
"Molybdenum-cofactor-containing enzymes: structure and mechanism.",
"Tungsten in biological systems.",
"Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to al... | [
1995,
1997,
1996,
1989,
1994,
1995,
1997
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1826,
3548,
4,
471
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Aldehyde ferredoxin oxidoreductase, N-terminal | Aldehyde ferredoxin oxidoreductase, N-terminal | Ald_Fedxn_OxRdtase_N | 3 |
IPR013984 | 13,984 | Aldehyde ferredoxin oxidoreductase, domain 2 | Ald_Fedxn_OxRdtase_dom2 | Homologous_superfamily | 5,606 | false | false | This superfamily represents an α-helical domain which is involved in binding the tungsten cofactor, and also contains an iron-sulphur cluster [ ]. Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [ ] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxyl... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.569.10"
] | [
""
] | [
5606
] | 1 | [] | [] | [] | 0 | [
"1aor",
"1b25",
"1b4n",
"4z3w",
"4z3x",
"4z3y",
"4z3z",
"4z40",
"6x1o",
"6x6u",
"8c0z",
"9g7j",
"9mqx"
] | 13 | [
"PUB00007125",
"PUB00007126",
"PUB00007127",
"PUB00007128",
"PUB00007129",
"PUB00007130",
"PUB00021189"
] | [
"9242907",
"8672295",
"2550230",
"8026480",
"7721730",
"9275170",
"10024458"
] | [
"Molybdenum-cofactor-containing enzymes: structure and mechanism.",
"Tungsten in biological systems.",
"Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes.",
"The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a mol... | [
1997,
1996,
1989,
1994,
1995,
1997,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1824,
3334,
4,
444
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Aldehyde ferredoxin oxidoreductase, domain 2 | Aldehyde ferredoxin oxidoreductase, domain 2 | Ald_Fedxn_OxRdtase_dom2 | 8 |
IPR013985 | 13,985 | Aldehyde ferredoxin oxidoreductase, domain 3 | Ald_Fedxn_OxRdtase_dom3 | Homologous_superfamily | 5,473 | false | false | This superfamily represents an α-helical domain involved in binding the tungsten cofactor [ ]. Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [ ] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [ ]. This family includes AOR, formaldehyde fer... | [
"GO:0016625",
"GO:0051536"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.599.10"
] | [
""
] | [
5473
] | 1 | [
"EC"
] | [
"1.2.7.5"
] | [
"EC:1.2.7.5"
] | 1 | [
"1aor",
"1b25",
"1b4n",
"4z3w",
"4z3x",
"4z3y",
"4z3z",
"4z40",
"6x1o",
"6x6u",
"8c0z",
"9g7j",
"9mqx"
] | 13 | [
"PUB00007125",
"PUB00007126",
"PUB00007127",
"PUB00007128",
"PUB00007129",
"PUB00007130",
"PUB00021189"
] | [
"9242907",
"8672295",
"2550230",
"8026480",
"7721730",
"9275170",
"10024458"
] | [
"Molybdenum-cofactor-containing enzymes: structure and mechanism.",
"Tungsten in biological systems.",
"Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes.",
"The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a mol... | [
1997,
1996,
1989,
1994,
1995,
1997,
1999
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Metazoa",
"unclassified sequences"
] | [
1687,
3288,
4,
494
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Homologous_superfamily | Aldehyde ferredoxin oxidoreductase, domain 3 | Aldehyde ferredoxin oxidoreductase, domain 3 | Ald_Fedxn_OxRdtase_dom3 | 9 |
IPR013986 | 13,986 | DExx box DNA helicase domain superfamily | DExx_box_DNA_helicase_dom_sf | Homologous_superfamily | 73,621 | false | false | This domain superfamily is found in DExx type DNA helicases, such as the hexameric essential helicases PcrA from Gram-positive bacteria and Rep and UvrD from Gram-negative bacteria [ ]. PcrA is essential for cell growth in Bacillus species, as it is required for rolling circle replication, unwinding DNA using an active... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.10.160"
] | [
""
] | [
73621
] | 1 | [
"EC"
] | [
"5.6.2.4"
] | [
"EC:5.6.2.4"
] | 1 | [
"1pjr",
"1qhg",
"1uaa",
"1w36",
"2is1",
"2is2",
"2is4",
"2is6",
"2pjr",
"3k70",
"3lfu",
"3pjr",
"4c2t",
"4c2u",
"4c30",
"5ld2",
"5mbv",
"6ppj",
"6ppr",
"6ppu",
"6sjb",
"6sje",
"6sjf",
"6sjg",
"6t2u",
"6t2v",
"7mr0",
"7mr1",
"7mr2",
"7mr3",
"7mr4",
"7sjr"... | 39 | [
"PUB00035955",
"PUB00035956",
"PUB00035957",
"PUB00035958"
] | [
"17574572",
"17499041",
"16236131",
"12065426"
] | [
"Directional loading and stimulation of PcrA helicase by the replication initiator protein RepD.",
"A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA.",
"Rep helicase suppresses short-homology-dependent illegitimate recombination in Escherichia coli.",
"Essential... | [
2007,
2007,
2005,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
459,
68557,
3245,
30,
1330
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
6,
4,
1,
3,
1,
1,
5
] | 7 | true | Homologous_superfamily | DExx box DNA helicase domain superfamily | DExx box DNA helicase domain superfamily | DExx_box_DNA_helicase_dom_sf | 9 |
IPR013987 | 13,987 | Protein YjdM, N-terminal | YjdM_N | Domain | 8,413 | false | false | This entry represents the N-terminal domain of YjdM, which is predicted to form a zinc-ribbon. YjdM is not involved in phosphonate metabolism [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08274"
] | [
"Zn_Ribbon_YjdM"
] | [
8413
] | 1 | [
"EC"
] | [
"3.11.1.2"
] | [
"EC:3.11.1.2"
] | 1 | [
"2akl"
] | 1 | [
"PUB00043019"
] | [
"8335257"
] | [
"Evidence for a fourteen-gene, phnC to phnP locus for phosphonate metabolism in Escherichia coli."
] | [
1993
] | 1 | [] | [
"IPR013991"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
8336,
14,
63
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Protein YjdM, N-terminal | Protein YjdM, N-terminal | YjdM_N | 3 |
IPR013988 | 13,988 | Protein YjdM, C-terminal | YjdM_C | Domain | 12,592 | false | false | This entry represents the C-terminal domain of YjdM. YjdM is not involved in phosphonate metabolism [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03831"
] | [
"YjdM"
] | [
12592
] | 1 | [
"EC"
] | [
"3.11.1.2"
] | [
"EC:3.11.1.2"
] | 1 | [
"2akk",
"2akl"
] | 2 | [
"PUB00043019"
] | [
"8335257"
] | [
"Evidence for a fourteen-gene, phnC to phnP locus for phosphonate metabolism in Escherichia coli."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
12439,
25,
128
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Protein YjdM, C-terminal | Protein YjdM, C-terminal | YjdM_C | 3 |
IPR013989 | 13,989 | Development/cell death domain | Dev_and_cell_death_domain | Domain | 6,499 | false | false | The DCD (Development and Cell Death) domain is found in plant proteins involved in development and cell death. The DCD domain is an ~130 amino acid long stretch that contains several mostly invariable motifs. These include a FGLP and a LFL motif at the N terminus and a PAQV and a PLxE motif towards the C terminus of th... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF10539",
"PS51222",
"SM00767"
] | [
"Dev_Cell_Death",
"DCD",
"DCD"
] | [
6170,
6435,
6145
] | 3 | [
"PROSITEDOC"
] | [
"PDOC51222"
] | [
"PROSITEDOC:PDOC51222"
] | 1 | [] | 0 | [
"PUB00033600"
] | [
"16008837"
] | [
"DCD - a novel plant specific domain in proteins involved in development and programmed cell death."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Catovirus CTV1",
"Eukaryota",
"ecological metagenomes"
] | [
22,
76,
1,
6388,
12
] | 5 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
45,
35,
1,
89
] | 4 | true | Domain | Development/cell death domain | Development/cell death domain | Dev_and_cell_death_domain | 3 |
IPR013990 | 13,990 | Water stress and hypersensitive response domain | WHy-dom | Domain | 5,872 | false | false | Water Stress and Hypersensitive response (WHy) domain is a region of unknown function found in several plant proteins involved in either the response to water stress or the response to bacterial infection [ ]. It is also found in some bacterial and archaeal proteins whose functions are not currently known. This domain ... | [
"GO:0009269"
] | [
"response to desiccation"
] | [
"biological_process"
] | 1 | [
"SMART"
] | [
"SM00769"
] | [
"WHy"
] | [
5872
] | 1 | [] | [] | [] | 0 | [
"1xo8",
"1yyc",
"3but"
] | 3 | [
"PUB00033601"
] | [
"15598830"
] | [
"The WHy domain mediates the response to desiccation in plants and bacteria."
] | [
2005
] | 1 | [
"IPR004864"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
357,
2876,
2625,
14
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
16,
17,
20
] | 3 | true | Domain | Water stress and hypersensitive response domain | Water stress and hypersensitive response domain | WHy-dom | 1 |
IPR013991 | 13,991 | PhnA protein N-terminal, proteobacterial | PhnaA_N_proteobac | Domain | 2,023 | false | false | The PhnA protein family includes the uncharacterised Escherichia coli protein PhnA and its homologues. The E. coli phnA gene is part of a large operon associated with alkylphosphonate uptake and carbon-phosphorus bond cleavage [ ]. The protein is not related to the characterised phosphonoacetate hydrolase designated Ph... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00782"
] | [
"PhnA_Zn_Ribbon"
] | [
2023
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00011671",
"PUB00015581"
] | [
"2155230",
"9300819"
] | [
"Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B.",
"Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond c... | [
1990,
1997
] | 2 | [
"IPR013987"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Halalkaliarchaeum desulfuricum",
"Protostomia",
"ecological metagenomes",
"uncultured virus"
] | [
1984,
1,
2,
35,
1
] | 5 | [] | [] | 0 | true | Domain | PhnA protein N-terminal, proteobacterial | PhnA protein N-terminal, proteobacterial | PhnaA_N_proteobac | 1 |
IPR013992 | 13,992 | Adenylate cyclase-associated CAP, N-terminal | Adenylate_cyclase-assoc_CAP_N | Conserved_site | 4,709 | false | false | This entry represents the N-terminal conserved motif of CAP proteins consisting of a single α-helix. CAP proteins are composed of an N-terminal conserved motif followed by an N-terminal ( ) and C-terminal ( ) domains which are separated by a Pro-rich region. Cyclase-associated proteins (CAPs) are highly conserved actin... | [
"GO:0003779",
"GO:0007010"
] | [
"actin binding",
"cytoskeleton organization"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF01213"
] | [
"CAP_N-CM"
] | [
4709
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-6798695",
"R-HSA-114608",
"R-HSA-428890",
"R-HSA-6798695",
"R-MMU-6798695",
"R-RNO-6798695",
"R-SCE-6798695",
"R-SPO-6798695"
] | [
"REACTOME:R-DDI-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-428890",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-6798695",
"REACTOME:R-SCE-6798695",
"REACTOME:R-SPO-6798695"
] | 8 | [] | 0 | [
"PUB00007159",
"PUB00022651",
"PUB00042568",
"PUB00042569",
"PUB00042570",
"PUB00042571",
"PUB00042579",
"PUB00042580"
] | [
"12351838",
"12962635",
"11919151",
"17635992",
"10658207",
"10594005",
"17376963",
"15004221"
] | [
"Crystallization of cyclase-associated protein from Dictyostelium discoideum.",
"Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum.",
"Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization.",
"Arabidopsis ... | [
2002,
2003,
2002,
2007,
2000,
2000,
2007,
2004
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
28,
4681
] | 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,
3,
2,
22,
8,
1,
6,
4,
1,
1,
19
] | 12 | true | Conserved_site | Adenylate cyclase-associated CAP, N-terminal | Adenylate cyclase-associated CAP, N-terminal | Adenylate_cyclase-assoc_CAP_N | 2 |
IPR013998 | 13,998 | Nebulin-like | Nebulin-like | Family | 5,997 | false | false | This entry include nebulin and nebulin-related-anchoring protein (N-RAP). | [
"GO:0003779"
] | [
"actin binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00510"
] | [
"NEBULIN"
] | [
5997
] | 1 | [
"REACTOME"
] | [
"R-HSA-390522"
] | [
"REACTOME:R-HSA-390522"
] | 1 | [] | 0 | [
"PUB00068426",
"PUB00068427",
"PUB00068428",
"PUB00085750",
"PUB00085752"
] | [
"14657273",
"11739655",
"12692149",
"20940435",
"26792324"
] | [
"N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes.",
"Targeting and functional role of N-RAP, a nebulin-related LIM protein, during myofibril assembly in cultured chick cardiomyocytes.",
"New N-RAP-binding partners alpha-actinin, filamin and Krp1 detected by yeast two-hy... | [
2004,
2001,
2003,
2010,
2016
] | 5 | [
"IPR055297"
] | [] | 1 | 0 | 1 | [
"Bilateria",
"Pantoea vagans"
] | [
5995,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
13,
16,
17
] | 4 | true | Family | Nebulin-like | Nebulin-like | Nebulin-like | 7 |
IPR014000 | 14,000 | DNA helicase E1, N-terminal, Papillomavirus | PPV_DNA_helicase_E1_N | Domain | 3,132 | false | false | Papillomaviruses (PPV) are a large family of DNA tumour viruses which give rise to warts in their host species. The helicase E1 protein is an ATP-dependent DNA helicase required for initiation of viral DNA replication [ , ]. It forms a complex with the viral E2 protein, which is a site-specific DNA-binding transcriptio... | [
"GO:0016817"
] | [
"hydrolase activity, acting on acid anhydrides"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00524"
] | [
"PPV_E1_N"
] | [
3132
] | 1 | [
"EC"
] | [
"5.6.2.4"
] | [
"EC:5.6.2.4"
] | 1 | [] | 0 | [
"PUB00024726",
"PUB00028030",
"PUB00028031",
"PUB00028032",
"PUB00028033",
"PUB00031575"
] | [
"10949036",
"8389467",
"2176744",
"9060646",
"9658141",
"15289463"
] | [
"Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus.",
"The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA helicase.",
"Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transact... | [
2000,
1993,
1990,
1997,
1998,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Papillomaviridae"
] | [
9,
3123
] | 2 | [] | [] | 0 | true | Domain | DNA helicase E1, N-terminal, Papillomavirus | DNA helicase E1, N-terminal, Papillomavirus | PPV_DNA_helicase_E1_N | 1 |
IPR014001 | 14,001 | Helicase superfamily 1/2, ATP-binding domain | Helicase_ATP-bd | Domain | 982,539 | false | false | This entry represents the DNA-binding domain of classical SF1 and SF2 helicases. It does not recognise bacterial DinG and eukaryotic Rad3 which differ from other SF1-SF2 helicases by the presence of a large insert after the Walker A (see ). Helicases have been classified in 5 superfamilies (SF1-SF5). All of the protein... | [] | [] | [] | 0 | [
"PROFILE",
"SMART"
] | [
"PS51192",
"SM00487"
] | [
"HELICASE_ATP_BIND_1",
"DEXDc"
] | [
941951,
913548
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-113418",
"R-BTA-1169408",
"R-BTA-1266695",
"R-BTA-141444",
"R-BTA-156827",
"R-BTA-159236",
"R-BTA-1810476",
"R-BTA-201722",
"R-BTA-2467813",
"R-BTA-2500257",
"R-BTA-3134963",
"R-BTA-3214858",
"R-BTA-3247509",
"R-BTA-429947",
"R-BTA-5663220",
"R-BTA-5696395",
"R-BTA-5696400",
... | [
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-141444",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-1810476",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-2467813",
"REACTOME:R-BTA-2500257",
"REACTOME:R-BTA-3134963",
"REACTOME:R-B... | 569 | [
"1a1v",
"1c4o",
"1cu1",
"1d2m",
"1d9x",
"1d9z",
"1fuu",
"1gku",
