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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR011284 | 11,284 | 3-oxoacyl-(acyl-carrier-protein) reductase | 3oxo_ACP_reduc | Family | 21,553 | false | false | This entry represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis found in many plant and bacterial species. This enzyme is involved in type II fatty acid biosynthesis, where the individual metabolic transformations are carried out by different ... | [
"GO:0004316",
"GO:0051287",
"GO:0006633"
] | [
"3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity",
"NAD binding",
"fatty acid biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01830"
] | [
"3oxo_ACP_reduc"
] | [
21553
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.1.1.100",
"GenProp0681",
"PWY-5367",
"PWY-5971",
"PWY-5973",
"PWY-5989",
"PWY-6282",
"PWY-6519",
"PWY-7388",
"PWY-7663",
"PWY-7664",
"PWY-7858",
"PWY-8173",
"PWY-8174",
"PWY-8175",
"PWY-8203",
"PWY-8279",
"PWY-8280",
"PWY-8427",
"PWYG-321"
] | [
"EC:1.1.1.100",
"GP:GenProp0681",
"METACYC:PWY-5367",
"METACYC:PWY-5971",
"METACYC:PWY-5973",
"METACYC:PWY-5989",
"METACYC:PWY-6282",
"METACYC:PWY-6519",
"METACYC:PWY-7388",
"METACYC:PWY-7663",
"METACYC:PWY-7664",
"METACYC:PWY-7858",
"METACYC:PWY-8173",
"METACYC:PWY-8174",
"METACYC:PWY-8... | 20 | [
"1edo",
"1i01",
"1q7b",
"1q7c",
"2c07",
"2cdh",
"2hq1",
"2nm0",
"2p68",
"2ph3",
"2pnf",
"2uvd",
"3emk",
"3enn",
"3f9i",
"3ftp",
"3grp",
"3lyl",
"3op4",
"3osu",
"3rro",
"3rsh",
"3sj7",
"3tzc",
"3tzh",
"3tzk",
"3u09",
"3woh",
"4afn",
"4ag3",
"4bnt",
"4bnu"... | 76 | [
"PUB00025859",
"PUB00028039",
"PUB00028040",
"PUB00083882"
] | [
"11669613",
"11544358",
"16225460",
"26975437"
] | [
"Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.",
"Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery.",
"Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum... | [
2001,
2001,
2006,
2016
] | 4 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
48,
20108,
1145,
252
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
6,
15
] | 4 | true | Family | 3-oxoacyl-(acyl-carrier-protein) reductase | 3-oxoacyl-(acyl-carrier-protein) reductase | 3oxo_ACP_reduc | 5 |
IPR011285 | 11,285 | 3-oxoacyl-(acyl-carrier-protein) reductase, putative | FabG-rel | Family | 2,548 | false | false | This entry represents a small, very well conserved family of proteins closely related to the FabG family, , and possibly equal in function. In all completed genomes with a member of this family, a FabG in is also found. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01831"
] | [
"fabG_rel"
] | [
2548
] | 1 | [] | [] | [] | 0 | [
"4iiu",
"4iiv",
"6nrp",
"7caw",
"7cax",
"7czc"
] | 6 | [] | [] | [] | [] | 0 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2531,
6,
11
] | 3 | [] | [] | 0 | true | Family | 3-oxoacyl-(acyl-carrier-protein) reductase, putative | 3-oxoacyl-(acyl-carrier-protein) reductase, putative | FabG-rel | 3 |
IPR011286 | 11,286 | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase | 2-deoxy-D-gluc_3_DH | Family | 4,624 | false | false | This entry describes 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases. This protein from Erwinia chrysanthemi has been characterised as an enzyme of pectin degradation [ ]. | [
"GO:0008678",
"GO:0051287"
] | [
"2-deoxy-D-gluconate 3-dehydrogenase activity",
"NAD binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01832"
] | [
"kduD"
] | [
4624
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1.127",
"PWY-6507",
"PWY-7562"
] | [
"EC:1.1.1.127",
"METACYC:PWY-6507",
"METACYC:PWY-7562"
] | 3 | [
"4hp8",
"4z9y",
"4za2"
] | 3 | [
"PUB00014561"
] | [
"1766386"
] | [
"Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation."
] | [
1991
] | 1 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes",
"uncultured marine thaumarchaeote AD1000_14_F02"
] | [
4608,
6,
9,
1
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase | 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase | 2-deoxy-D-gluc_3_DH | 1 |
IPR011287 | 11,287 | Poly(R)-hydroxyalkanoic acid synthase, class II | PHA_synth_II | Family | 1,447 | false | false | This entry represents the class II subfamily of poly(R)-hydroxyalkanoate synthases, which polymerises hydroxyacyl-CoAs, typically with six to fourteen carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids [ ]. These polymers accumulate as carbon and energy storage inclusions in ... | [
"GO:0016746",
"GO:0042619"
] | [
"acyltransferase activity",
"poly-hydroxybutyrate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01839"
] | [
"PHA_synth_II"
] | [
1447
] | 1 | [
"GP"
] | [
"GenProp0055"
] | [
"GP:GenProp0055"
] | 1 | [] | 0 | [
"PUB00013497"
] | [
"11418564"
] | [
"PhaC and PhaR are required for polyhydroxyalkanoic acid synthase activity in Bacillus megaterium."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
1445,
2
] | 2 | [] | [] | 0 | true | Family | Poly(R)-hydroxyalkanoic acid synthase, class II | Poly(R)-hydroxyalkanoic acid synthase, class II | PHA_synth_II | 2 |
IPR011288 | 11,288 | D-tagatose-bisphosphate aldolase, class II, subunit KbaY/GatY | TagBP_ald_KbaY/GatY | Family | 1,656 | false | false | Escherichia coli and other enteric bacteria contain two closely related D-tagatose 1,6-bisphosphate (TagBP)-specific aldolases - KbaYZ (also known as AgaYZ) and GatYZ. Unlike other class II aldolases, which are homodimeric enzymes, KbaYZ and GatYZ are heterodimers, and are comprised of subunits KbaY/GatY and GatY/GatZ.... | [
"GO:0008270",
"GO:0009025",
"GO:0005975"
] | [
"zinc ion binding",
"tagatose-bisphosphate aldolase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01858"
] | [
"tag_bisphos_ald"
] | [
1656
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.40",
"PWY-7077",
"PWY-7395",
"PWY-8324"
] | [
"EC:4.1.2.40",
"METACYC:PWY-7077",
"METACYC:PWY-7395",
"METACYC:PWY-8324"
] | 4 | [
"1gvf"
] | 1 | [
"PUB00014683",
"PUB00014684"
] | [
"11976750",
"8955298"
] | [
"Two class II D-tagatose-bisphosphate aldolases from enteric bacteria.",
"Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism."
] | [
2002,
1996
] | 2 | [
"IPR000771"
] | [
"IPR023788"
] | 1 | 1 | 0 | [
"Bacteria",
"Trichuris trichiura",
"metagenomes"
] | [
1653,
1,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | D-tagatose-bisphosphate aldolase, class II, subunit KbaY/GatY | D-tagatose-bisphosphate aldolase, class II, subunit KbaY/GatY | TagBP_ald_KbaY/GatY | 6 |
IPR011289 | 11,289 | Fructose-1,6-bisphosphate aldolase, class 2 | Fruc_bis_ald_class-2 | Family | 6,271 | false | false | Fructose-1,6-bisphosphate (FBP) aldolases reversibly cleave FBP to two triose phosphates, glycerone phophate and D-glyceraldehyde 3-phosphate. They play a key role in both glycolysis (FBP cleavage) and gluconeogenesis (FBP synthesis). These enzymes can be divide into two classes based on their mode of catalysis. Class ... | [
"GO:0004332",
"GO:0008270",
"GO:0006096",
"GO:0030388"
] | [
"fructose-bisphosphate aldolase activity",
"zinc ion binding",
"glycolytic process",
"fructose 1,6-bisphosphate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"NCBIFAM"
] | [
"TIGR01859"
] | [
"fruc_bis_ald_"
] | [
6271
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.2.13",
"GenProp0120",
"GenProp1286",
"PWY-1042",
"PWY-1861",
"PWY-5484",
"PWY-6142",
"PWY-7385",
"PWY-8178",
"PWY-8404"
] | [
"EC:4.1.2.13",
"GP:GenProp0120",
"GP:GenProp1286",
"METACYC:PWY-1042",
"METACYC:PWY-1861",
"METACYC:PWY-5484",
"METACYC:PWY-6142",
"METACYC:PWY-7385",
"METACYC:PWY-8178",
"METACYC:PWY-8404"
] | 10 | [
"1rv8",
"1rvg",
"2fjk",
"3c4u",
"3c52",
"3c56",
"3gak",
"3gay",
"3n9r",
"3n9s",
"3q94",
"4to8",
"5uck",
"5ucn",
"5ucp",
"5ucs",
"5ucz",
"5ud0",
"5ud1",
"5ud2",
"5ud3",
"5ud4",
"5vjf",
"7nc7",
"7ncc"
] | 25 | [
"PUB00005383",
"PUB00022639"
] | [
"1412694",
"14699122"
] | [
"Fructose-bisphosphate aldolases: an evolutionary history.",
"Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase."
] | [
1992,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
4,
6195,
30,
1,
41
] | 5 | [] | [] | 0 | true | Family | Fructose-1,6-bisphosphate aldolase, class 2 | Fructose-1,6-bisphosphate aldolase, class 2 | Fruc_bis_ald_class-2 | 2 |
IPR011290 | 11,290 | Nitrogenase iron-iron protein, alpha chain | Nase_Fe-Fe_asu | Family | 152 | false | false | This entry represents the all-iron variant of the nitrogenase component I alpha chain. Molybdenum-iron and vanadium iron forms are also found. The complete complex contains two alpha chains, two beta chains and two delta chains. The component I associates with component II also known as the iron protein which serves to... | [
"GO:0016163",
"GO:0051536",
"GO:0009399"
] | [
"nitrogenase activity",
"iron-sulfur cluster binding",
"nitrogen fixation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01861"
] | [
"ANFD"
] | [
152
] | 1 | [
"EC",
"GP"
] | [
"1.18.6.1",
"GenProp0631"
] | [
"EC:1.18.6.1",
"GP:GenProp0631"
] | 2 | [
"8boq",
"8oie",
"8pbb"
] | 3 | [] | [] | [] | [] | 0 | [
"IPR005974"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanobacteriota",
"metagenomes"
] | [
143,
7,
2
] | 3 | [] | [] | 0 | true | Family | Nitrogenase iron-iron protein, alpha chain | Nitrogenase iron-iron protein, alpha chain | Nase_Fe-Fe_asu | 5 |
IPR011291 | 11,291 | Peptidase M20A, peptidase V | Pept_M20A_peptidaseV | Family | 967 | false | false | This entry represents a small clade of dipeptidase enzymes from the Lactobacillaceae, which belong to MEROPS peptidase family M20A. The Lactococcus lactis enzyme has been shown to act on a wide range of dipeptides, but not larger peptides [ ]. The enzyme from Lactobacillus delbrueckii was originally characterised as a ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01886"
] | [
"dipeptidase"
] | [
967
] | 1 | [] | [] | [] | 0 | [
"1lfw"
] | 1 | [
"PUB00013828",
"PUB00079902"
] | [
"12176387",
"9171382"
] | [
"Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides.",
"Cloning and analysis of the pepV dipeptidase gene of Lactococcus lactis MG1363."
] | [
2002,
1997
] | 2 | [
"IPR010964"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
967
] | 1 | [] | [] | 0 | true | Family | Peptidase M20A, peptidase V | Peptidase M20A, peptidase V | Pept_M20A_peptidaseV | 2 |
IPR011292 | 11,292 | Na(+)-translocating NADH-quinone reductase subunit D | NqrD | Family | 4,234 | false | false | Na(+)-translocating NADH-quinone reductase (NQR) functions as a primary Na(+) pump in the respiratory chain of Gram-negative marine and halophilic bacteria [ ]. The NQR complex reduces ubiquinone-1 to ubiquinol by two successive reactions, which involve the co-factor FAD. The NQR complex is composed of six subunits, th... | [
"GO:0016655"
] | [
"oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00428",
"TIGR01939"
] | [
"NqrD",
"nqrD"
] | [
4029,
4229
] | 2 | [
"EC",
"GP"
] | [
"7.2.1.1",
"GenProp0129"
] | [
"EC:7.2.1.1",
"GP:GenProp0129"
] | 2 | [
"7xk3",
"7xk4",
"7xk5",
"7xk6",
"7xk7",
"8a1t",
"8a1u",
"8a1v",
"8a1w",
"8a1x",
"8a1y",
"8acw",
"8acy",
"8ad0",
"8evu",
"8ew3",
"9lrr",
"9u5g",
"9ud2",
"9ud3",
"9ud4",
"9ud5",
"9ud6",
"9ud8",
"9ud9",
"9uda",
"9udf",
"9udg",
"9uuu"
] | 29 | [
"PUB00013512"
] | [
"11248187"
] | [
"Recent progress in the Na(+)-translocating NADH-quinone reductase from the marine Vibrio alginolyticus."
