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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR012812 | 12,812 | Mannosyl-3-phosphoglycerate synthase | Osmo_MPG_synth | Family | 348 | false | false | This family consists of examples of mannosyl-3-phosphoglycerate synthase (MPGS), which together with mannosyl-3-phosphoglycerate phosphatase (MPGP), comprises a two-step pathway for mannosylglycerate biosynthesis. Mannosylglycerate is a compatible solute that tends to be restricted to extreme thermophiles of archaea an... | [
"GO:0050504",
"GO:0051479",
"GO:0005737"
] | [
"mannosyl-3-phosphoglycerate synthase activity",
"mannosylglycerate biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"NCBIFAM"
] | [
"PF09488",
"TIGR02460"
] | [
"Osmo_MPGsynth",
"osmo_MPGsynth"
] | [
348,
178
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"2.4.1.217",
"GenProp0281",
"PWY-5656"
] | [
"EC:2.4.1.217",
"GP:GenProp0281",
"METACYC:PWY-5656"
] | 3 | [
"2wvk",
"2wvl",
"2wvm",
"2zu7",
"2zu8",
"2zu9"
] | 6 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes",
"leotiomyceta"
] | [
75,
91,
13,
169
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Mannosyl-3-phosphoglycerate synthase | Mannosyl-3-phosphoglycerate synthase | Osmo_MPG_synth | 9 |
IPR012814 | 12,814 | Pyranose 2-oxidase | P2OX | Family | 253 | false | false | Fungal pyranose 2-oxidase (P2OX) catalyses the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O2 to H2O2. Peroxide production is believed to be important to the wood rot fungi in which this enzyme is found for lignin degradation [ , ... | [
"GO:0050233",
"GO:0050660"
] | [
"pyranose oxidase activity",
"flavin adenine dinucleotide binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02462"
] | [
"pyranose_ox"
] | [
253
] | 1 | [
"EC"
] | [
"1.1.3.10"
] | [
"EC:1.1.3.10"
] | 1 | [
"1tt0",
"1tzl",
"2f5v",
"2f6c",
"2igk",
"2igm",
"2ign",
"2igo",
"3bg6",
"3bg7",
"3bly",
"3fdy",
"3k4b",
"3k4c",
"3k4j",
"3k4k",
"3k4l",
"3k4m",
"3k4n",
"3lsh",
"3lsi",
"3lsk",
"3lsm",
"3pl8",
"4mif",
"4mig",
"4mih",
"4moe",
"4mof",
"4mog",
"4moh",
"4moi"... | 41 | [
"PUB00077038",
"PUB00077039"
] | [
"16349330",
"8661938"
] | [
"Pyranose Oxidase, a Major Source of H(2)O(2) during Wood Degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida.",
"Only C-2 specific glucose oxidase activity is expressed in ligninolytic cultures of the white rot fungus Phanerochaete chrysosporium."
] | [
1994,
1996
] | 2 | [
"IPR051473"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta"
] | [
20,
233
] | 2 | [] | [] | 0 | true | Family | Pyranose 2-oxidase | Pyranose 2-oxidase | P2OX | 8 |
IPR012815 | 12,815 | Mannosyl-3-phosphoglycerate phosphatase | MPG_Pase | Family | 446 | false | false | Members of this family are mannosyl-3-phosphoglycerate phosphatase ( ). It acts sequentially after mannosyl-3-phosphoglycerate synthase ( ) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles [ ]. | [
"GO:0050531",
"GO:0051479",
"GO:0005737"
] | [
"mannosyl-3-phosphoglycerate phosphatase activity",
"mannosylglycerate biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP"
] | [
"MF_00617"
] | [
"MPGP_rel"
] | [
446
] | 1 | [
"EC",
"METACYC"
] | [
"3.1.3.70",
"PWY-5656"
] | [
"EC:3.1.3.70",
"METACYC:PWY-5656"
] | 2 | [
"1wzc",
"1xvi",
"2zos"
] | 3 | [
"PUB00017808"
] | [
"11562374"
] | [
"Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes."
] | [
2001
] | 1 | [
"IPR006381"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Enterobacteriaceae"
] | [
14,
432
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Mannosyl-3-phosphoglycerate phosphatase | Mannosyl-3-phosphoglycerate phosphatase | MPG_Pase | 2 |
IPR012817 | 12,817 | Chlorocatechol 1,2-dioxygenase | Chlorcchol_dOase | Family | 107 | false | false | Members of this protein family are chlorocatechol 1,2-dioxygenases. This enzyme is a homodimeric intradiol dioxygenase that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is... | [
"GO:0005506"
] | [
"iron ion binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02465",
"cd03462"
] | [
"chlorocat_1_2",
"1_2-CCD"
] | [
85,
104
] | 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"... | [
"1.13.11.-",
"PWY-181",
"PWY-5163",
"PWY-5642",
"PWY-6068",
"PWY-6069",
"PWY-6084",
"PWY-6087",
"PWY-6089",
"PWY-6093",
"PWY-6094",
"PWY-6102",
"PWY-6107",
"PWY-6178",
"PWY-6190",
"PWY-6193",
"PWY-6336",
"PWY-6339",
"PWY-6667",
"PWY-7006",
"PWY-7009",
"PWY-7010",
"PWY-701... | [
"EC:1.13.11.-",
"METACYC:PWY-181",
"METACYC:PWY-5163",
"METACYC:PWY-5642",
"METACYC:PWY-6068",
"METACYC:PWY-6069",
"METACYC:PWY-6084",
"METACYC:PWY-6087",
"METACYC:PWY-6089",
"METACYC:PWY-6093",
"METACYC:PWY-6094",
"METACYC:PWY-6102",
"METACYC:PWY-6107",
"METACYC:PWY-6178",
"METACYC:PWY-... | 38 | [
"1s9a",
"2boy",
"3hgi",
"3hhx",
"3hhy",
"3hj8",
"3hjq",
"3hjs",
"3hkp",
"3i4v",
"3i4y",
"3i51",
"3o32",
"3o5u",
"3o6j",
"3o6r",
"3th1"
] | 17 | [
"PUB00015256",
"PUB00080933"
] | [
"10730195",
"16030237"
] | [
"Catechol dioxygenases.",
"Amino acids in positions 48, 52, and 73 differentiate the substrate specificities of the highly homologous chlorocatechol 1,2-dioxygenases CbnA and TcbC."
] | [
1999,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
107
] | 1 | [] | [] | 0 | true | Family | Chlorocatechol 1,2-dioxygenase | Chlorocatechol 1,2-dioxygenase | Chlorcchol_dOase | 6 |
IPR012818 | 12,818 | Precorrin-6Y methyltransferase | CbiE | Domain | 12,283 | false | false | Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants... | [
"GO:0008276",
"GO:0009236"
] | [
"protein methyltransferase activity",
"cobalamin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02467",
"cd11644"
] | [
"CbiE",
"Precorrin-6Y-MT"
] | [
11955,
12234
] | 2 | [
"EC",
"GP"
] | [
"2.1.1",
"GenProp0275"
] | [
"EC:2.1.1",
"GP:GenProp0275"
] | 2 | [
"2bb3"
] | 1 | [
"PUB00009744",
"PUB00014672",
"PUB00014680",
"PUB00014681",
"PUB00015657",
"PUB00035308",
"PUB00035309",
"PUB00035310",
"PUB00070131"
] | [
"11215515",
"11153269",
"12429089",
"1732195",
"12869542",
"17163662",
"16042605",
"12055304",
"23922391"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Multiple biosynthetic pathways for vitamin B12: variations on a central theme.",
"The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.",
"Biosynthesis of vitamin B12 in Pseudomonas... | [
2000,
2001,
2002,
1992,
2003,
2006,
2005,
2002,
2013
] | 9 | [
"IPR000878"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
610,
11570,
11,
92
] | 4 | [] | [] | 0 | true | Domain | Precorrin-6Y methyltransferase | Precorrin-6Y methyltransferase | CbiE | 7 |
IPR012820 | 12,820 | Sucrose synthase, plant/cyanobacteria | Sucrose_synthase_pln/cyn | Family | 5,641 | false | false | This entry represents sucrose synthase an enzyme that despite its name, generally uses rather produces sucrose. Sucrose plus UDP (or ADP) becomes D-fructose plus UDP-glucose (or ADP-glucose), which is then available for cell wall (or starch) biosynthesis. The enzyme is homologous to sucrose phosphate synthase, which ca... | [
"GO:0016157",
"GO:0005985"
] | [
"sucrose synthase activity",
"sucrose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR45839",
"TIGR02470"
] | [
"",
"sucr_synth"
] | [
5640,
4092
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"2.4.1.13",
"GenProp1639",
"PWY-3801"
] | [
"EC:2.4.1.13",
"GP:GenProp1639",
"METACYC:PWY-3801"
] | 3 | [
"3s27",
"3s28",
"3s29",
"4rbn"
] | 4 | [
"PUB00017811"
] | [
"11950997"
] | [
"Evolution of sucrose synthesis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
393,
5238,
10
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
40,
21,
113
] | 3 | true | Family | Sucrose synthase, plant/cyanobacteria | Sucrose synthase, plant/cyanobacteria | Sucrose_synthase_pln/cyn | 4 |
IPR012821 | 12,821 | Sucrose phosphate synthase, sucrose phosphatase-like domain | Sucrose_P_synth_Pase-like_dom | Domain | 486 | false | false | Sucrose phosphate synthase (SPS) and sucrose phosphate phosphatase (SPP) are the last two enzymes of sucrose biosynthesis. In cyanobacteria and plants, the C-terminal region of most or all versions of SPS has a domain homologous to the known SPP. This domain may serve a binding or regulatory rather than catalytic funct... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02471"
] | [
"sucr_syn_bact_C"
] | [
486
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR006380"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
472,
14
] | 2 | [] | [] | 0 | true | Domain | Sucrose phosphate synthase, sucrose phosphatase-like domain | Sucrose phosphate synthase, sucrose phosphatase-like domain | Sucrose_P_synth_Pase-like_dom | 7 |
IPR012822 | 12,822 | Sucrose-phosphate synthase, glycosyltransferase domain | SucroseP_synth_GlycoTrfase_dom | Domain | 474 | false | false | This family consists of the N-terminal regions, or in some cases the entirety, of bacterial proteins closely related to plant sucrose-phosphate synthases (SPS). The C-terminal domain ( ), found with most members of this family, resembles both bona fide plant sucrose-phosphate phosphatases (SPP) and the SPP-like domain ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02472"
] | [
"sucr_P_syn_N"
] | [
474
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
463,
11
] | 2 | [] | [] | 0 | true | Domain | Sucrose-phosphate synthase, glycosyltransferase domain | Sucrose-phosphate synthase, glycosyltransferase domain | SucroseP_synth_GlycoTrfase_dom | 4 |
IPR012823 | 12,823 | Flagellar export FliJ | Flagell_FliJ | Family | 10,192 | false | false | The bacterial flagellum consists of three major parts: the basal body (including the rod), the hook, and the filament. Outer components of the flagellum are transported to the assembly site by a specialised type III export apparatus, which is related to the type III secretion system (T3SS). FliJ is a soluble regulatory... | [
"GO:0071973",
"GO:0009288"
] | [
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"NCBIFAM"
] | [
"PF02050",
"TIGR02473"
] | [
"FliJ",
"flagell_FliJ"
] | [
10129,
8136
] | 2 | [
"GP",
"GP"
] | [
"GenProp0879",
"GenProp0885"
] | [
"GP:GenProp0879",
"GP:GenProp0885"
] | 2 | [
"3ajw",
"8ftw",
"8ftx"
] | 3 | [
"PUB00076721"
] | [
"25068520"
] | [
"Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate."