"1gl9",
"1gm5",
"1hei",
"1hv8",
"1m6n",
"1m74",
"1nkt",
"1nl3",
"1oyw",
"1oyy",
"1q0u",
"1qde",
"1qva",
"1rif",
"1s2m",
"1t5l",
"1t6n",
"1tf2",
"1tf5",
"1vec",
"1wp9",
"1wrb",
"1xti",
"1xtj"... | 1,289 | [
"PUB00004361",
"PUB00025034",
"PUB00033619",
"PUB00033620",
"PUB00033621"
] | [
"2546125",
"11087862",
"11839499",
"11545728",
"8385320"
] | [
"Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.",
"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.",
"Helicase structure and mechanism.",
"DExD/H box RNA helicases: from generic motors to specific ... | [
1989,
2000,
2002,
2001,
1993
] | 5 | [] | [
"IPR000330",
"IPR006935",
"IPR011492",
"IPR011545",
"IPR030100",
"IPR040980",
"IPR044078",
"IPR044573",
"IPR044762",
"IPR044774",
"IPR060542"
] | 0 | 11 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
11933,
447621,
467167,
47516,
8302
] | 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",... | [
807,
101,
485,
234,
21,
625,
339,
79,
401,
438,
76,
69,
1595
] | 13 | true | Domain | Helicase superfamily 1/2, ATP-binding domain | Helicase superfamily 1/2, ATP-binding domain | Helicase_ATP-bd | 3 |
IPR014003 | 14,003 | BBSome complex member BBS5, PH domain | BBS5_PH | Domain | 2,180 | false | false | BBS5 is part of the BBSome complex that may function as a coat complex required for sorting of specific membrane proteins to the primary cilia [ ]. Mutations in the BBS5 gene cause Bardet-Biedl syndrome 5 [ , ]. This entry represents the two tandem PH domains found at the N-terminal of BBS5 [ ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF07289",
"SM00683"
] | [
"BBL5",
"DM16"
] | [
2177,
2070
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-5620922",
"R-HSA-5620922",
"R-MMU-5620922"
] | [
"REACTOME:R-CEL-5620922",
"REACTOME:R-HSA-5620922",
"REACTOME:R-MMU-5620922"
] | 3 | [
"6vbu",
"6vbv",
"6vnw",
"6voa",
"6xtb"
] | 5 | [
"PUB00060532",
"PUB00073459",
"PUB00073460",
"PUB00153355"
] | [
"17574030",
"15137946",
"21344540",
"31951201"
] | [
"A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis.",
"Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene.",
"BBS genotype-phenotype assessment of a multiethnic patient cohort calls for a revision of t... | [
2007,
2004,
2011,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Bacilli",
"Eukaryota"
] | [
2,
2178
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
5,
6,
4,
5
] | 6 | true | Domain | BBSome complex member BBS5, PH domain | BBSome complex member BBS5, PH domain | BBS5_PH | 6 |
IPR014004 | 14,004 | Transport-associated and nodulation domain, bacteria | Transpt-assoc_nodulatn_dom_bac | Domain | 16,628 | false | false | The BON domain is typically ~60 residues long and has an α/β fold. There is a conserved glycine residue and several hydrophobic regions which suggests a binding function, and, actually, it contains a phospholipid-binding site , ]. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the ... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00749"
] | [
"BON"
] | [
16628
] | 1 | [] | [] | [] | 0 | [
"7a2d",
"7pvc",
"7vcm",
"8rjx",
"8zex"
] | 5 | [
"PUB00011888",
"PUB00101371",
"PUB00101372",
"PUB00101373"
] | [
"12878000",
"33315009",
"33847565",
"27112601"
] | [
"The BON domain: a putative membrane-binding domain.",
"Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.",
"Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress.",
"The Pota... | [
2003,
2020,
2021,
2016
] | 4 | [
"IPR007055"
] | [] | 1 | 0 | 1 | [
"Acidianus ambivalens",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1,
16486,
31,
110
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Transport-associated and nodulation domain, bacteria | Transport-associated and nodulation domain, bacteria | Transpt-assoc_nodulatn_dom_bac | 7 |
IPR014006 | 14,006 | Succinate dehydrogenase/fumarate reductase, flavoprotein subunit | Succ_Dhase_FrdA_Gneg | Family | 21,138 | false | false | This entry represents the flavoprotein subunit found in both the SQR and QFR enzymes. This subunit contains an N-terminal domain which binds the FAD cofactor, a central catalytic domain with an unusual fold, and a C-terminal domain whose role is unclear [ , , ]. The dicarboxylate binding site is located between the FAD... | [
"GO:0016627",
"GO:0050660",
"GO:0022900"
] | [
"oxidoreductase activity, acting on the CH-CH group of donors",
"flavin adenine dinucleotide binding",
"electron transport chain"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01812"
] | [
"sdhA_frdA_Gneg"
] | [
21138
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"1.3.5.1",
"GenProp1267",
"GenProp1391",
"GenProp1493",
"GenProp1515",
"GenProp1537",
"GenProp1672",
"GenProp1693",
"PWY-3781",
"PWY-4302",
"PWY-5392",
"PWY-561",
"PWY-5690",
"PWY-5913",
"PWY-6728",
"PWY-6969",
"PWY-7254",
"PWY-7279",
"PWY-7384",
"PWY-8086",
"R-CEL-71403",
... | [
"EC:1.3.5.1",
"GP:GenProp1267",
"GP:GenProp1391",
"GP:GenProp1493",
"GP:GenProp1515",
"GP:GenProp1537",
"GP:GenProp1672",
"GP:GenProp1693",
"METACYC:PWY-3781",
"METACYC:PWY-4302",
"METACYC:PWY-5392",
"METACYC:PWY-561",
"METACYC:PWY-5690",
"METACYC:PWY-5913",
"METACYC:PWY-6728",
"METACY... | 44 | [
"1e7p",
"1kf6",
"1kfy",
"1l0v",
"1nek",
"1nen",
"1qlb",
"1yq3",
"1yq4",
"1zoy",
"1zp0",
"2acz",
"2b76",
"2bs2",
"2bs3",
"2bs4",
"2fbw",
"2h88",
"2h89",
"2wdq",
"2wdr",
"2wdv",
"2wp9",
"2wqy",
"2ws3",
"2wu2",
"2wu5",
"3abv",
"3ae1",
"3ae2",
"3ae3",
"3ae4"... | 96 | [
"PUB00007431",
"PUB00015752",
"PUB00015792",
"PUB00028408",
"PUB00033856"
] | [
"10586875",
"12560550",
"9210286",
"11248702",
"9811659"
] | [
"Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution.",
"Architecture of succinate dehydrogenase and reactive oxygen species generation.",
"Succinate: quinone oxidoreductases. Variations on a conserved theme.",
"A third crystal form of Wolinella succinogenes quinol:fumarate reducta... | [
1999,
2003,
1997,
2001,
1998
] | 5 | [
"IPR030664"
] | [
"IPR005884",
"IPR011281"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
309,
15449,
5194,
186
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
6,
2,
2,
2,
2,
4,
1,
1,
1,
4,
2,
1,
7
] | 13 | true | Family | Succinate dehydrogenase/fumarate reductase, flavoprotein subunit | Succinate dehydrogenase/fumarate reductase, flavoprotein subunit | Succ_Dhase_FrdA_Gneg | 7 |
IPR014007 | 14,007 | Acetoin reductase | 23BDH | Family | 2,470 | false | false | One member of this family, as characterised in Klebsiella terrigena [ ], is able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also capable of irreversible reduction of diacetyl with NADH to acetoin. There has been a reuctance to classify the enzyme as either , which is (R,R)-butanediol dehydr... | [
"GO:0019152",
"GO:0045150"
] | [
"acetoin dehydrogenase (NAD+) activity",
"acetoin catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02415"
] | [
"23BDH"
] | [
2470
] | 1 | [
"EC",
"METACYC"
] | [
"1.1.1.304",
"PWY-6389"
] | [
"EC:1.1.1.304",
"METACYC:PWY-6389"
] | 2 | [
"1geg",
"3a28",
"3wtc",
"3wye"
] | 4 | [
"PUB00016700",
"PUB00017788"
] | [
"11577733",
"8444801"
] | [
"Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli.",
"Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes."
] | [
2001,
1993
] | 2 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
2397,
63,
10
] | 3 | [] | [] | 0 | true | Family | Acetoin reductase | Acetoin reductase | 23BDH | 4 |
IPR014008 | 14,008 | Cobalamin biosynthesis, precorrin-6Y methyltransferase, CbiT subunit | Cbl_synth_MTase_CbiT | Family | 11,013 | false | false | Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants... | [
"GO:0008276",
"GO:0009236"
] | [
"protein methyltransferase activity",
"cobalamin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02469"
] | [
"CbiT"
] | [
11013
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"2.1.1.196",
"GenProp0275",
"PWY-7377"
] | [
"EC:2.1.1.196",
"GP:GenProp0275",
"METACYC:PWY-7377"
] | 3 | [
"1f38",
"1kxz",
"1l3b",
"1l3c",
"1l3i",
"2yxd",
"3e05",
"3hm2",
"3njr"
] | 9 | [
"PUB00009744",
"PUB00014672",
"PUB00014680",
"PUB00014681",
"PUB00015657",
"PUB00035308",
"PUB00035309",
"PUB00035310",
"PUB00070131"
] | [
"11215515",
"11153269",
"12429089",
"1732195",
"12869542",
"17163662",
"16042605",
"12055304",
"23922391"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Multiple biosynthetic pathways for vitamin B12: variations on a central theme.",
"The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.",
"Biosynthesis of vitamin B12 in Pseudomonas... | [
2000,
2001,
2002,
1992,
2003,
2006,
2005,
2002,
2013
] | 9 | [] | [
"IPR006365",
"IPR023475"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
516,
10405,
12,
80
] | 4 | [] | [] | 0 | true | Family | Cobalamin biosynthesis, precorrin-6Y methyltransferase, CbiT subunit | Cobalamin biosynthesis, precorrin-6Y methyltransferase, CbiT subunit | Cbl_synth_MTase_CbiT | 7 |
IPR014009 | 14,009 | PIK-related kinase, FAT domain | PIK_FAT | Domain | 23,040 | false | false | Phosphatidylinositol kinase (PIK)-related kinases participate in meiotic and V(D)J recombination, chromosome maintenance and repair, cell cycle progression, and cell cycle checkpoints, and their dysfunction can result in a range of diseases, including immunodeficiency, neurological disorder and cancer. The catalytic ki... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51189"
] | [
"FAT"
] | [
23040
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.1",
"PDOC51189",
"R-CEL-1257604",
"R-CEL-1632852",
"R-CEL-165159",
"R-CEL-166208",
"R-CEL-3371571",
"R-CEL-380972",
"R-CEL-389357",
"R-CEL-5218920",
"R-CEL-5628897",
"R-CEL-5693607",
"R-CEL-6804757",
"R-CEL-8943724",
"R-CEL-9639288",
"R-CEL-975957",
"R-CEL-9856530",
"R-DDI-... | [
"EC:2.7.11.1",
"PROSITEDOC:PDOC51189",
"REACTOME:R-CEL-1257604",
"REACTOME:R-CEL-1632852",
"REACTOME:R-CEL-165159",
"REACTOME:R-CEL-166208",
"REACTOME:R-CEL-3371571",
"REACTOME:R-CEL-380972",
"REACTOME:R-CEL-389357",
"REACTOME:R-CEL-5218920",
"REACTOME:R-CEL-5628897",
"REACTOME:R-CEL-5693607",... | 199 | [
"3jbz",
"4jsn",
"4jsp",
"4jsv",
"4jsx",
"4jt5",
"4jt6",
"5flc",
"5fvm",
"5h64",
"5luq",
"5np0",
"5np1",
"5oej",
"5ojs",
"5w1r",
"5wbu",
"5wby",
"5x6o",
"5y3r",
"5y81",
"5yz0",
"5zcs",
"6bcu",
"6bcx",
"6emk",
"6ig9",
"6jxa",
"6jxc",
"6k9k",
"6k9l",
"6l53"... | 153 | [
"PUB00006515",
"PUB00033610"
] | [
"10782091",
"7569949"
] | [
"FAT: a novel domain in PIK-related kinases.",
"PIK-related kinases: DNA repair, recombination, and cell cycle checkpoints."
] | [
2000,
1995
] | 2 | [] | [
"IPR003151"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
23040
] | 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... | [
35,
6,
17,
11,
28,
16,
4,
10,
24,
5,
6,
67
] | 12 | true | Domain | PIK-related kinase, FAT domain | PIK-related kinase, FAT domain | PIK_FAT | 2 |
IPR014010 | 14,010 | REJ domain | REJ_dom | Domain | 4,557 | false | false | The REJ domain is an extracellular module of ~700 amino acids, which is found associated with other domains, such as EGF, the GPS proteolytic cleavage site, C-type lectin, SUEL-type lectin, LRR, LDL-A, PLAT, PKD [ , , ]. Although its function is unknown, the REJ domain has been shown to be required for cleavage to occu... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51111"
] | [
"REJ"
] | [
4557
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME"
] | [
"PDOC51111",
"R-HSA-5620916",
"R-MMU-5620916"
] | [
"PROSITEDOC:PDOC51111",
"REACTOME:R-HSA-5620916",
"REACTOME:R-MMU-5620916"
] | 3 | [] | 0 | [
"PUB00005758",
"PUB00006383",
"PUB00033611",
"PUB00101153"
] | [
"8666666",
"9285785",
"12482949",
"23762046"
] | [
"The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1.",
"Comparative analysis of the polycystic kidney disease 1 (PKD1) gene reveals an integral membrane glycoprotein with multiple evolutionary conserved domains.",
"Cleava... | [
1996,
1997,
2002,
2013
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Halomarina oriensis",
"metagenomes"
] | [
147,
4,
4401,
1,
4
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
11,
4,
21,
9,
10
] | 5 | true | Domain | REJ domain | REJ domain | REJ_dom | 8 |
IPR014012 | 14,012 | Helicase/SANT-associated domain | HSA_dom | Domain | 17,743 | false | false | The helicase/SANT-associated (HSA) domain is found in eukaryotic proteins, including Helicase SRCAP/p400/DOM [ ], Probable global transcription activator SNF2L2/brahma-homologue and Chromatin modification-related protein EAF1 [ ]. While each family has the core sequences that define the HSA domain, they each also have ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF07529",
"PS51204",
"SM00573"
] | [
"HSA",
"HSA",
"HSA"
] | [
16015,
17377,
14075
] | 3 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.-",
"PWY-7250",
"PDOC51204",
"R-BTA-1266695",
"R-BTA-201722",
"R-BTA-3214858",
"R-BTA-3247509",
"R-BTA-8939243",
"R-BTA-9764725",
"R-BTA-9933937",
"R-BTA-9933939",
"R-BTA-9933946",
"R-BTA-9933947",
"R-BTA-9934037",
"R-CEL-8939243",
"R-CEL-9764725",
"R-CEL-9933939",
"R-CEL-99... | [
"EC:3.6.4.-",
"METACYC:PWY-7250",
"PROSITEDOC:PDOC51204",
"REACTOME:R-BTA-1266695",
"REACTOME:R-BTA-201722",
"REACTOME:R-BTA-3214858",
"REACTOME:R-BTA-3247509",
"REACTOME:R-BTA-8939243",
"REACTOME:R-BTA-9764725",
"REACTOME:R-BTA-9933937",
"REACTOME:R-BTA-9933939",
"REACTOME:R-BTA-9933946",
"... | 70 | [
"4i6m",
"5i9e",
"5y81",
"6gej",
"6gen",
"6igm",
"6k15",
"6kw3",
"6kw4",
"6kw5",
"6lth",
"6ltj",
"6tda",
"6uxv",
"6uxw",
"6v8o",
"6v92",
"6vz4",
"6vzg",
"7c4j",
"7egm",
"7egp",
"7vdt",
"7vdv",
"7vvy",
"7vvz",
"7y8r",
"7yfn",
"7yfp",
"7zvw",
"8esc",
"8qku"... | 59 | [
"PUB00011448",
"PUB00033613",
"PUB00046117",
"PUB00101183"
] | [
"11779830",
"16024792",
"15045029",
"18408732"
] | [
"Systematic identification of novel protein domain families associated with nuclear functions.",
"Human SRCAP and Drosophila melanogaster DOM are homologs that function in the notch signaling pathway.",
"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z int... | [
2002,
2005,
2004,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Prevotella communis"
] | [
17742,
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... | [
27,
3,
76,
8,
34,
25,
3,
10,
24,
4,
4,
91
] | 12 | true | Domain | Helicase/SANT-associated domain | Helicase/SANT-associated domain | HSA_dom | 9 |
IPR014013 | 14,013 | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type | Helic_SF1/SF2_ATP-bd_DinG/Rad3 | Domain | 44,333 | false | false | This entry represents the ATP-binding domain found within bacterial DinG and eukaryotic Rad3 proteins, differing from other SF1 and SF2 helicases by the presence of a large insert after the Walker A motif [ ]. Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, a... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS51193"
] | [
"HELICASE_ATP_BIND_2"
] | [
44333
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"5.6.2",
"PDOC51192",
"R-BTA-113418",
"R-BTA-5696395",
"R-BTA-5696400",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-72086",
"R-BTA-73762",
"R-BTA-73772",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-73863",
"R-BTA-75953",
"R-BTA-75955",
"R-B... | [