] | [
2001
] | 1 | [
"IPR003667"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4149,
10,
75
] | 3 | [] | [] | 0 | true | Family | Na(+)-translocating NADH-quinone reductase subunit D | Na(+)-translocating NADH-quinone reductase subunit D | NqrD | 7 |
IPR011293 | 11,293 | Ion-translocating oxidoreductase complex, subunit RnfA/RsxA | Ion_transpt_RnfA/RsxA | Family | 5,931 | false | false | The six subunit complex RnfABCDGE in Rhodobacter capsulatus (Rhodopseudomonas capsulata) encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation [ , , ]. A closely related complex in Escherichia coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-cont... | [
"GO:0022900"
] | [
"electron transport chain"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00459",
"TIGR01943"
] | [
"RsxA_RnfA",
"rnfA"
] | [
5742,
5817
] | 2 | [
"GP"
] | [
"GenProp0130"
] | [
"GP:GenProp0130"
] | 1 | [
"7zc6",
"8ahx",
"8rb8",
"8rb9",
"8rbm",
"8rbq",
"9eri",
"9erj",
"9erk",
"9erl"
] | 10 | [
"PUB00007528",
"PUB00013513",
"PUB00020279",
"PUB00062387"
] | [
"9154934",
"12773378",
"8264535",
"10671439"
] | [
"Membrane localization, topology, and mutual stabilization of the rnfABC gene products in Rhodobacter capsulatus and implications for a new family of energy-coupling NADH oxidoreductases.",
"A reducing system of the superoxide sensor SoxR in Escherichia coli.",
"Identification of a new class of nitrogen fixatio... | [
1997,
2003,
1993,
2000
] | 4 | [
"IPR003667"
] | [
"IPR049674"
] | 1 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
5779,
3,
38,
111
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ion-translocating oxidoreductase complex, subunit RnfA/RsxA | Ion-translocating oxidoreductase complex, subunit RnfA/RsxA | Ion_transpt_RnfA/RsxA | 3 |
IPR011294 | 11,294 | 3-hydroxybutyrate dehydrogenase | 3-OHbutyrate_DH | Family | 9,958 | false | false | This entry represents a subfamily of the short chain dehydrogenases. Characterised members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polymers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accu... | [
"GO:0003858"
] | [
"3-hydroxybutyrate dehydrogenase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR01963"
] | [
"PHB_DH"
] | [
9958
] | 1 | [
"GP"
] | [
"GenProp0055"
] | [
"GP:GenProp0055"
] | 1 | [
"1wmb",
"1x1t",
"2q2q",
"2q2v",
"2q2w",
"2yz7",
"2ztl",
"2ztm",
"2ztu",
"2ztv",
"3v2h",
"3vdq",
"3vdr",
"3w8d",
"3w8e",
"3w8f",
"4trr",
"5b4t",
"5b4u",
"5b4v",
"5yss",
"6zzo",
"6zzp",
"6zzq",
"6zzs",
"8dt1",
"9c5h",
"9c5i",
"9c5j",
"9c5k",
"9c5l",
"9c5m"... | 34 | [] | [] | [] | [] | 0 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9807,
108,
43
] | 3 | [] | [] | 0 | true | Family | 3-hydroxybutyrate dehydrogenase | 3-hydroxybutyrate dehydrogenase | 3-OHbutyrate_DH | 7 |
IPR011295 | 11,295 | 2-polyprenyl-6-methoxyphenol 4-hydroxylase | UbiH | Family | 4,236 | false | false | This entry represents the FAD-dependent monooxygenase responsible for the second hydroxylation step in the aerobic ubiquinone biosynthetic pathway [ , , ]. The sequences in this entry are restricted to the proteobacteria. This family is closely related to the UbiF hydroxylase which catalyses the final hydroxylation ste... | [
"GO:0008681",
"GO:0006744"
] | [
"2-octaprenyl-6-methoxyphenol hydroxylase activity",
"ubiquinone biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01984"
] | [
"UbiH"
] | [
4236
] | 1 | [
"GP"
] | [
"GenProp1744"
] | [
"GP:GenProp1744"
] | 1 | [] | 0 | [
"PUB00013761",
"PUB00013848",
"PUB00061715"
] | [
"1339425",
"11583838",
"4572721"
] | [
"Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone.",
"Ubiquinone biosynthesis in microorganisms.",
"Pathway for ubiquinone biosynthesis in Escherichia coli K-12: gene-enzyme relationships and interme... | [
1992,
2001,
1973
] | 3 | [
"IPR010971"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Protostomia",
"metagenomes"
] | [
4200,
9,
27
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 2-polyprenyl-6-methoxyphenol 4-hydroxylase | 2-polyprenyl-6-methoxyphenol 4-hydroxylase | UbiH | 6 |
IPR011296 | 11,296 | Phosphotransferase system, trehalose-specific IIBC component | PTS_IIBC_treh | Domain | 4,020 | false | false | This entry represents the fused enzyme II B and C components of the trehalose-specific PTS sugar transporter system [ ]. Trehalose is converted to trehalose-6-phosphate in the process of translocation into the cell. These transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr) [ ... | [
"GO:0015574",
"GO:0015771",
"GO:0016020"
] | [
"trehalose transmembrane transporter activity",
"trehalose transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01992"
] | [
"PTS-IIBC-Tre"
] | [
4020
] | 1 | [
"GP",
"GP"
] | [
"GenProp0119",
"GenProp0271"
] | [
"GP:GenProp0119",
"GP:GenProp0271"
] | 2 | [] | 0 | [
"PUB00013774",
"PUB00013786",
"PUB00013790",
"PUB00013792",
"PUB00013795",
"PUB00013799"
] | [
"3023298",
"12003938",
"11260467",
"11553642",
"12454482",
"12949193"
] | [
"Transport of trehalose in Salmonella typhimurium.",
"Redundancy in periplasmic binding protein-dependent transport systems for trehalose, sucrose, and maltose in Sinorhizobium meliloti.",
"Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters.",
... | [
1986,
2002,
2001,
2001,
2002,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bioreactor metagenome"
] | [
4017,
2,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Phosphotransferase system, trehalose-specific IIBC component | Phosphotransferase system, trehalose-specific IIBC component | PTS_IIBC_treh | 3 |
IPR011297 | 11,297 | Phosphotransferase system, beta-glucoside-specific IIABC component | PTS_IIABC_b_glu | Family | 5,546 | false | false | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars... | [
"GO:0008982",
"GO:0009401",
"GO:0005886"
] | [
"protein-N(PI)-phosphohistidine-sugar phosphotransferase activity",
"phosphoenolpyruvate-dependent sugar phosphotransferase system",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01995"
] | [
"PTS-II-ABC-beta"
] | [
5546
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.-",
"GenProp0119",
"PWY-5129",
"PWY-6322",
"PWY-6369",
"PWY-6626",
"PWY-6682",
"PWY-6955",
"PWY-7077",
"PWY-7321",
"PWY-7740",
"PWY-7769",
"PWY-7886",
"PWY-7948",
"PWY-7975",
"PWY-8129",
"PWY-8324",
"PWY-8367",
"PWY-8392",
"PWY-8393",
"PWY-8394",
"PWY-8402"
] | [
"EC:2.7.1.-",
"GP:GenProp0119",
"METACYC:PWY-5129",
"METACYC:PWY-6322",
"METACYC:PWY-6369",
"METACYC:PWY-6626",
"METACYC:PWY-6682",
"METACYC:PWY-6955",
"METACYC:PWY-7077",
"METACYC:PWY-7321",
"METACYC:PWY-7740",
"METACYC:PWY-7769",
"METACYC:PWY-7886",
"METACYC:PWY-7948",
"METACYC:PWY-797... | 22 | [] | 0 | [
"PUB00000073",
"PUB00002162",
"PUB00003612",
"PUB00013840",
"PUB00017027",
"PUB00017028"
] | [
"2197982",
"1537788",
"8246840",
"7883710",
"7815935",
"11361063"
] | [
"The bacterial phosphoenolpyruvate: glycose phosphotransferase system.",
"Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.",
"Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.",
"New beta-glucoside ... | [
1990,
1992,
1993,
1995,
1994,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5537,
4,
5
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphotransferase system, beta-glucoside-specific IIABC component | Phosphotransferase system, beta-glucoside-specific IIABC component | PTS_IIABC_b_glu | 8 |
IPR011298 | 11,298 | FeS A-type assembly protein SufA, proteobacteria | SufA_proteobacteria | Family | 1,811 | false | false | This entry represents the SufA protein of the SUF system of iron-sulphur cluster biosynthesis from proteobacteria. This system performs FeS biosynthesis even during oxidative stress and tends to be absent in obligate anaerobic and microaerophilic bacteria. A-type assembly protein (ATAP) is a conserved and essential mem... | [
"GO:0051536",
"GO:0016226"
] | [
"iron-sulfur cluster binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR01997"
] | [
"sufA_proteo"
] | [
1811
] | 1 | [
"GP"
] | [
"GenProp0137"
] | [
"GP:GenProp0137"
] | 1 | [
"2d2a"
] | 1 | [
"PUB00003442",
"PUB00028014",
"PUB00030961",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640",
"PUB00058194",
"PUB00160405",
"PUB00160406"
] | [
"8875867",
"11498000",
"15050828",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785",
"17698959",
"32108236",
"33007329"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Incorporation of iron-sulphur clusters in membrane-bound proteins.",
"Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli.",
"How Escherichia coli and Saccharomyces cerevis... | [
1996,
2001,
2004,
2005,
2005,
2006,
2005,
2007,
2004,
2007,
2020,
2021
] | 12 | [
"IPR016092"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Effrenium voratum",
"metagenomes"
] | [
1807,
1,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | FeS A-type assembly protein SufA, proteobacteria | FeS A-type assembly protein SufA, proteobacteria | SufA_proteobacteria | 8 |
IPR011299 | 11,299 | PTS system glucose-specific IIBC component | PTS_IIBC_glc | Domain | 3,357 | false | false | This entry represents the combined B and C domains of the PTS transport system enzyme II specific for glucose transport [ ]. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name 'PTS system, glucose-specific IIABC component' while the Bacillus subti... | [
"GO:0055056",
"GO:1904659",
"GO:0016020"
] | [
"D-glucose transmembrane transporter activity",
"D-glucose transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02002"
] | [
"PTS-II-BC-glcB"
] | [
3357
] | 1 | [
"EC",
"GP"
] | [
"2.7.1.199",
"GenProp0119"
] | [
"EC:2.7.1.199",
"GP:GenProp0119"
] | 2 | [
"8qsr",
"8qst",
"9hnp"
] | 3 | [
"PUB00013751",
"PUB00013794"
] | [
"3023349",
"2120236"
] | [
"Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc.",
"The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease."
] | [
1986,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"invertebrate metagenome"
] | [
3351,
4,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | PTS system glucose-specific IIBC component | PTS system glucose-specific IIBC component | PTS_IIBC_glc | 6 |
IPR011300 | 11,300 | Phosphotransferase system, IIBC component | PTS_IIBC | Domain | 1,382 | false | false | This entry represents a group of fused B and C components of PTS enzyme II. This clade is a member of a larger family which contains enzyme II's specific for a variety of sugars including glucose ( ) and N-acetylglucosamine ( ). None of the members of this clade have been experimentally characterised. This clade includ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02003"
] | [
"PTS-II-BC-unk1"
] | [
1382
] | 1 | [
"GP"
] | [
"GenProp0119"
] | [
"GP:GenProp0119"
] | 1 | [
"5iws",
"6bvg"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
1381,
1
] | 2 | [] | [] | 0 | true | Domain | Phosphotransferase system, IIBC component | Phosphotransferase system, IIBC component | PTS_IIBC | 6 |
IPR011301 | 11,301 | PTS system, maltose/glucose-specific IIBC component | PTS_Mal/Glc-sp_IIBC_component | Family | 1,253 | false | false | This entry represents a family of PTS enzyme II fused B and C components including and most closely related to the MalX maltose and glucose-specific transporter of Escherichia coli [ ]. | [
"GO:0008982",
"GO:0009401"
] | [
"protein-N(PI)-phosphohistidine-sugar phosphotransferase activity",
"phosphoenolpyruvate-dependent sugar phosphotransferase system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02004"
] | [
"PTS-IIBC-malX"
] | [
1253
] | 1 | [
"GP"
] | [
"GenProp0119"
] | [
"GP:GenProp0119"
] | 1 | [] | 0 | [
"PUB00013824"
] | [
"1856179"
] | [
"The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5"
] | [
1252,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | PTS system, maltose/glucose-specific IIBC component | PTS system, maltose/glucose-specific IIBC component | PTS_Mal/Glc-sp_IIBC_component | 4 |
IPR011302 | 11,302 | FeS A-type assembly protein IscA, proteobacteria | IscA_proteobact | Family | 4,271 | false | false | This entry represents the IscA component of the ISC system for iron-sulphur cluster assembly. IscA is believed to act as a scaffold upon which 2Fe-2S clusters are assembled and subsequently transferred to ferredoxin [ , , ]. This clade is limited to the proteobacteria. A-type assembly protein (ATAP) is a conserved and ... | [
"GO:0051536",
"GO:0016226"
] | [
"iron-sulfur cluster binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01429",
"TIGR02011"
] | [
"Fe_S_insert_IscA",
"IscA"
] | [
915,
4271
] | 2 | [
"GP"
] | [
"GenProp0138"
] | [
"GP:GenProp0138"
] | 1 | [
"1r94",
"1r95",
"1s98"
] | 3 | [
"PUB00003442",
"PUB00013777",
"PUB00013850",
"PUB00028014",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640",
"PUB00035641",
"PUB00058194",
"PUB00160405",
"PUB00160406"
] | [
"8875867",
"11319236",
"11432781",
"11498000",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785",
"16730357",
"17698959",
"32108236",
"33007329"
] | [
"A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution.",
"Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin.",
"Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of ... | [
1996,
2001,
2001,
2001,
2005,
2005,
2006,
2005,
2007,
2004,
2006,
2007,
2020,
2021
] | 14 | [
"IPR016092"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
4208,
6,
55,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | FeS A-type assembly protein IscA, proteobacteria | FeS A-type assembly protein IscA, proteobacteria | IscA_proteobact | 2 |
IPR011303 | 11,303 | Ion-translocating oxidoreductase complex subunit RnfD, bacterial | RnfD_bac | Family | 7,336 | false | false | This entry describes the D subunit. The six-subunit complex RnfABCDGE in Rhodobacter capsulatus (Rhodopseudomonas capsulata) encodes a NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation [ ]. A closely related complex in Escherichia coli, RsxABCDGE (Reducer of SoxR), r... | [
"GO:0022900",
"GO:0016020"
] | [
"electron transport chain",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00462",
"TIGR01946"
] | [
"RsxD_RnfD",
"rnfD"
] | [
6905,
7246
] | 2 | [
"GP"
] | [
"GenProp0130"
] | [
"GP:GenProp0130"
] | 1 | [
"7zc6",
"8ahx",
"8rb8",
"8rb9",
"8rbm",
"8rbq",
"9eri",
"9erj",
"9erk",
"9erl"
] | 10 | [
"PUB00008135",
"PUB00013513",
"PUB00087510",
"PUB00088392",
"PUB00088393"
] | [
"9492268",
"12773378",
"27114876",
"23269825",
"24045950"
] | [
"Overexpression in Escherichia coli of the rnf genes from Rhodobacter capsulatus--characterization of two membrane-bound iron-sulfur proteins.",
"A reducing system of the superoxide sensor SoxR in Escherichia coli.",
"The role of Rnf in ion gradient formation in Desulfovibrio alaskensis.",
"The Rnf complex of... | [
1998,
2003,
2016,
2012,
2013
] | 5 | [
"IPR004338"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified sequences"
] | [
7198,
4,
5,
129
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ion-translocating oxidoreductase complex subunit RnfD, bacterial | Ion-translocating oxidoreductase complex subunit RnfD, bacterial | RnfD_bac | 8 |
IPR011305 | 11,305 | Energy-converting hydrogenase subunit EhaL family member MJ0518 | MJ0518 | Family | 17 | false | false | This entry represents Energy-converting hydrogenase subunit EhaL family member MJ0518 and related small membrane proteins that are predicted to be the EhaL transmembrane subunits of multisubunit membrane-bound [NiFe]-hydrogenase Eha complexes. Based on sequence similarity and genome context analysis, other organisms su... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF004953"
] | [
"EhaL"
] | [
17
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012
] | 5 | [
"IPR019211"
] | [] | 1 | 0 | 1 | [
"Methanomada group"
] | [
17
] | 1 | [] | [] | 0 | true | Family | Energy-converting hydrogenase subunit EhaL family member MJ0518 | Energy-converting hydrogenase subunit EhaL family member MJ0518 | MJ0518 | 1 |
IPR011307 | 11,307 | Tetrahydromethanopterin S-methyltransferase, subunit F | MeTrfase_F | Family | 100 | false | false | This group represents a tetrahydromethanopterin S-methyltransferase, subunit F which forms part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step [ ]. The complex is c... | [
"GO:0030269",
"GO:0015948",
"GO:0016020"
] | [
"tetrahydromethanopterin S-methyltransferase activity",
"methanogenesis",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PIRSF"
] | [
"MF_01099",
"PIRSF006523"
] | [
"MtrF",
"MtrF"
] | [
100,
65
] | 2 | [
"EC"
] | [
"7.2.1.4"
] | [
"EC:7.2.1.4"
] | 1 | [
"8q3v",
"8q54"
] | 2 | [
"PUB00005738"
] | [
"7737157"
] | [
"The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"ecological metagenomes"
] | [
97,
3
] | 2 | [] | [] | 0 | true | Family | Tetrahydromethanopterin S-methyltransferase, subunit F | Tetrahydromethanopterin S-methyltransferase, subunit F | MeTrfase_F | 3 |
IPR011308 | 11,308 | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaD | Prd_NiFe_hyd_3_EhaD | Family | 31 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF006581"
] | [
"EhaD"
] | [
31
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012
] | 5 | [
"IPR019213"
] | [] | 1 | 0 | 1 | [
"Methanomada group"
] | [
31
] | 1 | [] | [] | 0 | true | Family | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaD | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaD | Prd_NiFe_hyd_3_EhaD | 6 |
IPR011310 | 11,310 | Lipopolysaccharide core heptose(II)-phosphate phosphatase | LipoPS_heptP_Pase | Family | 802 | false | false | This entry represents lipopolysaccharide core heptose(II)-phosphate phosphatase, which catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. These proteins are related to cofactor-dependent phosphoglucomutases so distantly that the characteristic domain ( ) is not detected. Nonet... | [
"GO:0016791"
] | [
"phosphatase activity"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PIRSF"
] | [
"MF_01868",
"PIRSF011416"
] | [
"Ais",
"Ais-TraG-AfrS"
] | [
562,
799
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"3.1.3.-",
"PWY-4702",
"PWY-5491",
"PWY-6148",
"PWY-6352",
"PWY-6365",
"PWY-6366",
"PWY-6368",
"PWY-6456",
"PWY-6575",
"PWY-6627",
"PWY-6664",
"PWY-6686",
"PWY-6720",
"PWY-6724",
"PWY-6955",
"PWY-6990",
"PWY-6991",
"PWY-7018",
"PWY-7119",
"PWY-7321",
"PWY-7531",
"PWY-7771... | [
"EC:3.1.3.-",
"METACYC:PWY-4702",
"METACYC:PWY-5491",
"METACYC:PWY-6148",
"METACYC:PWY-6352",
"METACYC:PWY-6365",
"METACYC:PWY-6366",
"METACYC:PWY-6368",
"METACYC:PWY-6456",
"METACYC:PWY-6575",
"METACYC:PWY-6627",
"METACYC:PWY-6664",
"METACYC:PWY-6686",
"METACYC:PWY-6720",
"METACYC:PWY-6... | 36 | [] | 0 | [
"PUB00014617"
] | [
"12586342"
] | [
"Unexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase."