] | [
2014
] | 1 | [] | [
"IPR018006"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
10049,
17,
126
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar export FliJ | Flagellar export FliJ | Flagell_FliJ | 3 |
IPR012825 | 12,825 | 5,6-dimethylbenzimidazole synthase BluB | BluB | Family | 6,980 | false | false | A previously published hypothesis that BluB, involved in cobalamin biosynthesis [ , ], is cob(II)yrinic acid a,c-diamide reductase ( ) has now been contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis [ , ]. The BluB protein is related to the nitroreductase family. | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02476",
"cd02145"
] | [
"BluB",
"BluB"
] | [
6980,
2449
] | 2 | [
"EC",
"METACYC"
] | [
"1.13.11.79",
"PWY-5523"
] | [
"EC:1.13.11.79",
"METACYC:PWY-5523"
] | 2 | [
"2isj",
"2isk",
"2isl"
] | 3 | [
"PUB00002275",
"PUB00015657",
"PUB00047736",
"PUB00056791"
] | [
"7635831",
"12869542",
"17377583",
"17301238"
] | [
"Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus.",
"Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.",
"BluB cannibalizes flavin to form the lower ligand of vitamin B12.",
"Single-enzyme conve... | [
1995,
2003,
2007,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
183,
6713,
20,
64
] | 4 | [] | [] | 0 | true | Family | 5,6-dimethylbenzimidazole synthase BluB | 5,6-dimethylbenzimidazole synthase BluB | BluB | 1 |
IPR012826 | 12,826 | Flagellar motor switch FliN | FliN | Family | 11,930 | false | false | The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour [ ]. The switch co... | [
"GO:0006935",
"GO:0071973",
"GO:0009288",
"GO:0016020"
] | [
"chemotaxis",
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"NCBIFAM"
] | [
"TIGR02480"
] | [
"fliN"
] | [
11930
] | 1 | [
"GP",
"GP",
"GP"
] | [
"GenProp0883",
"GenProp1183",
"GenProp1194"
] | [
"GP:GenProp0883",
"GP:GenProp1183",
"GP:GenProp1194"
] | 3 | [
"1o6a",
"1yab",
"4yxb",
"4yxc",
"5xrw",
"8umd",
"8umx",
"8uox",
"8upl",
"8vib",
"8vid",
"8vkq",
"8vkr",
"8wiw",
"8wo5",
"8woe",
"8xp0",
"8xp1",
"8yjt",
"9n49",
"9n4z"
] | 21 | [
"PUB00001834",
"PUB00002083",
"PUB00002290",
"PUB00004790"
] | [
"8224881",
"2656645",
"8631704",
"1631122"
] | [
"Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.",
"Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.",
"A mutational analysis of the interaction between FliG and FliM, two compone... | [
1993,
1989,
1996,
1992
] | 4 | [
"IPR001172"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11761,
15,
154
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar motor switch FliN | Flagellar motor switch FliN | FliN | 1 |
IPR012827 | 12,827 | Hemerythrin, metal-binding domain | Hemerythrin_metal-bd | Domain | 8,727 | false | false | The hemerythrin family is composed of hemerythrin proteins found in invertebrates, and a broader collection of bacterial and archaeal homologues. Hemerythrin is an oxygen-binding protein found in the vascular system and coelomic fluid, or in muscles (myohemerythrin) in invertebrates [ ]. Many of the homologous proteins... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02481",
"cd12107"
] | [
"hemeryth_dom",
"Hemerythrin"
] | [
8420,
8687
] | 2 | [] | [] | [] | 0 | [
"1a7d",
"1a7e",
"1hmd",
"1hmo",
"1i4y",
"2avk",
"2awc",
"2awy",
"2hmq",
"2hmz",
"2mhr",
"3agt",
"3agu",
"3waq",
"3whn",
"4xpw",
"4xpx",
"4xpy",
"4xq1"
] | 19 | [
"PUB00001429",
"PUB00001615",
"PUB00003224",
"PUB00004613",
"PUB00005066"
] | [
"1425663",
"2065779",
"3681996",
"3856224",
"2362933"
] | [
"Ovohemerythrin, a major 14-kDa yolk protein distinct from vitellogenin in leech.",
"Primary structure of myohemerythrin from the annelid Nereis diversicolor.",
"Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution.",
"Active site structures of deoxyhemerythrin and oxyhemerythrin.",
"Th... | [
1992,
1991,
1987,
1985,
1990
] | 5 | [
"IPR012312"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
94,
7926,
512,
195
] | 4 | [] | [] | 0 | true | Domain | Hemerythrin, metal-binding domain | Hemerythrin, metal-binding domain | Hemerythrin_metal-bd | 7 |
IPR012828 | 12,828 | ATP-dependent 6-phosphofructokinase, prokaryotic | PFKA_ATP_prok | Family | 9,928 | false | false | 6-phosphofructokinase ( ), a key regulatory enzyme in glycolysis, catalyses the addition of phosphate from ATP to fructose 6-phosphate to give fructose 1,6-bisphosphate. This represents a key control step in glycolysis. This entry contains bacterial ATP-dependent 6-phosphofructokinases, which lack a β-hairpin loop pres... | [
"GO:0003872",
"GO:0005524",
"GO:0006002",
"GO:0006096"
] | [
"6-phosphofructokinase activity",
"ATP binding",
"fructose 6-phosphate metabolic process",
"glycolytic process"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00339",
"TIGR02482",
"cd00763"
] | [
"Phosphofructokinase_I_B1",
"PFKA_ATP",
"Bacterial_PFK"
] | [
9891,
9741,
2741
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.11",
"GenProp0694",
"GenProp1306",
"GenProp1407",
"GenProp1599",
"GenProp1705",
"PWY-1042",
"PWY-1861",
"PWY-5484",
"PWY-7385"
] | [
"EC:2.7.1.11",
"GP:GenProp0694",
"GP:GenProp1306",
"GP:GenProp1407",
"GP:GenProp1599",
"GP:GenProp1705",
"METACYC:PWY-1042",
"METACYC:PWY-1861",
"METACYC:PWY-5484",
"METACYC:PWY-7385"
] | 10 | [
"1mto",
"1pfk",
"1zxx",
"2pfk",
"3pfk",
"3u39",
"4a3s",
"4i36",
"4i4i",
"4i7e",
"4pfk",
"5xoe",
"5xz6",
"5xz7",
"5xz8",
"5xz9",
"5xza",
"6pfk"
] | 18 | [] | [] | [] | [] | 0 | [
"IPR012003"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"Opisthokonta",
"Siphoviridae sp. ctx254",
"metagenomes"
] | [
9829,
33,
12,
1,
53
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | ATP-dependent 6-phosphofructokinase, prokaryotic | ATP-dependent 6-phosphofructokinase, prokaryotic | PFKA_ATP_prok | 6 |
IPR012829 | 12,829 | Phosphofructokinase, mixed-substrate PFK group III | Phosphofructokinase_III | Family | 8,419 | false | false | This entry includes pyrophosphate--fructose 6-phosphate 1-phosphotransferase from Amycolatopsis methanolica [ ] and ATP-dependent 6-phosphofructokinase 2 from Streptomyces coelicolor [ ]. They catalyzes 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"
] | [
"MF_01976",
"TIGR02483"
] | [
"Phosphofructokinase_III",
"PFK_mixed"
] | [
8409,
6027
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.11",
"PWY-1042",
"PWY-1861",
"PWY-5484",
"PWY-7385"
] | [
"EC:2.7.1.11",
"METACYC:PWY-1042",
"METACYC:PWY-1861",
"METACYC:PWY-5484",
"METACYC:PWY-7385"
] | 5 | [] | 0 | [
"PUB00014446",
"PUB00017820"
] | [
"11717283",
"9055413"
] | [
"Different physiological roles of ATP- and PP(i)-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica.",
"Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)."
] | [
2001,
1997
] | 2 | [
"IPR012003"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
32,
8181,
10,
196
] | 4 | [] | [] | 0 | true | Family | Phosphofructokinase, mixed-substrate PFK group III | Phosphofructokinase, mixed-substrate PFK group III | Phosphofructokinase_III | 6 |
IPR012830 | 12,830 | Citrate utilization protein B | CitB | Family | 2,171 | false | false | This entry identifies proteins that are decribed as citrate utilization protein B, restricted to the proteobacteria. CitB [ ] has been identified in Salmonella and Escherichia coli as the signal transduction component of a two-component system for citrate in which CitA acts as a citrate transporter. This domain is also... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF27541",
"TIGR02484"
] | [
"CitB",
"CitB"
] | [
2171,
1961
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016702",
"PUB00016912",
"PUB00106878"
] | [
"15525640",
"1718953",
"30222098"
] | [
"Identification and characterization of a novel vitamin B12 (cobalamin) biosynthetic enzyme (CobZ) from Rhodobacter capsulatus, containing flavin, heme, and Fe-S cofactors.",
"Cloning and nucleotide sequence of the gene (citA) encoding a citrate carrier from Salmonella typhimurium.",
"The monofunctional cobalam... | [
2005,
1991,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
16,
2140,
2,
13
] | 4 | [] | [] | 0 | true | Family | Citrate utilization protein B | Citrate utilization protein B | CitB | 1 |
IPR012831 | 12,831 | Precorrin 3B synthase CobZ | CobZ | Family | 1,884 | false | false | Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02485"
] | [
"CobZ_N-term"
] | [
1884
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009744",
"PUB00014672",
"PUB00015657",
"PUB00016702",
"PUB00035308",
"PUB00035309",
"PUB00035310",
"PUB00070131",
"PUB00106694",
"PUB00106878"
] | [
"11215515",
"11153269",
"12869542",
"15525640",
"17163662",
"16042605",
"12055304",
"23922391",
"17630784",
"30222098"
] | [
"Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.",
"Multiple biosynthetic pathways for vitamin B12: variations on a central theme.",
"Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.",
"Identification and characterization of a novel vitamin B12 (cobalamin) bios... | [
2000,
2001,
2003,
2005,
2006,
2005,
2002,
2013,
2007,
2018
] | 10 | [
"IPR050315"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
7,
1871,
6
] | 3 | [] | [] | 0 | true | Family | Precorrin 3B synthase CobZ | Precorrin 3B synthase CobZ | CobZ | 2 |
IPR012832 | 12,832 | Reductive dehalogenase | RDH | Domain | 1,062 | false | false | This entry represents the C-terminal domain in corrin and 8-iron Fe-S cluster-containing reductive dehalogenase [ ] found primarily in halorespiring microorganisms such as Dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterised enzyme i... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02486"
] | [
"RDH"
] | [
1062
] | 1 | [
"EC"
] | [
"1.21.99.5"
] | [
"EC:1.21.99.5"
] | 1 | [
"4uqu",
"4ur0",
"4ur1",
"4ur2",
"4ur3",
"5m2g",
"5m8u",
"5m8w",
"5m8x",
"5m8y",
"5m8z",
"5m90",
"5m91",
"5m92",
"5ma0",
"5ma1",
"5ma2",
"5maa",
"5obi",
"5obp",
"8q4h"
] | 21 | [
"PUB00016698",
"PUB00016713"
] | [
"11097881",
"9224702"
] | [
"Trichloroethene reductive dehalogenase from Dehalococcoides ethenogenes: sequence of tceA and substrate range characterization.",
"Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus."
] | [
2000,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"unclassified sequences"
] | [
5,
1008,
49
] | 3 | [] | [] | 0 | true | Domain | Reductive dehalogenase | Reductive dehalogenase | RDH | 6 |
IPR012833 | 12,833 | Ribonucleoside-triphosphate reductase, anaerobic | NrdD | Family | 15,065 | false | false | This entry represents anaerobic, class III ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centred radical [ ], a C-terminal zinc binding site [ ], and a set of conserved active site cysteines and asparagines [ ]. This enzyme requires an activating component, NrdG, a radical-SAM domain containi... | [
"GO:0008998",
"GO:0016491",
"GO:0006260"
] | [
"ribonucleoside-triphosphate reductase (thioredoxin) activity",
"oxidoreductase activity",
"DNA replication"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"NCBIFAM",
"NCBIFAM",
"CDD"
] | [
"PF13597",
"TIGR02487",
"TIGR02827",
"cd01675"
] | [
"NRDD",
"NrdD",
"RNR_anaer_Bdell",
"RNR_III"
] | [
15065,
11333,
534,
8977
] | 4 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.1.98.6",
"GenProp0291",
"GenProp1343",
"GenProp1446",
"GenProp1484",
"GenProp1621",
"PWY-7187",
"PWY-7220",
"PWY-7222"
] | [
"EC:1.1.98.6",
"GP:GenProp0291",
"GP:GenProp1343",
"GP:GenProp1446",
"GP:GenProp1484",
"GP:GenProp1621",
"METACYC:PWY-7187",
"METACYC:PWY-7220",
"METACYC:PWY-7222"
] | 9 | [
"1h78",
"1h79",
"1h7a",
"1h7b",
"1hk8",
"4coi",
"4coj",
"4col",
"4com",
"4con",
"4u3e",
"8p23",
"8p27",
"8p28",
"8p2c",
"8p2d",
"8p2s",
"8p39"
] | 18 | [
"PUB00016693",
"PUB00016704",
"PUB00016706",
"PUB00033790",
"PUB00060768"
] | [
"11526118",
"10066165",
"12655046",
"10574800",
"15158709"
] | [
"Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4.",
"A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.",
"A metal-binding site in the catalytic subunit of anaerobic ribonucleotide... | [
2001,
1999,
2003,
1999,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
553,
12884,
198,
1041,
389
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonucleoside-triphosphate reductase, anaerobic | Ribonucleoside-triphosphate reductase, anaerobic | NrdD | 7 |
IPR012834 | 12,834 | Flagellar basal-body rod FlgG | FlgG_G_neg | Family | 9,799 | false | false | This family consists of the FlgG protein of the flagellar apparatus in bacteria. The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod [ ]. The rod consists of about 26 subunits of flgG in the distal portion, and flgB, flgC and flgF are ... | [
"GO:0071973",
"GO:0009426"
] | [
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum basal body, distal rod"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02488"
] | [
"flgG_G_neg"
] | [
9799
] | 1 | [
"GP"
] | [
"GenProp0880"
] | [
"GP:GenProp0880"
] | 1 | [
"5wrh",
"6jzr",
"7bin",
"7cbm",
"7cgo",
"7e80",
"7e82",
"7nvg",
"8wki",
"8wkk",
"8wl2",
"8wlp",
"8wlq",
"8wlt",
"8wo5",
"8woe",
"8z5u",
"8z5w",
"8z60"
] | 19 | [
"PUB00033604"
] | [
"15136044"
] | [
"In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella."
] | [
2004
] | 1 | [
"IPR020013"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9664,
24,
111
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar basal-body rod FlgG | Flagellar basal-body rod FlgG | FlgG_G_neg | 2 |
IPR012835 | 12,835 | Flagellar hook FlgE | FlgE_epsilon | Family | 449 | false | false | Members of this family are flagellar hook proteins, designated FlgE, as found in the epsilon subdivision of the proteobacteria (Helicobacter, Wolinella, and Campylobacter). These proteins differ significantly in architecture from proteins designated FlgE in other lineages; the N-terminal and C-terminal domains are homo... | [
"GO:0044781",
"GO:0009288"
] | [
"bacterial-type flagellum organization",
"bacterial-type flagellum"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02489"
] | [
"flgE_epsilon"
] | [
449
] | 1 | [] | [] | [] | 0 | [
"5az4",
"5jxl"
] | 2 | [
"PUB00017823"
] | [
"9658019"
] | [
"The central, surface-exposed region of the flagellar hook protein FlgE of Campylobacter jejuni shows hypervariability among strains."
] | [
1998
] | 1 | [
"IPR020013"
] | [] | 1 | 0 | 1 | [
"Campylobacterota",
"hydrothermal vent metagenome"
] | [
445,
4
] | 2 | [] | [] | 0 | true | Family | Flagellar hook FlgE | Flagellar hook FlgE | FlgE_epsilon | 8 |
IPR012836 | 12,836 | Flagellar basal-body rod FlgF | FlgF | Family | 6,129 | false | false | FlgF is a flagellar basal-body protein that along with FlgBCG composes the rod of bacterial flagellin [ ]. This entry contains proteins only from the proteobacteria, and not in the epsilon subdivision (where the architecture of the related FlgE protein differs substantially from other lineages). | [
"GO:0071973",
"GO:0030694"
] | [
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum basal body, rod"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02490"
] | [
"flgF"
] | [
6129
] | 1 | [
"GP"
] | [
"GenProp0880"
] | [
"GP:GenProp0880"
] | 1 | [
"8z5s",
"8z5u",
"8z5w",
"8z60"
] | 4 | [
"PUB00033604"
] | [
"15136044"
] | [
"In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella."