"EC:5.6.2",
"PROSITEDOC:PDOC51192",
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-5696400",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-BTA-6796648",
"REACTOME:R-BTA-72086",
"REACTOME:R-BTA-73762",
"R... | 144 | [
"2vl7",
"2vsf",
"3crv",
"3crw",
"4a15",
"5fmf",
"5h8c",
"5h8w",
"5ivw",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5of4",
"5oqj",
"5oqm",
"5sva",
"6fwr",
"6fws",
"6gym",
"6nmi",
"6o9l",
"6o9m",
"6ro4",
"7ad8",
"7egb",
"7egc",
"7ena",
"7enc",
"7k01",
"7k04",
"7lbm"... | 91 | [
"PUB00004361",
"PUB00025034",
"PUB00033619",
"PUB00033620",
"PUB00033621"
] | [
"2546125",
"11087862",
"11839499",
"11545728",
"8385320"
] | [
"Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.",
"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase.",
"Helicase structure and mechanism.",
"DExD/H box RNA helicases: from generic motors to specific ... | [
1989,
2000,
2002,
2001,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1321,
25596,
16893,
45,
478
] | 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",... | [
37,
4,
24,
13,
2,
44,
16,
3,
12,
16,
2,
2,
34
] | 13 | true | Domain | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type | Helic_SF1/SF2_ATP-bd_DinG/Rad3 | 3 |
IPR014014 | 14,014 | RNA helicase, DEAD-box type, Q motif | RNA_helicase_DEAD_Q_motif | Domain | 196,843 | false | false | RNA helicases from the DEAD-box family are found in almost all organisms and have important roles in RNA metabolism such as splicing, RNA transport, ribosome biogenesis, translation and RNA decay. They are enzymes that unwind double-stranded RNA molecules in an energy dependent fashion through the hydrolysis of NTP. DE... | [
"GO:0003724"
] | [
"RNA helicase activity"
] | [
"molecular_function"
] | 1 | [
"PROFILE"
] | [
"PS51195"
] | [
"Q_MOTIF"
] | [
196843
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.4.13",
"PDOC51195",
"R-BTA-1169408",
"R-BTA-156827",
"R-BTA-159236",
"R-BTA-429947",
"R-BTA-6791226",
"R-BTA-72163",
"R-BTA-72187",
"R-BTA-72649",
"R-BTA-72702",
"R-BTA-73856",
"R-BTA-9013418",
"R-BTA-975957",
"R-CEL-1169408",
"R-CEL-156827",
"R-CEL-159236",
"R-CEL-430039",
... | [
"EC:3.6.4.13",
"PROSITEDOC:PDOC51195",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-159236",
"REACTOME:R-BTA-429947",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-72187",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-73856",
"REACT... | 170 | [
"1fuu",
"1hv8",
"1q0u",
"1qde",
"1qva",
"1s2m",
"1t6n",
"1vec",
"1wrb",
"1xti",
"1xtj",
"1xtk",
"2db3",
"2g9n",
"2gxq",
"2gxs",
"2gxu",
"2hxy",
"2hyi",
"2i4i",
"2j0q",
"2j0s",
"2j0u",
"2kbe",
"2oxc",
"2pl3",
"2vso",
"2vsx",
"2xb2",
"2zu6",
"3b7g",
"3ber"... | 237 | [
"PUB00025797",
"PUB00030219",
"PUB00033617",
"PUB00033626"
] | [
"11171974",
"10404596",
"1531961",
"12535527"
] | [
"Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii.",
"Crystal structure of the ATPase domain of translation initiation factor 4A from Saccharomyces cerevisiae--the prototype of the DEAD box protein family.",
"Autogenous translation regulation by Escherichia coli ATPase ... | [
2001,
1999,
1992,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
484,
73784,
121449,
17,
1109
] | 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",... | [
219,
35,
99,
58,
4,
201,
114,
18,
79,
122,
20,
19,
313
] | 13 | true | Domain | RNA helicase, DEAD-box type, Q motif | RNA helicase, DEAD-box type, Q motif | RNA_helicase_DEAD_Q_motif | 6 |
IPR014015 | 14,015 | Helicase, superfamily 3, DNA virus | Helicase_SF3_DNA-vir | Domain | 16,699 | false | false | Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A (phosphate-binding loop or P-loop) and Walker B (Mg2+-binding aspartic acid) motifs. Superfamily 3 consists of helicases encoded mainly by small DNA viruses and some larg... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51206"
] | [
"SF3_HELICASE_1"
] | [
16699
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"5.6.2.4",
"PDOC51206"
] | [
"EC:5.6.2.4",
"PROSITEDOC:PDOC51206"
] | 2 | [
"1n25",
"1s9h",
"1svl",
"1svm",
"1svo",
"1tue",
"1u0j",
"2gxa",
"2h1l",
"2v9p",
"4e2i",
"4gdf",
"5a9k",
"5j40",
"5j47",
"5j4v",
"5j4y",
"7apd",
"7jse",
"7jsf",
"7jsg",
"7jsh",
"7jsi",
"7ola",
"7om0",
"8apl",
"8apm",
"8hwa",
"8hwb",
"8hwc",
"8hwd",
"8hwe"... | 87 | [
"PUB00014778",
"PUB00027539",
"PUB00033628",
"PUB00033629",
"PUB00033630"
] | [
"15037234",
"12774115",
"11689653",
"2156730",
"15718137"
] | [
"Evolutionary history and higher order classification of AAA+ ATPases.",
"Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen.",
"Common origin of four diverse families of large eukaryotic DNA viruses.",
"A new superfamily of putative NTP-binding domains encoded by genomes of sm... | [
2004,
2003,
2001,
1990,
2005
] | 5 | [] | [
"IPR001257"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
197,
7609,
596,
7819,
478
] | 5 | [
"Mus musculus",
"Zea mays"
] | [
1,
1
] | 2 | true | Domain | Helicase, superfamily 3, DNA virus | Helicase, superfamily 3, DNA virus | Helicase_SF3_DNA-vir | 5 |
IPR014016 | 14,016 | UvrD-like helicase, ATP-binding domain | UvrD-like_ATP-bd | Domain | 125,842 | false | false | This entry represents the ATP-binding domain found in AddA, AddB and UvrD-like helicases. This domain is also found in the bacterial helicase-nuclease complex AddAB, both in subunit AddA and AddB. The AddA subunit is responsible for the helicase activity. AddB also harbors a putative ATP-binding domain which does not p... | [
"GO:0005524"
] | [
"ATP binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF00580",
"PS51198"
] | [
"UvrD-helicase",
"UVRD_HELICASE_ATP_BIND"
] | [
114737,
119585
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"5.6.2.4",
"PDOC51198"
] | [
"EC:5.6.2.4",
"PROSITEDOC:PDOC51198"
] | 2 | [
"1pjr",
"1qhg",
"1qhh",
"1uaa",
"1w36",
"2is1",
"2is2",
"2is4",
"2is6",
"2pjr",
"3k70",
"3lfu",
"3pjr",
"3u44",
"3u4q",
"4c2t",
"4c2u",
"4c30",
"4ceh",
"4cei",
"4cej",
"5ld2",
"5mbv",
"6ppj",
"6ppr",
"6ppu",
"6sjb",
"6sje",
"6sjf",
"6sjg",
"6t2u",
"6t2v"... | 66 | [
"PUB00000949",
"PUB00004361",
"PUB00032879",
"PUB00033615",
"PUB00033616",
"PUB00084261"
] | [
"9288744",
"2546125",
"10199404",
"10679457",
"15538360",
"21071401"
] | [
"Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP.",
"Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.",
"Crystal structures of complexes of Pcr... | [
1997,
1989,
1999,
2000,
2004,
2011
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1269,
114601,
7624,
164,
2184
] | 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)... | [
6,
3,
4,
8,
4,
1,
6,
4,
2,
2,
11
] | 11 | true | Domain | UvrD-like helicase, ATP-binding domain | UvrD-like helicase, ATP-binding domain | UvrD-like_ATP-bd | 5 |
IPR014017 | 14,017 | UvrD-like helicase, C-terminal | UvrD-like_C | Domain | 106,607 | false | false | This entry represents the C-terminal domain in AddA, AddB and UvrD-like helicases. Helicases have been classified in 5 superfamilies (SF1-SF5). All of the proteins bind ATP and, consequently, all of them carry the classical Walker A (phosphate-binding loop or P-loop) and Walker B (Mg2+-binding aspartic acid) motifs. Fo... | [
"GO:0005524",
"GO:0016787"
] | [
"ATP binding",
"hydrolase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PROFILE"
] | [
"PF13361",
"PS51217"
] | [
"UvrD_C",
"UVRD_HELICASE_CTER"
] | [
103229,
86717
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"5.6.2.4",
"PDOC51198"
] | [
"EC:5.6.2.4",
"PROSITEDOC:PDOC51198"
] | 2 | [
"1pjr",
"1qhg",
"1qhh",
"1uaa",
"1w36",
"2is1",
"2is2",
"2is4",
"2is6",
"2pjr",
"3k70",
"3lfu",
"3pjr",
"3u44",
"3u4q",
"4c2t",
"4c2u",
"4c30",
"4ceh",
"4cei",
"4cej",
"5ld2",
"5mbv",
"6ppj",
"6ppr",
"6ppu",
"6sjb",
"6sje",
"6sjf",
"6sjg",
"6t2u",
"6t2v"... | 45 | [
"PUB00000949",
"PUB00004361",
"PUB00032879",
"PUB00033615",
"PUB00033616"
] | [
"9288744",
"2546125",
"10199404",
"10679457",
"15538360"
] | [
"Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP.",
"Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.",
"Crystal structures of complexes of Pcr... | [
1997,
1989,
1999,
2000,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1236,
97912,
5182,
149,
2128
] | 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)... | [
6,
3,
4,
7,
4,
1,
3,
4,
2,
2,
5
] | 11 | true | Domain | UvrD-like helicase, C-terminal | UvrD-like helicase, C-terminal | UvrD-like_C | 9 |
IPR014018 | 14,018 | SecA motor DEAD | SecA_motor_DEAD | Domain | 37,404 | false | false | SecA is a cytoplasmic protein of 800 to 960 amino acid residues. The eubacterial secA protein [ ] plays an important role in protein export. It interacts with the secY and secE components of the protein translocation system. It has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the ... | [] | [] | [] | 0 | [
"PROFILE"
] | [
"PS51196"
] | [
"SECA_MOTOR_DEAD"
] | [
37404
] | 1 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.4.2.8",
"PDOC01016",
"R-HSA-1222387",
"R-HSA-9636383",
"R-HSA-9760173"
] | [
"EC:7.4.2.8",
"PROSITEDOC:PDOC01016",
"REACTOME:R-HSA-1222387",
"REACTOME:R-HSA-9636383",
"REACTOME:R-HSA-9760173"
] | 5 | [
"1m6n",
"1m74",
"1nkt",
"1nl3",
"1tf2",
"1tf5",
"2fsf",
"2fsg",
"2fsh",
"2fsi",
"2ibm",
"2ipc",
"2vda",
"3bxz",
"3din",
"3dl8",
"3iqm",
"3iqy",
"3jux",
"3jv2",
"4uaq",
"4ys0",
"5eul",
"5k94",
"5k9t",
"6gox",
"6itc",
"6s0k",
"6sxh",
"6t4h",
"7xha",
"7xhb"... | 37 | [
"PUB00001183",
"PUB00001687",
"PUB00003757",
"PUB00014329",
"PUB00029100",
"PUB00033617",
"PUB00033618"
] | [
"2542029",
"7758587",
"8437571",
"12242434",
"12606717",
"1531961",
"16243836"
] | [
"SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.",
"Isolation and characterization of the cDNA for pea chloroplast SecA. Evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts.",
"SecA is plastid-enc... | [
1989,
1995,
1993,
2002,
2003,
1992,
2005
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctHip2",
"unclassified sequences"
] | [
4,
31995,
4586,
1,
818
] | 5 | [
"Arabidopsis thaliana",
"Danio rerio",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
13,
3,
1,
9,
13
] | 5 | true | Domain | SecA motor DEAD | SecA motor DEAD | SecA_motor_DEAD | 9 |
IPR014020 | 14,020 | Tensin phosphatase, C2 domain | Tensin_C2-dom | Domain | 21,414 | false | false | Tensins constitute an eukaryotic family of lipid phosphatases that are defined by the presence of two adjacent domains: a lipid phosphatase domain and a C2-like domain. The tensin-type C2 domain has a structure similar to the classical C2 domain (see ) that mediates the Ca2+-dependent membrane recruitment of several si... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF10409",
"PS51182",
"SM01326"
] | [
"PTEN_C2",
"C2_TENSIN",
"PTEN_C2"
] | [
19758,
21141,
20231
] | 3 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.3",
"PDOC51181",
"R-CEL-1660499",
"R-CEL-1855204",
"R-CEL-199418",
"R-CEL-202424",
"R-CEL-5689880",
"R-CEL-5689896",
"R-CEL-8875513",
"R-CEL-8948747",
"R-CEL-8948751",
"R-CFA-1660499",
"R-CFA-1855204",
"R-CFA-199418",
"R-CFA-202424",
"R-CFA-5689880",
"R-CFA-5689896",
"R-CFA-89... | [
"EC:3.1.3",
"PROSITEDOC:PDOC51181",
"REACTOME:R-CEL-1660499",
"REACTOME:R-CEL-1855204",
"REACTOME:R-CEL-199418",
"REACTOME:R-CEL-202424",
"REACTOME:R-CEL-5689880",
"REACTOME:R-CEL-5689896",
"REACTOME:R-CEL-8875513",
"REACTOME:R-CEL-8948747",
"REACTOME:R-CEL-8948751",
"REACTOME:R-CFA-1660499",
... | 59 | [
"1d5r",
"3awe",
"3awf",
"3awg",
"3n0a",
"3v0d",
"3v0e",
"3v0f",
"3v0g",
"3v0h",
"3v0i",
"3v0j",
"5bug",
"5bzx",
"5bzz",
"7jtx",
"7juk",
"7jul",
"7jvx",
"9c49"
] | 20 | [
"PUB00028325",
"PUB00033631",
"PUB00033632"
] | [
"10555148",
"11395408",
"11858936"
] | [
"Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association.",
"PTEN and myotubularin: novel phosphoinositide phosphatases.",
"PTEN: The down side of PI 3-kinase signalling."
] | [
1999,
2001,
2002
] | 3 | [] | [
"IPR055183"
] | 0 | 1 | 0 | [
"Armadillidium vulgare clopovirus",
"Eukaryota"
] | [
1,
21413
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
39,
2,
147,
10,
58,
35,
29,
51,
49
] | 9 | true | Domain | Tensin phosphatase, C2 domain | Tensin phosphatase, C2 domain | Tensin_C2-dom | 1 |
IPR014023 | 14,023 | Mononegavirales RNA-directed RNA polymerase catalytic domain | Mononeg_RNA_pol_cat | Domain | 12,600 | false | false | RNA-directed RNA polymerase (RdRp) ( ) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage [ , ]. It catalyses synthesis of the RNA strand complementary to a given RNA template, but the precise molecular mechanism remains unclear. The postulated RNA replication process is a tw... | [
"GO:0003968",
"GO:0004482",
"GO:0005524",
"GO:0006370"
] | [
"RNA-directed RNA polymerase activity",
"mRNA 5'-cap (guanine-N7-)-methyltransferase activity",
"ATP binding",
"7-methylguanosine mRNA capping"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM",
"PROFILE"
] | [
"PF00946",
"PS50526"
] | [
"Mononeg_RNA_pol",
"RDRP_SSRNA_NEG_NONSEG"
] | [
12535,
10875
] | 2 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.7.48",
"2.7.7.88",
"3.6.1.-",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289",
"PDOC50507",
"R-HSA-9820960",
"R-HSA-9820962",
"R-HSA-9828642",
"R-HSA-9828721",
"R-HSA-9828806",
"R-HSA-9833110",
"R-HSA... | [
"EC:2.7.7.48",
"EC:2.7.7.88",
"EC:3.6.1.-",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289",
"PROSITEDOC:PDOC50507",
"REACTOME:R-HSA-9820... | 21 | [
"5a22",
"5chs",
"6pzk",
"6u1x",
"6u5o",
"6ueb",
"6uen",
"6v85",
"6v86",
"7yer",
"7yes",
"7yet",
"7yot",
"7you",
"7yov",
"8fpi",
"8fpj",
"8fu3",
"8izl",
"8izm",
"8jsl",
"8jsm",
"8jsn",
"8kdb",
"8kdc",
"8snx",
"8sny",
"8x01",
"8yxl",
"8yxm",
"8yxp",
"8zpv"... | 68 | [
"PUB00009392",
"PUB00030617",
"PUB00033622",
"PUB00033623",
"PUB00033624",
"PUB00033625"
] | [
"9878607",
"9309225",
"2759231",
"8709232",
"11531403",
"10827187"
] | [
"Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.",
"Structure of the RNA-dependent RNA polymerase of poliovirus.",
"Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relat... | [
1998,
1997,
1989,
1996,
2001,
2000
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
9,
246,
12345
] | 3 | [
"Danio rerio"
] | [
1
] | 1 | true | Domain | Mononegavirales RNA-directed RNA polymerase catalytic domain | Mononegavirales RNA-directed RNA polymerase catalytic domain | Mononeg_RNA_pol_cat | 2 |
IPR014024 | 14,024 | Auxin efflux carrier, plant type | Auxin_eff_plant | Family | 5,223 | false | false | This entry is mostly composed of known or predicted PIN proteins from plants, though some homologous prokaryotic proteins are also included. The PIN proteins are components of auxin efflux systems from plants. These carriers are saturable, auxin-specific, and localized to the basal ends of auxin transport-competent cel... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR00946"
] | [
"2a69"
] | [
5223
] | 1 | [] | [] | [] | 0 | [
"7qp9",
"7qpa",
"7qpc",
"7wks",
"7wkw",
"7xxb",
"7y9t",
"7y9u",
"7y9v",
"8jh5",
"9g0w",
"9g0x",
"9g0z",
"9g10"
] | 14 | [
"PUB00033872",
"PUB00033873"
] | [
"16054428",
"15564124"
] | [
"Auxin transport.",
"PIN and AUX/LAX proteins: their role in auxin accumulation."