] | [
2003
] | 1 | [
"IPR013078"
] | [] | 1 | 0 | 1 | [
"Gammaproteobacteria",
"Plasmid R64"
] | [
801,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipopolysaccharide core heptose(II)-phosphate phosphatase | Lipopolysaccharide core heptose(II)-phosphate phosphatase | LipoPS_heptP_Pase | 7 |
IPR011311 | 11,311 | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaG | Prd_NiFe_hyd_3_EhaG | Family | 25 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF019136"
] | [
"EhaG"
] | [
25
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012
] | 5 | [
"IPR019212"
] | [] | 1 | 0 | 1 | [
"Methanomada group"
] | [
25
] | 1 | [] | [] | 0 | true | Family | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaG | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaG | Prd_NiFe_hyd_3_EhaG | 1 |
IPR011312 | 11,312 | Methanogenesis marker 7 protein | Menthan_mark_7 | Family | 256 | false | false | Members of this protein family, to date, are found in a completed prokaryotic genome if, and only if, the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [ ]. | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF019164",
"TIGR03274"
] | [
"UCP019164",
"methan_mark_7"
] | [
256,
236
] | 2 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [
"8s7v",
"8s7x",
"9h1l"
] | 3 | [
"PUB00060475"
] | [
"22070167"
] | [
"ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process."
] | [
2011
] | 1 | [
"IPR026327"
] | [] | 1 | 0 | 1 | [
"Archaea",
"ecological metagenomes"
] | [
250,
6
] | 2 | [] | [] | 0 | true | Family | Methanogenesis marker 7 protein | Methanogenesis marker 7 protein | Menthan_mark_7 | 9 |
IPR011314 | 11,314 | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaB | Prd_NiFe_hyd_3_EhaB | Family | 127 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF26645",
"PIRSF019706"
] | [
"EhaB",
"EhaB"
] | [
127,
114
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941",
"PUB00161043"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868",
"19495416"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012,
2009
] | 6 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"ecological metagenomes"
] | [
124,
3
] | 2 | [] | [] | 0 | true | Family | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaB | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaB | Prd_NiFe_hyd_3_EhaB | 9 |
IPR011315 | 11,315 | NTP pyrophosphohydrolase MazG-related, Rhizobiaceae-type | MazG-related_Rhizo-type | Family | 75 | false | false | Members of this group are distantly related to MazG-type NTP pyrophosphohydrolase. Conserved residues of the MazG domain (at least three of the Glu residues, Asp, Lys and Arg), including those shown to be functionally important [ ], are also conserved here. MazG protein of Thermotoga maritima has been shown to have bot... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036522"
] | [
"UCP036522_pph"
] | [
75
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013554",
"PUB00014610"
] | [
"12657645",
"12218018"
] | [
"Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities.",
"MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli."
] | [
2003,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Hyphomicrobiales"
] | [
75
] | 1 | [] | [] | 0 | true | Family | NTP pyrophosphohydrolase MazG-related, Rhizobiaceae-type | NTP pyrophosphohydrolase MazG-related, Rhizobiaceae-type | MazG-related_Rhizo-type | 2 |
IPR011318 | 11,318 | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaI | Prd_NiFe_hyd_3_EhaI | Family | 43 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF27656",
"PIRSF036537"
] | [
"Prd_NiFe_hyd_3_EhaI",
"EhaI"
] | [
43,
5
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Methanobacteriaceae",
"bioreactor metagenome"
] | [
42,
1
] | 2 | [] | [] | 0 | true | Family | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaI | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaI | Prd_NiFe_hyd_3_EhaI | 8 |
IPR011319 | 11,319 | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaK | Prd_NiFe_hyd_3_EhaK | Family | 67 | false | false | [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions [NiFe] hydrogenases consist of two subunits, hydrogenase large and hydrogenase small. The large subunit contains the binuclear [NiFe] active sit... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF27339",
"PIRSF036538"
] | [
"Prd_NiFe_hyd_3_EhaK",
"EhaK"
] | [
67,
11
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014600",
"PUB00035516",
"PUB00035517",
"PUB00035518",
"PUB00096941"
] | [
"10491142",
"15168611",
"16645307",
"15119826",
"22872868"
] | [
"Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins.",
"Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I.",
"Energy-converting [NiFe] hydrogenases... | [
1999,
2004,
2005,
2004,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Methanomada group",
"bioreactor metagenome"
] | [
66,
1
] | 2 | [] | [] | 0 | true | Family | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaK | Predicted [NiFe]-hydrogenase-3-type complex Eha, membrane protein EhaK | Prd_NiFe_hyd_3_EhaK | 4 |
IPR011320 | 11,320 | Ribonuclease H1, N-terminal | RNase_H1_N | Domain | 14,346 | false | false | This entry represents the N-terminal domain of RNase HI, which has a 3-layer α/β/α structure [ ]. This domain is lacking in retroviral and prokaryotic enzymes, but shows a striking structural similarity to the ribosomal protein L9 N-terminal domain, and may function as a regulatory RNA-binding module. However, the topo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01693"
] | [
"Cauli_VI"
] | [
14346
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2995383",
"R-HSA-9013404",
"R-HSA-9013408",
"R-HSA-9913635",
"R-RNO-2995383",
"R-RNO-9013404",
"R-RNO-9013408"
] | [
"REACTOME:R-HSA-2995383",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013408",
"REACTOME:R-HSA-9913635",
"REACTOME:R-RNO-2995383",
"REACTOME:R-RNO-9013404",
"REACTOME:R-RNO-9013408"
] | 7 | [
"1qhk",
"3bsu",
"6vrd",
"8swc"
] | 4 | [
"PUB00011751"
] | [
"10448044"
] | [
"NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"metagenomes"
] | [
3553,
10479,
21,
211,
82
] | 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)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
... | [
3,
5,
3,
6,
3,
1,
2,
8,
1,
1,
14
] | 11 | true | Domain | Ribonuclease H1, N-terminal | Ribonuclease H1, N-terminal | RNase_H1_N | 3 |
IPR011322 | 11,322 | Nitrogen regulatory PII-like, alpha/beta | N-reg_PII-like_a/b | Homologous_superfamily | 73,938 | false | false | This superfamily represents a structural domain found in the nitrogen regulatory protein PII, in ATP phosphribosyltransferases (C-terminal domain), in the divalent ion tolerance protein CutA1, and in some bacterial hypothetical proteins. This domain consists of a ferredoxin-like α/β sandwich, which forms trimeric struc... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF54913"
] | [
""
] | [
73938
] | 1 | [
"EC"
] | [
"2.4.2.17"
] | [
"EC:2.4.2.17"
] | 1 | [
"1gnk",
"1h3d",
"1hwu",
"1j2v",
"1kr4",
"1naq",
"1nh7",
"1nh8",
"1nza",
"1o51",
"1o5j",
"1osc",
"1p1l",
"1pil",
"1q1k",
"1qy7",
"1ufl",
"1uku",
"1ul3",
"1umj",
"1v3r",
"1v3s",
"1v6h",
"1v9o",
"1vfj",
"1vhf",
"1xk8",
"2cz4",
"2dcl",
"2e66",
"2eg1",
"2eg2"... | 173 | [
"PUB00003738",
"PUB00007506",
"PUB00014093",
"PUB00022501",
"PUB00035665",
"PUB00035666"
] | [
"1702507",
"7623666",
"12949080",
"14741209",
"16860774",
"17077491"
] | [
"Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense.",
"Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12.",
"The evolutionarily conserved trimeric structure of CutA1 proteins sugges... | [
1990,
1995,
2003,
2004,
2006,
2006
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2966,
62777,
3,
6603,
1589
] | 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",... | [
18,
1,
6,
2,
4,
4,
5,
1,
9,
10,
1,
1,
11
] | 13 | true | Homologous_superfamily | Nitrogen regulatory PII-like, alpha/beta | Nitrogen regulatory PII-like, alpha/beta | N-reg_PII-like_a/b | 8 |
IPR011323 | 11,323 | Mss4/translationally controlled tumour-associated TCTP | Mss4/transl-control_tumour | Homologous_superfamily | 8,189 | false | false | This superfamily represents a structural domain with a complex fold consisting of several coiled β-sheets. This domain exists as a duplication, consisting of a tandem repeat of two similar structural motifs. This entry represents copies of this structural motif in the following protein families: Mss4, which contains a ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:2.170.150.10"
] | [
""
] | [
8189
] | 1 | [] | [] | [] | 0 | [
"1fwq",
"1h6q",
"1h7y",
"1hxr",
"1txj",
"1yz1",
"2fu5",
"2hr9",
"2kwb",
"2loy",
"3ebm",
"3p3k",
"5o9k",
"5o9l",
"5o9m",
"6izb",
"6ize",
"6j2y"
] | 18 | [
"PUB00007168",
"PUB00014250"
] | [
"11473261",
"11258916"
] | [
"Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.",
"A helical turn motif in Mss4 is a critical determinant of Rab binding and nucleotide release."
] | [
2001,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
24,
8165
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
4,
3,
5,
16,
5,
1,
3,
11,
2,
2,
17
] | 12 | true | Homologous_superfamily | Mss4/translationally controlled tumour-associated TCTP | Mss4/translationally controlled tumour-associated TCTP | Mss4/transl-control_tumour | 9 |
IPR011324 | 11,324 | Cytotoxic necrotizing factor-like, catalytic | Cytotoxic_necrot_fac-like_cat | Homologous_superfamily | 30,732 | false | false | This entry represents the catalytic domain from several bacterial cytotoxic necrotizing factor proteins and the related dermonecrotic toxin (DNT) from Bordetella species. Cytotoxic necrotizing factor 1 (CNF1) is a toxin which in Escherichia coli forms a 4-layer α/β/β/α structure containing mixed β-sheets [ ]. CNF1 is e... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF64438"
] | [
""
] | [
30732
] | 1 | [
"EC"
] | [
"3.5.1.44"
] | [
"EC:3.5.1.44"
] | 1 | [
"1hq0",
"1hzg",
"1rv9",
"1rw0",
"1t8h",
"1u05",
"1xaf",
"1xfj",
"1z9t",
"2f9z",
"6dzd",
"6t0y",
"6t1b",
"6yhk",
"6yhm",
"6yhn",
"7f3v",
"7fbg",
"7w1g"
] | 19 | [
"PUB00011275",
"PUB00011276",
"PUB00019322",
"PUB00035667"
] | [
"12622819",
"12065482",
"11427886",
"16498617"
] | [
"Expression of cnf1 by Escherichia coli J96 involves a large upstream DNA region including the hlyCABD operon, and is regulated by the RfaH protein.",
"Identification of a receptor-binding domain of Bordetella dermonecrotic toxin.",
"Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizi... | [
2003,
2002,
2001,
2006
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
500,
28629,
2,
1006,
595
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3,
2,
3
] | 5 | true | Homologous_superfamily | Cytotoxic necrotizing factor-like, catalytic | Cytotoxic necrotizing factor-like, catalytic | Cytotoxic_necrot_fac-like_cat | 1 |
IPR011327 | 11,327 | Killer toxin, SMK, beta subunit | Killer_tox_SMK_b | Domain | 4 | false | false | This entry represents the beta subunit of SMK killer toxins that are secreted by several strains of yeasts. SMK toxin is encoded by a single open reading frame of chromosomal DNA (the SMK1 gene) and is translated in the form of a 222 amino acid preprotoxin. This preprotoxin is converted to the alpha and beta heterodime... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF21414",
"cd12839"
] | [
"SMK_beta_su",
"Killer_toxin_beta"
] | [
4,
4
] | 2 | [] | [] | [] | 0 | [
"1kvd",
"1kve"
] | 2 | [
"PUB00035671",
"PUB00035672"
] | [
"9016714",
"11748724"
] | [
"The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin.",
"Interaction of SMKT, a killer toxin produced by Pichia farinosa, with the yeast cell membranes."
] | [
1997,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Debaryomycetaceae"
] | [
4
] | 1 | [] | [] | 0 | true | Domain | Killer toxin, SMK, beta subunit | Killer toxin, SMK, beta subunit | Killer_tox_SMK_b | 6 |
IPR011328 | 11,328 | Salt-mediated killer toxin, alpha subunit | SMK_a | Homologous_superfamily | 3 | false | false | The killer toxin SMK (salt-mediated killer) from the halotolerant yeast Pichia farinosa acts to kill sensitive strains of yeast. SMK exhibits maximum activity under conditions of acidic pH and high salt concentration. It is composed of two distinct subunits, alpha and beta, which tightly interact with each other under ... | [] | [] | [] | 0 | [
"CATHGENE3D"
] | [
"G3DSA:4.10.420.10"
] | [
""
] | [
3
] | 1 | [] | [] | [] | 0 | [
"1kvd",
"1kve"
] | 2 | [
"PUB00035671",
"PUB00035672"
] | [
"9016714",
"11748724"
] | [
"The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin.",
"Interaction of SMKT, a killer toxin produced by Pichia farinosa, with the yeast cell membranes."
] | [
1997,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Millerozyma farinosa"
] | [
3
] | 1 | [] | [] | 0 | true | Homologous_superfamily | Salt-mediated killer toxin, alpha subunit | Salt-mediated killer toxin, alpha subunit | SMK_a | 2 |
IPR011329 | 11,329 | Killer toxin Kp4/SMK | Killer_tox_Kp4/SMK | Homologous_superfamily | 966 | false | false | This superfamily represents a structural fold found in the killer toxins Kp4 and SMK, consisting of two left-handed split β/αβ motifs, which is rarely found in other toxins; hence, these toxins may be evolutionarily or functionally related [ ]. Killer toxins are polypeptides secreted by some fungal species that kill se... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"SSF"
] | [
"SSF55221"
] | [
""
] | [
966
] | 1 | [] | [] | [] | 0 | [
"1kpt",
"1kvd",
"1kve"
] | 3 | [
"PUB00028852",
"PUB00035671",
"PUB00035672",
"PUB00035673"
] | [
"7582897",
"9016714",
"11748724",
"8145639"
] | [
"Structure and function of a virally encoded fungal toxin from Ustilago maydis: a fungal and mammalian Ca2+ channel inhibitor.",
"The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin.",
"Interaction of SMKT, a killer to... | [
1995,
1997,
2001,
1994
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Laribacter hongkongensis",
"Ustilago maydis P4 virus"
] | [
963,
2,
1
] | 3 | [] | [] | 0 | true | Homologous_superfamily | Killer toxin Kp4/SMK | Killer toxin Kp4/SMK | Killer_tox_Kp4/SMK | 8 |
IPR011330 | 11,330 | Glycoside hydrolase/deacetylase, beta/alpha-barrel | Glyco_hydro/deAcase_b/a-brl | Homologous_superfamily | 201,770 | false | false | This superfamily represents a structural domain found in glycoside hydrolase family 38 ( , e.g. alpha-mannosidase) [ ] and 57 ( , e.g. 4-alpha-glucanotransferase, N-terminal) [ ], as well as in NodB-like polysaccharide deacetylase and in some hypothetical proteins (e.g. TT1467, N-terminal domain). This domain consists ... | [
"GO:0005975"
] | [
"carbohydrate metabolic process"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF88713"
] | [
""
] | [
201770
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"REACTOME... | 21 | [
"1hty",
"1hww",
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"2alw",
"2b5d",
"2c1g",
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"2c71",
"2c79"... | 211 | [
"PUB00014074",
"PUB00030417"
] | [
"12618437",
"12960159"
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"Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor.",
"Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates."
] | [
2003,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3085,
156352,
39957,
71,
2305
] | 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",
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31,
21,
25,
44,
7,
27,
25,
8,
13,
31,
3,
2,
56
] | 13 | true | Homologous_superfamily | Glycoside hydrolase/deacetylase, beta/alpha-barrel | Glycoside hydrolase/deacetylase, beta/alpha-barrel | Glyco_hydro/deAcase_b/a-brl | 7 |
IPR011331 | 11,331 | Large ribosomal subunit protein eL37/eL43 | Ribosomal_eL37/eL43 | Homologous_superfamily | 13,424 | false | false | This superfamily represents the core domain of the large ribosomal subunit protein eL37/eL43 from archaea and eukaryotes, which where previously known as ribosomal proteins L37ae and L37e. Members of this group share a common rubredoxin-like metal-binding fold containing two CX(n)C motifs (where n is usually two) [ ]. | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:2.20.25.30"
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""
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13424
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"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-9759... | 64 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
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"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 681 | [
"PUB00030943"
] | [
"15184028"
] | [
"The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1694,
34,
11656,
40
] | 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... | [
18,
3,
2,
7,
11,
8,
2,
10,
14,
4,
4,
41
] | 12 | true | Homologous_superfamily | Large ribosomal subunit protein eL37/eL43 | Large ribosomal subunit protein eL37/eL43 | Ribosomal_eL37/eL43 | 6 |
IPR011332 | 11,332 | Zinc-binding ribosomal protein | Ribosomal_zn-bd | Homologous_superfamily | 124,548 | false | false | This superfamily represents a rubredoxin-like metal-binding fold found in bL32, bL33, eL37, eL43, eL40, eL42 and other ribosomal proteins. This domain contains two CX(n)C motifs (where n is usually two) [ , ]. | [
"GO:0006412"
] | [
"translation"
] | [
"biological_process"
] | 1 | [
"SSF"
] | [
"SSF57829"
] | [
""
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124548
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"REACTOME:R-BT... | 1,135 | [
"1ffk",
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"1qxf",
"1s72",
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"1vq4",
"1vq5"... | 2,208 | [
"PUB00030432",
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"15096641",
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"The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold.",
"The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit."