] | [
2004
] | 1 | [
"IPR020013"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6048,
4,
77
] | 3 | [] | [] | 0 | true | Family | Flagellar basal-body rod FlgF | Flagellar basal-body rod FlgF | FlgF | 8 |
IPR012837 | 12,837 | Ribonucleoside-triphosphate reductase activating, anaerobic | NrdG | Family | 8,573 | false | false | This enzyme [ ] is a member of the radical-SAM protein and utilises S-adenosyl methionine, an iron-sulphur cluster and a reductant (dihydroflavodoxin [ ]) to produce a glycine-centred radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, ). The two components form an alpha-2/beta-2 heterodim... | [
"GO:0043365",
"GO:0051539"
] | [
"[formate-C-acetyltransferase]-activating enzyme activity",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PIRSF",
"SFLD",
"NCBIFAM"
] | [
"PIRSF000368",
"SFLDF00299",
"TIGR02491"
] | [
"NrdG",
"anaerobic_ribonucleoside-triph",
"NrdG"
] | [
7501,
8422,
7430
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"1.97.1.-",
"GenProp0291",
"PWY-6530"
] | [
"EC:1.97.1.-",
"GP:GenProp0291",
"METACYC:PWY-6530"
] | 3 | [] | 0 | [
"PUB00016703",
"PUB00016711"
] | [
"11389585",
"11297442"
] | [
"Activation of class III ribonucleotide reductase from E. coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine.",
"Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center."
] | [
2001,
2001
] | 2 | [
"IPR034457"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"Viruses",
"unclassified sequences"
] | [
7925,
7,
13,
571,
57
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonucleoside-triphosphate reductase activating, anaerobic | Ribonucleoside-triphosphate reductase activating, anaerobic | NrdG | 2 |
IPR012838 | 12,838 | Pyruvate formate-lyase 1 activating enzyme | PFL1_activating | Family | 7,577 | false | false | Pyruvate formate lyase-activating enzyme is a 28kDa monomeric protein which is involved in the anerobic glucose metabolism pathway. It is a member of the radical S-adenosylmethionine family of enzymes which initiate radical catalysis. It is necessary to activate pyruvate formate lyase (PFL), which catalyses the convers... | [
"GO:0043365"
] | [
"[formate-C-acetyltransferase]-activating enzyme activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02493"
] | [
"PFLA"
] | [
7577
] | 1 | [
"EC",
"GP"
] | [
"1.97.1.4",
"GenProp0943"
] | [
"EC:1.97.1.4",
"GP:GenProp0943"
] | 2 | [
"3c8f",
"3cb8",
"8fo0",
"8fol",
"8fsi"
] | 5 | [
"PUB00044952"
] | [
"15581584"
] | [
"Pyruvate formate-lyase activating enzyme: elucidation of a novel mechanism for glycyl radical formation."
] | [
2005
] | 1 | [
"IPR012839"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified Caudoviricetes"
] | [
7504,
48,
23,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Pyruvate formate-lyase 1 activating enzyme | Pyruvate formate-lyase 1 activating enzyme | PFL1_activating | 9 |
IPR012839 | 12,839 | Organic radical enzyme activase | Organic_radical_activase | Family | 11,931 | false | false | This subset of the radical-SAM domain includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centred radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, , ) and the anaerobic ribonucleotide reductase activating enzyme (... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PIRSF"
] | [
"PIRSF000371"
] | [
"PFL_act_enz"
] | [
11931
] | 1 | [
"EC"
] | [
"1.97.1"
] | [
"EC:1.97.1"
] | 1 | [
"3c8f",
"3cb8",
"8fo0",
"8fol",
"8fsi"
] | 5 | [
"PUB00016705",
"PUB00016707",
"PUB00016708",
"PUB00090957"
] | [
"15153112",
"12704244",
"14735297",
"28183913"
] | [
"Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity.",
"Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum.",
"Genes involved in the anaerobic degradation of toluene in a denitr... | [
2004,
2003,
2004,
2017
] | 4 | [
"IPR034457"
] | [
"IPR012838",
"IPR033974",
"IPR040074"
] | 1 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes",
"unclassified Caudoviricetes"
] | [
33,
11824,
3,
69,
2
] | 5 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Family | Organic radical enzyme activase | Organic radical enzyme activase | Organic_radical_activase | 9 |
IPR012840 | 12,840 | Anaerobic ribonucleoside-triphosphate reductase activating protein | NrdG2 | Family | 3,491 | false | false | This enzyme is a member of the radical-SAM family. It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, ) and presumably fulfils the identical function as NrdG [ , ], which utilises S-adenosyl methionine, an iron-sulphur cluster and a reductant (dihydroflavodoxin) to pr... | [] | [] | [] | 0 | [
"SFLD",
"NCBIFAM"
] | [
"SFLDG01094",
"TIGR02495"
] | [
"Uncharacterised_Radical_SAM_Su",
"NrdG2"
] | [
3452,
3431
] | 2 | [
"GP"
] | [
"GenProp0291"
] | [
"GP:GenProp0291"
] | 1 | [] | 0 | [
"PUB00016703",
"PUB00016711",
"PUB00093688"
] | [
"11389585",
"11297442",
"26536144"
] | [
"Activation of class III ribonucleotide reductase from E. coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine.",
"Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center.",
"A Ferredoxin Disulfide Reductase ... | [
2001,
2001,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
339,
2896,
3,
159,
94
] | 5 | [] | [] | 0 | true | Family | Anaerobic ribonucleoside-triphosphate reductase activating protein | Anaerobic ribonucleoside-triphosphate reductase activating protein | NrdG2 | 8 |
IPR012842 | 12,842 | Type 3 secretion system stator protein SctL/SctL2 | T3SS_SctL/SctL2 | Family | 2,131 | false | false | This entry represents Type 3 secretion system stator proteins (also referred to HrpE-like proteins), which are the cytoplasmic components of bacterial type III secretion systems [ ]. Type 3 secretion systems (T3SSs) are used by many different Gram-negative pathogens and symbionts to inject bacterial effector proteins i... | [
"GO:0030254"
] | [
"protein secretion by the type III secretion system"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02499"
] | [
"HrpE_YscL_not"
] | [
2131
] | 1 | [
"GP"
] | [
"GenProp0052"
] | [
"GP:GenProp0052"
] | 1 | [] | 0 | [
"PUB00034695",
"PUB00097915",
"PUB00097916",
"PUB00097917"
] | [
"16672607",
"20453832",
"24722491",
"30107569"
] | [
"Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL.",
"Deciphering the assembly of the Yersinia type III secretion injectisome.",
"Functional characterization of the type III secretion ATPase SsaN encoded by Salmonella pathogenicity island 2.",
"Bacterial t... | [
2006,
2010,
2014,
2018
] | 4 | [] | [
"IPR010586"
] | 0 | 1 | 0 | [
"Bacteria",
"metagenomes"
] | [
2124,
7
] | 2 | [] | [] | 0 | true | Family | Type 3 secretion system stator protein SctL/SctL2 | Type 3 secretion system stator protein SctL/SctL2 | T3SS_SctL/SctL2 | 6 |
IPR012843 | 12,843 | YscD | YscD | Family | 1,497 | false | false | This family represents YscD from proteobacteria and similar putative type III secretion system bacteria such as HrpQ in Pseudomonas syringae, and EscD in enteropathogenic Escherichia coli. In the Chlamydiae, this entry describes the C-terminal 400 residues of a longer protein. YscD is a single-pass inner membrane prote... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02500"
] | [
"type_III_yscD"
] | [
1497
] | 1 | [
"GP"
] | [
"GenProp0052"
] | [
"GP:GenProp0052"
] | 1 | [
"4a0e",
"4alz",
"4d9v"
] | 3 | [
"PUB00020581",
"PUB00076172"
] | [
"1860816",
"23908767"
] | [
"Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica.",
"In situ structural analysis of the Yersinia enterocolitica injectisome."
] | [
1991,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bracon brevicornis",
"metagenomes"
] | [
1494,
1,
2
] | 3 | [] | [] | 0 | true | Family | YscD | YscD | YscD | 8 |
IPR012844 | 12,844 | Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain | DhaM_N | Domain | 4,815 | false | false | In Escherichia coli and many other bacteria, unlike the yeasts and a few bacteria such as Citrobacter freundii, the dihydroxyacetone kinase (also called glycerone kinase) transfers a phosphate from a phosphoprotein rather than from ATP. The dihydroxyacetone kinase of Escherichia coli consists of three subunits: DhaK, D... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02364"
] | [
"dha_pts"
] | [
4815
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.7.1.121",
"GenProp1146",
"GenProp1324"
] | [
"EC:2.7.1.121",
"GP:GenProp1146",
"GP:GenProp1324"
] | 3 | [
"3b48",
"3cr3",
"3ct6"
] | 3 | [
"PUB00033180"
] | [
"11350937"
] | [
"The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor."
] | [
2001
] | 1 | [
"IPR004701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Ecdysozoa",
"Methanobacteriota",
"metagenomes"
] | [
4702,
3,
100,
10
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain | Dihydroxyacetone kinase phosphotransferase subunit, N-terminal domain | DhaM_N | 8 |
IPR012845 | 12,845 | RNA polymerase sigma factor, FliA/WhiG | RNA_pol_sigma_FliA_WhiG | Family | 10,988 | false | false | Most members of this family are the flagellar operon sigma factor FliA, controlling transcription of bacterial flagellar genes by RNA polymerase. An exception is the sigma factor WhiG in the genus Streptomyces, involved in the production of sporulating aerial mycelium. The bacterial core RNA polymerase complex, which c... | [
"GO:0003677",
"GO:0003899",
"GO:0016987",
"GO:0006352",
"GO:0006355"
] | [
"DNA binding",
"DNA-directed RNA polymerase activity",
"sigma factor activity",
"DNA-templated transcription initiation",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"NCBIFAM"
] | [
"TIGR02479"
] | [
"FliA_WhiG"
] | [
10988
] | 1 | [] | [] | [] | 0 | [
"1rp3",
"1sc5",
"6pfj",
"6pfv",
"6pmi",
"6pmj"
] | 6 | [
"PUB00000061",
"PUB00002181",
"PUB00004340",
"PUB00088319"
] | [
"3052291",
"1597408",
"3092189",
"25596450"
] | [
"Structure and function of bacterial sigma factors.",
"The sigma 70 family: sequence conservation and evolutionary relationships.",
"Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.",
"Plastid sigma factors: Their individual functions and regulation in transcription."... | [
1988,
1992,
1986,
2015
] | 4 | [] | [
"IPR028617"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
10807,
12,
169
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | RNA polymerase sigma factor, FliA/WhiG | RNA polymerase sigma factor, FliA/WhiG | RNA_pol_sigma_FliA_WhiG | 4 |
IPR012846 | 12,846 | Acetolactate synthase, large subunit, biosynthetic | Acetolactate_synth_lsu | Family | 32,325 | false | false | Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this entry also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyac... | [
"GO:0000287",
"GO:0003984",
"GO:0030976",
"GO:0050660",
"GO:0009082"
] | [
"magnesium ion binding",
"acetolactate synthase activity",
"thiamine pyrophosphate binding",
"flavin adenine dinucleotide binding",
"branched-chain amino acid biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 5 | [
"NCBIFAM"
] | [
"TIGR00118"
] | [
"acolac_lg"
] | [
32325
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.2.1.6",
"GenProp0162",
"GenProp0163",
"GenProp0164",
"GenProp1342",
"PWY-5101",
"PWY-5103",
"PWY-5104",
"PWY-5938",
"PWY-5939",
"PWY-6389",
"PWY-7111"
] | [
"EC:2.2.1.6",
"GP:GenProp0162",
"GP:GenProp0163",
"GP:GenProp0164",
"GP:GenProp1342",
"METACYC:PWY-5101",
"METACYC:PWY-5103",
"METACYC:PWY-5104",
"METACYC:PWY-5938",
"METACYC:PWY-5939",
"METACYC:PWY-6389",
"METACYC:PWY-7111"
] | 12 | [
"1jsc",
"1n0h",
"1t9a",
"1t9b",
"1t9c",
"1t9d",
"1ybh",
"1yhy",
"1yhz",
"1yi0",
"1yi1",
"1z8n",
"3e9y",
"3ea4",
"5fem",
"5ims",
"5k2o",
"5k3s",
"5k6q",
"5k6r",
"5k6t",
"5wj1",
"5wkc",
"6bd3",
"6bd9",
"6dek",
"6del",
"6dem",
"6den",
"6deo",
"6dep",
"6deq"... | 52 | [] | [] | [] | [] | 0 | [
"IPR045229"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
796,
27530,
3606,
393
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
3,
1,
5,
1,
1,
8
] | 7 | true | Family | Acetolactate synthase, large subunit, biosynthetic | Acetolactate synthase, large subunit, biosynthetic | Acetolactate_synth_lsu | 7 |
IPR012847 | 12,847 | Sucrose phosphatase, plant/cyanobacteria | Sucrose_phosphatase_pln/cyn | Family | 1,647 | false | false | This entry describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). However, a closely related group of sequences from bacteria and archaea may prove to catalyze the same reaction. SPP is a member of the Class IIB subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleop... | [
"GO:0000287",
"GO:0050307",
"GO:0005986"
] | [
"magnesium ion binding",
"sucrose-phosphate phosphatase activity",
"sucrose biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR01485"
] | [
"SPP_plant-cyano"
] | [
1647
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.1.3.24",
"PWY-7238",
"PWY-7347"
] | [
"EC:3.1.3.24",
"METACYC:PWY-7238",
"METACYC:PWY-7347"
] | 3 | [
"1s2o",
"1tj3",
"1tj4",
"1tj5",
"1u2s",
"1u2t",
"2b1q",
"2b1r",
"2d2v"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
222,
1425
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
18,
6,
24
] | 3 | true | Family | Sucrose phosphatase, plant/cyanobacteria | Sucrose phosphatase, plant/cyanobacteria | Sucrose_phosphatase_pln/cyn | 2 |
IPR012848 | 12,848 | Aspartic peptidase, N-terminal | Aspartic_peptidase_N | Domain | 6,409 | false | false | This entry represents the N-terminal domain of the aspartic peptidases. | [
"GO:0004190",
"GO:0006508"
] | [
"aspartic-type endopeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF07966"
] | [
"A1_Propeptide"
] | [
6409
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.4.23",
"GenProp1728",
"R-CEL-2022377",
"R-CFA-1442490",
"R-CFA-2022377",
"R-CFA-2132295",
"R-CFA-5683826",
"R-CFA-6798695",
"R-CFA-77387",
"R-HSA-1442490",
"R-HSA-2022377",
"R-HSA-2132295",
"R-HSA-5683826",
"R-HSA-6798695",
"R-HSA-77387",
"R-HSA-9018519",
"R-MMU-1442490",
"R-MMU... | [
"EC:3.4.23",
"GP:GenProp1728",
"REACTOME:R-CEL-2022377",
"REACTOME:R-CFA-1442490",
"REACTOME:R-CFA-2022377",
"REACTOME:R-CFA-2132295",
"REACTOME:R-CFA-5683826",
"REACTOME:R-CFA-6798695",
"REACTOME:R-CFA-77387",
"REACTOME:R-HSA-1442490",
"REACTOME:R-HSA-2022377",
"REACTOME:R-HSA-2132295",
"RE... | 27 | [
"1avf",
"1htr",
"1tzs",
"2psg",
"2x0b",
"3psg",
"3vcm",
"4amt",
"5mkt",
"5ux4"
] | 10 | [
"PUB00000093",
"PUB00000349",
"PUB00001330"
] | [
"2194475",
"1851433",
"6795036"
] | [
"The structure and function of the aspartic proteinases.",
"Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.",
"Gastric proteinases--structure, function, evolution and mechanism of action."