] | [
2005,
2004
] | 2 | [
"IPR004776"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Embryophyta",
"Methanomada group"
] | [
100,
5118,
5
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
42,
16,
36
] | 3 | true | Family | Auxin efflux carrier, plant type | Auxin efflux carrier, plant type | Auxin_eff_plant | 9 |
IPR014026 | 14,026 | UDP-glucose/GDP-mannose dehydrogenase, dimerisation | UDP-Glc/GDP-Man_DH_dimer | Domain | 61,802 | false | false | This entry represents an α helical region that serves as the dimerisation interface for these enzymes [ , ]. The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde inte... | [
"GO:0016616",
"GO:0051287"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"NAD binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00984"
] | [
"UDPG_MGDP_dh"
] | [
61802
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.22",
"PWY-7346",
"PWY-7820",
"R-BTA-173599",
"R-CEL-173599",
"R-DME-173599",
"R-GGA-173599",
"R-HSA-173599",
"R-MMU-173599",
"R-RNO-173599"
] | [
"EC:1.1.1",
"EC:1.1.1.22",
"METACYC:PWY-7346",
"METACYC:PWY-7820",
"REACTOME:R-BTA-173599",
"REACTOME:R-CEL-173599",
"REACTOME:R-DME-173599",
"REACTOME:R-GGA-173599",
"REACTOME:R-HSA-173599",
"REACTOME:R-MMU-173599",
"REACTOME:R-RNO-173599"
] | 11 | [
"1dli",
"1dlj",
"1mfz",
"1muu",
"1mv8",
"2o3j",
"2q3e",
"2qg4",
"2y0c",
"2y0d",
"2y0e",
"3g79",
"3gg2",
"3itk",
"3khu",
"3ojl",
"3ojo",
"3phl",
"3pid",
"3pjg",
"3pln",
"3plr",
"3prj",
"3ptz",
"3tdk",
"3tf5",
"3vtf",
"4a7p",
"4edf",
"4r16",
"4rjt",
"4xr9"... | 45 | [
"PUB00002546",
"PUB00003005",
"PUB00009417",
"PUB00009418",
"PUB00009419",
"PUB00009420",
"PUB00009421",
"PUB00027324",
"PUB00028366"
] | [
"2470755",
"9013585",
"12031484",
"11533493",
"11554764",
"12135385",
"9864323",
"12705829",
"10841783"
] | [
"Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa.",
"Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol.",
"Molecular cloning ... | [
1989,
1997,
2002,
2001,
2001,
2002,
1999,
2003,
2000
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1832,
51395,
7392,
84,
1099
] | 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",... | [
8,
1,
1,
1,
2,
3,
6,
2,
13,
3,
8
] | 11 | true | Domain | UDP-glucose/GDP-mannose dehydrogenase, dimerisation | UDP-glucose/GDP-mannose dehydrogenase, dimerisation | UDP-Glc/GDP-Man_DH_dimer | 1 |
IPR014027 | 14,027 | UDP-glucose/GDP-mannose dehydrogenase, C-terminal | UDP-Glc/GDP-Man_DH_C | Domain | 60,219 | false | false | This entry represents the C-terminal substrate-binding domain of these enzymes. Structural studies indicate that this domain forms an incomplete dinucleotide binding fold [ , ]. The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxida... | [
"GO:0016616",
"GO:0051287"
] | [
"oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor",
"NAD binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF03720",
"SM00984"
] | [
"UDPG_MGDP_dh_C",
"UDPG_MGDP_dh_C"
] | [
59822,
59910
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1",
"1.1.1.22",
"PWY-7346",
"PWY-7820",
"R-BTA-173599",
"R-CEL-173599",
"R-DME-173599",
"R-GGA-173599",
"R-HSA-173599",
"R-MMU-173599",
"R-RNO-173599"
] | [
"EC:1.1.1",
"EC:1.1.1.22",
"METACYC:PWY-7346",
"METACYC:PWY-7820",
"REACTOME:R-BTA-173599",
"REACTOME:R-CEL-173599",
"REACTOME:R-DME-173599",
"REACTOME:R-GGA-173599",
"REACTOME:R-HSA-173599",
"REACTOME:R-MMU-173599",
"REACTOME:R-RNO-173599"
] | 11 | [
"1dli",
"1dlj",
"1mfz",
"1muu",
"1mv8",
"2o3j",
"2q3e",
"2qg4",
"2y0c",
"2y0d",
"2y0e",
"3g79",
"3gg2",
"3itk",
"3khu",
"3ojl",
"3ojo",
"3phl",
"3pid",
"3pjg",
"3pln",
"3plr",
"3prj",
"3ptz",
"3tdk",
"3tf5",
"3vtf",
"4a7p",
"4edf",
"4r16",
"4rjt",
"4xr9"... | 45 | [
"PUB00002546",
"PUB00003005",
"PUB00009417",
"PUB00009418",
"PUB00009419",
"PUB00009420",
"PUB00009421",
"PUB00027324",
"PUB00028366"
] | [
"2470755",
"9013585",
"12031484",
"11533493",
"11554764",
"12135385",
"9864323",
"12705829",
"10841783"
] | [
"Purification and characterization of guanosine diphospho-D-mannose dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas aeruginosa.",
"Properties and kinetic analysis of UDP-glucose dehydrogenase from group A streptococci. Irreversible inhibition by UDP-chloroacetol.",
"Molecular cloning ... | [
1989,
1997,
2002,
2001,
2001,
2002,
1999,
2003,
2000
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1776,
50934,
6483,
21,
1005
] | 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,
1,
1,
2,
2,
6,
2,
8,
4,
9
] | 11 | true | Domain | UDP-glucose/GDP-mannose dehydrogenase, C-terminal | UDP-glucose/GDP-mannose dehydrogenase, C-terminal | UDP-Glc/GDP-Man_DH_C | 7 |
IPR014030 | 14,030 | Beta-ketoacyl synthase-like, N-terminal domain | KAS_N | Domain | 166,284 | false | false | This entry represents the N-terminal domain of beta-ketoacyl-ACP synthases and polyketide synthases. 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 a component of a number of enzymatic systems, including fatty acid synt... | [] | [] | [] | 0 | [
"PFAM",
"PFAM"
] | [
"PF00109",
"PF13723"
] | [
"ketoacyl-synt",
"Ketoacyl-synt_2"
] | [
161917,
4428
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"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.-",
"GenProp1220",
"GenProp1315",
"GenProp1415",
"GenProp1436",
"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",
"... | [
"EC:2.3.1",
"EC:2.3.1.-",
"GP:GenProp1220",
"GP:GenProp1315",
"GP:GenProp1415",
"GP:GenProp1436",
"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:... | 241 | [
"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"
] | [
31,
122172,
42630,
8,
1443
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
15,
6,
11,
9,
2,
8,
6,
9,
16,
4,
2,
2,
41
] | 13 | true | Domain | Beta-ketoacyl synthase-like, N-terminal domain | Beta-ketoacyl synthase-like, N-terminal domain | KAS_N | 5 |
IPR014031 | 14,031 | Beta-ketoacyl synthase, C-terminal domain | KAS_C | Domain | 155,298 | false | false | This entry represents the C-terminal domain of beta-ketoacyl-ACP synthases. The active site is contained in a cleft between N-and C-terminal domains, with residues from both domains contributing to substrate binding and catalysis [ ]. It is also found in polyketide synthases such as Non-reducing polyketide synthase nsc... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02801"
] | [
"Ketoacyl-synt_C"
] | [
155298
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"GP",
"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.-",
"GenProp1220",
"GenProp1315",
"GenProp1415",
"GenProp1436",
"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",
"... | [
"EC:2.3.1",
"EC:2.3.1.-",
"GP:GenProp1220",
"GP:GenProp1315",
"GP:GenProp1415",
"GP:GenProp1436",
"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:... | 240 | [
"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"... | 354 | [
"PUB00000791",
"PUB00001385",
"PUB00024434",
"PUB00082314",
"PUB00154590",
"PUB00154591"
] | [
"3076376",
"2209605",
"11152607",
"25372119",
"19799378",
"23368997"
] | [
"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.",
"The crystal struc... | [
1988,
1990,
2001,
2015,
2009,
2013
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
29,
113293,
40702,
7,
1267
] | 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,
4,
6,
9,
16,
5,
2,
2,
41
] | 13 | true | Domain | Beta-ketoacyl synthase, C-terminal domain | Beta-ketoacyl synthase, C-terminal domain | KAS_C | 3 |
IPR014032 | 14,032 | Peptidase A24A, prepilin type IV, bacterial | Peptidase_A24A_bac | Family | 11,674 | false | false | Cysteine protease activity is dependent on an active dyad of cysteine and histidine, the order and spacing of these residues varying in the 20 or so known families. Cysteine proteases have been grouped into two clans (CA and CB). Families C1, C2 and C10 are loosely termed papain-like and belong to clan CA; five cystein... | [] | [] | [] | 0 | [
"PRINTS"
] | [
"PR00864"
] | [
"PREPILNPTASE"
] | [
11674
] | 1 | [
"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",
"... | [
"2.1.1.-",
"3.4.23.43",
"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... | [
"EC:2.1.1.-",
"EC:3.4.23.43",
"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"... | 147 | [] | 0 | [
"PUB00000522",
"PUB00003577"
] | [
"8439290",
"7845226"
] | [
"Evolutionary families of peptidases.",
"Families of cysteine peptidases."
] | [
1993,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11467,
10,
197
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Peptidase A24A, prepilin type IV, bacterial | Peptidase A24A, prepilin type IV, bacterial | Peptidase_A24A_bac | 3 |
IPR014033 | 14,033 | Arginase | Arginase | Family | 9,919 | false | false | L-Arginine is converted to nitric oxide and citrulline by the enzyme nitric oxide synthase and by the enzyme arginase as a part of the hepatic urea cycle [ ]. Arginase is a manganese metalloenzyme containing a metal-activated hydroxide ion, a critical nucleophile in metalloenzymes that catalyze hydrolysis or hydration ... | [
"GO:0004053",
"GO:0046872",
"GO:0006525"
] | [
"arginase activity",
"metal ion binding",
"arginine metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR01229",
"cd09989"
] | [
"rocF_arginase",
"Arginase"
] | [
9001,
9581
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"3.5.3.1",
"GenProp0643",
"GenProp1300",
"GenProp1428",
"PWY-31",
"PWY-46",
"PWY-4984",
"PWY-6922",
"R-BTA-6798695",
"R-BTA-70635",
"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",
... | [
"EC:3.5.3.1",
"GP:GenProp0643",
"GP:GenProp1300",
"GP:GenProp1428",
"METACYC:PWY-31",
"METACYC:PWY-46",
"METACYC:PWY-4984",
"METACYC:PWY-6922",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70635",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70635",
"REACTOME:R-HSA-9837999",
"REACTOME:R-MMU-6798... | 27 | [
"1cev",
"1d3v",
"1hq5",
"1hqf",
"1hqg",
"1hqh",
"1hqx",
"1p8m",
"1p8n",
"1p8o",
"1p8p",
"1p8q",
"1p8r",
"1p8s",
"1pq3",
"1r1o",
"1rla",
"1t4p",
"1t4r",
"1t4s",
"1t4t",
"1t5f",
"1t5g",
"1ta1",
"1tbh",
"1tbj",
"1tbl",
"1wva",
"1wvb",
"1zpe",
"1zpg",
"2aeb"... | 146 | [
"PUB00017651"
] | [
"10931887"
] | [
"Phylogeny of related functions: the case of polyamine biosynthetic enzymes."
] | [
2000
] | 1 | [
"IPR006035"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Fadolivirus FV1/VV64",
"Methanobacteriati",
"metagenomes"
] | [
5588,
3953,
1,
333,
44
] | 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,
2,
2,
3,
3,
2,
8,
1,
2
] | 9 | true | Family | Arginase | Arginase | Arginase | 6 |
IPR014034 | 14,034 | Ferritin, conserved site | Ferritin_CS | Conserved_site | 6,690 | false | false | null | [] | [] | [] | 0 | [
"PROSITE",
"PROSITE"
] | [
"PS00204",
"PS00540"
] | [
"FERRITIN_2",
"FERRITIN_1"
] | [
6042,
3102
] | 2 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.16.3.1",
"PDOC00181",
"R-BTA-6798695",
"R-BTA-917937",
"R-CFA-432722",
"R-CFA-6798695",
"R-CFA-917937",
"R-GGA-432722",
"R-GGA-6798695",
"R-GGA-917937",
"R-HSA-3000480",
"R-HSA-432722",
"R-HSA-6798695",
"R-HSA-917937",
"R-MMU-432722",
"R-MMU-6798695",
"R-MMU-917937",
"R-RNO-4327... | [
"EC:1.16.3.1",
"PROSITEDOC:PDOC00181",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-917937",
"REACTOME:R-CFA-432722",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-917937",
"REACTOME:R-GGA-432722",
"REACTOME:R-GGA-6798695",
"REACTOME:R-GGA-917937",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-432722",
... | 20 | [
"1aew",
"1bg7",
"1dat",
"1fha",
"1gwg",
"1h96",
"1hrs",
"1ier",
"1ies",
"1lb3",
"1mfr",
"1r03",
"1rcc",
"1rcd",
"1rce",
"1rcg",
"1rci",
"1xz1",
"1xz3",
"2cei",
"2chi",
"2cih",
"2clu",
"2cn6",
"2cn7",
"2ffx",
"2fg4",
"2fg8",
"2fha",
"2g4h",
"2gyd",
"2iu2"... | 414 | [
"PUB00000049",
"PUB00001349",
"PUB00002586"
] | [
"3304136",
"3032619",
"2211706"
] | [
"Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms.",
"Iron transport and storage.",
"Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean."
] | [
1987,
1987,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
8,
6682
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
24,
1,
11,
1,
22,
18,
7,
32,
15
] | 9 | true | Conserved_site | Ferritin, conserved site | Ferritin, conserved site | Ferritin_CS | 5 |
IPR014036 | 14,036 | DeoR-like transcriptional repressor, C-terminal sensor domain | DeoR-like_C | Domain | 67,250 | false | false | DeoR-like transcription repressors occur in diverse bacteria and archaea, as regulators of sugar and nucleoside metabolic systems. The effector molecules for DeoR-like regulators are generally phosphorylated intermediates of the relevant metabolic pathway. The C-terminal sensor domain of DeoR-like transcription repress... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00455"
] | [
"DeoRC"
] | [
67250
] | 1 | [
"GP",
"GP",
"GP"
] | [
"GenProp0457",
"GenProp0458",
"GenProp0713"
] | [
"GP:GenProp0457",
"GP:GenProp0458",
"GP:GenProp0713"
] | 3 | [
"7l6l"
] | 1 | [
"PUB00057235",
"PUB00057236",
"PUB00067928",
"PUB00106374",
"PUB00153710",
"PUB00153711"
] | [
"16376935",
"18844374",
"10714997",
"20935102",
"24334671",
"29914986"
] | [
"Diversification of catalytic activities and ligand interactions in the protein fold shared by the sugar isomerases, eIF2B, DeoR transcription factors, acyl-CoA transferases and methenyltetrahydrofolate synthetase.",
"Quaternary structural transitions in the DeoR-type repressor UlaR control transcriptional readou... | [
2006,
2008,
2000,
2010,
2014,
2018
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Punavirus",
"unclassified sequences"
] | [
66748,
43,
152,
2,
305
] | 5 | [
"Escherichia coli (strain K12)"
] | [
11
] | 1 | true | Domain | DeoR-like transcriptional repressor, C-terminal sensor domain | DeoR-like transcriptional repressor, C-terminal sensor domain | DeoR-like_C | 9 |
IPR014038 | 14,038 | Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain | EF1B_bsu/dsu_GNE | Domain | 11,173 | false | false | Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept... | [
"GO:0003746",
"GO:0006414"
] | [
"translation elongation factor activity",
"translational elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART",
"CDD"
] | [
"PF00736",
"SM00888",
"cd00292"
] | [
"EF1_GNE",
"EF1_GNE",
"EF1B"
] | [
11163,
10908,
10744
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-156842",
"R-DDI-156842",
"R-DME-156842",
"R-HSA-156842",
"R-MMU-156842",
"R-RNO-156842",
"R-SCE-156842",
"R-SPO-156842"
] | [
"REACTOME:R-BTA-156842",
"REACTOME:R-DDI-156842",
"REACTOME:R-DME-156842",
"REACTOME:R-HSA-156842",
"REACTOME:R-MMU-156842",
"REACTOME:R-RNO-156842",
"REACTOME:R-SCE-156842",
"REACTOME:R-SPO-156842"
] | 8 | [
"1b64",
"1f60",
"1g7c",
"1gh8",
"1ije",
"1ijf",
"2b7b",
"2b7c",
"2n51",
"2yy3",
"5o8w",
"7csl"
] | 12 | [
"PUB00033951",
"PUB00033952",
"PUB00033953"
] | [
"12932732",
"15922593",
"12762045"
] | [
"Elongation factors in protein biosynthesis.",
"Elongation factors on the ribosome.",
"Structural studies of eukaryotic elongation factors."