] | [
2004,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5048,
53357,
65287,
19,
837
] | 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",... | [
63,
7,
11,
15,
3,
35,
28,
8,
54,
50,
11,
10,
84
] | 13 | true | Homologous_superfamily | Zinc-binding ribosomal protein | Zinc-binding ribosomal protein | Ribosomal_zn-bd | 3 |
IPR011334 | 11,334 | UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal | UDP-acyl_GlcNac_deAcase_C | Homologous_superfamily | 14,486 | false | false | This superfamily represents the C-terminal domain. UDP-3-O-N-acetylglucosamine deacetylases are zinc-dependent metalloamidases that catalyse the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide (the major constituent of the outer membrane) into the membrane in Gram-negative b... | [
"GO:0103117",
"GO:0009245"
] | [
"UDP-3-O-acyl-N-acetylglucosamine deacetylase activity",
"lipid A biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.1700.10"
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""
] | [
14486
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
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"3.5.1.108",
"PWY-8073",
"PWY-8245",
"PWY-8283"
] | [
"EC:3.5.1.108",
"METACYC:PWY-8073",
"METACYC:PWY-8245",
"METACYC:PWY-8283"
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"1xxe",
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"2ier",
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"3u1y",
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"4fw4",
"4fw5",
"4fw6",
"4fw7",
"4is9",
"4isa",
"4j3d",
"4lcf",
"4lcg"... | 95 | [
"PUB00029703",
"PUB00032543",
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] | [
"12819349",
"15667205",
"17296300"
] | [
"Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis.",
"Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design.",
"Amphipathic benzoic acid derivatives: synthesis and binding i... | [
2003,
2005,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"unclassified sequences"
] | [
13415,
1,
781,
289
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
1,
6,
5
] | 4 | true | Homologous_superfamily | UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal | UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal | UDP-acyl_GlcNac_deAcase_C | 5 |
IPR011335 | 11,335 | Restriction endonuclease type II-like | Restrct_endonuc-II-like | Homologous_superfamily | 230,831 | false | false | This superfamily represents the core structure found in most type II restriction endonucleases, consisting of a 3-layer α/β/α topology with mixed β-sheets. This core structure can be found in the restriction endonucleases EcoRI, EcoRV, BamHI, BglI, BglII, BstyI, PvuII, MunI, NseI, NgoIV, BsobI, HincII, MspI, FokI (C-te... | [] | [] | [] | 0 | [
"SSF"
] | [
"SSF52980"
] | [
""
] | [
230831
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"REACTOME:R-DME-5696400",
"REACTOME:R-DME-6782135",
"REACTOME:R-DRE-5693568",
"REACTOM... | 36 | [
"1avq",
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"1az4",
"1azo",
"1b94",
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"1b97",
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"1dmu",
"1eo3",
"1eo4",
"1eon",
"1eoo",
"1eop",
"1eri",
"1es8",
"1esg"... | 265 | [
"PUB00035691",
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"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups of restriction endonucleases.",
"Structure and function of type II restriction endonucleases."
] | [
2005,
2003,
2002,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
5113,
191614,
26602,
3772,
2,
3728
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
28,
4,
31,
6,
9,
35,
12,
4,
13,
29,
3,
4,
38
] | 13 | true | Homologous_superfamily | Restriction endonuclease type II-like | Restriction endonuclease type II-like | Restrct_endonuc-II-like | 8 |
IPR011336 | 11,336 | Restriction endonuclease, type II, EcoRI/MunI | Restrct_endonuc_II_EcoRI/MunI | Homologous_superfamily | 203 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.580.10"
] | [
""
] | [
203
] | 1 | [
"EC"
] | [
"3.1.21.4"
] | [
"EC:3.1.21.4"
] | 1 | [
"1ckq",
"1cl8",
"1d02",
"1eri",
"1qc9",
"1qps",
"1qrh",
"1qri",
"2oxv"
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"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035695",
"PUB00035696",
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"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups of restriction endonucleases.",
"Structure and function of type II restriction endonucleases.",
"Sol... | [
2005,
2003,
2002,
2001,
2001,
2001,
2004,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cetraspora pellucida",
"Plasmid P6",
"metagenomes",
"virus sp. ctr1v16"
] | [
2,
190,
2,
1,
7,
1
] | 6 | [] | [] | 0 | true | Homologous_superfamily | Restriction endonuclease, type II, EcoRI/MunI | Restriction endonuclease, type II, EcoRI/MunI | Restrct_endonuc_II_EcoRI/MunI | 3 |
IPR011337 | 11,337 | DNA mismatch repair MutH/Type II restriction enzyme Sau3AI | DNA_rep_MutH/RE_typeII_Sau3AI | Domain | 3,352 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [
"GO:0003677",
"GO:0004519"
] | [
"DNA binding",
"endonuclease activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART",
"CDD"
] | [
"PF02976",
"SM00927",
"cd00583"
] | [
"MutH",
"MutH",
"MutH-like"
] | [
3352,
3272,
2489
] | 3 | [] | [] | [] | 0 | [
"1azo",
"2aoq",
"2aor",
"2azo",
"4pxg"
] | 5 | [
"PUB00007435",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035697",
"PUB00035705",
"PUB00035707"
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"9482749",
"15770420",
"14576294",
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"11557805",
"11316811",
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"Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between d... | [
1998,
2005,
2003,
2002,
2001,
2001,
2004,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"Methanobacteriati",
"metagenomes"
] | [
3308,
1,
11,
32
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DNA mismatch repair MutH/Type II restriction enzyme Sau3AI | DNA mismatch repair MutH/Type II restriction enzyme Sau3AI | DNA_rep_MutH/RE_typeII_Sau3AI | 3 |
IPR011338 | 11,338 | Restriction endonuclease, type II, BamHI/BglIII/BstY | BamHI/BglII/BstY | Homologous_superfamily | 595 | false | false | Restriction endonucleases BamHI, BglII, BstYI and OkrAI share a strong structural consensus mapping to the α/β core domain, represented by this superfamily. BamHI recognises the DNA sequence GGATCC and cleaves after G-1 [ ], BglII recognises AGATCT and cleaves after A-1 [ ], BstYI recognises RGATCY and cleaves after th... | [
"GO:0000287",
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"magnesium ion binding",
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"CATHGENE3D"
] | [
"G3DSA:3.40.91.20"
] | [
""
] | [
595
] | 1 | [
"EC"
] | [
"3.1.21.4"
] | [
"EC:3.1.21.4"
] | 1 | [
"1bam",
"1bhm",
"1d2i",
"1dfm",
"1es8",
"1esg",
"1sdo",
"1vrr",
"2bam",
"2p0j",
"3bam",
"3odh"
] | 12 | [
"PUB00024656",
"PUB00028457",
"PUB00031005",
"PUB00042313",
"PUB00110633"
] | [
"10882125",
"11175900",
"15099740",
"17437717",
"20833632"
] | [
"Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.",
"Structure of free BglII reveals an unprecedented scissor-like motion for opening an endonuclease.",
"Crystal structure of BstYI at 1.85A resolution: a thermophilic restriction endonuclease with overlapping specificities to BamHI and BglII... | [
2000,
2001,
2004,
2007,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Opisthokonta",
"ecological metagenomes"
] | [
23,
546,
3,
2,
21
] | 5 | [] | [] | 0 | true | Homologous_superfamily | Restriction endonuclease, type II, BamHI/BglIII/BstY | Restriction endonuclease, type II, BamHI/BglIII/BstY | BamHI/BglII/BstY | 6 |
IPR011339 | 11,339 | Iron-sulfur cluster assembly scaffold protein IscU | ISCU | Family | 9,404 | false | false | This entry represents IscU from the ISC system, a homologue of the N-terminal region of NifU (NIF system), an Fe-S cluster assembly protein found mostly in nitrogen-fixing bacteria. IscU is a scaffold protein on which Fe-S clusters are assembled before transfer to apoproteins [ , ]. This family includes largely proteob... | [
"GO:0005506",
"GO:0051536",
"GO:0016226"
] | [
"iron ion binding",
"iron-sulfur cluster binding",
"iron-sulfur cluster assembly"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01999"
] | [
"iscU"
] | [
9404
] | 1 | [
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0138",
"GenProp1163",
"R-DME-1362409",
"R-DME-9865881",
"R-HSA-1362409",
"R-HSA-9694301",
"R-HSA-9854311",
"R-HSA-9865881",
"R-MMU-1362409",
"R-MMU-9854311",
"R-MMU-9865881",
"R-PFA-1362409",
"R-SCE-1362409",
"R-SCE-9865881",
"R-SPO-1362409",
"R-SPO-9865881"
] | [
"GP:GenProp0138",
"GP:GenProp1163",
"REACTOME:R-DME-1362409",
"REACTOME:R-DME-9865881",
"REACTOME:R-HSA-1362409",
"REACTOME:R-HSA-9694301",
"REACTOME:R-HSA-9854311",
"REACTOME:R-HSA-9865881",
"REACTOME:R-MMU-1362409",
"REACTOME:R-MMU-9854311",
"REACTOME:R-MMU-9865881",
"REACTOME:R-PFA-1362409"... | 16 | [
"1q48",
"1r9p",
"1wfz",
"2kqk",
"2l4x",
"3lvl",
"5kz5",
"5t0v",
"5tre",
"5wkp",
"5wlw",
"6nzu",
"6uxe",
"6w1d",
"6wi2",
"6wih",
"7rtk",
"8pk8",
"8pk9",
"8pka",
"8rmc",
"8rmd",
"8rme",
"8rmf",
"8rmg",
"8tvt"
] | 26 | [
"PUB00003442",
"PUB00028014",
"PUB00035635",
"PUB00035636",
"PUB00035637",
"PUB00035638",
"PUB00035639",
"PUB00035640",
"PUB00035642",
"PUB00101898"
] | [
"8875867",
"11498000",
"16221578",
"16211402",
"16843540",
"15937904",
"17350000",
"15278785",
"16964969",
"34824239"
] | [
"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,
2006,
2021
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Marine Group I thaumarchaeote",
"Viruses",
"unclassified sequences"
] | [
4913,
4396,
1,
9,
85
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
10,
1,
4,
1,
1,
5,
2,
1,
4,
3,
2,
1,
9
] | 13 | true | Family | Iron-sulfur cluster assembly scaffold protein IscU | Iron-sulfur cluster assembly scaffold protein IscU | ISCU | 6 |
IPR011340 | 11,340 | Cysteine desulfurase-related | Cys_dSase-rel | Family | 3,740 | false | false | This entry describes probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. The most closely related characterised proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys resi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR01976"
] | [
"am_tr_V_VC1184"
] | [
3740
] | 1 | [] | [] | [] | 0 | [
"3cai"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
3641,
24,
15,
60
] | 4 | [] | [] | 0 | true | Family | Cysteine desulfurase-related | Cysteine desulfurase-related | Cys_dSase-rel | 9 |
IPR011342 | 11,342 | Shikimate dehydrogenase | Shikimate_DH | Family | 18,678 | false | false | The shikimate pathway links the metabolism of carbohydrates to the biosynthesis of aromatic compounds and is essential for the biosynthesis of aromatic amino acids and other aromatic compounds in bacteria, eukaryotic microorganisms and plants [ ]. It is a seven-step pathway which converts phosphoenolpyruvate and erythr... | [
"GO:0004764",
"GO:0050661",
"GO:0019632"
] | [
"shikimate 3-dehydrogenase (NADP+) activity",
"NADP binding",
"shikimate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR00507"
] | [
"aroE"
] | [
18678
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"METACYC"
] | [
"1.1.1.25",
"GenProp0001",
"GenProp1478",
"GenProp1643",
"PWY-6163"
] | [
"EC:1.1.1.25",
"GP:GenProp0001",
"GP:GenProp1478",
"GP:GenProp1643",
"METACYC:PWY-6163"
] | 5 | [
"1nvt",
"1nyt",
"1p74",
"1p77",
"1wxd",
"2cy0",
"2d5c",
"2egg",
"2ev9",
"2gpt",
"2hk7",
"2hk8",
"2hk9",
"2o7q",
"2o7s",
"3don",
"3doo",
"3fbt",
"3o8q",
"3pgj",
"3phg",
"3phh",
"3phi",
"3phj",
"3pwz",
"3sef",
"3tnl",
"3toz",
"4foo",
"4fos",
"4fpx",
"4fq8"... | 40 | [
"PUB00014334",
"PUB00028041",
"PUB00028042",
"PUB00028043"
] | [
"15012217",
"3883995",
"12906831",
"12837789"
] | [
"THE SHIKIMATE PATHWAY.",
"The purification of shikimate dehydrogenase from Escherichia coli.",
"Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution.",
"The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode."