] | [
1990,
1991,
1981
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Nocardioides humilatus"
] | [
6408,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
1,
34,
26,
17
] | 6 | true | Domain | Aspartic peptidase, N-terminal | Aspartic peptidase, N-terminal | Aspartic_peptidase_N | 3 |
IPR012849 | 12,849 | Abl-interactor, homeo-domain homologous domain | Abl-interactor_HHR_dom | Domain | 8,173 | false | false | The region is found towards the N terminus of a number of adaptor proteins that interact with Abl-family tyrosine kinases [ ]. More specifically, it is termed the homeo-domain homologous region (HHR), as it is similar to the DNA-binding region of homeo-domain proteins [ ]. Other homeo-domain proteins have been implicat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07815"
] | [
"Abi_HHR"
] | [
8173
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2029482",
"R-HSA-4420097",
"R-HSA-5663213",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013423",
"R-HSA-9664422",
"R-MMU-2029482",
"R-MMU-4420097",
"R-MMU-5663213",
"R-MMU-9013149",
"R-MMU-9013404",
"R-MMU-9013423",
"R-RNO-2029482",
"R-RNO-4420097",
"R-RNO-5663213",
"R-RNO-90131... | [
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-4420097",
"REACTOME:R-HSA-5663213",
"REACTOME:R-HSA-9013149",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013423",
"REACTOME:R-HSA-9664422",
"REACTOME:R-MMU-2029482",
"REACTOME:R-MMU-4420097",
"REACTOME:R-MMU-5663213",
"REACTOME:R-MMU-9013149",
"REACTOM... | 18 | [
"3p8c",
"4n78",
"7usc",
"7usd",
"7use"
] | 5 | [
"PUB00016372",
"PUB00016604"
] | [
"7590236",
"12011975"
] | [
"Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity.",
"In search of a function for the E3B1/Abi2/Argbp1/NESH family (Review)."
] | [
1995,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
8173
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
52,
3,
18,
25,
25
] | 6 | true | Domain | Abl-interactor, homeo-domain homologous domain | Abl-interactor, homeo-domain homologous domain | Abl-interactor_HHR_dom | 6 |
IPR012850 | 12,850 | Alpha-amylase, C-terminal beta-sheet | A-amylase_bs_C | Domain | 3,672 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004556",
"GO:0005509",
"GO:0005975"
] | [
"alpha-amylase activity",
"calcium ion binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"SMART"
] | [
"PF07821",
"SM00810"
] | [
"Alpha-amyl_C2",
"Alpha-amyl_C2"
] | [
3669,
3620
] | 2 | [
"EC"
] | [
"3.2.1.1"
] | [
"EC:3.2.1.1"
] | 1 | [
"1amy",
"1ava",
"1bg9",
"1ht6",
"1p6w",
"1rp8",
"1rp9",
"1rpk",
"2qps",
"2qpu",
"3bsg",
"3bsh",
"3wn6"
] | 13 | [
"PUB00004870",
"PUB00005266",
"PUB00016439",
"PUB00016510",
"PUB00027666"
] | [
"7624375",
"8535779",
"9571044",
"8196040",
"11141191"
] | [
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrolases.",
"Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.",
"Crystal and molecular struc... | [
1995,
1995,
1998,
1994,
2001
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
173,
3497,
2
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
10,
28,
24
] | 3 | true | Domain | Alpha-amylase, C-terminal beta-sheet | Alpha-amylase, C-terminal beta-sheet | A-amylase_bs_C | 8 |
IPR012851 | 12,851 | Spore coat protein CotF-like | Spore_coat_CotF-like | Family | 5,847 | false | false | The Coat F proteins contribute to the Bacillales spore coat. They occur multiple times in the genomes in which they are found. Bacillus subtilis endospore protein coats protect them and may play a role in their germination [ ]. Spore coat protein F, on the outer surface of the endospore, is one of a suite of proteins t... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07875",
"PTHR39183"
] | [
"Coat_F",
""
] | [
5430,
2943
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044606",
"PUB00044607"
] | [
"18723620",
"14711677"
] | [
"Characterization of spores of Bacillus subtilis that lack most coat layers.",
"Species differentiation of a diverse suite of Bacillus spores by mass spectrometry-based protein profiling."
] | [
2008,
2004
] | 2 | [] | [
"IPR016493",
"IPR017022"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5808,
5,
34
] | 3 | [
"Arabidopsis thaliana"
] | [
1
] | 1 | true | Family | Spore coat protein CotF-like | Spore coat protein CotF-like | Spore_coat_CotF-like | 4 |
IPR012852 | 12,852 | Calcium binding and coiled-coil domain-like | CALCOCO1-like | Domain | 2,561 | false | false | Calcium-binding and coiled-coil domain-containing protein 1 (Calcoco1) from Mus musculus ( ) binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1 ( ), and thus enhances transcriptional activation by a number of nuclear receptors. Calcoco1 has a central coiled-coil region with three leucine ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07888"
] | [
"CALCOCO1"
] | [
2561
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5357905",
"R-BTA-936440",
"R-HSA-5357905",
"R-HSA-936440",
"R-MMU-5357905",
"R-MMU-936440",
"R-RNO-5357905",
"R-RNO-936440"
] | [
"REACTOME:R-BTA-5357905",
"REACTOME:R-BTA-936440",
"REACTOME:R-HSA-5357905",
"REACTOME:R-HSA-936440",
"REACTOME:R-MMU-5357905",
"REACTOME:R-MMU-936440",
"REACTOME:R-RNO-5357905",
"REACTOME:R-RNO-936440"
] | 8 | [] | 0 | [
"PUB00016596"
] | [
"14690606"
] | [
"CoCoA, a nuclear receptor coactivator which acts through an N-terminal activation domain of p160 coactivators."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Opisthokonta"
] | [
36,
2525
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
29,
12,
6,
10
] | 4 | true | Domain | Calcium binding and coiled-coil domain-like | Calcium binding and coiled-coil domain-like | CALCOCO1-like | 6 |
IPR012853 | 12,853 | Chloramphenicol phosphotransferase-like | CPT | Family | 2,762 | false | false | The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT, ) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group ... | [
"GO:0005524",
"GO:0016740"
] | [
"ATP binding",
"transferase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PIRSF",
"CDD"
] | [
"PF07931",
"PIRSF007531",
"cd00227"
] | [
"CPT",
"CPT",
"CPT"
] | [
2762,
2059,
37
] | 3 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.1.-",
"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.-",
"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-7975",
"METACYC:PWY-8... | 21 | [
"1grq",
"1grr",
"1qhn",
"1qhs",
"1qhx",
"1qhy"
] | 6 | [
"PUB00016586",
"PUB00027902"
] | [
"11468347",
"10835366"
] | [
"Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity.",
"The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism."
] | [
2001,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"metagenomes",
"uncultured Caudovirales phage"
] | [
2646,
100,
2,
13,
1
] | 5 | [
"Homo sapiens"
] | [
1
] | 1 | true | Family | Chloramphenicol phosphotransferase-like | Chloramphenicol phosphotransferase-like | CPT | 3 |
IPR012854 | 12,854 | Copper amine oxidase-like, N-terminal | Cu_amine_oxidase-like_N | Domain | 21,514 | false | false | Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing ( ) and copper-containing ( ). Copper-containing AO act as a disulphide-linked homodimer. They cata... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07833"
] | [
"Cu_amine_oxidN1"
] | [
21514
] | 1 | [
"EC",
"GP"
] | [
"1.4.3.21",
"GenProp1402"
] | [
"EC:1.4.3.21",
"GP:GenProp1402"
] | 2 | [
"1d6u",
"1d6y",
"1d6z",
"1dyu",
"1jrq",
"1lvn",
"1oac",
"1qaf",
"1qak",
"1qal",
"1spu",
"2w0q",
"2wgq",
"2wo0",
"2wof",
"2woh",
"6ezz",
"6grr",
"8imd"
] | 19 | [
"PUB00005251",
"PUB00010699",
"PUB00010700",
"PUB00010701",
"PUB00016565"
] | [
"8591028",
"9048544",
"9405045",
"8805580",
"10576737"
] | [
"Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.",
"Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.",
"Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the... | [
1995,
1997,
1997,
1996,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2,
21351,
15,
7,
139
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
2,
1
] | 2 | true | Domain | Copper amine oxidase-like, N-terminal | Copper amine oxidase-like, N-terminal | Cu_amine_oxidase-like_N | 3 |
IPR012856 | 12,856 | D-aminopeptidase, domain B | DAP_B_dom | Domain | 674 | false | false | D-aminopeptidase ( ) is a dimeric enzyme with each monomer being composed of three domains. Domain B is organised to form a β barrel made up of eight antiparallel β strands. It is connected to domain A, the catalytic domain, by an eight-residue sequence, and also interacts with both domains A and C via non-covalent bon... | [
"GO:0004177"
] | [
"aminopeptidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07930"
] | [
"DAP_B"
] | [
674
] | 1 | [
"EC"
] | [
"3.4.11.19"
] | [
"EC:3.4.11.19"
] | 1 | [
"1ei5"
] | 1 | [
"PUB00013322"
] | [
"10986464"
] | [
"Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"bioreactor metagenome",
"leotiomyceta"
] | [
281,
1,
392
] | 3 | [] | [] | 0 | true | Domain | D-aminopeptidase, domain B | D-aminopeptidase, domain B | DAP_B_dom | 1 |
IPR012858 | 12,858 | Dendritic cell-specific transmembrane protein-like | DC_STAMP-like | Domain | 4,592 | false | false | This group of sequences is similar to a region of the dendritic cell-specific transmembrane protein (DC-STAMP, ). This is thought to be a novel receptor protein that shares no identity with other multimembrane-spanning proteins [ ]. It is thought to have seven putative transmembrane regions [ ], two of which are found ... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF07782"
] | [
"DC_STAMP"
] | [
4592
] | 1 | [
"REACTOME"
] | [
"R-HSA-8874211"
] | [
"REACTOME:R-HSA-8874211"
] | 1 | [] | 0 | [
"PUB00016463"
] | [
"11169400"
] | [
"DC-STAMP, a novel multimembrane-spanning molecule preferentially expressed by dendritic cells."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Nocardioides malaquae"
] | [
4591,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
52,
5,
9,
7,
10
] | 6 | true | Domain | Dendritic cell-specific transmembrane protein-like | Dendritic cell-specific transmembrane protein-like | DC_STAMP-like | 2 |
IPR012859 | 12,859 | Archaeal Type IV pilin, N-terminal | Pilin_N_archaeal | Domain | 2,821 | false | false | This entry represents the N-terminal domain of archaeal pilins, which play important roles in surface adhesion. Sequences covered by this domain are not mixed up with sequences having such an extremely high sequence conservation as described in [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07790"
] | [
"Pilin_N"
] | [
2821
] | 1 | [] | [] | [] | 0 | [
"8fj5",
"8gi2",
"8rey"
] | 3 | [
"PUB00069628"
] | [
"23794623"
] | [
"Novel archaeal adhesion pilins with a conserved N terminus."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Saline Natrinema sp. J7-1 virus 2",
"unclassified sequences"
] | [
2773,
2,
1,
45
] | 4 | [] | [] | 0 | true | Domain | Archaeal Type IV pilin, N-terminal | Archaeal Type IV pilin, N-terminal | Pilin_N_archaeal | 2 |
IPR012860 | 12,860 | Arf3-interacting protein 1, N-terminal domain | Afi1_N | Domain | 1,871 | false | false | This domain occurs at the N terminus of Afi1 (Arf3-interacting protein 1), a protein necessary for vesicle trafficking in yeast. This domain is the interacting region of the protein which binds to Arf3. Afi1 is distributed asymmetrically at the plasma membrane and is required for polarized distribution of Arf3 but not ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07792"
] | [
"Afi1"
] | [
1871
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00057274"
] | [
"18397879"
] | [
"Afi1p functions as an Arf3p polarization-specific docking factor for development of polarity."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1871
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1,
1
] | 4 | true | Domain | Arf3-interacting protein 1, N-terminal domain | Arf3-interacting protein 1, N-terminal domain | Afi1_N | 7 |
IPR012861 | 12,861 | Protein of unknown function DUF1634 | DUF1634 | Family | 1,945 | false | false | This family contains many hypothetical bacterial and archaeal proteins. A few members of this family are annotated as being putative transmembrane proteins, and the region in question in fact contains many hydrophobic residues. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07843"
] | [
"DUF1634"
] | [
1945
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
126,
1806,
13
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF1634 | Protein of unknown function DUF1634 | DUF1634 | 9 |
IPR012862 | 12,862 | Protein of unknown function DUF1635 | DUF1635 | Family | 2,544 | false | false | The members of this family include sequences that are parts of hypothetical proteins expressed by plant species. The region in question is about 170 amino acids long. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07795",
"PTHR33431"
] | [
"DUF1635",
""
] | [
2541,
2469
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
2544
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
23,
5,
11
] | 3 | true | Family | Protein of unknown function DUF1635 | Protein of unknown function DUF1635 | DUF1635 | 4 |
IPR012864 | 12,864 | Cysteine oxygenase/2-aminoethanethiol dioxygenase | PCO/ADO | Family | 6,306 | false | false | This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. PCOs oxidize N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation [ ]. ADO is responsible for endogenous cysteamine dioxygenase activity [ ]. | [
"GO:0016702"
] | [
"oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF07847",
"PTHR22966"
] | [
"PCO_ADO",
""
] | [
6015,
6040
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.13.11.20",
"PWY-5331",
"R-DDI-1614558",
"R-HSA-1614558",
"R-MMU-1614558"
] | [
"EC:1.13.11.20",
"METACYC:PWY-5331",
"REACTOME:R-DDI-1614558",
"REACTOME:R-HSA-1614558",
"REACTOME:R-MMU-1614558"
] | 5 | [
"6s0p",
"6s7e",
"6sbp",
"7chi",
"7chj",
"7cxz",
"7lvz",
"7rei",
"8u9j",
"8uan",
"9dma",
"9dxb",
"9dxu",
"9dxv",
"9dy4"
] | 15 | [
"PUB00074379",
"PUB00074380"
] | [
"24599061",
"17581819"
] | [
"Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway.",
"Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase."