] | [
2003,
2005,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
886,
4,
10241,
42
] | 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... | [
21,
2,
16,
3,
13,
10,
1,
7,
19,
1,
1,
15
] | 12 | true | Domain | Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain | Translation elongation factor EF1B, beta/delta subunit, guanine nucleotide exchange domain | EF1B_bsu/dsu_GNE | 3 |
IPR014039 | 14,039 | Translation elongation factor EFTs/EF1B, dimerisation | Transl_elong_EFTs/EF1B_dimer | Domain | 29,597 | false | false | Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept... | [
"GO:0003746",
"GO:0006414"
] | [
"translation elongation factor activity",
"translational elongation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00889"
] | [
"EF_TS"
] | [
29597
] | 1 | [
"REACTOME"
] | [
"R-HSA-5389840"
] | [
"REACTOME:R-HSA-5389840"
] | 1 | [
"1aip",
"1efu",
"1tfe",
"1xb2",
"3agp",
"3agq",
"3avt",
"3avu",
"3avv",
"3avw",
"3avx",
"3avy",
"3mmp",
"3vnu",
"3vnv",
"4fwt",
"4pc1",
"4pc2",
"4pc3",
"4pc6",
"4pc7",
"4q7j",
"4r71",
"7vmx"
] | 24 | [
"PUB00033951",
"PUB00033952",
"PUB00033953"
] | [
"12932732",
"15922593",
"12762045"
] | [
"Elongation factors in protein biosynthesis.",
"Elongation factors on the ribosome.",
"Structural studies of eukaryotic elongation factors."
] | [
2003,
2005,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
24866,
4141,
1,
588,
1
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
1,
1,
1,
1,
4,
6,
8,
6,
1,
21
] | 11 | true | Domain | Translation elongation factor EFTs/EF1B, dimerisation | Translation elongation factor EFTs/EF1B, dimerisation | Transl_elong_EFTs/EF1B_dimer | 5 |
IPR014041 | 14,041 | ESCRT-II complex, Vps25 subunit, N-terminal winged helix | ESCRT-II_cplx_Vps25-sub_N | Homologous_superfamily | 3,843 | false | false | This superfamily represents the N-terminal winged helix domain of the vps25 subunit (vacuolar protein sorting-associated protein 25) of the endosome-associated complex ESCRT-II (Endosomal Sorting Complexes Required for Transport protein II). ESCRT (ESCRT-I, -II, -III) complexes orchestrate efficient sorting of ubiquiti... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.10.570"
] | [
""
] | [
3843
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-917729",
"R-DDI-917729",
"R-DME-917729",
"R-DRE-917729",
"R-HSA-917729",
"R-HSA-9610379",
"R-MMU-917729",
"R-RNO-917729",
"R-SCE-917729",
"R-SPO-917729"
] | [
"REACTOME:R-BTA-917729",
"REACTOME:R-DDI-917729",
"REACTOME:R-DME-917729",
"REACTOME:R-DRE-917729",
"REACTOME:R-HSA-917729",
"REACTOME:R-HSA-9610379",
"REACTOME:R-MMU-917729",
"REACTOME:R-RNO-917729",
"REACTOME:R-SCE-917729",
"REACTOME:R-SPO-917729"
] | 10 | [
"1u5t",
"1w7p",
"1xb4",
"2zme",
"3cuq",
"7pb9"
] | 6 | [
"PUB00019520",
"PUB00019521",
"PUB00032375",
"PUB00035959"
] | [
"12194858",
"15469844",
"15579210",
"17215868"
] | [
"Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body.",
"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes.",
"Crystal structure of subunit VPS25 of the endosomal t... | [
2002,
2004,
2004,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Candidatus Heimdallarchaeum",
"Eukaryota",
"unclassified sequences"
] | [
2,
3830,
11
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
2,
1,
2,
1,
4,
5,
1,
3,
8,
1,
1,
8
] | 12 | true | Homologous_superfamily | ESCRT-II complex, Vps25 subunit, N-terminal winged helix | ESCRT-II complex, Vps25 subunit, N-terminal winged helix | ESCRT-II_cplx_Vps25-sub_N | 9 |
IPR014042 | 14,042 | Glutathione synthase, alpha-helical | Glutathione_synthase_a-hlx | Homologous_superfamily | 6,022 | false | false | This superfamily represents an α-helical domain found in glutathione synthetase ( ) (GSS), a homodimeric enzyme that catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to phosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis, the first step being catalyse... | [
"GO:0004363",
"GO:0005524",
"GO:0016874",
"GO:0006750"
] | [
"glutathione synthase activity",
"ATP binding",
"ligase activity",
"glutathione biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:1.10.1080.10"
] | [
""
] | [
6022
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.2.3",
"PWY-8043",
"R-DDI-174403",
"R-HSA-174403",
"R-HSA-5579006",
"R-MMU-174403",
"R-RNO-174403",
"R-SCE-174403",
"R-SPO-174403"
] | [
"EC:6.3.2.3",
"METACYC:PWY-8043",
"REACTOME:R-DDI-174403",
"REACTOME:R-HSA-174403",
"REACTOME:R-HSA-5579006",
"REACTOME:R-MMU-174403",
"REACTOME:R-RNO-174403",
"REACTOME:R-SCE-174403",
"REACTOME:R-SPO-174403"
] | 9 | [
"1m0t",
"1m0w",
"2hgs",
"2wyo",
"3kaj",
"3kak",
"3kal",
"5oes",
"5oet",
"5oeu",
"5oev",
"8fbz"
] | 12 | [
"PUB00035960"
] | [
"15981742"
] | [
"Physiological and pathological aspects of GSH metabolism."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
243,
5774,
5
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
2,
5,
6,
6,
2,
12,
6,
1,
1,
32
] | 12 | true | Homologous_superfamily | Glutathione synthase, alpha-helical | Glutathione synthase, alpha-helical | Glutathione_synthase_a-hlx | 1 |
IPR014044 | 14,044 | CAP domain | CAP_dom | Domain | 75,932 | false | false | This entry represents the CAP domain common to all members of the CAP superfamily. The CAP domain forms a unique 3 layer α-β-α fold with some, though not all, of the structural elements found in proteases [ ]. The cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) superfamily protein... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF00188",
"SM00198"
] | [
"CAP",
"SCP"
] | [
75492,
44102
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6798695",
"R-CEL-6798695",
"R-DDI-204005",
"R-DDI-2132295",
"R-DDI-5694530",
"R-DDI-6798695",
"R-HSA-1989781",
"R-HSA-6798695",
"R-MMU-6798695"
] | [
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DDI-204005",
"REACTOME:R-DDI-2132295",
"REACTOME:R-DDI-5694530",
"REACTOME:R-DDI-6798695",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-6798695"
] | 9 | [
"1cfe",
"1qnx",
"1rc9",
"1smb",
"1u53",
"1wvr",
"1xta",
"1xx5",
"2dda",
"2ddb",
"2epf",
"2giz",
"2vzn",
"3mz8",
"3nt8",
"3q2r",
"3q2u",
"3u3l",
"3u3n",
"3u3u",
"4aiw",
"4d53",
"4g2u",
"4h0a",
"4ifa",
"4ly5",
"4nui",
"4nuk",
"4nun",
"4nuo",
"4p27",
"4tpv"... | 40 | [
"PUB00016669",
"PUB00020314",
"PUB00054006"
] | [
"12625841",
"12759345",
"18824526"
] | [
"New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor.",
"Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily.",
"The CAP superfamily: cysteine-rich secretory proteins, antigen 5, and p... | [
2003,
2003,
2008
] | 3 | [] | [
"IPR014258",
"IPR034113",
"IPR034117",
"IPR034121",
"IPR047832",
"IPR047899"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
421,
27298,
47943,
24,
246
] | 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... | [
77,
42,
23,
98,
41,
30,
3,
89,
42,
3,
43
] | 11 | true | Domain | CAP domain | CAP domain | CAP_dom | 6 |
IPR014046 | 14,046 | Diadenylate cyclase | C-di-AMP_synthase | Family | 8,277 | false | false | Diadenylate cyclase catalyses the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a signaling compound secreted into the host's cytosol by bacterial pathogens, such as Listeria monocytogenes. This compound triggers the cytosolic surveillance pathway (CSP), a host pathway of innate immunity [ ]. Apart fro... | [
"GO:0004016",
"GO:0006171"
] | [
"adenylate cyclase activity",
"cAMP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF"
] | [
"PIRSF004793"
] | [
"UCP004793"
] | [
8277
] | 1 | [
"EC"
] | [
"2.7.7.85"
] | [
"EC:2.7.7.85"
] | 1 | [
"2fb5",
"4rv7",
"6huw",
"9g69"
] | 4 | [
"PUB00070986",
"PUB00078858",
"PUB00078859",
"PUB00079209",
"PUB00079210"
] | [
"20508090",
"26240071",
"23716572",
"24939848",
"23192352"
] | [
"c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response.",
"An Essential Poison: Synthesis and Degradation of Cyclic Di-AMP in Bacillus subtilis.",
"Cyclic di-AMP is critical for Listeria monocytogenes growth, cell wall homeostasis, and establishment of infection."... | [
2010,
2015,
2013,
2014,
2013
] | 5 | [] | [
"IPR034693",
"IPR034701"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctES717",
"unclassified sequences"
] | [
8159,
7,
1,
110
] | 4 | [] | [] | 0 | true | Family | Diadenylate cyclase | Diadenylate cyclase | C-di-AMP_synthase | 1 |
IPR014047 | 14,047 | Chromate transporter, long chain | Chr_Tranpt_l_chain | Family | 13,128 | false | false | This entry represents the long chain chromate transporters [ , , ]. The protein reduces chromate accumulation and is essential for chromate resistance. They appear to have arisen from a gene fusion event of two short chain transporters [ ]. | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF004810",
"TIGR00937"
] | [
"ChrA",
"2A51"
] | [
12985,
12165
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009527",
"PUB00009528",
"PUB00053869",
"PUB00061603"
] | [
"2152903",
"2180932",
"19581367",
"17986256"
] | [
"Cloning, nucleotide sequence, and expression of the chromate resistance determinant of Pseudomonas aeruginosa plasmid pUM505.",
"Nucleotide sequence and expression of a plasmid-encoded chromate resistance determinant from Alcaligenes eutrophus.",
"Short-chain chromate ion transporter proteins from Bacillus sub... | [
1990,
1990,
2009,
2007
] | 4 | [
"IPR003370"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
12164,
843,
36,
85
] | 4 | [] | [] | 0 | true | Family | Chromate transporter, long chain | Chromate transporter, long chain | Chr_Tranpt_l_chain | 2 |
IPR014048 | 14,048 | Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding | MethylDNA_cys_MeTrfase_DNA-bd | Domain | 59,502 | false | false | Synonym(s): 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase This entry represents the DNA binding region of 6-O-methylguanine-DNA methyltransferases. The repair of DNA containing O6-alkylated guanine is carried out by DNA-[protein]-cysteine S-methyltransferase ( ). The major mutagenic an... | [
"GO:0003824",
"GO:0006281"
] | [
"catalytic activity",
"DNA repair"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"NCBIFAM",
"CDD"
] | [
"PF01035",
"TIGR00589",
"cd06445"
] | [
"DNA_binding_1",
"ogt",
"ATase"
] | [
59494,
47777,
58369
] | 3 | [
"EC",
"REACTOME"
] | [
"2.1.1.63",
"R-HSA-5657655"
] | [
"EC:2.1.1.63",
"REACTOME:R-HSA-5657655"
] | 2 | [
"1eh6",
"1eh7",
"1eh8",
"1mgt",
"1qnt",
"1sfe",
"1t38",
"1t39",
"1wrj",
"1yfh",
"2g7h",
"2kif",
"2kim",
"3gva",
"3gx4",
"3gyh",
"3kzy",
"3kzz",
"3l00",
"4bhb",
"4bhc",
"4enj",
"4enk",
"4enm",
"4enn",
"4hdu",
"4hdv",
"4wx9",
"4wxc",
"4wxd",
"4zyd",
"4zye"... | 78 | [
"PUB00000053",
"PUB00004404"
] | [
"3052269",
"1579490"
] | [
"Regulation and expression of the adaptive response to alkylating agents.",
"Isolation and partial characterisation of a Chinese hamster O6-alkylguanine-DNA alkyltransferase cDNA."
] | [
1988,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1024,
53321,
4375,
28,
754
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
2,
7,
1,
3,
5,
2,
1,
5,
1,
1
] | 10 | true | Domain | Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding | Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding | MethylDNA_cys_MeTrfase_DNA-bd | 7 |
IPR014049 | 14,049 | Glutathione synthase, N-terminal, eukaryotic | Glutathione_synthase_N_euk | Homologous_superfamily | 5,993 | false | false | This superfamily represents the N-terminal domain found in eukaryotic glutathione synthetase ( ) (GSS), a homodimeric enzyme that catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to phosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis, the first step b... | [
"GO:0004363",
"GO:0005524"
] | [
"glutathione synthase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.1490.80"
] | [
""
] | [
5993
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.2.3",
"PWY-8043",
"R-DDI-174403",
"R-HSA-174403",
"R-HSA-5579006",
"R-MMU-174403",
"R-RNO-174403",
"R-SCE-174403",
"R-SPO-174403"
] | [
"EC:6.3.2.3",
"METACYC:PWY-8043",
"REACTOME:R-DDI-174403",
"REACTOME:R-HSA-174403",
"REACTOME:R-HSA-5579006",
"REACTOME:R-MMU-174403",
"REACTOME:R-RNO-174403",
"REACTOME:R-SCE-174403",
"REACTOME:R-SPO-174403"
] | 9 | [
"1m0t",
"1m0w",
"2hgs",
"3kaj",
"3kak",
"3kal",
"5oes",
"5oet",
"5oeu",
"5oev",
"8fbz"
] | 11 | [
"PUB00035960"
] | [
"15981742"
] | [
"Physiological and pathological aspects of GSH metabolism."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
240,
5748,
5
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
1,
2,
3,
15,
8,
2,
17,
6,
1,
1,
30
] | 12 | true | Homologous_superfamily | Glutathione synthase, N-terminal, eukaryotic | Glutathione synthase, N-terminal, eukaryotic | Glutathione_synthase_N_euk | 3 |
IPR014051 | 14,051 | Phosphoesterase, HXTX | Phosphoesterase_HXTX | Domain | 5,113 | false | false | This entry represents a domain found in a number of known and predicted phosphoesterases. These include bacterial and archaeal 2',5' RNA ligases, and a family of predicted phosphoesterases known as the YjcG family. The 2',5' RNA ligases perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-ph... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF02834"
] | [
"LigT_PEase"
] | [
5113
] | 1 | [
"EC"
] | [
"3.1.4.58"
] | [
"EC:3.1.4.58"
] | 1 | [
"1iuh",
"1vdx",
"1vgj",
"2fyh",
"5h7e",
"5h7f"
] | 6 | [
"PUB00013642",
"PUB00016758",
"PUB00017746"
] | [
"12466548",
"8940112",
"12798681"
] | [
"Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily.",
"The 2'-5' RNA ligase of Escherichia coli. Purification, cloning, and genomic disruption.",
"Crystal structure of the 2'-5' RNA ligase from Thermus thermophilus HB8."