] | [
1999,
1985,
2003,
2003
] | 4 | [
"IPR022893"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
712,
16955,
718,
293
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
2,
13
] | 4 | true | Family | Shikimate dehydrogenase | Shikimate dehydrogenase | Shikimate_DH | 8 |
IPR011343 | 11,343 | Deoxyribose-phosphate aldolase | DeoC | Family | 25,130 | false | false | Aldolases play important roles in essential metabolic pathways, such as gluconeogenesis and glycolysis. They are classified with respect to their catalytic mechanism into two classes: class I adolases are are characterised by formation of covalent Schiff base intermediates, while class II aldolases are metallodependent... | [
"GO:0004139",
"GO:0009264",
"GO:0005737"
] | [
"deoxyribose-phosphate aldolase activity",
"deoxyribonucleotide catabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"PIRSF001357",
"PTHR10889",
"TIGR00126",
"cd00959"
] | [
"DeoC",
"",
"deoC",
"DeoC"
] | [
20123,
25042,
24054,
22442
] | 4 | [
"EC",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.2.4",
"GenProp1559",
"PWY-7180",
"PWY-8060",
"R-BTA-6798695",
"R-BTA-71336",
"R-CEL-6798695",
"R-CEL-71336",
"R-HSA-6798695",
"R-HSA-71336",
"R-MMU-6798695",
"R-MMU-71336"
] | [
"EC:4.1.2.4",
"GP:GenProp1559",
"METACYC:PWY-7180",
"METACYC:PWY-8060",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-71336",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-71336",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-71336"
] | 12 | [
"1j2w",
"1jcj",
"1jcl",
"1ktn",
"1mzh",
"1n7k",
"1p1x",
"1ub3",
"1vcv",
"2a4a",
"3ndo",
"3ng3",
"3ngj",
"3npu",
"3npv",
"3npw",
"3npx",
"3nq2",
"3nq8",
"3nqv",
"3nr0",
"3oa3",
"3q2d",
"3qyq",
"3r12",
"3r13",
"4eiv",
"4xbk",
"4xbs",
"5c2x",
"5c5y",
"5c6m"... | 51 | [
"PUB00000628",
"PUB00016149",
"PUB00021873",
"PUB00027586",
"PUB00028044",
"PUB00040690",
"PUB00060480",
"PUB00060481",
"PUB00060482",
"PUB00060483",
"PUB00080613",
"PUB00153747"
] | [
"1730028",
"11598300",
"15388928",
"12529358",
"4923156",
"16843441",
"13950007",
"5972827",
"5793710",
"5816380",
"12467706",
"25284756"
] | [
"Deoxyribose 5-phosphate aldolase of Bacillus cereus: purification and properties.",
"Observation of covalent intermediates in an enzyme mechanism at atomic resolution.",
"Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.",
"The first crystal ... | [
1992,
2001,
2004,
2003,
1970,
2006,
1962,
1966,
1969,
1969,
2003,
2015
] | 12 | [
"IPR002915"
] | [
"IPR023649",
"IPR028581"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine phage"
] | [
532,
20387,
3789,
421,
1
] | 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"
] | [
1,
1,
2,
1,
7,
6,
1,
6
] | 8 | true | Family | Deoxyribose-phosphate aldolase | Deoxyribose-phosphate aldolase | DeoC | 6 |
IPR011344 | 11,344 | Single-stranded DNA-binding protein | ssDNA-bd | Family | 53,697 | false | false | Single-stranded DNA-binding protein (SSB) plays an important role in DNA replication, recombination and repair. It binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism [ , , , ]. | [
"GO:0003697",
"GO:0006260"
] | [
"single-stranded DNA binding",
"DNA replication"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PANTHER",
"NCBIFAM"
] | [
"MF_00984",
"PIRSF002070",
"PTHR10302",
"TIGR00621"
] | [
"SSB",
"SSB",
"",
"ssb"
] | [
41533,
28426,
47794,
46896
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-9837999",
"R-CEL-9913635",
"R-DME-9837999",
"R-DME-9913635",
"R-HSA-2151201",
"R-HSA-9837999",
"R-HSA-9913635",
"R-MMU-9837999",
"R-MMU-9913635",
"R-RNO-9837999",
"R-RNO-9913635",
"R-SCE-9837999"
] | [
"REACTOME:R-CEL-9837999",
"REACTOME:R-CEL-9913635",
"REACTOME:R-DME-9837999",
"REACTOME:R-DME-9913635",
"REACTOME:R-HSA-2151201",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9913635",
"REACTOME:R-MMU-9837999",
"REACTOME:R-MMU-9913635",
"REACTOME:R-RNO-9837999",
"REACTOME:R-RNO-9913635",
"REACTOM... | 12 | [
"1eqq",
"1eyg",
"1kaw",
"1qvc",
"1s3o",
"1se8",
"1sru",
"1ue1",
"1ue5",
"1ue6",
"1ue7",
"1x3e",
"1x3f",
"1x3g",
"1z9f",
"2cwa",
"2dud",
"2fxq",
"2ihe",
"2ihf",
"2vw9",
"3a5u",
"3afp",
"3afq",
"3eiv",
"3lgj",
"3pgz",
"3tqy",
"3udg",
"3ull",
"3ulp",
"3vdy"... | 59 | [
"PUB00074161",
"PUB00074162",
"PUB00074163",
"PUB00094198"
] | [
"18937104",
"20360609",
"21784244",
"27519413"
] | [
"SSB as an organizer/mobilizer of genome maintenance complexes.",
"Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein.",
"SSB functions as a sliding platform that migrates on DNA via reptation.",
"Escherichia coli RadD Protein Functionally ... | [
2008,
2010,
2011,
2016
] | 4 | [
"IPR000424"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
3,
45753,
6091,
1086,
9,
755
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
25,
1,
1,
1,
2,
7,
3,
1,
18,
7,
1,
35
] | 12 | true | Family | Single-stranded DNA-binding protein | Single-stranded DNA-binding protein | ssDNA-bd | 9 |
IPR011346 | 11,346 | High-molecular-weight cytochrome c | Cyt_cc3 | Family | 9 | false | false | Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulphydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of ... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF000026"
] | [
"Cytochrome_cc3"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"1gws",
"1h29",
"2cvc",
"2e84"
] | 4 | [
"PUB00021717",
"PUB00025401",
"PUB00028007",
"PUB00028008"
] | [
"12356749",
"12467575",
"11041344",
"10606770"
] | [
"Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.",
"The crystal structure of the hexadeca-heme cytochrome Hmc and a structural model of its complex with cytochrome c(3).",
"Dele... | [
2002,
2002,
2000,
2000
] | 4 | [
"IPR054813"
] | [] | 1 | 0 | 1 | [
"Desulfovibrionaceae"
] | [
9
] | 1 | [] | [] | 0 | true | Family | High-molecular-weight cytochrome c | High-molecular-weight cytochrome c | Cyt_cc3 | 4 |
IPR011348 | 11,348 | 17beta-dehydrogenase | 17beta_DH | Family | 1,768 | false | false | This entry represents 17beta-hydroxysteroid dehydrogenases (17B-HSDs), a group of enzymes which catalyse the last step in the biosynthesis of all androgens and estrogens -the reversible NAD(P)-linked transfer of a hydride to and from the 17-position of steroid molecules [ ]. A total of six isozymes have been identified... | [
"GO:0004303",
"GO:0006703",
"GO:0005737"
] | [
"estradiol 17-beta-dehydrogenase [NAD(P)+] activity",
"estrogen biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF000095"
] | [
"17beta-HSD"
] | [
1768
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.1.1.62",
"R-HSA-193144",
"R-HSA-2453902",
"R-MMU-193144",
"R-RNO-193144"
] | [
"EC:1.1.1.62",
"REACTOME:R-HSA-193144",
"REACTOME:R-HSA-2453902",
"REACTOME:R-MMU-193144",
"REACTOME:R-RNO-193144"
] | 5 | [
"1a27",
"1bhs",
"1dht",
"1equ",
"1fds",
"1fdt",
"1fdu",
"1fdv",
"1fdw",
"1i5r",
"1iol",
"1jtv",
"1qyv",
"1qyw",
"1qyx",
"3dey",
"3dhe",
"3hb4",
"3hb5",
"3klm",
"3klp",
"3km0",
"6cgc",
"6cge",
"6dtp",
"6mnc",
"6mne",
"7x3z"
] | 28 | [
"PUB00023623",
"PUB00024639",
"PUB00028053",
"PUB00095624"
] | [
"7663947",
"9927655",
"8943783",
"10753906"
] | [
"Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution.",
"Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+.",
"Expression and regulation of 17 beta-hydroxysteroid dehydrogenase t... | [
1995,
1999,
1996,
2000
] | 4 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Staphylococcus haemolyticus",
"Vertebrata"
] | [
2,
1766
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
5,
4,
4
] | 4 | true | Family | 17beta-dehydrogenase | 17beta-dehydrogenase | 17beta_DH | 9 |
IPR011356 | 11,356 | Peptidase M17, leucine aminopeptidase/peptidase B | Leucine_aapep/pepB | Family | 38,870 | false | false | The majority of members of this family are zinc-dependent exopeptidases belonging to MEROPS peptidase family M17 (leucyl aminopeptidase, clan MF). Leucyl aminopeptidase (LAP; ) selectively release N-terminal amino acid residues from polypeptides and proteins; in general they are involved in the processing, catabolism a... | [
"GO:0030145",
"GO:0070006",
"GO:0019538",
"GO:0005737"
] | [
"manganese ion binding",
"metalloaminopeptidase activity",
"protein metabolic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"PANTHER",
"CDD"
] | [
"PR00481",
"PTHR11963",
"cd00433"
] | [
"LAMNOPPTDASE",
"",
"Peptidase_M17"
] | [
37755,
38779,
35001
] | 3 | [
"EC",
"EC",
"EC"
] | [
"3.4.11",
"3.4.11.1",
"3.4.11.10"
] | [
"EC:3.4.11",
"EC:3.4.11.1",
"EC:3.4.11.10"
] | 3 | [
"1bll",
"1bpm",
"1bpn",
"1gyt",
"1lam",
"1lan",
"1lap",
"1lcp",
"2ewb",
"2hb6",
"2hc9",
"2j9a",
"3h8e",
"3h8f",
"3h8g",
"3ij3",
"3jru",
"3kqx",
"3kqz",
"3kr4",
"3kr5",
"3kzw",
"3pei",
"3t8w",
"4efd",
"4k3n",
"4ksi",
"4r6t",
"4r76",
"4r7m",
"4x2t",
"4zi6"... | 69 | [
"PUB00000202",
"PUB00000522",
"PUB00001416",
"PUB00003579",
"PUB00004713",
"PUB00011211",
"PUB00011212",
"PUB00011213",
"PUB00011215",
"PUB00014575"
] | [
"1908238",
"8439290",
"1555602",
"7674922",
"2395881",
"8703509",
"10449417",
"10970742",
"8506345",
"2670557"
] | [
"Structural and immunological evidence for the identity of prolyl aminopeptidase with leucyl aminopeptidase.",
"Evolutionary families of peptidases.",
"Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants.",
"Evolutio... | [
1991,
1993,
1992,
1995,
1990,
1996,
1999,
2000,
1993,
1989
] | 10 | [] | [
"IPR008330",
"IPR023042"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
85,
28757,
9280,
3,
745
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
16,
2,
5,
14,
2,
7,
8,
3,
7,
1,
26
] | 11 | true | Family | Peptidase M17, leucine aminopeptidase/peptidase B | Peptidase M17, leucine aminopeptidase/peptidase B | Leucine_aapep/pepB | 5 |
IPR011363 | 11,363 | Dorsal-related immunity factor Dif | Dif | Family | 173 | false | false | The Dorsal morphogen directs formation of the Drosophila dorsoventral axis by both activating and repressing transcription. It contains an N-terminal Rel homology domain (RHD), which is responsible for DNA binding and regulated nuclear import, and a C-terminal domain (CTD) that contains activation and repression motifs... | [
"GO:0003700",
"GO:0006357",
"GO:0005634",
"GO:0005737"
] | [
"DNA-binding transcription factor activity",
"regulation of transcription by RNA polymerase II",
"nucleus",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF001716"
] | [
"Dorsal"
] | [
173
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-1169091",
"R-DME-1810476",
"R-DME-202424",
"R-DME-209400",
"R-DME-209406",
"R-DME-209560",
"R-DME-214842",
"R-DME-214844",
"R-DME-214869",
"R-DME-2871837",
"R-DME-3134963",
"R-DME-445989",
"R-DME-4755510",
"R-DME-5607764",
"R-DME-5621575",
"R-DME-9020702",
"R-DME-933542",
"R... | [
"REACTOME:R-DME-1169091",
"REACTOME:R-DME-1810476",
"REACTOME:R-DME-202424",
"REACTOME:R-DME-209400",
"REACTOME:R-DME-209406",
"REACTOME:R-DME-209560",
"REACTOME:R-DME-214842",
"REACTOME:R-DME-214844",
"REACTOME:R-DME-214869",
"REACTOME:R-DME-2871837",
"REACTOME:R-DME-3134963",
"REACTOME:R-DME... | 18 | [] | 0 | [
"PUB00014581",
"PUB00014582",
"PUB00073044"
] | [
"12077338",
"3118464",
"8242747"
] | [
"The Dorsal Rel homology domain plays an active role in transcriptional regulation.",
"Dorsal, an embryonic polarity gene in Drosophila, is homologous to the vertebrate proto-oncogene, c-rel.",
"Dif, a dorsal-related gene that mediates an immune response in Drosophila."
] | [
2002,
1987,
1993
] | 3 | [
"IPR000451"
] | [] | 1 | 0 | 1 | [
"Bilateria"
] | [
173
] | 1 | [
"Drosophila melanogaster"
] | [
3
] | 1 | true | Family | Dorsal-related immunity factor Dif | Dorsal-related immunity factor Dif | Dif | 7 |
IPR011364 | 11,364 | Breast cancer type 1 susceptibility protein (BRCA1) | BRCA1 | Family | 1,233 | false | false | Breast cancer is a common malignancy, affecting 1 in 8 women. A major contributary factor in disease development lies in a positive family history, a correlation that is striking for early-onset breast cancer. Mutations in the DNA-damage repair protein BRCA1 [ , ] are believed to be responsible for 45% of inherited bre... | [
"GO:0003677",
"GO:0004842",
"GO:0008270",
"GO:0006281",
"GO:0005634"
] | [
"DNA binding",
"ubiquitin-protein transferase activity",
"zinc ion binding",
"DNA repair",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00493"
] | [
"BRSTCANCERI"
] | [
1233
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"... | [
"2.3.2.27",
"PWY-7511",
"R-HSA-1221632",
"R-HSA-3108214",
"R-HSA-5685938",
"R-HSA-5685942",
"R-HSA-5689901",
"R-HSA-5693554",
"R-HSA-5693565",
"R-HSA-5693568",
"R-HSA-5693571",
"R-HSA-5693579",
"R-HSA-5693607",
"R-HSA-5693616",
"R-HSA-6796648",
"R-HSA-6804756",
"R-HSA-69473",
"R-HS... | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-HSA-1221632",
"REACTOME:R-HSA-3108214",
"REACTOME:R-HSA-5685938",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5689901",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693565",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693571",
"REACTOME:R-HSA-5693579",... | 53 | [
"1jnx",
"1l0b",
"1n5o",
"1t15",
"1t29",
"1t2u",
"1t2v",
"1y98",
"2ing",
"3coj",
"3k0h",
"3k0k",
"3k15",
"3k16",
"3pxa",
"3pxb",
"3pxc",
"3pxd",
"3pxe",
"4ifi",
"4igk",
"4jlu",
"4ofb",
"4u4a",
"4y18",
"4y2g",
"6g2i",
"8rs8"
] | 28 | [
"PUB00014583",
"PUB00014584",
"PUB00014805",
"PUB00017952",
"PUB00066908"
] | [
"10198641",
"8232556",
"14576433",
"10500182",
"10724175"
] | [
"Centrosome amplification and a defective G2-M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells.",
"BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription.",
"The BRCT domain is a phospho-protein binding domain.",
... | [
1999,
1993,
2003,
1999,
2000
] | 5 | [
"IPR031099"
] | [] | 1 | 0 | 1 | [
"Eumetazoa"
] | [
1233
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
53,
28,
7
] | 3 | true | Family | Breast cancer type 1 susceptibility protein (BRCA1) | Breast cancer type 1 susceptibility protein (BRCA1) | BRCA1 | 3 |
IPR011365 | 11,365 | Cytokine IL-3/IL-5/GM-CSF receptor common beta chain | IL3_rcpt_beta | Family | 27 | false | false | This group represents a cytokine IL-3/IL-5/GM-CSF receptor common beta chain. Please see the following relevant reference: [ ]. | [
"GO:0004896",
"GO:0019221",
"GO:0016020"
] | [
"cytokine receptor activity",
"cytokine-mediated signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF001956"
] | [
"IL3R_beta_c"
] | [
27
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-512988",
"R-HSA-5673001",
"R-HSA-5683826",
"R-HSA-5688849",
"R-HSA-5688890",
"R-HSA-912526",
"R-MMU-512988",
"R-MMU-5673001",
"R-MMU-912526"
] | [
"REACTOME:R-HSA-512988",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-5683826",
"REACTOME:R-HSA-5688849",
"REACTOME:R-HSA-5688890",
"REACTOME:R-HSA-912526",
"REACTOME:R-MMU-512988",
"REACTOME:R-MMU-5673001",
"REACTOME:R-MMU-912526"
] | 9 | [] | 0 | [
"PUB00014585"
] | [
"9794243"
] | [
"Regulation of proliferation, differentiation and survival by the IL-3/IL-5/GM-CSF receptor family."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Euarchontoglires"
] | [
27
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
7,
3
] | 3 | true | Family | Cytokine IL-3/IL-5/GM-CSF receptor common beta chain | Cytokine IL-3/IL-5/GM-CSF receptor common beta chain | IL3_rcpt_beta | 8 |
IPR011375 | 11,375 | MfnE family | MfnE | Family | 228 | false | false | This family includes the MJ0458 protein from Methanocaldococcus jannaschii (Methanococcus jannaschii), which was predicted to be related to aspartokinase and uridylate kinase [ ]. MJ0458 has been characterised and renamed as MfnE. It functions as a 5-(aminomethyl)-3-furanmethanol phosphate kinase in the methanofuran bi... | [] | [] | [] | 0 | [
"PIRSF",
"CDD"
] | [
"PIRSF004857",
"cd04240"
] | [
"Kin_aa_kin",
"AAK_UC"
] | [
219,
114
] | 2 | [] | [] | [] | 0 | [
"7qrh"
] | 1 | [
"PUB00077118",
"PUB00077119"
] | [
"26100040",
"22002406"
] | [
"Identification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii.",
"A new class of adenylate kinase in methanogens is related to uridylate kinase."
] | [
2015,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Pseudomonadati",
"groundwater metagenome"
] | [
208,
19,
1
] | 3 | [] | [] | 0 | true | Family | MfnE family | MfnE family | MfnE | 6 |
IPR011379 | 11,379 | NTP Pyrophosphohydrolase MazG-related, GP37 | MazG-related_GP37 | Family | 2,105 | false | false | Members of this group are distantly related to MazG-type NTP pyrophosphohydrolase. Conserved residues of the MazG domain (at least three of the Glu residues, Asp, Lys and Arg), which include those shown to be functionally important [ ], are also conserved here. MazG protein of Thermotoga maritima has been shown to have... | [] | [] | [] | 0 | [
"PIRSF",
"CDD"
] | [
"PIRSF006639",
"cd11541"
] | [
"UCP006639_pph",
"NTP-PPase_u4"
] | [
1387,
2058
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013554",
"PUB00014610"
] | [
"12657645",
"12218018"
] | [
"Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities.",
"MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli."