] | [
2014,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"hydrothermal vent metagenome"
] | [
27,
6278,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
24,
1,
3,
1,
3,
2,
308,
2,
59
] | 9 | true | Family | Cysteine oxygenase/2-aminoethanethiol dioxygenase | Cysteine oxygenase/2-aminoethanethiol dioxygenase | PCO/ADO | 1 |
IPR012865 | 12,865 | Protein of unknown function DUF1642 | DUF1642 | Family | 1,349 | false | false | This entry represents a group of phage and prophage proteins whose function is not known. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07852"
] | [
"DUF1642"
] | [
1349
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobaculum halobium",
"Viruses",
"Zophobas morio"
] | [
966,
1,
381,
1
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF1642 | Protein of unknown function DUF1642 | DUF1642 | 3 |
IPR012867 | 12,867 | Domain of unknown function DUF1648 | DUF1648 | Domain | 7,336 | false | false | This domain is found in proteins expressed by bacterial and archaeal species. One such protein is immunity protein SdpI ( ) from Bacillus subtilis, which provides protection for the cell against the toxic effects of its own SdpC killing factor, and also functions as a receptor/signal transduction protein [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07853"
] | [
"DUF1648"
] | [
7336
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00055038"
] | [
"16469701"
] | [
"A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
299,
6933,
50,
54
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1648 | Domain of unknown function DUF1648 | DUF1648 | 2 |
IPR012869 | 12,869 | CopG-like ribbon-helix-helix domain | RHH_5 | Domain | 891 | false | false | This entry represents a domain found in a group of bacterial proteins that form a ribbon-helix-helix fold. This fold occurs in many examples of bacterial antitoxins [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07878"
] | [
"RHH_5"
] | [
891
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075548"
] | [
"15864262"
] | [
"Prokaryotic toxin-antitoxin stress response loci."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Viruses",
"metagenomes"
] | [
11,
855,
9,
16
] | 4 | [] | [] | 0 | true | Domain | CopG-like ribbon-helix-helix domain | CopG-like ribbon-helix-helix domain | RHH_5 | 6 |
IPR012870 | 12,870 | Protein of unknown function DUF1666 | DUF1666 | Family | 3,099 | false | false | These sequences are derived from hypothetical plant proteins of unknown function. The region in question is approximately 250 residues long. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07891"
] | [
"DUF1666"
] | [
3099
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Spermatophyta"
] | [
3099
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
33,
9,
28
] | 3 | true | Family | Protein of unknown function DUF1666 | Protein of unknown function DUF1666 | DUF1666 | 8 |
IPR012871 | 12,871 | Protein of unknown function DUF1677, Oryza sativa | DUF1668_ORYSA | Family | 4,407 | false | false | The hypothetical proteins found in this family are expressed by Oryza sativa (Rice) and are of unknown function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07893"
] | [
"DUF1668"
] | [
4407
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Motilibacter peucedani"
] | [
4406,
1
] | 2 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
243,
10
] | 2 | true | Family | Protein of unknown function DUF1677, Oryza sativa | Protein of unknown function DUF1677, Oryza sativa | DUF1668_ORYSA | 2 |
IPR012873 | 12,873 | Protein of unknown function DUF1672 | DUF1672 | Family | 473 | false | false | This family is composed of hypothetical bacterial proteins of unknown function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07901"
] | [
"DUF1672"
] | [
473
] | 1 | [] | [] | [] | 0 | [
"4qpv"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
471,
2
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF1672 | Protein of unknown function DUF1672 | DUF1672 | 5 |
IPR012874 | 12,874 | Protein of unknown function DUF1673, Methanosarcina species | DUF1673_METspp | Family | 297 | false | false | This family contains hypothetical proteins of unknown function found in Methanosarcina acetivorans and Methanosarcina mazei. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07895"
] | [
"DUF1673"
] | [
297
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Methanomicrobia",
"ecological metagenomes"
] | [
294,
3
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF1673, Methanosarcina species | Protein of unknown function DUF1673, Methanosarcina species | DUF1673_METspp | 8 |
IPR012875 | 12,875 | Succinate dehydrogenase assembly factor 4 | SDHF4 | Family | 6,893 | false | false | This entry includes SDHF4 from animals, Sdh8 from budding yeasts and some uncharacterised proteins from bacteria. Sdh8 is required for assembly of succinate dehydrogenase (SDH). It interacts with the catalytic Sdh1 subunit in the mitochondrial matrix, facilitating its association with Sdh2 and the subsequent assembly o... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07896"
] | [
"DUF1674"
] | [
6893
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-9854311",
"R-HSA-9854311",
"R-MMU-9854311",
"R-SCE-9854311",
"R-SPO-9854311"
] | [
"REACTOME:R-DDI-9854311",
"REACTOME:R-HSA-9854311",
"REACTOME:R-MMU-9854311",
"REACTOME:R-SCE-9854311",
"REACTOME:R-SPO-9854311"
] | 5 | [
"2k5k",
"8dyd",
"8dye"
] | 3 | [
"PUB00092519"
] | [
"24954416"
] | [
"SDHAF4 promotes mitochondrial succinate dehydrogenase activity and prevents neurodegeneration."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured virus"
] | [
3054,
3808,
30,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
1,
3,
2,
1,
1,
2,
3,
1,
1,
2
] | 12 | true | Family | Succinate dehydrogenase assembly factor 4 | Succinate dehydrogenase assembly factor 4 | SDHF4 | 3 |
IPR012876 | 12,876 | Protein of unknown function DUF1677, plant | DUF1677_pln | Family | 4,485 | false | false | The sequences found in this family are all derived from hypothetical plant proteins of unknown function. The region features a number of highly conserved cysteine residues. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07911",
"PTHR33108"
] | [
"DUF1677",
""
] | [
4485,
4375
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4485
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
29,
44,
53
] | 3 | true | Family | Protein of unknown function DUF1677, plant | Protein of unknown function DUF1677, plant | DUF1677_pln | 5 |
IPR012877 | 12,877 | Uncharacterised oxidoreductase Dhs-27 | Dhs-27 | Family | 2,238 | false | false | This region is found in a number of Caenorhabditis elegans and Caenorhabditis briggsae proteins, in one case ( ) as a repeat. In many of the family members, this region is associated with the CHK region described by SMART as being found in zinc finger-C4 and HLH domain-containing kinases. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07914"
] | [
"DUF1679"
] | [
2238
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
45,
2193
] | 2 | [
"Caenorhabditis elegans"
] | [
37
] | 1 | true | Family | Uncharacterised oxidoreductase Dhs-27 | Uncharacterised oxidoreductase Dhs-27 | Dhs-27 | 6 |
IPR012878 | 12,878 | Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain | Beta-AFase-like_GH127_cat | Domain | 16,879 | false | false | This entry represents the catalytic domain of Non-reducing end beta-L-arabinofuranosidase from Bifidobacterium longum (Beta-AFase) and similar proteins widespread among all cellular organisms that belong to the glycoside hydrolase family 127 (GH127). This domain folds into an (α/α)6 barrel [ ]. Beta-AFase, an unusual b... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07944"
] | [
"Beta-AFase-like_GH127_cat"
] | [
16879
] | 1 | [] | [] | [] | 0 | [
"3wkw",
"3wkx",
"3wre",
"3wrf",
"3wrg",
"4qjy",
"4qk0",
"5mqo",
"5opj",
"6ex6",
"6yqh",
"7bzl",
"7dif",
"7exu",
"7exv",
"7exw",
"8k7x",
"8k7y",
"8qf2",
"8qf8"
] | 20 | [
"PUB00075450",
"PUB00151606"
] | [
"24385433",
"24680821"
] | [
"Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member.",
"Crystal structure of glycoside hydrolase family 127 β-l-arabinofuranosidase from Bifidobacterium longum."
] | [
2014,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
81,
13498,
3151,
149
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
9,
10,
24
] | 3 | true | Domain | Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain | Non-reducing end beta-L-arabinofuranosidase-like, GH127 catalytic domain | Beta-AFase-like_GH127_cat | 7 |
IPR012879 | 12,879 | PAT complex subunit CCDC47 | CCDC47 | Family | 4,841 | false | false | This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes [ ]. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by ... | [
"GO:0005509",
"GO:0032469",
"GO:0005783"
] | [
"calcium ion binding",
"endoplasmic reticulum calcium ion homeostasis",
"endoplasmic reticulum"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF07946",
"PTHR12883"
] | [
"CCDC47",
""
] | [
4827,
4777
] | 2 | [] | [] | [] | 0 | [
"6w6l",
"7tm3",
"7tut",
"9i78"
] | 4 | [
"PUB00097217",
"PUB00097218",
"PUB00097241",
"PUB00097242",
"PUB00097243"
] | [
"12475939",
"32814900",
"32820719",
"30401460",
"25009997"
] | [
"Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein.",
"An intramembrane chaperone complex facilitates membrane protein biogenesis.",
"An ER translocon for multi-pass membrane protein biogenesis.",
"Bi-allelic CCDC47 Vari... | [
2002,
2020,
2020,
2018,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Candidatus Heimdallarchaeum aukensis",
"Eukaryota"
] | [
1,
4840
] | 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... | [
8,
1,
1,
2,
2,
4,
1,
4,
2,
1,
1,
10
] | 12 | true | Family | PAT complex subunit CCDC47 | PAT complex subunit CCDC47 | CCDC47 | 9 |
IPR012880 | 12,880 | Gryzun, putative trafficking through Golgi | Gryzun | Domain | 1,653 | false | false | The proteins featured in this family are all eukaryotic, and many of them are annotated as being Gryzun. Gryzun is distantly related to, but distinct from, the Trs130 subunit of the TRAPP complex but is absent from S. cerevisiae. RNAi of human Gryzun ( ) blocks Golgi exit. Thus the family is likely to be involved with ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07919"
] | [
"Gryzun"
] | [
1653
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00075580"
] | [
"19942856"
] | [
"A genome-wide RNA interference screen identifies two novel components of the metazoan secretory pathway."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1653
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Gryzun, putative trafficking through Golgi | Gryzun, putative trafficking through Golgi | Gryzun | 7 |
IPR012881 | 12,881 | Protein of unknown function DUF1685 | DUF1685 | Family | 4,078 | false | false | The members of this family are hypothetical eukaryotic proteins of unknown function. The region in question is approximately 100 amino acid residues long. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07939"
] | [
"DUF1685"
] | [
4078
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
4078
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
48,
20,
27
] | 3 | true | Family | Protein of unknown function DUF1685 | Protein of unknown function DUF1685 | DUF1685 | 2 |
IPR012883 | 12,883 | ERp29, N-terminal | ERp29_N | Domain | 1,274 | false | false | ERp29 ( ) is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle [ , ]. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organised into a... | [
"GO:0009306",
"GO:0005788"
] | [
"protein secretion",
"endoplasmic reticulum lumen"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF07912",
"cd03007"
] | [
"ERp29_N",
"PDI_a_ERp29_N"
] | [
1274,
243
] | 2 | [] | [] | [] | 0 | [
"1g7e",
"1ovn",
"2c0e",
"2c0f",
"2c0g",
"2c1y",
"2qc7"
] | 7 | [
"PUB00014099",
"PUB00016490",
"PUB00029610"
] | [
"11435111",
"10727933",
"12941941"
] | [
"Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.",
"Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis.",
"Crystal struct... | [
2001,
2000,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1274
] | 1 | [
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
2,
3
] | 4 | true | Domain | ERp29, N-terminal | ERp29, N-terminal | ERp29_N | 8 |
IPR012885 | 12,885 | Sdz-33, F-box domain | F-box_Sdz-33 | Domain | 4,855 | false | false | This entry represents an F-box domain in Sdz-33, Sdz-15, Hecw-1 and uncharacterised proteins in Caenorhabditis elegans. F-box associated domain-containing protein SDZ-33 (Sdz-33) functions as the substrate recognition component of the E3 ubiquitin-protein ligase complex, mediating the ubiquitination and subsequent prot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07735"
] | [
"FBA_2"
] | [
4855
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-CEL-4641258",
"R-CEL-983168"
] | [
"REACTOME:R-CEL-4641258",
"REACTOME:R-CEL-983168"
] | 2 | [] | 0 | [
"PUB00091144",
"PUB00160782",
"PUB00160783"
] | [
"22089131",
"33514673",
"2208913"
] | [
"Natural polymorphisms in C. elegans HECW-1 E3 ligase affect pathogen avoidance behaviour.",
"<i>Caenorhabditis elegans</i> F-Box Protein Promotes Axon Regeneration by Inducing Degradation of the Mad Transcription Factor.",
"[Long-term experience with a PACS subsystem]."