] | [
2002,
1996,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Hyperionvirus sp.",
"unclassified sequences"
] | [
476,
4443,
32,
1,
161
] | 5 | [] | [] | 0 | true | Domain | Phosphoesterase, HXTX | Phosphoesterase, HXTX | Phosphoesterase_HXTX | 3 |
IPR014052 | 14,052 | DNA primase, small subunit, eukaryotic/archaeal | DNA_primase_ssu_euk/arc | Family | 4,900 | false | false | This entry represents the eukaryotic and archaeal DNA primase small subunit proteins known as PRIM1 and PriS, respectively [ , ], and does not include bacterial or viral proteins. Bacterial DNA primase adopts a different fold to archaeal and eukaryotic primases [ ]. In human, PRIM1 deficiency has been associated with p... | [
"GO:0003899",
"GO:0006269"
] | [
"DNA-directed RNA polymerase activity",
"DNA replication, synthesis of primer"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR00335",
"cd04860"
] | [
"primase_sml",
"AE_Prim_S"
] | [
4481,
4808
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"2.7.7.-",
"PWY-6322",
"PWY-6626",
"PWY-6749",
"PWY-6955",
"PWY-6998",
"PWY-7127",
"PWY-7419",
"PWY-7529",
"PWY-7706",
"PWY-7719",
"PWY-7735",
"PWY-7737",
"PWY-7769",
"PWY-7888",
"PWY-7904",
"PWY-8117",
"PWY-8179",
"R-CEL-113501",
"R-CEL-68952",
"R-CEL-68962",
"R-CEL-69091"... | [
"EC:2.7.7.-",
"METACYC:PWY-6322",
"METACYC:PWY-6626",
"METACYC:PWY-6749",
"METACYC:PWY-6955",
"METACYC:PWY-6998",
"METACYC:PWY-7127",
"METACYC:PWY-7419",
"METACYC:PWY-7529",
"METACYC:PWY-7706",
"METACYC:PWY-7719",
"METACYC:PWY-7735",
"METACYC:PWY-7737",
"METACYC:PWY-7769",
"METACYC:PWY-7... | 65 | [
"1g71",
"1v33",
"1v34",
"1zt2",
"4bpu",
"4bpw",
"4bpx",
"4lik",
"4lil",
"4lim",
"4mhq",
"4mm2",
"4rr2",
"5exr",
"5of3",
"5ofn",
"6r4s",
"6r4t",
"6r4u",
"6r5d",
"6r5e",
"6rb4",
"7opl",
"7u5c",
"7uy8",
"8b9a",
"8b9b",
"8b9c",
"8b9d",
"8d0b",
"8d0k",
"8d9d"... | 51 | [
"PUB00005693",
"PUB00044946",
"PUB00091304",
"PUB00106864",
"PUB00106865"
] | [
"2023935",
"16027112",
"26095544",
"25550159",
"33060134"
] | [
"Mutations in conserved yeast DNA primase domains impair DNA replication in vivo.",
"Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members.",
"A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-t... | [
1991,
2005,
2015,
2015,
2020
] | 5 | [
"IPR002755"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Eukaryota",
"Fervidobacterium pennivorans",
"ecological metagenomes"
] | [
797,
4096,
1,
6
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
2,
1,
1,
6,
3,
1,
1,
5,
1,
1,
4
] | 12 | true | Family | DNA primase, small subunit, eukaryotic/archaeal | DNA primase, small subunit, eukaryotic/archaeal | DNA_primase_ssu_euk/arc | 4 |
IPR014053 | 14,053 | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr | ForMFR_H4MPT_ForTrfase | Family | 1,139 | false | false | Formylmethanofuran:tetrahyromethanopterin formyltransferase (Ftr) is involved in C1 metabolism in methanogenic archaea, sulphate-reducing archaea and methylotrophic bacteria. It catalyses the following reversible reaction: N-formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahyd... | [
"GO:0030270",
"GO:0006730"
] | [
"formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity",
"one-carbon metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PIRSF",
"NCBIFAM"
] | [
"MF_00579",
"NF002554",
"PIRSF006414",
"TIGR03119"
] | [
"FTR",
"PRK02114.1",
"Ftr_formyl_trnsf",
"one_C_fhcD"
] | [
962,
1136,
1057,
1044
] | 4 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.101",
"GenProp0671",
"PWY-5209",
"PWY-7784",
"PWY-8305"
] | [
"EC:2.3.1.101",
"GP:GenProp0671",
"METACYC:PWY-5209",
"METACYC:PWY-7784",
"METACYC:PWY-8305"
] | 5 | [
"1ftr",
"1m5h",
"1m5s",
"2fhj",
"2fhk",
"6s6y"
] | 6 | [
"PUB00005787",
"PUB00016939",
"PUB00016940"
] | [
"9195883",
"12192072",
"12123819"
] | [
"Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.",
"Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.",
"Generation of for... | [
1997,
2002,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cladocopium goreaui",
"unclassified sequences"
] | [
345,
763,
2,
29
] | 4 | [] | [] | 0 | true | Family | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr | Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr | ForMFR_H4MPT_ForTrfase | 9 |
IPR014055 | 14,055 | CRISPR-associated protein, Csx11 | CRISPR-assoc_prot_Csx11 | Family | 99 | false | false | Members of this uncommon, sporadically distributed Cas protein family are large (>900 amino acids) and strictly associated, so far, with CRISPR-associated (Cas) gene clusters. Nearby Cas genes always include members of the RAMP superfamily and the six-gene CRISPR-associated RAMP module. Species in which it is found, so... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02682"
] | [
"cas_csx11"
] | [
99
] | 1 | [
"GP"
] | [
"GenProp0021"
] | [
"GP:GenProp0021"
] | 1 | [] | 0 | [
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890"
] | [
"17442114",
"17379808",
"16545108",
"21699496",
"24459147"
] | [
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with euka... | [
2007,
2007,
2006,
2011,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota"
] | [
80,
19
] | 2 | [] | [] | 0 | true | Family | CRISPR-associated protein, Csx11 | CRISPR-associated protein, Csx11 | CRISPR-assoc_prot_Csx11 | 9 |
IPR014056 | 14,056 | Type II toxin-antitoxin system RelE/ParE-like toxin, predicted | TypeIITA-like_toxin_pred | Family | 4,289 | false | false | Members of this protein family are small, generally only 100 amino acids in length. The gene is almost invariably the upstream member of a gene pair, where the downstream member is a predicted DNA-binding protein. These gene pairs, when found on the bacterial chromosome, are often located within prophage regions, but a... | [] | [] | [] | 0 | [
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF028744",
"PTHR41791",
"TIGR02683"
] | [
"Addict_mod_HI1419",
"",
"upstrm_HI1419"
] | [
4071,
4277,
4236
] | 3 | [
"GP"
] | [
"GenProp0471"
] | [
"GP:GenProp0471"
] | 1 | [] | 0 | [
"PUB00153573"
] | [
"27455323"
] | [
"Type II Toxin-Antitoxin Systems in the Unicellular Cyanobacterium Synechocystis sp. PCC 6803."
] | [
2016
] | 1 | [
"IPR009241"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
4206,
3,
10,
70
] | 4 | [] | [] | 0 | true | Family | Type II toxin-antitoxin system RelE/ParE-like toxin, predicted | Type II toxin-antitoxin system RelE/ParE-like toxin, predicted | TypeIITA-like_toxin_pred | 1 |
IPR014057 | 14,057 | Uncharacterized protein HI1420 | HI1420 | Family | 5,442 | false | false | Members of this bacterial protein family are small, at roughly 100 amino acids. The gene is almost invariably the downstream member of a gene pair. It is a predicted DNA-binding protein from a clade within the helix-turn-helix family. These gene pairs, when found on the bacterial chromosome, are located often with prop... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"PF21716",
"PTHR40275",
"TIGR02684"
] | [
"dnstrm_HI1420",
"",
"dnstrm_HI1420"
] | [
5361,
4966,
4550
] | 3 | [
"GP"
] | [
"GenProp0471"
] | [
"GP:GenProp0471"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanosarcina mazei",
"Peduoviridae",
"unclassified sequences"
] | [
5343,
17,
1,
2,
79
] | 5 | [] | [] | 0 | true | Family | Uncharacterized protein HI1420 | Uncharacterized protein HI1420 | HI1420 | 8 |
IPR014058 | 14,058 | Pteridine reductase | Pteridine_reductase | Family | 62 | false | false | Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02685"
] | [
"pter_reduc_Leis"
] | [
62
] | 1 | [] | [] | [] | 0 | [
"1e7w",
"1e92",
"1mxf",
"1mxh",
"1p33",
"1w0c",
"2bf7",
"2bfa",
"2bfm",
"2bfo",
"2bfp",
"2c7v",
"2qhx",
"2vz0",
"2wd7",
"2wd8",
"2x9g",
"2x9n",
"2x9v",
"2xox",
"2yhi",
"2yhu",
"3bmc",
"3bmn",
"3bmo",
"3bmq",
"3gn1",
"3gn2",
"3h4v",
"3jq6",
"3jq7",
"3jq8"... | 106 | [] | [] | [] | [] | 0 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Trypanosomatidae"
] | [
62
] | 1 | [] | [] | 0 | true | Family | Pteridine reductase | Pteridine reductase | Pteridine_reductase | 6 |
IPR014059 | 14,059 | TraI/TrwC, conjugative relaxase domain | TraI/TrwC_relax | Domain | 3,094 | false | false | This is the conjugative relaxase domain found in the N-terminal region of TraI and TrwC [ ]. TrwC is a relaxase-helicase that acts in plasmid R388 conjugation [ ]. The relaxase domain has DNA cleavage and strand transfer activities. Members of this family are typically found near other genes characteristic of conjugati... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02686"
] | [
"relax_trwC"
] | [
3094
] | 1 | [
"EC",
"EC"
] | [
"5.6.2.-",
"5.6.2.3"
] | [
"EC:5.6.2.-",
"EC:5.6.2.3"
] | 2 | [
"1omh",
"1osb",
"1p4d",
"1qx0",
"1s6m",
"1zm5",
"2a0i",
"2cdm",
"2q7t",
"2q7u",
"3l57",
"3l6t",
"4pcb",
"5n8o",
"8a1b",
"8a1c",
"9f0x",
"9f0y",
"9f0z",
"9f10",
"9f11",
"9f12"
] | 22 | [
"PUB00034512",
"PUB00091215"
] | [
"12837798",
"28457609"
] | [
"A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core.",
"Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation."
] | [
2003,
2017
] | 2 | [
"IPR014862"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3059,
13,
22
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | TraI/TrwC, conjugative relaxase domain | TraI/TrwC, conjugative relaxase domain | TraI/TrwC_relax | 9 |
IPR014060 | 14,060 | Alkaline phosphatase-like protein PglZ | PglZ | Family | 1,473 | false | false | This family includes the Alkaline phosphatase-like protein PglZ from Bacillus cereus and Escherichia coli, putative phosphatases and core proteins of a type 1 BREX system. BREX systems (bacteriophage exclusion) provide immunity against bacteriophage. This system allows phage adsorption but prevents phage DNA replicatio... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02687"
] | [
""
] | [
1473
] | 1 | [
"GP"
] | [
"GenProp0472"
] | [
"GP:GenProp0472"
] | 1 | [
"9nv3"
] | 1 | [
"PUB00093365",
"PUB00097935"
] | [
"25452498",
"30418590"
] | [
"BREX is a novel phage resistance system widespread in microbial genomes.",
"BREX system of Escherichia coli distinguishes self from non-self by methylation of a specific DNA site."
] | [
2015,
2019
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
1429,
2,
36,
6
] | 4 | [] | [] | 0 | true | Family | Alkaline phosphatase-like protein PglZ | Alkaline phosphatase-like protein PglZ | PglZ | 6 |
IPR014061 | 14,061 | Lon-like protease BrxL-like | BrxL-like | Family | 2,168 | false | false | This family includes Lon-like protease BrxL from Bacillus cereus and similar proteins. BrxL is part of a type 1 BREX system. BREX systems (bacteriophage exclusion) provide immunity against bacteriophage, a system that allows phage adsorption but prevents phage DNA replication, without degradation of the phage DNA [ ]. ... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF13337",
"TIGR02688"
] | [
"BrxL_ATPase",
""
] | [
2168,
1979
] | 2 | [
"GP"
] | [
"GenProp0472"
] | [
"GP:GenProp0472"
] | 1 | [
"8emc",
"8emh"
] | 2 | [
"PUB00093365"
] | [
"25452498"
] | [
"BREX is a novel phage resistance system widespread in microbial genomes."
] | [
2015
] | 1 | [] | [
"IPR013473"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
122,
1971,
5,
21,
49
] | 5 | [] | [] | 0 | true | Family | Lon-like protease BrxL-like | Lon-like protease BrxL-like | BrxL-like | 6 |
IPR014063 | 14,063 | Arsenate resistance ArsH | Arsenate-R_ArsH | Family | 6,195 | false | false | Members of this protein family occur in arsenate resistance operons that include at least two different types of arsenate reductase. ArsH is not required for arsenate resistance in some systems. This family belongs to the larger family of NADPH-dependent FMN reductases ( ). ArsH from the cyanobacterium Synechocystis sp... | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR43590",
"TIGR02690"
] | [
"",
"resist_ArsH"
] | [
6195,
5821
] | 2 | [
"GP"
] | [
"GenProp0474"
] | [
"GP:GenProp0474"
] | 1 | [
"2fzv",
"2q62",
"7ple"
] | 3 | [
"PUB00072057"
] | [
"22304305"
] | [
"ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
5186,
2,
995,
12
] | 4 | [] | [] | 0 | true | Family | Arsenate resistance ArsH | Arsenate resistance ArsH | Arsenate-R_ArsH | 6 |
IPR014064 | 14,064 | Arsenate reductase ArsC | Arsenate_reductase_ArsC | Family | 2,390 | false | false | This family describes the well-studied thioredoxin-dependent arsenate reductase of Staphylococcus aureus plasmid pI258 and other mechanistically similar arsenate reductases. The mechanism involves an intramolecular disulphide bond cascade, and aligned members of this family have four absolutely conserved Cys residues. ... | [
"GO:0004725",
"GO:0030612",
"GO:0046685"
] | [
"protein tyrosine phosphatase activity",
"arsenate reductase (thioredoxin) activity",
"response to arsenic-containing substance"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM"
] | [
"MF_01624",
"NF010053",
"TIGR02691"
] | [
"Arsenate_reduct",
"PRK13530.1",
"arsC_pI258_fam"
] | [
1377,
1483,
2388
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"1.20.4.4",
"GenProp0474",
"PWY-8101"
] | [
"EC:1.20.4.4",
"GP:GenProp0474",
"METACYC:PWY-8101"
] | 3 | [
"1jf8",
"1jfv",
"1jl3",
"1ljl",
"1lju",
"1lk0",
"1rxe",
"1rxi",
"1z2d",
"1z2e",
"2cd7",
"2fxi",
"2ipa"
] | 13 | [
"PUB00027047"
] | [
"12072565"
] | [
"All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Phytophthora kernoviae 00238/432",
"ecological metagenomes"
] | [
2379,
4,
7
] | 3 | [] | [] | 0 | true | Family | Arsenate reductase ArsC | Arsenate reductase ArsC | Arsenate_reductase_ArsC | 8 |
IPR014065 | 14,065 | tRNA adenylyltransferase | tRNA_adenylyltransferase | Family | 4,733 | false | false | The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3 -end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family rep... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02692"
] | [
"tRNA_CCA_actino"
] | [
4733
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
4538,
195
] | 2 | [] | [] | 0 | true | Family | tRNA adenylyltransferase | tRNA adenylyltransferase | tRNA_adenylyltransferase | 7 |
IPR014066 | 14,066 | Arsenite oxidase subunit AioA/Iodate reductase subunit IdrA, large subunit | AioA/IdrA_lsu | Family | 549 | false | false | This entry represents a group of prokaryotic molybdopterin-containing oxidoreductases, including Arsenite oxidase subunit AioA from Alcaligenes faecalis and Iodate reductase subunit IdrA from Pseudomonas sp. AioA is the large subunit of an arsenite oxidase complex in which the small subunit is a Rieske protein. This en... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02693"
] | [
"arsenite_ox_L"
] | [
549
] | 1 | [
"GP"
] | [
"GenProp0473"
] | [
"GP:GenProp0473"
] | 1 | [
"1g8j",
"1g8k",
"4aay",
"5nqd",
"8ccq",
"8cff",
"8cgs",
"8ch9",
"8ed4",
"8r3a",
"8rtl",
"8rtm"
] | 12 | [
"PUB00034441",
"PUB00100773",
"PUB00100802"
] | [
"12679550",
"32190953",
"34215855"
] | [
"Arsenite oxidase, an ancient bioenergetic enzyme.",
"A novel dimethylsulfoxide reductase family of molybdenum enzyme, Idr, is involved in iodate respiration by Pseudomonas sp. SCT.",
"Genetic and phylogenetic analysis of dissimilatory iodate-reducing bacteria identifies potential niches across the world's ocea... | [
2003,
2020,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
11,
518,
20
] | 3 | [] | [] | 0 | true | Family | Arsenite oxidase subunit AioA/Iodate reductase subunit IdrA, large subunit | Arsenite oxidase subunit AioA/Iodate reductase subunit IdrA, large subunit | AioA/IdrA_lsu | 1 |
IPR014067 | 14,067 | Arsenite oxidase subunit AioB/Iodate reductase subunit IdrB, small subunit | AioB/IdrB_ssu | Family | 471 | false | false | This entry represents a group of prokaryotic molybdopterin-containing oxidoreductases, including Arsenite oxidase subunit AioB from Alcaligenes faecalis and Iodate reductase subunit IdrB from Pseudomonas sp. AioB is the small subunit of an arsenite oxidase complex. It is a Rieske protein and appears to rely on the Tat ... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02694",
"cd03476"
] | [
"arsenite_ox_S",
"Rieske_ArOX_small"
] | [
471,
126
] | 2 | [
"GP"
] | [
"GenProp0473"
] | [
"GP:GenProp0473"
] | 1 | [
"1g8j",
"1g8k",
"4aay",
"5nqd",
"8ccq",
"8cff",
"8cgs",
"8ch9",
"8ed4",
"8r3a",
"8rtl",
"8rtm"
] | 12 | [
"PUB00034441",
"PUB00100773",
"PUB00100802",
"PUB00100806"
] | [
"12679550",
"32190953",
"34215855",
"1331097"
] | [
"Arsenite oxidase, an ancient bioenergetic enzyme.",
"A novel dimethylsulfoxide reductase family of molybdenum enzyme, Idr, is involved in iodate respiration by Pseudomonas sp. SCT.",
"Genetic and phylogenetic analysis of dissimilatory iodate-reducing bacteria identifies potential niches across the world's ocea... | [
2003,
2020,
2022,
1992
] | 4 | [
"IPR014349"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
27,
420,
24
] | 3 | [] | [] | 0 | true | Family | Arsenite oxidase subunit AioB/Iodate reductase subunit IdrB, small subunit | Arsenite oxidase subunit AioB/Iodate reductase subunit IdrB, small subunit | AioB/IdrB_ssu | 9 |
IPR014068 | 14,068 | Azurin | Azurin | Family | 2,340 | false | false | Azurin is a blue copper-binding protein in the plastocyanin/azurin family. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities. The copp... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02695",
"cd13922"
] | [
"azurin",
"Azurin"
] | [
2195,
2314
] | 2 | [
"GP"
] | [
"GenProp0473"
] | [
"GP:GenProp0473"
] | 1 | [
"1a4a",
"1a4b",
"1a4c",
"1ag0",
"1aiz",
"1azb",
"1azc",
"1azn",
"1azr",
"1azu",
"1bex",
"1cc3",
"1cuo",
"1dyz",
"1dz0",
"1e5y",
"1e5z",
"1e65",
"1e67",
"1etj",
"1ezl",
"1gr7",
"1i53",
"1ils",
"1ilu",
"1joi",
"1jvl",
"1jvo",
"1jze",
"1jzf",
"1jzg",
"1jzh"... | 134 | [
"PUB00082904",
"PUB00082905",
"PUB00082906",
"PUB00082907",
"PUB00082908"
] | [
"12438386",
"14981543",
"14630027",
"12393814",
"20169379"
] | [
"The bacterial redox protein azurin induces apoptosis in J774 macrophages through complex formation and stabilization of the tumor suppressor protein p53.",
"Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer.",
"Bacterial cupredoxin azurin and its interactions with the... | [
2002,
2004,
2003,
2002,
2010
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
2321,
2,
17
] | 3 | [] | [] | 0 | true | Family | Azurin | Azurin | Azurin | 3 |
IPR014069 | 14,069 | Guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase | GPSI/PNP | Family | 4,536 | false | false | The of the characterisation of two proteins from Streptomyces coelicolor has been presented [ ]. The protein in this family was shown to have poly(A) polymerase activity and may be responsible for polyadenylating RNA in this species. It has also been shown that a nearly identical plasmid-encoded protein from Streptomyc... | [
"GO:0004654",
"GO:0006402",
"GO:0005737"
] | [
"polyribonucleotide nucleotidyltransferase activity",
"mRNA catabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02696"
] | [
"pppGpp_PNP"
] | [
4536
] | 1 | [
"EC"
] | [
"2.7.7.8"
] | [
"EC:2.7.7.8"
] | 1 | [
"1e3h",
"1e3p",
"7ld5",
"8wwp",
"8wx0",
"8wxf"
] | 6 | [
"PUB00034388",
"PUB00034501"
] | [
"14645289",
"8113189"
] | [
"The Streptomyces coelicolor polynucleotide phosphorylase homologue, and not the putative poly(A) polymerase, can polyadenylate RNA.",
"Purification and properties of ATP:GTP 3'-pyrophosphotransferase (guanosine pentaphosphate synthetase) from Streptomyces antibioticus."