] | [
2003,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
7,
1704,
5,
345,
44
] | 5 | [] | [] | 0 | true | Family | NTP Pyrophosphohydrolase MazG-related, GP37 | NTP Pyrophosphohydrolase MazG-related, GP37 | MazG-related_GP37 | 5 |
IPR011381 | 11,381 | Histone-lysine N-methyltransferase SUV39H1/2-like | H3-K9_MeTrfase_SUV39H1/2-like | Family | 2,059 | false | false | Members of this family trimethylate 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate, including histone-lysine N-methyltransferase Su(var)3-9 from Drosophila melanogaster and its orthologue from human, SUV39H1. SUV39H1 also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents ... | [
"GO:0046974",
"GO:0005634"
] | [
"histone H3K9 methyltransferase activity",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PIRSF",
"PROFILE"
] | [
"PIRSF009343",
"PS51579"
] | [
"SUV39_SET",
"SAM_MT43_SUVAR39_3"
] | [
2004,
1364
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.1.1.-",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601",
"PWY-6045"... | [
"EC:2.1.1.-",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",
"METACYC:PWY-5... | 150 | [
"1mvh",
"1mvx",
"2r3a",
"6box",
"6bp4",
"6p0r",
"6z2a",
"9isz",
"9it4"
] | 9 | [
"PUB00006319",
"PUB00007132",
"PUB00014403",
"PUB00014448",
"PUB00014462",
"PUB00050320",
"PUB00054125",
"PUB00057957",
"PUB00057958",
"PUB00058070",
"PUB00058071",
"PUB00058072",
"PUB00058073",
"PUB00058074",
"PUB00058077",
"PUB00058078",
"PUB00058079",
"PUB00058080"
] | [
"7897657",
"12039029",
"10202156",
"10949293",
"10848615",
"18485871",
"12826405",
"16225687",
"21858014",
"14690609",
"14690610",
"14702045",
"14765126",
"11701123",
"16858404",
"16449642",
"16818776",
"18004385"
] | [
"Universal catalytic domain structure of AdoMet-dependent methyltransferases.",
"SET-domain proteins of the Su(var)3-9, E(z) and trithorax families.",
"Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component... | [
1995,
2002,
1999,
2000,
2000,
2008,
2003,
2005,
2011,
2003,
2003,
2004,
2004,
2001,
2006,
2006,
2006,
2007
] | 18 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
2059
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
4,
3,
5,
7,
12,
1
] | 6 | true | Family | Histone-lysine N-methyltransferase SUV39H1/2-like | Histone-lysine N-methyltransferase SUV39H1/2-like | H3-K9_MeTrfase_SUV39H1/2-like | 2 |
IPR011385 | 11,385 | Putative site-specific recombinase Gcr | Site-sp_rcmbase | Family | 2,177 | false | false | This group represents a putative site-specific recombinase Gcr [ ]. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF10136",
"PIRSF015380"
] | [
"SpecificRecomb",
"Site-sp_rcmb"
] | [
2177,
1652
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014618"
] | [
"9079926"
] | [
"Inversion of Moraxella lacunata type 4 pilin gene sequences by a Neisseria gonorrhoeae site-specific recombinase."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2164,
4,
9
] | 3 | [] | [] | 0 | true | Family | Putative site-specific recombinase Gcr | Putative site-specific recombinase Gcr | Site-sp_rcmbase | 9 |
IPR011386 | 11,386 | Putative ATP-NAD kinase | Put_ATP-NAD_kin | Family | 1,639 | false | false | Members of this group are predicted to be kinases (possibly ATP-NAD kinases, ) on the basis of distant sequence similarity. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF016907"
] | [
"Kin_ATP-NAD"
] | [
1639
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR039065"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
536,
1083,
20
] | 3 | [] | [] | 0 | true | Family | Putative ATP-NAD kinase | Putative ATP-NAD kinase | Put_ATP-NAD_kin | 2 |
IPR011388 | 11,388 | Sphingolipid delta4-desaturase | DES1/DES2 | Family | 4,776 | false | false | This group represents sphingolipid delta-4 desaturase (DEGS), an integral membrane protein required for sphingosine biosynthesis. It converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) [ ]. Delta4-desaturated sphingolipids provide an early signal that triggers the entry into both meiotic and sper... | [
"GO:0042284",
"GO:0030148",
"GO:0016020"
] | [
"sphingolipid delta-4 desaturase activity",
"sphingolipid biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"CDD"
] | [
"PIRSF017228",
"cd03508"
] | [
"Sphnglp_dlt4_des",
"Delta4-sphingolipid-FADS-like"
] | [
4169,
4700
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.19.17",
"PWY-5129",
"R-BTA-1660661",
"R-BTA-6798695",
"R-CEL-1660661",
"R-CEL-6798695",
"R-DME-1660661",
"R-DME-6798695",
"R-GGA-1660661",
"R-GGA-433584",
"R-GGA-6798695",
"R-HSA-1660661",
"R-HSA-6798695",
"R-MMU-1660661",
"R-MMU-6798695",
"R-RNO-1660661",
"R-RNO-6798695",
"R... | [
"EC:1.14.19.17",
"METACYC:PWY-5129",
"REACTOME:R-BTA-1660661",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-1660661",
"REACTOME:R-CEL-6798695",
"REACTOME:R-DME-1660661",
"REACTOME:R-DME-6798695",
"REACTOME:R-GGA-1660661",
"REACTOME:R-GGA-433584",
"REACTOME:R-GGA-6798695",
"REACTOME:R-HSA-1660661"... | 21 | [] | 0 | [
"PUB00014620"
] | [
"11937514"
] | [
"Identification and characterization of a sphingolipid delta 4-desaturase family."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Emiliania huxleyi virus 86 (isolate United Kingdom/English Channel/1999)",
"Eukaryota",
"Pseudomonadati",
"viral metagenome"
] | [
1,
4763,
11,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (stra... | [
4,
2,
2,
1,
3,
4,
1,
1,
6,
1,
2
] | 11 | true | Family | Sphingolipid delta4-desaturase | Sphingolipid delta4-desaturase | DES1/DES2 | 4 |
IPR011390 | 11,390 | Insulin-like growth factor binding protein-related protein (IGFBP-rP), MAC25 | IGFBP_rP_mac25 | Family | 3,852 | false | false | Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological effects, such as increasing the permeability of cells to monosaccharides, amino acids and fatty acids, and accelerating glycolysis and glycogen synthesis in the liver [ ]. Insulin ... | [
"GO:0005520",
"GO:0001558",
"GO:0005576"
] | [
"insulin-like growth factor binding",
"regulation of cell growth",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF018239",
"PTHR14186"
] | [
"IGFBP_rP_mac25",
""
] | [
1406,
3852
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2559582",
"R-HSA-381426",
"R-HSA-8957275",
"R-MMU-381426",
"R-MMU-8957275"
] | [
"REACTOME:R-HSA-2559582",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-8957275"
] | 5 | [
"3tjq",
"3zxb"
] | 2 | [
"PUB00003970",
"PUB00003972",
"PUB00003973",
"PUB00013535",
"PUB00013536",
"PUB00013537",
"PUB00013538",
"PUB00013539",
"PUB00013540",
"PUB00013541",
"PUB00013542",
"PUB00014624",
"PUB00023078",
"PUB00037375",
"PUB00053639",
"PUB00053640",
"PUB00053641",
"PUB00053642"
] | [
"503234",
"6243748",
"6107857",
"11874691",
"9822601",
"9725901",
"7519375",
"9660801",
"12379487",
"12379489",
"7504269",
"9745429",
"2036417",
"9141131",
"10601981",
"8735594",
"8683595",
"1319992"
] | [
"Nucleotide sequence of a cDNA clone encoding human preproinsulin.",
"Sequence of the human insulin gene.",
"Hormone families: pancreatic hormones and homologous growth factors.",
"IGF-binding protein-5: flexible player in the IGF system and effector on its own.",
"Structure of the IGF-binding domain of the... | [
1979,
1980,
1980,
2002,
1998,
1998,
1994,
1998,
2002,
2002,
1993,
1998,
1991,
1997,
1999,
1996,
1996,
1992
] | 18 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
3852
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
1,
6,
10,
10
] | 5 | true | Family | Insulin-like growth factor binding protein-related protein (IGFBP-rP), MAC25 | Insulin-like growth factor binding protein-related protein (IGFBP-rP), MAC25 | IGFBP_rP_mac25 | 7 |
IPR011391 | 11,391 | Acetoin catabolism kinase AcoX | AcoX_kinase | Family | 835 | false | false | Members of this group are involved in acetoin catabolism [ , , ] and are encoded in the aco operon. They are predicted to be kinases (possibly ATP-NAD kinases, ) on the basis of distant sequence similarity. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF018567"
] | [
"AcoX"
] | [
835
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00002145",
"PUB00014625",
"PUB00014626"
] | [
"2061286",
"7813883",
"8206840"
] | [
"Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism.",
"Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway.",
"Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase... | [
1991,
1994,
1994
] | 3 | [
"IPR039065"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Geodia barretti",
"ecological metagenomes"
] | [
26,
797,
2,
10
] | 4 | [] | [] | 0 | true | Family | Acetoin catabolism kinase AcoX | Acetoin catabolism kinase AcoX | AcoX_kinase | 7 |
IPR011392 | 11,392 | Tellurite resistance, TerY | Tellurite-R_TerY | Family | 2,114 | false | false | This group represents a phage/colicin/tellurite resistance cluster protein, TerY type. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF020634"
] | [
"TerY_vWA"
] | [
2114
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Geodia barretti",
"Methanomicrobiales",
"Plasmid R478",
"metagenomes"
] | [
2086,
2,
15,
1,
10
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Tellurite resistance, TerY | Tellurite resistance, TerY | Tellurite-R_TerY | 4 |
IPR011395 | 11,395 | Alpha glucuronidase | Glyco_hydro_67_aGlcAse | Family | 2,707 | false | false | Alpha-glucuronidases belong to an ensemble of enzymes, which are central to the recycling of photosynthetic biomass. To date, all of the alpha-glucuronidases are classified as family 67 glycosidases, which catalyze the hydrolysis via the investing mechanism [ ]. They hydrolyze the alpha1,2-glycosidic bond between 4-O-m... | [
"GO:0046559",
"GO:0045493",
"GO:0005576"
] | [
"alpha-glucuronidase activity",
"xylan catabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF029900"
] | [
"Alpha-glucuronds"
] | [
2707
] | 1 | [
"EC"
] | [
"3.2.1.139"
] | [
"EC:3.2.1.139"
] | 1 | [
"1gqi",
"1gqj",
"1gqk",
"1gql",
"1h41",
"1k9d",
"1k9e",
"1k9f",
"1l8n",
"1mqp",
"1mqq",
"1mqr"
] | 12 | [
"PUB00014285",
"PUB00026672",
"PUB00028600"
] | [
"11937059",
"14573597",
"12654910"
] | [
"The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A.",
"Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications.",
"The alpha-glucuronidase, GlcA67A, of Cellvibrio japon... | [
2002,
2004,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
1923,
779,
5
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Alpha glucuronidase | Alpha glucuronidase | Glyco_hydro_67_aGlcAse | 5 |
IPR011396 | 11,396 | Phosphorothioated DNA-binding restriction endonuclease | PT_DNA_restrict | Family | 1,746 | false | false | This entry represents a group of proteins from bacteria that are distantly related to the C-terminal half of the type IV restriction endonuclease McrA from Streptomyces coelicolor ( ), which can act on phosphorothioated DNA (PT-DNA), as do members of this family. This family was previously known as UCP030850. | [] | [] | [] | 0 | [
"NCBIFAM",
"PIRSF"
] | [
"NF045808",
"PIRSF030850"
] | [
"PT-DNA_restrict",
"UCP030850"
] | [
1353,
1660
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154747"
] | [
"30409991"
] | [
"Structural basis for the recognition of sulfur in phosphorothioated DNA."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanogaster sp. ANME-2c ERB4",
"Caudovirales sp. ctilw2",
"metagenomes"
] | [
1735,
1,
1,
9
] | 4 | [] | [] | 0 | true | Family | Phosphorothioated DNA-binding restriction endonuclease | Phosphorothioated DNA-binding restriction endonuclease | PT_DNA_restrict | 5 |
IPR011397 | 11,397 | Intramembrane metalloprotease YhfC | YhfC | Family | 1,723 | false | false | This family includes proteins that are mainly from Firmicutes and Proteobacteria. Family members bear the consensus signature of -EExxR- the second motif -HxxxE- and the third motif -H/Qxxxs-. The fourth motif, -HxxxB-, is shared by the PrsW proteases ( ) and the CPBP ( ), and APH-1 families. There are currently no exp... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF10086",
"PIRSF033101"
] | [
"YhfC",
"UCP033101"
] | [
1723,
1383
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00091031"
] | [
"21570408"
] | [
"Expansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Sar",
"metagenomes"
] | [
53,
1646,
4,
20
] | 4 | [] | [] | 0 | true | Family | Intramembrane metalloprotease YhfC | Intramembrane metalloprotease YhfC | YhfC | 2 |
IPR011399 | 11,399 | Nitrous oxide reductase expression regulator NosR | NosR | Family | 1,845 | false | false | The bacterial protein NosR is involved in N 2 O respiration. It is a membrane bound iron-sulphur flavoprotein that is required for the transcription of nosZ genes and also for cellular activity of its homologue, NosZ [ ]. | [
"GO:0003677",
"GO:0045893",
"GO:0016020"
] | [
"DNA binding",
"positive regulation of DNA-templated transcription",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF"
] | [
"PIRSF036354"
] | [
"NosR"
] | [
1845
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00053871"
] | [
"15743947"
] | [
"Functional domains of NosR, a novel transmembrane iron-sulfur flavoprotein necessary for nitrous oxide respiration."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
1825,
20
] | 2 | [] | [] | 0 | true | Family | Nitrous oxide reductase expression regulator NosR | Nitrous oxide reductase expression regulator NosR | NosR | 4 |
IPR011400 | 11,400 | Eukaryotic translation initiation factor 3 subunit B | EIF3B | Family | 8,453 | false | false | Eukaryotic translation initiation factor 3 subunit B (EIF3B) is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. EIF3B is considered to be the major scaffolding subunit and interacts with subunits A, G, I, and J [ ... | [
"GO:0003723",
"GO:0003743",
"GO:0031369",
"GO:0006413",
"GO:0005852"
] | [
"RNA binding",
"translation initiation factor activity",
"translation initiation factor binding",
"translational initiation",
"eukaryotic translation initiation factor 3 complex"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"HAMAP",
"PIRSF",
"PANTHER"
] | [
"MF_03001",
"PIRSF036424",
"PTHR14068"
] | [
"eIF3b",
"eIF3b",
""
] | [
4518,
4197,
8452
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-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 | [
"2krb",
"2nlw",
"3ns5",
"3ns6",
"4nox",
"4u1f",
"4uer",
"5a5u",
"5k1h",
"6fec",
"6fyx",
"6fyy",
"6gsm",
"6gsn",
"6ybt",
"6zce",
"6zmw",
"6zon",
"6zp4",
"6zu9",
"6zvj",
"7a09",
"7qp6",
"7qp7",
"8cah",
"8cas",
"8oz0",
"8pj1",
"8pj2",
"8pj3",
"8pj4",
"8pj5"... | 36 | [
"PUB00055362",
"PUB00064778"
] | [
"20862284",
"18599441"
] | [
"Crystal structure of the RNA recognition motif of yeast translation initiation factor eIF3b reveals differences to human eIF3b.",
"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
] | [
2010,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"viral metagenome"
] | [
8452,
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... | [
15,
1,
1,
2,
9,
3,
1,
3,
4,
1,
1,
4
] | 12 | true | Family | Eukaryotic translation initiation factor 3 subunit B | Eukaryotic translation initiation factor 3 subunit B | EIF3B | 8 |
IPR011402 | 11,402 | Phospholipase D, plant | PLipase_D_pln | Family | 4,813 | false | false | This entry represents the plant phospholipase D (PLD), a calcium-dependent enzyme that hydrolyses glycerol-phospholipids at the terminal phosphodiesteric bond. Arabidopsis PLD has been implicated in plant response to macronutrient availability [ ]. PLD alpha 1 from Setaria italica (foxtail millet) has been linked to dr... | [
"GO:0004630",
"GO:0005509",
"GO:0046470",
"GO:0016020"
] | [
"D-type glycerophospholipase activity",
"calcium ion binding",
"phosphatidylcholine metabolic process",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF"
] | [
"PIRSF036470"
] | [
"PLD_plant"
] | [
4813
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.1.4.4",
"PWY-3561",
"PWY-7039"
] | [
"EC:3.1.4.4",
"METACYC:PWY-3561",
"METACYC:PWY-7039"
] | 3 | [
"6kz8",
"6kz9"
] | 2 | [
"PUB00076682",
"PUB00076683"
] | [
"26260942",
"20490504"
] | [
"Phospholipase Dε enhances Braasca napus growth and seed production in response to nitrogen availability.",
"Overexpression of a PLDα1 gene from Setaria italica enhances the sensitivity of Arabidopsis to abscisic acid and improves its drought tolerance."