] | [
2011,
2021,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Caenorhabditis",
"Thermodesulfobium acidiphilum"
] | [
4854,
1
] | 2 | [
"Caenorhabditis elegans"
] | [
183
] | 1 | true | Domain | Sdz-33, F-box domain | Sdz-33, F-box domain | F-box_Sdz-33 | 8 |
IPR012886 | 12,886 | Formiminotransferase, N-terminal subdomain | Formiminotransferase_N | Domain | 5,185 | false | false | The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer being comprised of two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed β-pleated sheet and five α-helices, which are arranged on the ex... | [
"GO:0005542",
"GO:0016740"
] | [
"folic acid binding",
"transferase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF07837",
"SM01222"
] | [
"FTCD_N",
"FTCD_N"
] | [
5179,
5087
] | 2 | [
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.2.5",
"PWY-5030",
"R-DDI-70921",
"R-HSA-70921",
"R-MMU-70921",
"R-RNO-70921"
] | [
"EC:2.1.2.5",
"METACYC:PWY-5030",
"REACTOME:R-DDI-70921",
"REACTOME:R-HSA-70921",
"REACTOME:R-MMU-70921",
"REACTOME:R-RNO-70921"
] | 6 | [
"1qd1",
"1tt9",
"2pfd"
] | 3 | [
"PUB00007432"
] | [
"10673422"
] | [
"The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
38,
1750,
3237,
160
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
22,
7,
1,
10,
2,
40
] | 7 | true | Domain | Formiminotransferase, N-terminal subdomain | Formiminotransferase, N-terminal subdomain | Formiminotransferase_N | 7 |
IPR012887 | 12,887 | GDP-fucose pyrophosphorylase domain | GDP_fucose_pyrophosphorylase | Domain | 3,903 | false | false | This entry represents the fucose pyrophosphorylase domain found at the N-terminal of the bifunctional L-Fucokinase/GDP-Fucose Pyrophosphorylase (FKP) enzymes such as FKGP from Arabidopsis and L-fucose kinase from animals [ , ]. In fucose-1-phosphate guanylyltransferase from human, this is the main domain of the protein... | [
"GO:0016772"
] | [
"transferase activity, transferring phosphorus-containing groups"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07959"
] | [
"Fucose_pyrophosphorylase"
] | [
3903
] | 1 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"2.7.1.52",
"2.7.7.30",
"PWY-6",
"R-HSA-6787639",
"R-MMU-6787639"
] | [
"EC:2.7.1.52",
"EC:2.7.7.30",
"METACYC:PWY-6",
"REACTOME:R-HSA-6787639",
"REACTOME:R-MMU-6787639"
] | 5 | [
"5yys",
"9iis",
"9iit"
] | 3 | [
"PUB00015901",
"PUB00016201",
"PUB00155376",
"PUB00155377",
"PUB00155378"
] | [
"9804772",
"14686921",
"15774760",
"18199744",
"30242642"
] | [
"GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme.",
"Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose.",
"Human symbionts use a host-like pathway for surface fucosylation.",
"A bifunctional enzyme with L-fucokinase and GDP-L-fuco... | [
1998,
2004,
2005,
2008,
2019
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
452,
3443,
8
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
9,
2,
2,
15,
4,
5,
13,
7
] | 8 | true | Domain | GDP-fucose pyrophosphorylase domain | GDP-fucose pyrophosphorylase domain | GDP_fucose_pyrophosphorylase | 9 |
IPR012889 | 12,889 | L-fucose isomerase, N-terminal-2 | Fucose_isomerase_N2 | Domain | 3,020 | false | false | Proteins containing this domain are similar to L-fucose isomerase expressed by Escherichia coli ( , ). This enzyme corresponds to glucose-6-phosphate isomerase in glycolysis, and converts an aldo-hexose to a ketose to prepare it for aldol cleavage. The enzyme is a hexamer, with each subunit being wedge-shaped and compo... | [
"GO:0008736",
"GO:0006004",
"GO:0005737"
] | [
"L-fucose isomerase activity",
"fucose metabolic process",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07882"
] | [
"Fucose_iso_N2"
] | [
3020
] | 1 | [
"EC"
] | [
"5.3.1.25"
] | [
"EC:5.3.1.25"
] | 1 | [
"1fui",
"3a9r",
"3a9s",
"3a9t",
"4c20",
"4c21",
"4c22",
"6k1f",
"6k1g"
] | 9 | [
"PUB00007428"
] | [
"9367760"
] | [
"Structure and mechanism of L-fucose isomerase from Escherichia coli."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
8,
2956,
4,
52
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | L-fucose isomerase, N-terminal-2 | L-fucose isomerase, N-terminal-2 | Fucose_isomerase_N2 | 3 |
IPR012891 | 12,891 | GCK domain | GCK_dom | Domain | 1,421 | false | false | This domain is found in proteins carrying other domains known to be involved in intracellular signalling pathways indicating that it might also be involved in these pathways. It has 4 highly conserved cysteine residues, suggesting that it can bind zinc ions. Moreover, it is found repeated in some members of this entry ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF07802",
"SM01227"
] | [
"GCK",
"GCK"
] | [
1366,
1376
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00099757"
] | [
"19011240"
] | [
"Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1421
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
39,
5,
8
] | 3 | true | Domain | GCK domain | GCK domain | GCK_dom | 3 |
IPR012892 | 12,892 | Gp58-like | Gp58 | Domain | 354 | false | false | Sequences found in this entry are derived from a number of bacteriophage and prophage proteins. They are similar to gp58 ( ), a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07902"
] | [
"Gp58"
] | [
354
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016531"
] | [
"7828907"
] | [
"Characterization of the genome region encoding structural proteins of Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Psylliodes chrysocephalus",
"Viruses"
] | [
314,
1,
39
] | 3 | [] | [] | 0 | true | Domain | Gp58-like | Gp58-like | Gp58 | 2 |
IPR012893 | 12,893 | HipA-like, C-terminal | HipA-like_C | Domain | 17,708 | false | false | The members of this entry are similar to a region close to the C terminus of the HipA protein expressed by various bacterial species (for example ). This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis [ ]. When expressed alone, ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07804"
] | [
"HipA_C"
] | [
17708
] | 1 | [] | [] | [] | 0 | [
"2wiu",
"3akj",
"3akk",
"3akl",
"3dnt",
"3dnu",
"3dnv",
"3fbr",
"3hzi",
"3tpb",
"3tpd",
"3tpe",
"3tpt",
"3tpv",
"4pu3",
"4pu4",
"4pu5",
"4yg7",
"5k98",
"7ab3",
"7ab4",
"7ab5",
"7vkb",
"7vkc",
"7wcf",
"8ezr",
"8ezs"
] | 27 | [
"PUB00016369",
"PUB00016440",
"PUB00055674"
] | [
"8021189",
"1715862",
"21098302"
] | [
"Autoregulation of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis.",
"Structure and organization of hip, an operon that affects lethality due to inhibition of peptidoglycan or DNA synthesis.",
"Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cel... | [
1994,
1991,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"IncJ plasmid R391",
"Methanosarcinaceae",
"Siphoviridae sp. ctg0K17",
"unclassified sequences"
] | [
17293,
29,
1,
5,
1,
379
] | 6 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | HipA-like, C-terminal | HipA-like, C-terminal | HipA-like_C | 6 |
IPR012896 | 12,896 | Integrin beta subunit, tail | Integrin_bsu_tail | Domain | 11,507 | false | false | This entry represents the tail domain of the integrin beta subunit. It forms a four-stranded β-sheet that contains parallel and antiparallel strands and faces an α helix found at the N terminus of this domain [ ]. Interactions between the α-helix and the β-sheet are mostly hydrophobic and involve a disulphide bond. The... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF07965",
"SM01242"
] | [
"Integrin_B_tail",
"Integrin_B_tail"
] | [
10080,
11497
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1566948",
"R-BTA-166016",
"R-BTA-198933",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-3000178",
"R-BTA-6798695",
"R-CEL-114608",
"R-CEL-1236973",
"R-CEL-2129379",
"R-CEL-216083",
"R-CEL-2173789",
"R-CEL-3000157",
"R-CEL-3000170",
"R-CEL-3000178",
... | [
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-3000178",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-1236973",
"REACTOME:R-C... | 158 | [
"1jv2",
"1l5g",
"1m1x",
"1u8c",
"3fcs",
"3ije",
"3k6s",
"3k71",
"3k72",
"4cak",
"4g1e",
"4g1m",
"4mmx",
"4mmy",
"4mmz",
"4neh",
"4nen",
"4o02",
"4um8",
"5es4",
"6avq",
"6avr",
"6avu",
"6bxj",
"6mk0",
"6msl",
"6msu",
"6naj",
"7la4",
"7nwl",
"7nxd",
"7usl"... | 68 | [
"PUB00006148",
"PUB00009789",
"PUB00015915",
"PUB00015985",
"PUB00026539",
"PUB00035000",
"PUB00035002",
"PUB00057248",
"PUB00160425"
] | [
"9009218",
"12297042",
"14689578",
"2467745",
"11546839",
"12361595",
"12234368",
"12388743",
"28510180"
] | [
"A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.",
"Integrins: bidirectional, allosteric signaling machines.",
"Integrin clipping: a novel adhesion switch?",
"A novel vitronectin receptor integrin (alpha v beta x... | [
1997,
2002,
2004,
1989,
2001,
2002,
2002,
2002,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
11507
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
28,
3,
32,
19,
32
] | 6 | true | Domain | Integrin beta subunit, tail | Integrin beta subunit, tail | Integrin_bsu_tail | 3 |
IPR012897 | 12,897 | Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain | K_chnl_volt-dep_Kv1.4_TID | Domain | 688 | false | false | Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr... | [
"GO:0005249",
"GO:0030955",
"GO:0006813",
"GO:0016020"
] | [
"voltage-gated potassium channel activity",
"potassium ion binding",
"potassium ion transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF07941"
] | [
"K_channel_TID"
] | [
688
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1296072",
"R-MMU-1296072",
"R-RNO-1296072"
] | [
"REACTOME:R-HSA-1296072",
"REACTOME:R-MMU-1296072",
"REACTOME:R-RNO-1296072"
] | 3 | [
"1kn7",
"1zto"
] | 2 | [
"PUB00001055",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00006577",
"PUB00007312",
"PUB00008322",
"PUB00009378",
"PUB00009391",
"PUB00016528",
"PUB00036044"
] | [
"1772658",
"1879548",
"1373731",
"2448635",
"2451788",
"2555158",
"10798390",
"9305895",
"11178249",
"10712896",
"12590144",
"11343973"
] | [
"The molecular biology of K+ channels.",
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso... | [
1991,
1991,
1992,
1988,
1988,
1989,
2000,
1997,
2000,
2000,
2003,
2000
] | 12 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Opisthokonta"
] | [
2,
686
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
3
] | 4 | true | Domain | Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain | Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain | K_chnl_volt-dep_Kv1.4_TID | 5 |
IPR012899 | 12,899 | LTXXQ motif family protein | LTXXQ | Family | 9,433 | false | false | This family summarizes bacterial proteins related to CpxP, a periplasmic protein that forms part of a two-component system which acts as a global modulator of cell-envelope stress in Gram-negative bacteria. CpxP aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to al... | [
"GO:0042597"
] | [
"periplasmic space"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF",
"CDD"
] | [
"PF07813",
"PIRSF034445",
"cd09916"
] | [
"LTXXQ",
"CpxP_Spy",
"CpxP_like"
] | [
8874,
2799,
4696
] | 3 | [] | [] | [] | 0 | [
"3itf",
"3o39",
"3oeo",
"3qzc",
"5ihf",
"5io8",
"5wnw",
"5wo1",
"5wo2",
"5wo3",
"6bie",
"6owx",
"6owy",
"6owz"
] | 14 | [
"PUB00016508",
"PUB00016553",
"PUB00055384",
"PUB00061476"
] | [
"9068658",
"9473036",
"20799348",
"21239493"
] | [
"A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells.",
"CpxP, a stress-combative member of the Cpx regulon.",
"The crystal structure Escherichia coli Spy.",
"Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP pro... | [
1997,
1998,
2010,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermococcus litoralis",
"unclassified sequences"
] | [
9324,
19,
1,
89
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | LTXXQ motif family protein | LTXXQ motif family protein | LTXXQ | 8 |
IPR012900 | 12,900 | G-box binding protein, multifunctional mosaic region | MFMR | Domain | 3,421 | false | false | This region is often found to the N terminus of the basic-leucine zipper domain ( ). It is between 150 and 200 amino acids in length. The N-terminal half of this domain is rich in proline residues and has been termed the PRD (proline rich domain) [ ], whereas the C-terminal half is more polar and has been called the MF... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07777"
] | [
"MFMR"
] | [
3421
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016443",
"PUB00016500"
] | [
"11722549",
"8127687"
] | [
"Plant bZIP G-box binding factors. Modular structure and activation mechanisms.",
"Novel conserved sequence motifs in plant G-box binding proteins and implications for interactive domains."