] | [
2003,
1994
] | 2 | [
"IPR012162"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Mesangiospermae",
"metagenomes"
] | [
4461,
2,
73
] | 3 | [] | [] | 0 | true | Family | Guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase | Guanosine pentaphosphate synthetase I/polyribonucleotide nucleotidyltransferase | GPSI/PNP | 1 |
IPR014070 | 14,070 | Wolbachia palindromic element (WPE) | WPE_wolbac | Domain | 132 | false | false | This domain conceptually resembles , the Rickettsial palindromic element (RPE) domain. In both cases, a protein-coding palindromic element spreads through a genome, inserting usually in protein-coding regions. The additional protein coding sequence is thought to allow function of the host protein because of location in... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02697"
] | [
"WPE_wolbac"
] | [
132
] | 1 | [
"GP"
] | [
"GenProp0476"
] | [
"GP:GenProp0476"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Arthropoda",
"Wolbachia"
] | [
27,
105
] | 2 | [] | [] | 0 | true | Domain | Wolbachia palindromic element (WPE) | Wolbachia palindromic element (WPE) | WPE_wolbac | 1 |
IPR014071 | 14,071 | Copper transport repressor CopY/TcrY | Cu_transp_CopY/TcrY | Family | 1,856 | false | false | This family includes metal-fist type transcriptional repressors of copper transport systems such as copYZAB of Enterococcus hirae and tcrYAZB (transferable copper resistance) of an Enterococcus faecium (Streptococcus faecium) plasmid. High levels of copper can displace zinc and prevent binding by the repressor, activat... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02698"
] | [
"CopY_TcrY"
] | [
1856
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR005650"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"bioreactor metagenome"
] | [
1853,
3
] | 2 | [] | [] | 0 | true | Family | Copper transport repressor CopY/TcrY | Copper transport repressor CopY/TcrY | Cu_transp_CopY/TcrY | 7 |
IPR014072 | 14,072 | Archaeoflavoprotein AfpA | Archaeoflavo_AfpA | Family | 180 | false | false | The prototypical member of this archaeal protein family is AF1518 from Archaeoglobus fulgidus. This homodimer with two non-covalently bound FMN cofactors can receive electrons from ferredoxin, but not from a number of other electron donors such as NADH or rubredoxin. It can then donate electrons to various reductases [... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02699"
] | [
"archaeo_AfpA"
] | [
180
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034516"
] | [
"14679228"
] | [
"Flavin mononucleotide-binding flavoprotein family in the domain Archaea."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Pseudodesulfovibrio hydrargyri",
"ecological metagenomes"
] | [
177,
1,
2
] | 3 | [] | [] | 0 | true | Family | Archaeoflavoprotein AfpA | Archaeoflavoprotein AfpA | Archaeoflavo_AfpA | 3 |
IPR014073 | 14,073 | Archaeal dihydromethanopterin reductase | DmrX | Family | 121 | false | false | This entry describes one of two paralogous families of archaeal flavoproteins, the other being described by . Proteins in this family have been recently characterised as dihydromethanopterin reductases [ ]. | [
"GO:0016645",
"GO:0051539",
"GO:1901285"
] | [
"oxidoreductase activity, acting on the CH-NH group of donors",
"4 iron, 4 sulfur cluster binding",
"5,6,7,8-tetrahydromethanopterin biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02700"
] | [
"flavo_MJ0208"
] | [
121
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075347"
] | [
"23995635"
] | [
"Discovery and characterization of the first archaeal dihydromethanopterin reductase, an iron-sulfur flavoprotein from Methanosarcina mazei."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"bioreactor metagenome"
] | [
120,
1
] | 2 | [] | [] | 0 | true | Family | Archaeal dihydromethanopterin reductase | Archaeal dihydromethanopterin reductase | DmrX | 7 |
IPR014074 | 14,074 | Carboxysome shell carbonic anhydrase | Carboxysome_shell_carb_anhy | Family | 233 | false | false | This entry describes a carboxysome shell protein that proves to be a novel class, designated epsilon, of carbonic anhydrase. It tends to be encoded near genes for RuBisCo and other carboxysome shell proteins [ , ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02701"
] | [
"shell_carb_anhy"
] | [
233
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.1",
"PWY-241",
"PWY-5743",
"PWY-5744",
"PWY-5789",
"PWY-6142",
"PWY-7115",
"PWY-7117"
] | [
"EC:4.2.1.1",
"METACYC:PWY-241",
"METACYC:PWY-5743",
"METACYC:PWY-5744",
"METACYC:PWY-5789",
"METACYC:PWY-6142",
"METACYC:PWY-7115",
"METACYC:PWY-7117"
] | 8 | [
"2fgy",
"8thm",
"9g4t"
] | 3 | [
"PUB00015068",
"PUB00096656"
] | [
"14729686",
"17012396"
] | [
"A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell.",
"Characterization of the carboxysomal carbonic anhydrase CsoSCA from Halothiobacillus neapolitanus."
] | [
2004,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Paulinella",
"unclassified sequences"
] | [
217,
5,
11
] | 3 | [] | [] | 0 | true | Family | Carboxysome shell carbonic anhydrase | Carboxysome shell carbonic anhydrase | Carboxysome_shell_carb_anhy | 4 |
IPR014075 | 14,075 | SUF system FeS cluster assembly, SufR regulator, cyanobacteria | SUF_FeS_clus_asmb_SufR_cyano | Family | 337 | false | false | This entry represents members of the SufR cyanobacterial protein family of transcriptional regulators that control the SUF system. In all cases, the sufR gene is encoded near SUF system genes but in the opposite direction. This DNA-binding protein belongs to the DeoR family of helix-loop-helix proteins. All members als... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02702"
] | [
"SufR_cyano"
] | [
337
] | 1 | [
"GP"
] | [
"GenProp0137"
] | [
"GP:GenProp0137"
] | 1 | [] | 0 | [
"PUB00003442",
"PUB00028014",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640"
] | [
"8875867",
"11498000",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Incorporation of iron-sulphur clusters in membrane-bound proteins.",
"How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.",
"Mechanisms of iron-sulfur cluster assembly: the SUF machinery.",
... | [
1996,
2001,
2005,
2005,
2006,
2005,
2007,
2004
] | 8 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota"
] | [
337
] | 1 | [] | [] | 0 | true | Family | SUF system FeS cluster assembly, SufR regulator, cyanobacteria | SUF system FeS cluster assembly, SufR regulator, cyanobacteria | SUF_FeS_clus_asmb_SufR_cyano | 8 |
IPR014077 | 14,077 | Carboxysome shell vertex protein CsoS4B | CsoS4B | Family | 214 | false | false | This entry describes the Carboxysome shell vertex protein CsoS4B (also known as carboxysome operon protein orfB). It distinguishes one of two closely related paralogs encoded by nearby genes in the carboxysome operons of a number of cyanobacteria and chemoautotrophic bacteria. More distantly related proteins are compon... | [
"GO:0031469"
] | [
"bacterial microcompartment"
] | [
"cellular_component"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02704"
] | [
"carboxysome_B"
] | [
214
] | 1 | [] | [] | [] | 0 | [
"6jy5"
] | 1 | [
"PUB00096632"
] | [
"19844578"
] | [
"The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier."
] | [
2009
] | 1 | [
"IPR004992"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Paulinella",
"unclassified sequences"
] | [
201,
4,
9
] | 3 | [] | [] | 0 | true | Family | Carboxysome shell vertex protein CsoS4B | Carboxysome shell vertex protein CsoS4B | CsoS4B | 7 |
IPR014078 | 14,078 | Nucleoside triphosphatase YtkD | Nudix_YtkD | Family | 1,653 | false | false | The proteins in this entry belong to the nudix family and includes the putative 8-oxo-dGTP diphosphatase YtkD from E. coli. These sequences share some sequence identity with Escherichia coli MutT but appear not to be functionally interchangeable with it. It functions, in conjunction with MutT, to protect vegetatively g... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02705",
"cd04665"
] | [
"nudix_YtkD",
"NUDIX_RppH"
] | [
1076,
1488
] | 2 | [
"GP"
] | [
"GenProp1396"
] | [
"GP:GenProp1396"
] | 1 | [
"4jzs",
"4jzt",
"4jzu",
"4jzv"
] | 4 | [
"PUB00034389",
"PUB00034390"
] | [
"14761999",
"15576788"
] | [
"The ytkD (mutTA) gene of Bacillus subtilis encodes a functional antimutator 8-Oxo-(dGTP/GTP)ase and is under dual control of sigma A and sigma F RNA polymerases.",
"Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily."
] | [
2004,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Tritrichomonas musculus",
"metagenomes"
] | [
1646,
2,
5
] | 3 | [] | [] | 0 | true | Family | Nucleoside triphosphatase YtkD | Nucleoside triphosphatase YtkD | Nudix_YtkD | 2 |
IPR014079 | 14,079 | Phosphate butyryltransferase | Phosphate_butyryltransferase | Family | 909 | false | false | Members of this family are phosphate butyryltransferase enzymes, also called phosphotransbutyrylase. In general, this enzyme is found in butyrate-producing anaerobic bacteria, encoded next to the gene for butyrate kinase. Together, these two enzymes represent what may be the less common of two pathways for butyrate pro... | [
"GO:0016740",
"GO:0050182",
"GO:0019605"
] | [
"transferase activity",
"phosphate butyryltransferase activity",
"butyrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02706"
] | [
"P_butyryltrans"
] | [
909
] | 1 | [
"EC",
"GP"
] | [
"2.3.1.19",
"GenProp0910"
] | [
"EC:2.3.1.19",
"GP:GenProp0910"
] | 2 | [
"7vg9"
] | 1 | [] | [] | [] | [] | 0 | [
"IPR012147"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"bioreactor metagenome"
] | [
905,
4
] | 2 | [] | [] | 0 | true | Family | Phosphate butyryltransferase | Phosphate butyryltransferase | Phosphate_butyryltransferase | 3 |
IPR014080 | 14,080 | L-lactate oxidase | L_lactate_ox | Family | 207 | false | false | Members of this entry oxidize L-lactate to pyruvate, reducing molecular oxygen to hydrogen peroxide. The enzyme is known in Aerococcus viridans, Streptococcus iniae, and some strains of Streptococcus pyogenes where it appears to contribute to virulence. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02708"
] | [
"L_lactate_ox"
] | [
207
] | 1 | [] | [] | [] | 0 | [
"2du2",
"2e77",
"2j6x",
"2nli",
"2zfa",
"4rje",
"4yl2",
"5ebu",
"7f1y",
"7f20",
"7f21",
"7f22",
"8ufy"
] | 13 | [] | [] | [] | [] | 0 | [
"IPR012133"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
207
] | 1 | [] | [] | 0 | true | Family | L-lactate oxidase | L-lactate oxidase | L_lactate_ox | 6 |
IPR014081 | 14,081 | Branched-chain phosphotransacylase | Brnchd-chn_Ptransacetylase | Family | 14 | false | false | This entry distinguishes branched-chain phosphotransacylases like that of Enterococcus faecalis from closely related subfamilies of phosphate butyryltransferase , ( ) and phosphate acetyltransferase , ( ). Members of this family and of show considerable cross reactivity, and the occurrence of a member of either family ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02709"
] | [
"branched_ptb"
] | [
14
] | 1 | [] | [] | [] | 0 | [
"1yco"
] | 1 | [] | [] | [] | [] | 0 | [
"IPR012147"
] | [] | 1 | 0 | 1 | [
"Enterococcus faecalis"
] | [
14
] | 1 | [] | [] | 0 | true | Family | Branched-chain phosphotransacylase | Branched-chain phosphotransacylase | Brnchd-chn_Ptransacetylase | 4 |
IPR014082 | 14,082 | CRISPR-associated protein, Cas02710 | CRISPR-assoc_prot_Cas02710 | Family | 313 | false | false | This entry represents a family of Cas proteins encoded exclusively in the vicinity of CRISPR repeats and other Cas proteins in Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum), Thermus thermophilus (Deinococcus-Thermus), Chloroflexus aurantiacus (Chloroflexi), and Thermomicrobium roseum (Therm... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02710"
] | [
""
] | [
313
] | 1 | [
"GP"
] | [
"GenProp0021"
] | [
"GP:GenProp0021"
] | 1 | [] | 0 | [
"PUB00020781",
"PUB00043286",
"PUB00043287",
"PUB00043288",
"PUB00060621",
"PUB00071890",
"PUB00085051"
] | [
"16292354",
"17442114",
"17379808",
"16545108",
"21699496",
"24459147",
"24817877"
] | [
"A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes.",
"Evolutionary conservation of sequence and secondary structures in CRISPR repeats.",
"CRISPR provides acquired resistance against viruses in prokaryotes.",
"A putative RNA-interference-base... | [
2005,
2007,
2007,
2006,
2011,
2014,
2014
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
47,
261,
5
] | 3 | [] | [] | 0 | true | Family | CRISPR-associated protein, Cas02710 | CRISPR-associated protein, Cas02710 | CRISPR-assoc_prot_Cas02710 | 6 |
IPR014083 | 14,083 | Cation/acetate symporter ActP | Cation/Ac_symporter_ActP | Family | 1,209 | false | false | This entry represents the cation/acetate symporter ActP from Gammaproteobacteria. ActP transports acetate and is also able to transport glycolate [ ]. | [
"GO:0015123",
"GO:0043879",
"GO:0005886"
] | [
"acetate transmembrane transporter activity",
"glycolate transmembrane transporter activity",
"plasma membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01426",
"TIGR02711"
] | [
"Acet_symport_ActP",
"symport_actP"
] | [
1184,
1130
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034522"
] | [
"14563880"
] | [
"The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli."