] | [
2015,
2010
] | 2 | [
"IPR015679"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
4813
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
41,
33,
52
] | 3 | true | Family | Phospholipase D, plant | Phospholipase D, plant | PLipase_D_pln | 1 |
IPR011404 | 11,404 | Pyrophosphate--fructose 6-phosphate 1-phosphotransferase | PPi-PFK | Family | 3,729 | false | false | This entry represents pyrophosphate--fructose 6-phosphate 1-phosphotransferase, initially described as XF0274 type [ ]. It catalyses the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis [ , ]. | [
"GO:0047334",
"GO:0006096"
] | [
"diphosphate-fructose-6-phosphate 1-phosphotransferase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP"
] | [
"MF_01978"
] | [
"Phosphofructokinase_II_B2"
] | [
3729
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.7.1.90",
"PWY-1042",
"PWY-8178"
] | [
"EC:2.7.1.90",
"METACYC:PWY-1042",
"METACYC:PWY-8178"
] | 3 | [
"3hno",
"3k2q"
] | 2 | [
"PUB00014634",
"PUB00074133",
"PUB00074135"
] | [
"14585511",
"19054082",
"24508689"
] | [
"Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase.",
"Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Methylococcus capsulatus Bath.",
"Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Xanthomonas campestri... | [
2003,
2008,
2014
] | 3 | [
"IPR022953"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
3642,
5,
82
] | 3 | [] | [] | 0 | true | Family | Pyrophosphate--fructose 6-phosphate 1-phosphotransferase | Pyrophosphate--fructose 6-phosphate 1-phosphotransferase | PPi-PFK | 7 |
IPR011405 | 11,405 | Pyrophosphate-dependent phosphofructokinase SMc01852 type | PPi-PFK_SMc01852 | Family | 1,127 | false | false | This entry represents a family of pyrophosphate-dependent phosphofructokinases. It catalyses the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis [ , ]. | [
"GO:0047334",
"GO:0006096"
] | [
"diphosphate-fructose-6-phosphate 1-phosphotransferase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"PIRSF"
] | [
"MF_01977",
"NF005121",
"PIRSF036484"
] | [
"Phosphofructokinase_II_P",
"PRK06555.1",
"PPi-PFK_SMc01852"
] | [
1006,
1127,
891
] | 3 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.7.1.90",
"PWY-1042",
"PWY-8178"
] | [
"EC:2.7.1.90",
"METACYC:PWY-1042",
"METACYC:PWY-8178"
] | 3 | [] | 0 | [
"PUB00074136",
"PUB00074137"
] | [
"20868748",
"16480155"
] | [
"Characterization of recombinant pyrophosphate-dependent 6-phosphofructokinase from halotolerant methanotroph Methylomicrobium alcaliphilum 20Z.",
"Identification and cloning of the gene encoding pyrophosphate-dependent 6-phosphofructokinase of Methylomonas methanica."
] | [
2010,
2005
] | 2 | [
"IPR022953"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified Candidatus Thermoprofundales"
] | [
1024,
65,
33,
5
] | 4 | [] | [] | 0 | true | Family | Pyrophosphate-dependent phosphofructokinase SMc01852 type | Pyrophosphate-dependent phosphofructokinase SMc01852 type | PPi-PFK_SMc01852 | 4 |
IPR011406 | 11,406 | Globin, trematode | Globin_trematode | Family | 27 | false | false | Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric gl... | [
"GO:0005506",
"GO:0019825",
"GO:0020037",
"GO:0015671"
] | [
"iron ion binding",
"oxygen binding",
"heme binding",
"oxygen transport"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PIRSF"
] | [
"PIRSF036488"
] | [
"Myoglobin_tremt"
] | [
27
] | 1 | [] | [] | [] | 0 | [
"1h97",
"1kfr"
] | 2 | [
"PUB00014637",
"PUB00014638",
"PUB00014639",
"PUB00016016",
"PUB00029465",
"PUB00035865",
"PUB00035866",
"PUB00035867",
"PUB00035868",
"PUB00035869",
"PUB00035870",
"PUB00035871",
"PUB00035872",
"PUB00035873",
"PUB00035877",
"PUB00055462",
"PUB00055463",
"PUB00153677"
] | [
"9006947",
"9006948",
"9675199",
"15096613",
"12962627",
"16600051",
"17540514",
"11092893",
"11481493",
"15598488",
"16888280",
"15598493",
"15339940",
"15804833",
"17084861",
"17540516",
"17701548",
"21495624"
] | [
"Trematode myoglobins, functional molecules with a distal tyrosine.",
"Solution of 1H NMR structure of the heme cavity in the oxygen-avid myoglobin from the trematode Paramphistomum epiclitum.",
"Trematode hemoglobins show exceptionally high oxygen affinity.",
"Ancestral hemoglobins in Archaea.",
"Human bra... | [
1997,
1997,
1998,
2004,
2003,
2006,
2007,
2001,
2001,
2005,
2006,
2005,
2004,
2004,
2007,
2007,
2007,
2011
] | 18 | [] | [] | 0 | 0 | null | [
"Digenea"
] | [
27
] | 1 | [] | [] | 0 | true | Family | Globin, trematode | Globin, trematode | Globin_trematode | 8 |
IPR011408 | 11,408 | Aldehyde dehydrogenase | Aldehyde_DH | Family | 1,705 | false | false | This group represents a predicted aldehyde dehydrogenase with a duplicated domain. Even though the proteins in this entry belong to the aldehyde dehydrogenase family, the active site cysteine and glutamate residues are not conserved. Their activity is, therefore, not clear. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036490"
] | [
"Aldedh_dupl"
] | [
1705
] | 1 | [] | [] | [] | 0 | [
"6mvr",
"6mvs",
"6mvt",
"6mvu"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes",
"uncultured marine group II/III euryarchaeote KM3_57_F04"
] | [
1333,
356,
15,
1
] | 4 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
4
] | 3 | true | Family | Aldehyde dehydrogenase | Aldehyde dehydrogenase | Aldehyde_DH | 6 |
IPR011410 | 11,410 | Nucleoside diphosphate kinase 7 | NDPK7 | Family | 1,538 | false | false | The nm23-H7 nucleoside diphosphate kinase (also known as NDPk7 or NME7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, alt... | [
"GO:0004550",
"GO:0005524"
] | [
"nucleoside diphosphate kinase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF"
] | [
"PIRSF036503"
] | [
"NDK7"
] | [
1538
] | 1 | [
"EC",
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.11.1",
"3.1.11.-",
"R-BTA-380270",
"R-BTA-380320",
"R-HSA-380270",
"R-HSA-380320",
"R-MMU-380270",
"R-MMU-380320",
"R-RNO-380270",
"R-RNO-380320"
] | [
"EC:2.7.11.1",
"EC:3.1.11.-",
"REACTOME:R-BTA-380270",
"REACTOME:R-BTA-380320",
"REACTOME:R-HSA-380270",
"REACTOME:R-HSA-380320",
"REACTOME:R-MMU-380270",
"REACTOME:R-MMU-380320",
"REACTOME:R-RNO-380270",
"REACTOME:R-RNO-380320"
] | 10 | [
"6u42",
"7rro",
"7ung",
"8g2z",
"8g3d",
"8glv",
"8i7r",
"8iyj",
"8j07",
"8otz",
"8sf7",
"8snb",
"8to0",
"9cpb",
"9cpc",
"9fqr"
] | 16 | [
"PUB00014641",
"PUB00085496",
"PUB00085503"
] | [
"11768308",
"15726650",
"19421718"
] | [
"The human Nm23/nucleoside diphosphate kinases.",
"Expression of the nm23 homologues nm23-H4, nm23-H6, and nm23-H7 in human gastric and colon cancer.",
"The NM23 family in development."
] | [
2000,
2005,
2009
] | 3 | [
"IPR001564"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
1538
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
3,
4,
5
] | 5 | true | Family | Nucleoside diphosphate kinase 7 | Nucleoside diphosphate kinase 7 | NDPK7 | 1 |
IPR011411 | 11,411 | NTP pyrophosphohydrolase MazG-related, YvdC | MazG-related_YvdC | Family | 1,276 | false | false | Members of this group are distantly related to MazG-type NTP pyrophosphohydrolase. Conserved residues of the MazG domain (at least three of the Glu residues, Asp, Lys and Arg), including those shown to be functionally important [ ], are also conserved here. MazG protein of Thermotoga maritima has been shown to have bot... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036521"
] | [
"UCP036521_pph"
] | [
1276
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013554",
"PUB00014610"
] | [
"12657645",
"12218018"
] | [
"Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities.",
"MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli."
] | [
2003,
2002
] | 2 | [
"IPR047046"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Viruses",
"metagenomes"
] | [
29,
1223,
8,
16
] | 4 | [] | [] | 0 | true | Family | NTP pyrophosphohydrolase MazG-related, YvdC | NTP pyrophosphohydrolase MazG-related, YvdC | MazG-related_YvdC | 3 |
IPR011412 | 11,412 | Coronamic acid biosynthesis thioesterase CmaT | CmaT_thioesters | Family | 2 | false | false | This group represents a coronamic acid biosynthesis thioesterase CmaT. Please see the following relevant reference: [ ]. | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036539"
] | [
"CmaT_thioesters"
] | [
2
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014642"
] | [
"8002582"
] | [
"The biosynthetic gene cluster for coronamic acid, an ethylcyclopropyl amino acid, contains genes homologous to amino acid-activating enzymes and thioesterases."
] | [
1994
] | 1 | [
"IPR012223"
] | [] | 1 | 0 | 1 | [
"Pseudomonas syringae"
] | [
2
] | 1 | [] | [] | 0 | true | Family | Coronamic acid biosynthesis thioesterase CmaT | Coronamic acid biosynthesis thioesterase CmaT | CmaT_thioesters | 7 |
IPR011413 | 11,413 | Uncharacterised conserved protein UCP036540 | UCP036540_AIR | Family | 1,136 | false | false | Members of this family belong to a large group that also contains thiamine monophosphate kinase ( ), hydrogenase maturation factor HypE ( ), AIR synthase, FGAM synthase ( ), selenophosphate synthase ( ), and other groups. In AIR synthase, the N-terminal domain forms the dimer interface of the protein and, upon dimerisa... | [] | [] | [] | 0 | [
"PIRSF",
"CDD"
] | [
"PIRSF036540",
"cd02192"
] | [
"UCP036540_AIR",
"PurM-like3"
] | [
1076,
1110
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014643"
] | [
"10508786"
] | [
"X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution."
] | [
1999
] | 1 | [
"IPR006283"
] | [
"IPR017668",
"IPR024030"
] | 1 | 2 | 0 | [
"Archaea",
"Bacteria",
"Ricinus communis",
"ecological metagenomes"
] | [
246,
879,
1,
10
] | 4 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP036540 | Uncharacterised conserved protein UCP036540 | UCP036540_AIR | 3 |
IPR011414 | 11,414 | Uncharacterised conserved protein UCP036541 | UCP036541_AIR | Family | 26 | false | false | Members of this family belong to a large group that also contains thiamine monophosphate kinase, hydrogenase maturation factor HypE ( ), AIR synthase, FGAM synthase ( ), selenophosphate synthetase ( ), and other groups. In AIR synthase, the N-terminal domain forms the dimer interface of the protein and, upon dimerisati... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036541"
] | [
"UCP036541_AIR"
] | [
26
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014643"
] | [
"10508786"
] | [
"X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution."
] | [
1999
] | 1 | [
"IPR006283"
] | [] | 1 | 0 | 1 | [
"Methanomada group"
] | [
26
] | 1 | [] | [] | 0 | true | Family | Uncharacterised conserved protein UCP036541 | Uncharacterised conserved protein UCP036541 | UCP036541_AIR | 8 |
IPR011415 | 11,415 | Predicted bifunctional spore maturation protein, fused SpmA/SpmB | SpmA_SpmB | Family | 2,976 | false | false | This group contains two-domain proteins that are fusions of spore maturation protein A (SpmA) and spore maturation protein B (SpmB). SpmA and SpmB are thought to be involved in spore core dehydration in Bacillus subtilis. Spore dehydration is important for heat resistance, and for processing the spore germination prote... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036542"
] | [
"SpmA_SpmB"
] | [
2976
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009933",
"PUB00014609",
"PUB00014645"
] | [
"7642500",
"1548223",
"8188581"
] | [
"The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5*, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration.",
"Isolation and sequence analysis of dacB, which encodes a sporulation-specific penicillin-binding protein in Bacillus subtilis.",
"Stu... | [
1995,
1992,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
2933,
43
] | 2 | [] | [] | 0 | true | Family | Predicted bifunctional spore maturation protein, fused SpmA/SpmB | Predicted bifunctional spore maturation protein, fused SpmA/SpmB | SpmA_SpmB | 9 |
IPR011416 | 11,416 | Predicted RNA-binding protein YdrC-type, Chlamydia | YdrC-type_chlamyd | Family | 21 | false | false | This group contains homologues of Escherichia coli YrdC with an additional unique short (~100 aa) C-terminal domain. In accordance with its proposed role as a translation factor, YrdC preferentially binds dsRNA, likely via a depression on the surface of the protein [ ]. However, members of both this group lack the C-te... | [] | [] | [] | 0 | [
"PIRSF"
] | [
"PIRSF036543"
] | [
"YdrC_chlamyd"
] | [
21
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00011086",
"PUB00011089"
] | [
"11206077",
"1325384"
] | [
"The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding.",
"Isolation and characterization of SUA5, a novel gene required for normal growth in Saccharomyces cerevisiae."
] | [
2000,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Chlamydia"
] | [
21
] | 1 | [] | [] | 0 | true | Family | Predicted RNA-binding protein YdrC-type, Chlamydia | Predicted RNA-binding protein YdrC-type, Chlamydia | YdrC-type_chlamyd | 4 |
IPR011417 | 11,417 | AP180 N-terminal homology (ANTH) domain | ANTH_dom | Domain | 27,473 | false | false | The AP180 N-terminal homology (ANTH) domain is a membrane binding domain found in endocytotic accessory proteins, such as AP180. AP180 has been implicated in the formation of clathrin-coated pits. The ANTH domain is involved in phosphatidylinositol 4,5-bisphosphate (also known as PIP2) binding. The ANTH domain containi... | [
"GO:0005543"
] | [
"phospholipid binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07651"
] | [
"ANTH"
] | [
27473
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-432722",
"R-CEL-8856825",
"R-CEL-8856828",
"R-DME-432722",
"R-DME-8856825",
"R-DME-8856828",
"R-HSA-432722",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-9696264",
"R-HSA-9700645",
"R-HSA-9725370",
"R-MMU-432722",
"R-MMU-8856825",
"R-MMU-8856828",
"R-MMU-9696264",
"R-RNO-432722",
... | [
"REACTOME:R-CEL-432722",
"REACTOME:R-CEL-8856825",
"REACTOME:R-CEL-8856828",
"REACTOME:R-DME-432722",
"REACTOME:R-DME-8856825",
"REACTOME:R-DME-8856828",
"REACTOME:R-HSA-432722",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-9696264",
"REACTOME:R-HSA-9700645",
"REACTOME:R... | 21 | [
"1hf8",
"1hfa",
"1hg2",
"1hg5",
"1hx8",
"3zyk",
"3zyl",
"3zym",
"5ahv",
"5oo7",
"7b2l",
"7jxv",
"7ost"
] | 13 | [
"PUB00014713",
"PUB00014714"
] | [
"12740367",
"12742163"
] | [
"Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains.",
"ENTH/ANTH domains expand to the Golgi."
] | [
2003,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Satyrvirus sp.",
"Splendidivirga corallicola"
] | [
27471,
1,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
75,
3,
142,
13,
24,
26,
2,
47,
35,
3,
2,
116
] | 12 | true | Domain | AP180 N-terminal homology (ANTH) domain | AP180 N-terminal homology (ANTH) domain | ANTH_dom | 1 |
IPR011419 | 11,419 | ATP12, ATP synthase F1-assembly protein | ATP12_ATP_synth-F1-assembly | Family | 7,443 | false | false | This entry represents a group proteins from eukaryotes and bacteria that may have chaperone activity and be involved in F1 ATPase complex assembly. The eukaryotic proteins include yeast ATP12 [ ] and mammalian homologue ATPAF2 (ATP synthase mitochondrial F1 complex assembly factor 2) [ ], which are required for assembl... | [
"GO:0043461"
] | [
"proton-transporting ATP synthase complex assembly"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF07542",
"PTHR21013"
] | [
"ATP12",
""
] | [
7254,
7290
] | 2 | [] | [] | [] | 0 | [
"2p4x",
"2r31",
"2r6i",
"2zd2"
] | 4 | [
"PUB00014715",
"PUB00081959"
] | [
"1826907",
"12965202"
] | [
"Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase.",
"Differential expression of ATPAF1 and ATPAF2 genes encoding F(1)-ATPase assembly proteins in mouse tissues."