] | [
2001,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Streptophytina"
] | [
3421
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
23,
14,
54
] | 3 | true | Domain | G-box binding protein, multifunctional mosaic region | G-box binding protein, multifunctional mosaic region | MFMR | 2 |
IPR012901 | 12,901 | Carnosine N-methyltransferase | CARME | Family | 6,098 | false | false | This family includes Carnosine N-methyltransferase ( ), conserved from yeast to human, that catalyses the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. It a... | [
"GO:0008757"
] | [
"S-adenosylmethionine-dependent methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PANTHER",
"SMART"
] | [
"PF07942",
"PTHR12303",
"SM01296"
] | [
"CARME",
"",
"N2227"
] | [
6031,
6014,
5888
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.1.1.22",
"R-DDI-70921",
"R-DME-70921",
"R-GGA-70921",
"R-HSA-70921",
"R-MMU-70921",
"R-RNO-70921",
"R-SCE-70921",
"R-SPO-70921"
] | [
"EC:2.1.1.22",
"REACTOME:R-DDI-70921",
"REACTOME:R-DME-70921",
"REACTOME:R-GGA-70921",
"REACTOME:R-HSA-70921",
"REACTOME:R-MMU-70921",
"REACTOME:R-RNO-70921",
"REACTOME:R-SCE-70921",
"REACTOME:R-SPO-70921"
] | 9 | [
"5x62",
"5yf0",
"5yf1",
"5yf2"
] | 4 | [
"PUB00098813",
"PUB00098814",
"PUB00098815",
"PUB00158949"
] | [
"26001783",
"29463897",
"28654751",
"38514639"
] | [
"UPF0586 Protein C9orf41 Homolog Is Anserine-producing Methyltransferase.",
"Molecular basis for histidine N1 position-specific methylation by CARNMT1.",
"Substrate Recognition Mechanism of the Putative Yeast Carnosine N-methyltransferase.",
"An evolutionary mechanism to assimilate new nutrient sensors into t... | [
2015,
2018,
2017,
2024
] | 4 | [] | [
"IPR016853"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota"
] | [
29,
6069
] | 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... | [
16,
2,
3,
1,
4,
1,
1,
3,
3,
2,
1,
10
] | 12 | true | Family | Carnosine N-methyltransferase | Carnosine N-methyltransferase | CARME | 1 |
IPR012902 | 12,902 | Prokaryotic N-terminal methylation site | N_methyl_site | PTM | 126,085 | false | false | This short motif directs methylation of the conserved phenylalanine residue. It is most often found at the N terminus of pilins and other proteins involved in secretion (see , , and ). | [] | [] | [] | 0 | [
"PFAM",
"PROSITE",
"NCBIFAM"
] | [
"PF07963",
"PS00409",
"TIGR02532"
] | [
"N_methyl",
"PROKAR_NTER_METHYL",
"IV_pilin_GFxxxE"
] | [
116930,
83217,
116067
] | 3 | [
"GP"
] | [
"GenProp0295"
] | [
"GP:GenProp0295"
] | 1 | [
"1ay2",
"1oqw",
"2hi2",
"2hil",
"2m7g",
"2pil",
"3jc8",
"3jc9",
"3sok",
"5g23",
"5g24",
"5kua",
"5vxx",
"5vxy",
"5wda",
"6gv9",
"6vk9",
"6xxd",
"6xxe",
"7tgg",
"8p2v",
"8p36",
"8p3b",
"8pfb",
"8pij",
"8piz",
"8pjp",
"8qqd",
"8qqj",
"8tj2",
"8tob",
"8tum"... | 36 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
16,
123338,
51,
144,
2536
] | 5 | [
"Escherichia coli (strain K12)"
] | [
8
] | 1 | true | PTM | Prokaryotic N-terminal methylation site | Prokaryotic N-terminal methylation site | N_methyl_site | 6 |
IPR012903 | 12,903 | Nif11 domain | Nif11 | Domain | 1,625 | false | false | This domain is found mainly in the Cyanobacteria and in Proteobacteria such as the nitrogen-fixing bacterium Azotobacter vinelandii. It is found in Nif11, a protein described in Azotobacter as linked to nitrogen fixation [ ]. It also constitutes a leader peptide in Nif11-derived peptides (N11P), which are thought to be... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07862"
] | [
"Nif11"
] | [
1625
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016451",
"PUB00055015",
"PUB00068006"
] | [
"2644218",
"20500830",
"20479271"
] | [
"Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii.",
"Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family.",
"Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobact... | [
1989,
2010,
2010
] | 3 | [] | [
"IPR022516"
] | 0 | 1 | 0 | [
"Bacteria",
"Methanoplanus endosymbiosus",
"Mycobacterium phage Mendokysei",
"ecological metagenomes"
] | [
1589,
5,
1,
30
] | 4 | [] | [] | 0 | true | Domain | Nif11 domain | Nif11 domain | Nif11 | 6 |
IPR012904 | 12,904 | 8-oxoguanine DNA glycosylase, N-terminal | OGG_N | Domain | 7,197 | false | false | The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity ( ) and DNA lyase acti... | [
"GO:0003684",
"GO:0008534",
"GO:0006289"
] | [
"damaged DNA binding",
"oxidized purine nucleobase lesion DNA N-glycosylase activity",
"nucleotide-excision repair"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF07934"
] | [
"OGG_N"
] | [
7197
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.2.2.-",
"4.2.99.18",
"PWY-2681",
"PWY-5316",
"PWY-5381",
"PWY-7342",
"PWY-7564",
"PWY-8106",
"R-DME-110329",
"R-DME-110330",
"R-DME-110331",
"R-DME-110357",
"R-HSA-110328",
"R-HSA-110329",
"R-HSA-110330",
"R-HSA-110331",
"R-HSA-110357",
"R-HSA-5649702",
"R-HSA-9656255",
"R-H... | [
"EC:3.2.2.-",
"EC:4.2.99.18",
"METACYC:PWY-2681",
"METACYC:PWY-5316",
"METACYC:PWY-5381",
"METACYC:PWY-7342",
"METACYC:PWY-7564",
"METACYC:PWY-8106",
"REACTOME:R-DME-110329",
"REACTOME:R-DME-110330",
"REACTOME:R-DME-110331",
"REACTOME:R-DME-110357",
"REACTOME:R-HSA-110328",
"REACTOME:R-HSA... | 34 | [
"1ebm",
"1fn7",
"1hu0",
"1ko9",
"1lwv",
"1lww",
"1lwy",
"1m3h",
"1m3q",
"1n39",
"1n3a",
"1n3c",
"1yqk",
"1yql",
"1yqm",
"1yqr",
"2i5w",
"2nob",
"2noe",
"2nof",
"2noh",
"2noi",
"2nol",
"2noz",
"2xhi",
"3f0z",
"3f10",
"3i0w",
"3i0x",
"3ih7",
"3ktu",
"4ejy"... | 73 | [
"PUB00013719",
"PUB00016467"
] | [
"10706276",
"11902834"
] | [
"Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA.",
"Reciprocal \"flipping\" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase."
] | [
2000,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
549,
2186,
4409,
53
] | 4 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
3,
3,
3,
14,
4,
1,
3,
4,
1,
4
] | 10 | true | Domain | 8-oxoguanine DNA glycosylase, N-terminal | 8-oxoguanine DNA glycosylase, N-terminal | OGG_N | 6 |
IPR012905 | 12,905 | PA-IL-like | PA-IL | Family | 145 | false | false | The members of this family are similar to the galactophilic lectin-1 expressed by Pseudomonas aeruginosa (PA-IL, ). Lectins recognising specific carbohydrates found on the surface of host cells are known to be involved in the initiation of infections by this organism. The protein is thought to be organised into an exte... | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07828",
"PIRSF020485"
] | [
"PA-IL",
"PA-IL"
] | [
145,
11
] | 2 | [] | [] | [] | 0 | [
"1l7l",
"1oko",
"1uoj",
"2vxj",
"2wyf",
"3zyb",
"3zyf",
"3zyh",
"4a6s",
"4al9",
"4cp9",
"4cpb",
"4ljh",
"4lk6",
"4lk7",
"4lkd",
"4lke",
"4lkf",
"4yw6",
"4yw7",
"4ywa",
"5d21",
"5mih",
"5odu",
"5ofi",
"5ofx",
"5ofz",
"6ygq",
"6yo3",
"6yoh",
"7fio",
"7fjh"... | 38 | [
"PUB00016484"
] | [
"1429650"
] | [
"Analysis of the amino acid sequence of the Pseudomonas aeruginosa galactophilic PA-I lectin."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Acyrthosiphon pisum",
"Bacteria"
] | [
1,
144
] | 2 | [] | [] | 0 | true | Family | PA-IL-like | PA-IL-like | PA-IL | 1 |
IPR012906 | 12,906 | Transcriptional repressor PaaX-like, N-terminal | PaaX-like_N | Domain | 8,167 | false | false | This entry describes the N-terminal region of Transcriptional repressor PaaX from Escherichia coli and similar bacterial proteins. PaaX is involved in metabolism of phenylacetic acid [ , , ]. The gene product has been shown to bind to the promoter sites and repress their transcription [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07848"
] | [
"PaaX"
] | [
8167
] | 1 | [] | [] | [] | 0 | [
"3kfw",
"3l09",
"8a39"
] | 3 | [
"PUB00010200",
"PUB00015494",
"PUB00015522"
] | [
"9748275",
"11260461",
"10766858"
] | [
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.",
"Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in ... | [
1998,
2001,
2000
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Opisthokonta",
"Siphoviridae sp. ctiMP24",
"unclassified sequences"
] | [
33,
8075,
2,
1,
56
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Transcriptional repressor PaaX-like, N-terminal | Transcriptional repressor PaaX-like, N-terminal | PaaX-like_N | 1 |
IPR012907 | 12,907 | Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal | Peptidase_S11_C | Domain | 22,267 | false | false | Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif... | [
"GO:0009002",
"GO:0006508"
] | [
"serine-type D-Ala-D-Ala carboxypeptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF07943",
"SM00936"
] | [
"PBP5_C",
"PBP5_C"
] | [
22091,
20322
] | 2 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.4.16.4",
"PWY-5265",
"PWY-6471"
] | [
"EC:3.4.16.4",
"METACYC:PWY-5265",
"METACYC:PWY-6471"
] | 3 | [
"1hd8",
"1nj4",
"1nzo",
"1nzu",
"1sdn",
"1xp4",
"1z6f",
"3a3j",
"3beb",
"3bec",
"3it9",
"3ita",
"3itb",
"3mfd",
"3mzd",
"3mze",
"3mzf",
"4drt",
"4k91",
"5fsr",
"5j8x",
"5tr7",
"6ntz",
"6osu"
] | 24 | [
"PUB00000522",
"PUB00003576",
"PUB00016400"
] | [
"8439290",
"7845208",
"10967102"
] | [
"Evolutionary families of peptidases.",
"Families of serine peptidases.",
"Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution."
] | [
1993,
1994,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stx2-converting phage 1717",
"unclassified sequences"
] | [
22026,
41,
1,
199
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal | Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal | Peptidase_S11_C | 4 |
IPR012908 | 12,908 | GPI inositol-deacylase PGAP1-like alpha/beta domain | PGAP1-ab_dom-like | Domain | 10,150 | false | false | This domain is found in GPI inositol-deacylase PGAP1 and related proteins. It is found toward the N terminus and it is a lipase domain with a typical α/β/α hydrolase architecture [ ]. PGAP1 is an endoplasmic reticulum membrane protein with a catalytic serine-containing motif that is conserved in a number of lipases. PG... | [
"GO:0016788"
] | [
"hydrolase activity, acting on ester bonds"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07819"
] | [
"PGAP1"
] | [
10150
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162791",
"R-MMU-162791",
"R-RNO-162791"
] | [
"REACTOME:R-HSA-162791",
"REACTOME:R-MMU-162791",
"REACTOME:R-RNO-162791"
] | 3 | [
"6wpx",
"6wpy",
"8k9q",
"8k9r",
"8k9t"
] | 5 | [
"PUB00055596",
"PUB00094351",
"PUB00155994"
] | [
"14734546",
"6319176",
"38167496"
] | [
"Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p.",
"Hepatic adenylate cyclase and phosphodiesterase activity during acute ethionine intoxication.",
"Molecular basis of the inositol deacylase PGAP1 involved in quality control of GPI-AP biogen... | [
2004,
1984,
2024
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"Viruses",
"metagenomes"
] | [
3564,
6550,
2,
5,
29
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
13,
1,
2,
1,
3,
1,
2,
6,
3,
1,
1,
26
] | 12 | true | Domain | GPI inositol-deacylase PGAP1-like alpha/beta domain | GPI inositol-deacylase PGAP1-like alpha/beta domain | PGAP1-ab_dom-like | 6 |
IPR012909 | 12,909 | PHA accumulation regulator DNA-binding, N-terminal | PHA_DNA-bd_N | Domain | 5,168 | false | false | This domain is found at the N terminus of the polyhydroxyalkanoate (PHA) synthesis regulators. These regulators have been shown to directly bind DNA and PHA [ ]. The invariant nature of this domain compared to the C-terminal domain(s) suggests that it contains the DNA-binding function. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07879"
] | [
"PHB_acc_N"
] | [
5168
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00013500"
] | [
"12081972"
] | [
"A repressor protein, PhaR, regulates polyhydroxyalkanoate (PHA) synthesis via its direct interaction with PHA."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5097,
9,
62
] | 3 | [] | [] | 0 | true | Domain | PHA accumulation regulator DNA-binding, N-terminal | PHA accumulation regulator DNA-binding, N-terminal | PHA_DNA-bd_N | 4 |
IPR012910 | 12,910 | TonB-dependent receptor, plug domain | Plug_dom | Domain | 352,625 | false | false | This entry represents the plug domain, which has been shown to be an independently folding subunit of the TonB-dependent receptors [ ]. It acts as the channel gate, blocking the pore until the channel is bound by a ligand. At this point it undergoes conformational changes and opens the channel. In Escherichia coli the ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07715"
] | [
"Plug"
] | [
352625
] | 1 | [
"GP",
"REACTOME",
"REACTOME"
] | [
"GenProp0543",
"R-HSA-9638334",
"R-HSA-9638482"
] | [
"GP:GenProp0543",
"REACTOME:R-HSA-9638334",
"REACTOME:R-HSA-9638482"
] | 3 | [
"1by3",
"1by5",
"1fcp",
"1fep",
"1fi1",
"1kmo",
"1kmp",
"1nqe",
"1nqf",
"1nqg",
"1nqh",
"1pnz",
"1po0",
"1po3",
"1qff",
"1qfg",
"1qjq",
"1qkc",
"1ujw",
"1xkh",
"1xkw",
"2fcp",
"2grx",
"2gsk",
"2guf",
"2hdf",
"2hdi",
"2iah",
"2o5p",
"2w16",
"2w6t",
"2w6u"... | 152 | [
"PUB00006673",
"PUB00014980",
"PUB00014981",
"PUB00014984",
"PUB00014986",
"PUB00015225",
"PUB00035726",
"PUB00035727"
] | [
"9886293",
"14499604",
"9865695",
"12652322",
"11872840",
"15111112",
"15993072",
"12957833"
] | [
"Crystal structure of the outer membrane active transporter FepA from Escherichia coli.",
"The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation.",
"Transmembrane sig... | [
1999,
2003,
1998,
2003,
2002,
2004,
2005,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5,
348587,
502,
18,
3513
] | 5 | [
"Escherichia coli (strain K12)"
] | [
10
] | 1 | true | Domain | TonB-dependent receptor, plug domain | TonB-dependent receptor, plug domain | Plug_dom | 4 |
IPR012911 | 12,911 | Protein serine/threonine phosphatase 2C, C-terminal | PP2C_C | Domain | 4,539 | false | false | Protein phosphatase 2C (PP2C, also known as Protein phosphatase 1) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteristic of mammalian PP2Cs. This domain consists of three antiparallel α helices, one... | [
"GO:0000287",
"GO:0004721",
"GO:0030145"
] | [
"magnesium ion binding",
"phosphoprotein phosphatase activity",
"manganese ion binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PFAM"
] | [
"PF07830"
] | [
"PP2C_C"
] | [
4539
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.16",
"R-BTA-1169408",
"R-BTA-2173795",
"R-BTA-380972",
"R-HSA-1169408",
"R-HSA-2173795",
"R-HSA-380972",
"R-HSA-9700645",
"R-HSA-9725370",
"R-MMU-1169408",
"R-MMU-2173795",
"R-MMU-380972",
"R-RNO-1169408",
"R-RNO-2173795",
"R-RNO-380972"
] | [
"EC:3.1.3.16",
"REACTOME:R-BTA-1169408",
"REACTOME:R-BTA-2173795",
"REACTOME:R-BTA-380972",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-2173795",
"REACTOME:R-HSA-380972",
"REACTOME:R-HSA-9700645",
"REACTOME:R-HSA-9725370",
"REACTOME:R-MMU-1169408",
"REACTOME:R-MMU-2173795",
"REACTOME:R-MMU-38097... | 15 | [
"1a6q",
"3fxj",
"3fxk",
"3fxl",
"3fxm",
"3fxo",
"4ra2",
"4raf",
"4rag"
] | 9 | [
"PUB00001297"
] | [
"9003755"
] | [
"Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
4539
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
16,
13,
10,
19
] | 5 | true | Domain | Protein serine/threonine phosphatase 2C, C-terminal | Protein serine/threonine phosphatase 2C, C-terminal | PP2C_C | 3 |
IPR012912 | 12,912 | Plasmid pRiA4b, Orf3-like domain | Plasmid_pRiA4b_Orf3-like | Domain | 8,494 | false | false | Members of this entry are similar to the protein product of ORF-3 ( ) found on plasmid pRiA4 in the bacterium Agrobacterium rhizogenes. This plasmid is responsible for tumorigenesis at wound sites of plants infected by this bacterium, but the ORF-3 product does not seem to be involved in the pathogenetic process [ ]. O... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07929",
"PTHR41878"
] | [
"PRiA4_ORF3",
""
] | [
8493,
5307
] | 2 | [] | [] | [] | 0 | [
"2i1s"
] | 1 | [
"PUB00016577"
] | [
"2226811"
] | [
"Characterization of the virA gene of the agropine-type plasmid pRiA4 of Agrobacterium rhizogenes."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
182,
7422,
766,
124
] | 4 | [] | [] | 0 | true | Domain | Plasmid pRiA4b, Orf3-like domain | Plasmid pRiA4b, Orf3-like domain | Plasmid_pRiA4b_Orf3-like | 3 |
IPR012913 | 12,913 | Protein OS9-like domain | OS9-like_dom | Domain | 7,513 | false | false | This entry represents a domain found in the OS9 protein, which is a lectin that functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD) [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07915"
] | [
"PRKCSH"
] | [
7513
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-382556",
"R-HSA-5358346",
"R-HSA-5362768",
"R-HSA-5678895",
"R-HSA-901032",
"R-MMU-382556",
"R-MMU-5358346",
"R-RNO-382556",
"R-RNO-5358346",
"R-SPO-5358346"
] | [
"REACTOME:R-HSA-382556",
"REACTOME:R-HSA-5358346",
"REACTOME:R-HSA-5362768",
"REACTOME:R-HSA-5678895",
"REACTOME:R-HSA-901032",
"REACTOME:R-MMU-382556",
"REACTOME:R-MMU-5358346",
"REACTOME:R-RNO-382556",
"REACTOME:R-RNO-5358346",
"REACTOME:R-SPO-5358346"
] | 10 | [
"3aih",
"6f99",
"6f9a",
"6vk3",
"8kes",
"8ket",
"8kev",
"9lwu",
"9og0",
"9uav"
] | 10 | [
"PUB00086554"
] | [
"17932042"
] | [
"OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum."