] | [
2003
] | 1 | [
"IPR001734"
] | [] | 1 | 0 | 1 | [
"Beauveria bassiana D1-5",
"Gammaproteobacteria"
] | [
1,
1208
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Cation/acetate symporter ActP | Cation/acetate symporter ActP | Cation/Ac_symporter_ActP | 9 |
IPR014084 | 14,084 | Urea carboxylase | Urea_COase | Family | 3,684 | false | false | Members of this family are ATP-dependent urea carboxylases, including characterised members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae (Baker's yeast). The allophanate hydrolase domain of the yeast enzyme is not included in this entry and is represented by an a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02712"
] | [
"urea_carbox"
] | [
3684
] | 1 | [
"GP"
] | [
"GenProp0481"
] | [
"GP:GenProp0481"
] | 1 | [
"3va7",
"5i8i"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3149,
511,
24
] | 3 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Urea carboxylase | Urea carboxylase | Urea_COase | 3 |
IPR014085 | 14,085 | Allophanate hydrolase | Allophanate_hydrolase | Domain | 4,863 | false | false | Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has dive... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02713"
] | [
"allophanate_hyd"
] | [
4863
] | 1 | [
"EC",
"GP"
] | [
"3.5.1.54",
"GenProp0481"
] | [
"EC:3.5.1.54",
"GP:GenProp0481"
] | 2 | [
"4cp8",
"4gyr",
"4gys",
"4iss",
"4ist",
"5i8i"
] | 6 | [
"PUB00017563",
"PUB00035563",
"PUB00035564",
"PUB00035565",
"PUB00035566",
"PUB00043469"
] | [
"6124544",
"15595822",
"17015445",
"12032064",
"12521300",
"15796980"
] | [
"Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast.",
"Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate.",
"A second fatty acid amide hydrolase with variable distribut... | [
1982,
2004,
2006,
2002,
2002,
2005
] | 6 | [
"IPR023631"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
4372,
462,
6,
23
] | 4 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Allophanate hydrolase | Allophanate hydrolase | Allophanate_hydrolase | 4 |
IPR014086 | 14,086 | Cyanuric acid hydrolase/Barbiturase | AtzD/Barbiturase | Family | 1,173 | false | false | Cyanuric acid hydrolases (AtzD) and barbiturases are homologous and found almost exclusively in bacteria [ ]. AtzD hydrolyses cyanuric acid to release carboxybiuret, which spontaneously decarboxylates to biuret [ ]. Barbiturase catalyses the ring-opening of barbituric acid to ureidomalonic acid [ ]. Although the AtzD/b... | [
"GO:0016812"
] | [
"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"NCBIFAM"
] | [
"MF_01989",
"PF09663",
"TIGR02714"
] | [
"Cyc_amidohydrol",
"Amido_AtzD_TrzD",
"amido_AtzD_TrzD"
] | [
1099,
1173,
1125
] | 3 | [
"EC",
"EC",
"METACYC",
"METACYC"
] | [
"3.5.2",
"3.5.2.15",
"PWY-5169",
"PWY-8025"
] | [
"EC:3.5.2",
"EC:3.5.2.15",
"METACYC:PWY-5169",
"METACYC:PWY-8025"
] | 4 | [
"4bvq",
"4bvr",
"4bvs",
"4bvt",
"4nq3",
"5hwe",
"5hxu",
"5hxz",
"5hy0",
"5hy1",
"5hy2",
"5hy4",
"5t13",
"6bum",
"6bun",
"6buo",
"6bup",
"6buq",
"6bur",
"6cwj",
"6dhj"
] | 21 | [
"PUB00034391",
"PUB00060791"
] | [
"11485332",
"22730121"
] | [
"Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase.",
"Defining Sequence Space and Reaction Products within the Cyanuric Acid Hydrolase (AtzD)/Barbiturase Protein Family."
] | [
2001,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes",
"uncultured marine thaumarchaeote KM3_67_E04"
] | [
1074,
86,
12,
1
] | 4 | [] | [] | 0 | true | Family | Cyanuric acid hydrolase/Barbiturase | Cyanuric acid hydrolase/Barbiturase | AtzD/Barbiturase | 3 |
IPR014087 | 14,087 | 1-carboxybiuret hydrolase, AtzE subunit | Carboxybiuret_hydro_AtzE | Family | 1,621 | false | false | Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has dive... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02715"
] | [
"amido_AtzE"
] | [
1621
] | 1 | [] | [] | [] | 0 | [
"6c62",
"6c6g"
] | 2 | [
"PUB00035563",
"PUB00035564",
"PUB00035565",
"PUB00035566",
"PUB00092869"
] | [
"15595822",
"17015445",
"12032064",
"12521300",
"29523689"
] | [
"Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate.",
"A second fatty acid amide hydrolase with variable distribution among placental mammals.",
"Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalyti... | [
2004,
2006,
2002,
2002,
2018
] | 5 | [
"IPR000120"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Beauveria bassiana D1-5",
"mine drainage metagenome"
] | [
1618,
1,
2
] | 3 | [] | [] | 0 | true | Family | 1-carboxybiuret hydrolase, AtzE subunit | 1-carboxybiuret hydrolase, AtzE subunit | Carboxybiuret_hydro_AtzE | 2 |
IPR014088 | 14,088 | Bacteriochlorophyllide d C-20 methyltransferase | BchU | Family | 41 | false | false | Members of this protein family include bacteriochlorophyllide d C-20 (also known as methyltransferaseS-adenosylmethionine-dependent C-20 methyltransferase or BchU), part of the pathway of bacteriochlorophyll c production in photosynthetic green sulphur bacteria [ , ]. The position modified by this enzyme represents the... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02716"
] | [
"C20_methyl_CrtF"
] | [
41
] | 1 | [] | [] | [] | 0 | [
"1x19",
"1x1a",
"1x1b",
"1x1c",
"1x1d"
] | 5 | [
"PUB00006319",
"PUB00034526",
"PUB00034527",
"PUB00054125",
"PUB00057957",
"PUB00057958"
] | [
"7897657",
"15090495",
"15792807",
"12826405",
"16225687",
"21858014"
] | [
"Universal catalytic domain structure of AdoMet-dependent methyltransferases.",
"The bchU gene of Chlorobium tepidum encodes the c-20 methyltransferase in bacteriochlorophyll c biosynthesis.",
"In vitro activity of C-20 methyltransferase, BchU, involved in bacteriochlorophyll c biosynthetic pathway in green sul... | [
1995,
2004,
2005,
2003,
2005,
2011
] | 6 | [
"IPR016461"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
41
] | 1 | [] | [] | 0 | true | Family | Bacteriochlorophyllide d C-20 methyltransferase | Bacteriochlorophyllide d C-20 methyltransferase | BchU | 3 |
IPR014089 | 14,089 | Acetate-CoA ligase [ADP-forming], alpha domain | AcCoA-synth-alpha | Domain | 440 | false | false | This group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which they have been characterised [ , , ]. In most species this protein is bifunctional, existing as fused α-β domains. In Pyrococcus and related species, however, the domains exist as separa... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02717"
] | [
"AcCoA-syn-alpha"
] | [
440
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.2.1.13",
"PWY-5483",
"PWY-5535",
"PWY-8305"
] | [
"EC:6.2.1.13",
"METACYC:PWY-5483",
"METACYC:PWY-5535",
"METACYC:PWY-8305"
] | 4 | [
"2csu"
] | 1 | [
"PUB00034392",
"PUB00034393",
"PUB00034394"
] | [
"8830684",
"10375639",
"11069669"
] | [
"Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.",
"Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia.",
"Early lateral transfer of g... | [
1996,
1999,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
229,
181,
26,
4
] | 4 | [] | [] | 0 | true | Domain | Acetate-CoA ligase [ADP-forming], alpha domain | Acetate-CoA ligase [ADP-forming], alpha domain | AcCoA-synth-alpha | 5 |
IPR014090 | 14,090 | Siderophore transporter, RhtX/FptX family | Siderophore_transpt_RhtX/FptX | Family | 237 | false | false | RhtX from Sinorhizobium meliloti 1021 and FptX from Pseudomonas aeruginosa appear to be single polypeptide transporters, from the major facilitator family for import of siderophores as a means to import iron. This function was suggested by proximity to siderophore biosynthesis genes and then confirmed by study of knock... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02718"
] | [
"sider_RhtX_FptX"
] | [
237
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR024371"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
237
] | 1 | [] | [] | 0 | true | Family | Siderophore transporter, RhtX/FptX family | Siderophore transporter, RhtX/FptX family | Siderophore_transpt_RhtX/FptX | 8 |
IPR014091 | 14,091 | Transcriptional repressor poly-beta-hydroxybutyrate-responsive | Tscrpt_rep_PHB_PhaQ | Family | 241 | false | false | Members of this family are transcriptional regulatory proteins found in the vicinity of poly-beta-hydroxybutyrate (PHB) operons in several species of Bacillus. This protein appears to have repressor activity modulated by PHB itself. This protein belongs to the larger PadR family. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02719"
] | [
"repress_PhaQ"
] | [
241
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
241
] | 1 | [] | [] | 0 | true | Family | Transcriptional repressor poly-beta-hydroxybutyrate-responsive | Transcriptional repressor poly-beta-hydroxybutyrate-responsive | Tscrpt_rep_PHB_PhaQ | 6 |
IPR014092 | 14,092 | Pyruvate oxidase | Pyruvate_oxidase | Family | 1,277 | false | false | Members of this family are examples of pyruvate oxidase ( ), such as POXB from Lactiplantibacillus plantarum [ ], an enzyme with FAD and TPP as cofactors that catalyses the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase ( ) as in Escherich... | [
"GO:0047112"
] | [
"pyruvate oxidase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02720"
] | [
"pyruv_oxi_spxB"
] | [
1277
] | 1 | [] | [] | [] | 0 | [
"1pow",
"1pox",
"1v5e",
"1v5f",
"1v5g",
"1y9d",
"2dji",
"2ez4",
"2ez8",
"2ez9",
"2ezt",
"2ezu",
"4fee",
"4feg",
"4kgd",
"6haf"
] | 16 | [
"PUB00034530"
] | [
"15175288"
] | [
"Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum."
] | [
2004
] | 1 | [
"IPR047211"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
1277
] | 1 | [] | [] | 0 | true | Family | Pyruvate oxidase | Pyruvate oxidase | Pyruvate_oxidase | 3 |
IPR014093 | 14,093 | Thiamine kinase | Thiamine_kinase | Family | 1,554 | false | false | Members of this family are the ycfN gene product of Escherichia coli, now identified as the salvage enzyme thiamine kinase (ThiK), and additional proteobacterial homologues taken to be orthologs with equivalent function. | [
"GO:0019165",
"GO:0006772",
"GO:0016310"
] | [
"thiamine kinase activity",
"thiamine metabolic process",
"phosphorylation"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01604",
"TIGR02721"
] | [
"Thiamine_kinase",
"ycfN_thiK"
] | [
1491,
957
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"2.7.1.89",
"GenProp1219",
"PWY-6896"
] | [
"EC:2.7.1.89",
"GP:GenProp1219",
"METACYC:PWY-6896"
] | 3 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
1552,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Thiamine kinase | Thiamine kinase | Thiamine_kinase | 1 |
IPR014094 | 14,094 | Penicillin-binding protein activator LpoB | LpoB | Family | 3,981 | false | false | This entry represents penicillin-binding protein activator LpoB. It has been suggested that penicillin-binding protein activator LpoB acts as a regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b) [ , ]. | [] | [] | [] | 0 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_01889",
"PF13036",
"PTHR40593",
"TIGR02722"
] | [
"LpoB",
"LpoB",
"",
"lp_"
] | [
1174,
3968,
2688,
2619
] | 4 | [] | [] | [] | 0 | [
"2mii",
"4q6l",
"4q6v",
"4q6z",
"5t10",
"5t11"
] | 6 | [
"PUB00056804",
"PUB00056805"
] | [
"21183073",
"21183074"
] | [
"Regulation of peptidoglycan synthesis by outer-membrane proteins.",
"Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases."
] | [
2010,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3898,
6,
77
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Penicillin-binding protein activator LpoB | Penicillin-binding protein activator LpoB | LpoB | 6 |
IPR014095 | 14,095 | Phenylphosphate carboxylase, alpha subunit | Phenyl_P_COase_a | Family | 19 | false | false | Members of this protein family are the predicted alpha subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. T... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02723"
] | [
"phenyl_P_alpha"
] | [
19
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034531"
] | [
"15231788"
] | [
"Phenylphosphate carboxylase: a new C-C lyase involved in anaerobic phenol metabolism in Thauera aromatica."
] | [
2004
] | 1 | [
"IPR002830"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
19
] | 1 | [] | [] | 0 | true | Family | Phenylphosphate carboxylase, alpha subunit | Phenylphosphate carboxylase, alpha subunit | Phenyl_P_COase_a | 9 |
IPR014096 | 14,096 | Phenylphosphate carboxylase, beta subunit | Phenyl_P_COase_b | Family | 35 | false | false | Members of this protein family are the beta subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. This beta su... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02724"
] | [
"phenyl_P_beta"
] | [
35
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034531"
] | [
"15231788"
] | [
"Phenylphosphate carboxylase: a new C-C lyase involved in anaerobic phenol metabolism in Thauera aromatica."
] | [
2004
] | 1 | [
"IPR002830"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"mine drainage metagenome"
] | [
2,
32,
1
] | 3 | [] | [] | 0 | true | Family | Phenylphosphate carboxylase, beta subunit | Phenylphosphate carboxylase, beta subunit | Phenyl_P_COase_b | 4 |
IPR014097 | 14,097 | Phenylphosphate carboxylase, gamma subunit | Phenyl_P_COase_g | Family | 22 | false | false | Members of this protein family are the gamma subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. The gamma s... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF09662",
"TIGR02725"
] | [
"Phenyl_P_gamma",
"phenyl_P_gamma"
] | [
22,
13
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
22
] | 1 | [] | [] | 0 | true | Family | Phenylphosphate carboxylase, gamma subunit | Phenylphosphate carboxylase, gamma subunit | Phenyl_P_COase_g | 8 |
IPR014098 | 14,098 | Phenylphosphate carboxylase, delta subunit | Phenyl_P_COase_d | Family | 13 | false | false | Members of this protein family are the delta subunit of phenylphosphate carboxylase. Phenol (methyl-benzene) is converted to phenylphosphate, then para-carboxylated by this four-subunit enzyme, with the release of phosphate, to 4-hydroxybenzoate. The enzyme contains neither biotin nor thiamin pyrophosphate. This delta ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02726"
] | [
"phenyl_P_delta"
] | [
13
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR010023"
] | [] | 1 | 0 | 1 | [
"Betaproteobacteria"
] | [
13
] | 1 | [] | [] | 0 | true | Family | Phenylphosphate carboxylase, delta subunit | Phenylphosphate carboxylase, delta subunit | Phenyl_P_COase_d | 5 |
IPR014099 | 14,099 | Spore coat protein GerQ | Spore_coat_GerQ | Family | 1,470 | false | false | Members of this protein family are the spore coat protein GerQ of endospore-forming Firmicutes (low GC Gram-positive bacteria) [ ]. This protein is cross-linked by a spore coat-associated transglutaminase. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"NCBIFAM"
] | [
"PF09671",
"PIRSF038931",
"TIGR02728"
] | [
"Spore_GerQ",
"GerQ",
"spore_gerQ"
] | [
1470,
1075,
1384
] | 3 | [] | [] | [] | 0 | [
"8zra"
] | 1 | [
"PUB00073674"
] | [
"12644503"
] | [
"Identification of a new gene essential for germination of Bacillus subtilis spores with Ca2+-dipicolinate."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
1469,
1
] | 2 | [] | [] | 0 | true | Family | Spore coat protein GerQ | Spore coat protein GerQ | Spore_coat_GerQ | 7 |
IPR014101 | 14,101 | Prolycopene isomerase | CrtISO | Family | 989 | false | false | This entry represents the Prolycopene isomerase (CrtISO) from Arabidopsis thaliana. Members of this family are predominantly found in plants and cyanobacteria. CrtISO is a carotene cis-trans-isomerase ( ) that converts 7,9,9'-tri-cis-neurosporene to 9'-cis-neurosporene and 7,9,9',7'-tetra-cis-lycopene (also known as pr... | [
"GO:0046608",
"GO:0016117"
] | [
"carotenoid isomerase activity",
"carotenoid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02730"
] | [
"carot_isom"
] | [
989
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"5.2.1.13",
"GenProp1763",
"PWY-6475"
] | [
"EC:5.2.1.13",
"GP:GenProp1763",
"METACYC:PWY-6475"
] | 3 | [] | 0 | [
"PUB00034536",
"PUB00084348"
] | [
"15557094",
"11884677"
] | [
"Analysis in vitro of the enzyme CRTISO establishes a poly-cis-carotenoid biosynthesis pathway in plants.",
"Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation, and photomorphogenesis."
] | [
2004,
2002
] | 2 | [
"IPR045892"
] | [] | 1 | 0 | 1 | [
"Cyanophyceae",
"Eukaryota"
] | [
323,
666
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
3,
11
] | 3 | true | Family | Prolycopene isomerase | Prolycopene isomerase | CrtISO | 9 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.