] | [
1991,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2889,
4529,
25
] | 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,
2,
1,
2,
4,
2,
1,
3,
8,
1,
1,
5
] | 12 | true | Family | ATP12, ATP synthase F1-assembly protein | ATP12, ATP synthase F1-assembly protein | ATP12_ATP_synth-F1-assembly | 8 |
IPR011420 | 11,420 | Nitrogen regulatory AreA, N-terminal | AreA_N | Domain | 202 | false | false | The AreA nitrogen regulatory proteins (which are GATA type transcription factors) share a highly conserved N terminus and have at the C terminus. | [
"GO:0003677",
"GO:0008270",
"GO:0042128",
"GO:0005634"
] | [
"DNA binding",
"zinc ion binding",
"nitrate assimilation",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF07573"
] | [
"AreA_N"
] | [
202
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycetocola zhujimingii",
"leotiomyceta"
] | [
1,
201
] | 2 | [] | [] | 0 | true | Domain | Nitrogen regulatory AreA, N-terminal | Nitrogen regulatory AreA, N-terminal | AreA_N | 9 |
IPR011421 | 11,421 | BCNT-C domain | BCNT-C | Domain | 4,277 | false | false | Vertebrate BCNT (named after Bucentaur) protein is found in the nucleus and cytosol. Gene duplication of the ancestral BCNT gene leads to the h-type BCNT or craniofacial development protein 1 (CFDP1) gene and the ruminant-specific p97BCNT or craniofacial development protein 2 (CFDP2) gene. The h-type BCNT proteins cont... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF07572",
"PS51279"
] | [
"BCNT",
"BCNT_C"
] | [
4270,
4229
] | 2 | [] | [] | [] | 0 | [
"8qyv",
"8qz0"
] | 2 | [
"PUB00019215",
"PUB00043792",
"PUB00043793"
] | [
"12832649",
"16384818",
"14720462"
] | [
"A transposable element-mediated gene divergence that directly produces a novel type bovine Bcnt protein including the endonuclease domain of RTE-1.",
"A tandem gene duplication followed by recruitment of a retrotransposon created the paralogous bucentaur gene (bcntp97) in the ancestral ruminant.",
"The Drosoph... | [
2003,
2006,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Streptomyces actuosus"
] | [
4276,
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... | [
3,
1,
1,
1,
2,
1,
1,
3,
5,
1,
1,
12
] | 12 | true | Domain | BCNT-C domain | BCNT-C domain | BCNT-C | 6 |
IPR011422 | 11,422 | BRCA1-associated 2/ETP1, RRM | BRAP2/ETP1_RRM | Domain | 5,140 | false | false | This entry represents the RNA-binding domain (also referred to as RNA recognition motif (RRM)) of BRAP2 and its homologues. This entry includes human BRCA1-associated protein (BRAP/BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63) and its homo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07576"
] | [
"BRAP2"
] | [
5140
] | 1 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.2.27",
"PWY-7511",
"R-CEL-5673000",
"R-CEL-5675221",
"R-HSA-5673000",
"R-HSA-5675221",
"R-HSA-6802946",
"R-HSA-6802955",
"R-HSA-9649948",
"R-MMU-5673000",
"R-MMU-5675221"
] | [
"EC:2.3.2.27",
"METACYC:PWY-7511",
"REACTOME:R-CEL-5673000",
"REACTOME:R-CEL-5675221",
"REACTOME:R-HSA-5673000",
"REACTOME:R-HSA-5675221",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802955",
"REACTOME:R-HSA-9649948",
"REACTOME:R-MMU-5673000",
"REACTOME:R-MMU-5675221"
] | 11 | [] | 0 | [
"PUB00014718",
"PUB00033420",
"PUB00054094",
"PUB00084641",
"PUB00084644",
"PUB00084647"
] | [
"9497340",
"14724641",
"10508479",
"19416103",
"15340083",
"20040518"
] | [
"Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs.",
"Ras regulates assembly of mitogenic signalling complexes through the effector protein IMP.",
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.",
"ETP1/YHL010c is a ... | [
1998,
2004,
1999,
2009,
2004,
2010
] | 6 | [] | [
"IPR034931",
"IPR034932"
] | 0 | 2 | 0 | [
"Eukaryota"
] | [
5140
] | 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... | [
11,
1,
2,
2,
4,
2,
1,
5,
4,
1,
1,
12
] | 12 | true | Domain | BRCA1-associated 2/ETP1, RRM | BRCA1-associated 2/ETP1, RRM | BRAP2/ETP1_RRM | 7 |
IPR011425 | 11,425 | Mediator of RNA polymerase II transcription subunit 9 | Med9 | Family | 2,480 | false | false | This entry represents subunit Med9 of the Mediator complex. Subunit Med9 is part of the middle module of the Mediator complex [ ]; this associates with the core polymerase subunits to form the RNA polymerase II holoenzyme. Med9 alternatively known as the chromosome segregation protein, CSE2 ( ) is required, along with ... | [
"GO:0003712",
"GO:0006357",
"GO:0016592"
] | [
"transcription coregulator activity",
"regulation of transcription by RNA polymerase II",
"mediator complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07544"
] | [
"Med9"
] | [
2480
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1989781",
"R-HSA-381340",
"R-HSA-9833110"
] | [
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-381340",
"REACTOME:R-HSA-9833110"
] | 3 | [
"5oqm",
"5sva",
"6w1s",
"6xp5",
"7emf",
"7ena",
"7enc",
"7enj",
"7lbm",
"7nvr",
"7ui9",
"7uif",
"7uig",
"7uio",
"8cen",
"8ceo",
"8gxq",
"8gxs",
"8t1i",
"8t1l",
"8t9d",
"8tqw",
"8trh"
] | 23 | [
"PUB00014720",
"PUB00053705"
] | [
"8336709",
"19077037"
] | [
"CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae.",
"Saccharomyces cerevisiae Med9 comprises two functionally distinct domains that play different roles in transcriptional regulation."
] | [
1993,
2009
] | 2 | [] | [
"IPR039242"
] | 0 | 1 | 0 | [
"Eukaryota",
"Hylemonella gracilis"
] | [
2478,
2
] | 2 | [
"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)"
] | [
1,
2,
1,
1,
1,
2,
1
] | 7 | true | Family | Mediator of RNA polymerase II transcription subunit 9 | Mediator of RNA polymerase II transcription subunit 9 | Med9 | 8 |
IPR011426 | 11,426 | CamS sex pheromone cAM373 | CamS | Family | 2,493 | false | false | This family includes CamS ( ), from which Staphylococcus aureus sex pheromone staph-cAM373 is processed. It also includes a number of uncharacterised bacterial proteins. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07537",
"PIRSF012509"
] | [
"CamS",
"CamS"
] | [
2493,
2346
] | 2 | [] | [] | [] | 0 | [
"2qx2",
"3ib5",
"3n2q",
"4hn3"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhizophagus irregularis",
"metagenomes"
] | [
2489,
2,
2
] | 3 | [] | [] | 0 | true | Family | CamS sex pheromone cAM373 | CamS sex pheromone cAM373 | CamS | 2 |
IPR011427 | 11,427 | Chlamydia polymorphic membrane, middle domain | Polymorphic_membr_middle | Domain | 612 | false | false | This domain is found in several Chlamydia polymorphic membrane proteins [ ]. Chlamydia pneumoniae (Chlamydophila pneumoniae) is an obligate intracellular bacterium and a common human pathogen causing infection of the upper and lower respiratory tract. This domain is found between the β-helical repeats ( ) and the C-ter... | [
"GO:0019867"
] | [
"outer membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF07548"
] | [
"ChlamPMP_M"
] | [
612
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014841"
] | [
"11254597"
] | [
"Expression of Chlamydia pneumoniae polymorphic membrane protein family genes."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Chlamydia"
] | [
612
] | 1 | [] | [] | 0 | true | Domain | Chlamydia polymorphic membrane, middle domain | Chlamydia polymorphic membrane, middle domain | Polymorphic_membr_middle | 9 |
IPR011428 | 11,428 | Spore coat protein X/V | Spore_coat_X/V | Domain | 735 | false | false | This domain is found in the Bacilli coat protein X as a tandem repeat and as a single domain in coat protein V. The proteins are found in the insoluble fraction [ ]. | [
"GO:0030435",
"GO:0031160"
] | [
"sporulation resulting in formation of a cellular spore",
"spore wall"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF07552"
] | [
"Coat_X"
] | [
735
] | 1 | [] | [] | [] | 0 | [
"9lgh"
] | 1 | [
"PUB00014723"
] | [
"8509331"
] | [
"Cloning and characterization of a cluster of genes encoding polypeptides present in the insoluble fraction of the spore coat of Bacillus subtilis."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhizophagus irregularis"
] | [
734,
1
] | 2 | [] | [] | 0 | true | Domain | Spore coat protein X/V | Spore coat protein X/V | Spore_coat_X/V | 6 |
IPR011430 | 11,430 | U3 small nucleolar RNA-associated protein 20, N-terminal | UTP20_N | Domain | 4,665 | false | false | This entry represents a region of tetratricopeptide-like (TPR) repeats found towards the N-terminal of eukaryotic proteins including U3 small nucleolar RNA-associated protein 20 from yeast and the human homologue, also known as Small subunit processome component 20 homolog or DRIM (Down-Regulated In Metastasis) ( ). DR... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07539"
] | [
"UTP20_N"
] | [
4665
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-6790901",
"R-HSA-6791226",
"R-MMU-6791226",
"R-SCE-6791226",
"R-SPO-6791226"
] | [
"REACTOME:R-HSA-6790901",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226",
"REACTOME:R-SCE-6791226",
"REACTOME:R-SPO-6791226"
] | 5 | [
"6ke6",
"6lqp",
"6lqq",
"6lqr",
"6lqs",
"6lqt",
"6lqu",
"6lqv",
"6rxu",
"6rxv",
"6rxx",
"6rxz",
"6zqb",
"6zqc",
"6zqd",
"6zqe",
"7ajt",
"7aju",
"7d4i",
"7d5t",
"7d63",
"7mq8",
"7mq9",
"7mqa",
"7suk",
"9g33",
"9n6v",
"9n6w",
"9n6x",
"9n6y",
"9n6z",
"9n70"... | 41 | [
"PUB00014724",
"PUB00014725",
"PUB00101284",
"PUB00101285",
"PUB00101286"
] | [
"9673349",
"12837249",
"17498821",
"32943522",
"31378463"
] | [
"Differential gene expression in mammary carcinoma cell lines: identification of DRIM, a new gene down-regulated in metastasis.",
"A panoramic view of yeast noncoding RNA processing.",
"Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA processing.",
"Cryo-EM structure of 90<i>S</i> small r... | [
1998,
2003,
2007,
2020,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4665
] | 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... | [
9,
1,
3,
1,
1,
3,
1,
1,
2,
1,
1,
34
] | 12 | true | Domain | U3 small nucleolar RNA-associated protein 20, N-terminal | U3 small nucleolar RNA-associated protein 20, N-terminal | UTP20_N | 1 |
IPR011431 | 11,431 | Protein trafficking Pga2 | Trafficking_Pga2 | Family | 1,102 | false | false | A Saccharomyces cerevisiae (Baker's yeast) member of this family (PGA2, ) is a single pass membrane protein which is implicated in protein trafficking and processing of glycosylated proteins [ , ]. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF07543",
"PIRSF022909",
"PTHR28199"
] | [
"PGA2",
"UCP022909",
""
] | [
1078,
330,
1013
] | 3 | [] | [] | [] | 0 | [] | 0 | [
"PUB00019458",
"PUB00044766"
] | [
"14690591",
"16943325"
] | [
"Assigning function to yeast proteins by integration of technologies.",
"A survey of essential gene function in the yeast cell division cycle."
] | [
2003,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1102
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | Protein trafficking Pga2 | Protein trafficking Pga2 | Trafficking_Pga2 | 7 |
IPR011432 | 11,432 | Heme-binding protein Shr-like, Hb-interacting domain | Shr-like_HID | Domain | 599 | false | false | This entry represents the Hb-interacting domain (HID), which is found duplicated in Heme-binding protein Shr from Streptococcus pyogenes, a potentially lethal human pathogen, and in one to six copies in other uncharacterised bacterial proteins. Shr is a virulence factor that captures Hb and binds to the oxidized form o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07550"
] | [
"Shr-like_HID"
] | [
599
] | 1 | [] | [] | [] | 0 | [
"6dkq",
"7cud",
"7cue",
"8dov"
] | 4 | [
"PUB00100888",
"PUB00155965"
] | [
"30301765",
"36693107"
] | [
"The <i>Streptococcus pyogenes</i> Shr protein captures human hemoglobin using two structurally unique binding domains.",
"The Shr receptor from <i>Streptococcus pyogenes</i> uses a cap and release mechanism to acquire heme-iron from human hemoglobin."
] | [
2018,
2023
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
597,
2
] | 2 | [] | [] | 0 | true | Domain | Heme-binding protein Shr-like, Hb-interacting domain | Heme-binding protein Shr-like, Hb-interacting domain | Shr-like_HID | 5 |
IPR011434 | 11,434 | Putative host cell surface-exposed lipoprotein Ltp-like, HTH region | Ltp-like_HTH | Domain | 1,999 | false | false | This entry represents a domain found as 1 to 5 copies in proteins from bacteria and virus, including Putative host cell surface-exposed lipoprotein from Streptococcus phage TP-J34 (Ltp, ), a superinfection exclusion protein. This domain shows a three-helix bundle belonging to the HTH superfamily [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07553"
] | [
"Lipoprotein_Ltp"
] | [
1999
] | 1 | [] | [] | [] | 0 | [
"4eqq"
] | 1 | [
"PUB00101011"
] | [
"23692331"
] | [
"X-ray structure of a superinfection exclusion lipoprotein from phage TP-J34 and identification of the tape measure protein as its target."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Pancrustacea",
"Viruses",
"metagenomes"
] | [
1907,
8,
5,
64,
15
] | 5 | [] | [] | 0 | true | Domain | Putative host cell surface-exposed lipoprotein Ltp-like, HTH region | Putative host cell surface-exposed lipoprotein Ltp-like, HTH region | Ltp-like_HTH | 1 |
IPR011435 | 11,435 | Na(+), Li(+), K(+)/H(+) antiporter subunit A/B | UmpAB | Family | 3,163 | false | false | UmpAB function as a two-component Na+(Li+, K+)/H+ antiporter [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07556"
] | [
"DUF1538"
] | [
3163
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00092442"
] | [
"28652569"
] | [
"Characterization of a novel two-component Na+(Li+, K+)/H+ antiporter from Halomonas zhaodongensis."
] | [
2017
] | 1 | [] | [
"IPR048123"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Podoviridae sp. ctxJ29",
"unclassified sequences"
] | [
2836,
99,
130,
1,
97
] | 5 | [] | [] | 0 | true | Family | Na(+), Li(+), K(+)/H(+) antiporter subunit A/B | Na(+), Li(+), K(+)/H(+) antiporter subunit A/B | UmpAB | 7 |
IPR011436 | 11,436 | Domain of unknown function DUF1539 | DUF1539 | Domain | 38 | false | false | This domain is found in a small number of Chlamydia proteins of unknown function. It occurs together with . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07560"
] | [
"DUF1539"
] | [
38
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
38
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1539 | Domain of unknown function DUF1539 | DUF1539 | 5 |
IPR011437 | 11,437 | Domain of unknown function DUF1540 | DUF1540 | Domain | 4,975 | false | false | These proteins have four conserved cysteines, which is suggestive of a metal binding function. This domain may be found on its own or duplicated in the proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07561"
] | [
"DUF1540"
] | [
4975
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanoperedens nitratireducens",
"Eukaryota",
"metagenomes",
"unclassified Caudoviricetes"
] | [
4921,
1,
4,
45,
4
] | 5 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1540 | Domain of unknown function DUF1540 | DUF1540 | 7 |
IPR011438 | 11,438 | Domain of unknown function DUF1541 | DUF1541 | Domain | 1,546 | false | false | This domain is found in several hypothetical bacterial proteins as a tandem repeat. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07563"
] | [
"DUF1541"
] | [
1546
] | 1 | [] | [] | [] | 0 | [
"2ky9",
"4fib",
"4mdw"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"bioreactor metagenome"
] | [
1540,
3,
3
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1541 | Domain of unknown function DUF1541 | DUF1541 | 9 |
IPR011439 | 11,439 | Domain of unknown function DUF1542 | DUF1542 | Domain | 1,146 | false | false | This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh [ ]. Some members are involved in antibiotic resistance (e.g. and ) [ ] and/or cellular adhesion (e.g. ) [ ]. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci [ ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07564"
] | [
"DUF1542"
] | [
1146
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014727",
"PUB00014728",
"PUB00065268",
"PUB00097823",
"PUB00097824"
] | [
"10332717",
"12438342",
"22977243",
"33465168",
"22921469"
] | [
"Mrp--a new auxiliary gene essential for optimal expression of methicillin resistance in Staphylococcus aureus.",
"Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus.",
"The extracellular protein factor Epf from Streptococcus pyogenes is a cell surface ad... | [
1999,
2002,
2012,
2021,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Heliocybe sulcata",
"human gut metagenome"
] | [
1140,
1,
5
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1542 | Domain of unknown function DUF1542 | DUF1542 | 2 |
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