] | [
2007
] | 1 | [
"IPR044865"
] | [] | 1 | 0 | 1 | [
"Eukaryota",
"bird metagenome"
] | [
7511,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
2,
3,
2,
44,
10,
1,
2,
11,
1,
2,
8
] | 12 | true | Domain | Protein OS9-like domain | Protein OS9-like domain | OS9-like_dom | 5 |
IPR012914 | 12,914 | Purine catabolism PurC-like domain | PucR_dom | Domain | 16,084 | false | false | This domain is found in the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR, ). PucR is thought to be a transcriptional regulator of genes involved in the purine degradation pathway, and may contain a LysR-like DNA-binding domain [ ]. It is similar to LysR-type regulators in that it represses ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07905"
] | [
"PucR"
] | [
16084
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00016396",
"PUB00057827"
] | [
"11344136",
"12029039"
] | [
"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator.",
"Transcription analysis of the Bacillus subtilis PucR regulon and identification of a cis-acting sequence required for PucR-regulate... | [
2001,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
16033,
4,
47
] | 3 | [] | [] | 0 | true | Domain | Purine catabolism PurC-like domain | Purine catabolism PurC-like domain | PucR_dom | 3 |
IPR012916 | 12,916 | RED-like, N-terminal | RED_N | Domain | 4,263 | false | false | This domain contains sequences that are similar to the N-terminal region of Red protein ( ). This and related proteins contain a RED repeat which consists of a number of RE and RD sequence elements [ ]. The region in question has several conserved NLS sequences and a putative trimeric coiled-coil region [ ], suggesting... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07808"
] | [
"RED_N"
] | [
4263
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-72163",
"R-MMU-72163",
"R-RNO-72163"
] | [
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-72163"
] | 3 | [
"5o9z",
"6q8i",
"8qo9",
"8qzs"
] | 4 | [
"PUB00016574",
"PUB00090272",
"PUB00090273"
] | [
"10216252",
"28781166",
"22351768"
] | [
"Isolation, sequencing and expression of RED, a novel human gene encoding an acidic-basic dipeptide repeat.",
"Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.",
"RED, a spindle pole-associated protein, is required for kinetochore localization of MAD1, mitotic progression, and activ... | [
1999,
2017,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Acetivibrio clariflavus (strain DSM 19732 / NBRC 101661 / EBR45)",
"Eukaryota"
] | [
1,
4262
] | 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",
"Schizosaccharomyces pombe (stra... | [
4,
1,
1,
1,
11,
6,
1,
5,
6,
1,
9
] | 11 | true | Domain | RED-like, N-terminal | RED-like, N-terminal | RED_N | 5 |
IPR012917 | 12,917 | Protein of unknown function DUF3294 | DUF3294 | Family | 331 | false | false | This family was annotated as mitochondrial ribosomal protein Mrp8, based on the presumed similarity of the S.cerevisiae protein to an E.coli mitochondrial ribosomal protein. However, this similarity is spurious, and the function is not known. | [] | [] | [] | 0 | [
"PFAM",
"PIRSF"
] | [
"PF07957",
"PIRSF022944"
] | [
"DUF3294",
"Ribosomal_MRP8_mit"
] | [
331,
59
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Pseudomonadota"
] | [
1,
326,
4
] | 3 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Family | Protein of unknown function DUF3294 | Protein of unknown function DUF3294 | DUF3294 | 2 |
IPR012918 | 12,918 | RTP801-like | RTP801-like | Family | 2,244 | false | false | RTP801, also known as REDD1, is the protein product of a hypoxia-inducible factor 1 (HIF-1)- responsive gene and is thought to be involved in various cellular processes [ ]. Both RTP801 and RTP801-like (REDD2) work downstream of AKT and upstream of TSC2 to inhibit mTOR, a serine/threonine kinase that plays an essential... | [
"GO:0009968",
"GO:0005737"
] | [
"negative regulation of signal transduction",
"cytoplasm"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF07809",
"PTHR12478"
] | [
"RTP801_C",
""
] | [
2243,
2218
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5628897",
"R-DME-5628897",
"R-DRE-5628897",
"R-HSA-5628897",
"R-MMU-5628897",
"R-RNO-5628897",
"R-XTR-5628897"
] | [
"REACTOME:R-BTA-5628897",
"REACTOME:R-DME-5628897",
"REACTOME:R-DRE-5628897",
"REACTOME:R-HSA-5628897",
"REACTOME:R-MMU-5628897",
"REACTOME:R-RNO-5628897",
"REACTOME:R-XTR-5628897"
] | 7 | [
"3lq9",
"7mop"
] | 2 | [
"PUB00016594",
"PUB00057842",
"PUB00057843"
] | [
"11884613",
"15632201",
"16423342"
] | [
"Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis.",
"The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway.",
"scylla and charybde, homologues of the human apoptotic gene RTP801, are required for h... | [
2002,
2005,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2244
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
5,
5,
5
] | 5 | true | Family | RTP801-like | RTP801-like | RTP801-like | 5 |
IPR012919 | 12,919 | SUN domain | SUN_dom | Domain | 19,313 | false | false | Sad1/UNC-84 (SUN)-domain proteins are inner nuclear membrane (INM) proteins that are part of bridging complexes linking cytoskeletal elements with the nucleoskeleton. Originally identified based on an ~150-amino acid region of homology between the C terminus of the Schizosaccharomyces pombe Sad1 protein and the Caenorh... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF07738",
"PS51469"
] | [
"Sad1_UNC",
"SUN"
] | [
18899,
16623
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-983168",
"R-DME-983168",
"R-HSA-1221632",
"R-HSA-983168",
"R-MMU-983168"
] | [
"REACTOME:R-CEL-983168",
"REACTOME:R-DME-983168",
"REACTOME:R-HSA-1221632",
"REACTOME:R-HSA-983168",
"REACTOME:R-MMU-983168"
] | 5 | [
"3unp",
"4dxr",
"4dxs",
"4dxt",
"4fi9",
"5ed8",
"5ywz",
"6r15",
"6r16",
"6r2i",
"6wmd",
"6wme",
"6wmf",
"6wmg",
"7z8y",
"8b46",
"8b5x"
] | 17 | [
"PUB00057231",
"PUB00072664",
"PUB00072665",
"PUB00100392"
] | [
"15611647",
"16923827",
"19807882",
"18820457"
] | [
"Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex.",
"The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope.",
"Characterization of SUN-domain proteins at the higher plant nuclear envelope.",
"Drosophi... | [
2004,
2006,
2010,
2007
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"marine sediment metagenome"
] | [
12,
19300,
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... | [
23,
11,
57,
9,
38,
14,
2,
15,
32,
2,
2,
21
] | 12 | true | Domain | SUN domain | SUN domain | SUN_dom | 4 |
IPR012920 | 12,920 | Ribosomal RNA methyltransferase, SPB1-like, C-terminal | rRNA_MeTfrase_SPB1-like_C | Domain | 4,547 | false | false | This domain is found at the C terminus SPB1-like proteins. This domain interacts with the meandering tail of Erb1 and its removal is required to form the pre-mature inter-subunit surface of the Arx1/Nog2 particle [ , ]. SPB1 is an adoMet-dependent rRNA methyltransferase required for proper assembly of pre-ribosomal par... | [
"GO:0008168",
"GO:0006364",
"GO:0005634"
] | [
"methyltransferase activity",
"rRNA processing",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07780"
] | [
"Spb1_C"
] | [
4547
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.1.1.-",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601",
"PWY-6045"... | [
"EC:2.1.1.-",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",
"METACYC:PWY-5... | 149 | [
"6elz",
"6em5",
"6ylx",
"7nac",
"7nad",
"7ohr",
"7ohv",
"7r6k",
"7r6q",
"7r72",
"7r7a",
"7u0h",
"8esq",
"8esr",
"8etc",
"8etj",
"8fkp",
"8fkq",
"8fkr",
"8fks",
"8fkt",
"8fku",
"8fkv",
"8fkw",
"8fkx",
"8fky",
"8i9t",
"8i9v",
"8i9w",
"8i9x",
"8i9y",
"8i9z"... | 35 | [
"PUB00016377",
"PUB00056208",
"PUB00068804",
"PUB00068805",
"PUB00100534",
"PUB00100535"
] | [
"10556316",
"15546625",
"10648622",
"22195017",
"32668200",
"29245012"
] | [
"Spb1p is a putative methyltransferase required for 60S ribosomal subunit biogenesis in Saccharomyces cerevisiae.",
"Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage.",
"Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind ... | [
1999,
2004,
2000,
2011,
2020,
2017
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
4545,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
3,
2,
1,
2,
1,
1,
4,
2,
1,
1,
12
] | 12 | true | Domain | Ribosomal RNA methyltransferase, SPB1-like, C-terminal | Ribosomal RNA methyltransferase, SPB1-like, C-terminal | rRNA_MeTfrase_SPB1-like_C | 8 |
IPR012921 | 12,921 | Spen paralogue and orthologue SPOC, C-terminal | SPOC_C | Domain | 14,460 | false | false | Spen (split end) proteins regulate the expression of key transcriptional effectors in diverse signalling pathways. They are large proteins characterised by N-terminal RNA-binding motifs and a highly conserved C-terminal SPOC (Spen paralog and ortholog C-terminal) domain. The function of the SPOC domain is unknown, but ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07744"
] | [
"SPOC"
] | [
14460
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1221632",
"R-HSA-9013422",
"R-HSA-9845323",
"R-MMU-9013422"
] | [
"REACTOME:R-HSA-1221632",
"REACTOME:R-HSA-9013422",
"REACTOME:R-HSA-9845323",
"REACTOME:R-MMU-9013422"
] | 4 | [
"1ow1",
"2rt5",
"4bxz",
"5kxf",
"6ic8",
"6ic9",
"6q2v",
"6q5y",
"7z1k",
"7z27",
"8ou1"
] | 11 | [
"PUB00013949"
] | [
"12897056"
] | [
"A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling."
] | [
2003
] | 1 | [] | [
"IPR010912"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
14460
] | 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... | [
53,
2,
22,
6,
19,
13,
1,
17,
18,
1,
1,
33
] | 12 | true | Domain | Spen paralogue and orthologue SPOC, C-terminal | Spen paralogue and orthologue SPOC, C-terminal | SPOC_C | 5 |
IPR012922 | 12,922 | ORF D-335-like | ORF_D-335 | Domain | 123 | false | false | The sequences featured in this family are similar to a probable integrase ( ) expressed by the SSV1 virus of the archaeon Sulfolobus shibatae. This protein may be necessary for the integration of the virus into the host genome by a process of site-specific recombination [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07935"
] | [
"SSV1_ORF_D-335"
] | [
123
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014897"
] | [
"1926776"
] | [
"Complete nucleotide sequence of the virus SSV1 of the archaebacterium Sulfolobus shibatae."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Aporhodopirellula aestuarii",
"Fuselloviridae",
"Sulfolobaceae"
] | [
1,
9,
113
] | 3 | [] | [] | 0 | true | Domain | ORF D-335-like | ORF D-335-like | ORF_D-335 | 7 |
IPR012923 | 12,923 | Chromosome segregation in meiosis protein 3 | Csm3 | Domain | 3,984 | false | false | This entry represents a domain found in a group of proteins, including Csm3 from budding yeasts, Swi3 from fission yeasts and TIPIN from animals. They are involved in DNA replication and the maintenance of replication fork stability [ , , ]. | [
"GO:0006974",
"GO:0031297",
"GO:0005634"
] | [
"DNA damage response",
"replication fork processing",
"nucleus"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF07962"
] | [
"Swi3"
] | [
3984
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5693607",
"R-HSA-5693607",
"R-MMU-5693607",
"R-RNO-5693607"
] | [
"REACTOME:R-DME-5693607",
"REACTOME:R-HSA-5693607",
"REACTOME:R-MMU-5693607",
"REACTOME:R-RNO-5693607"
] | 4 | [
"6skl",
"6xwx",
"7pfo",
"7plo",
"7pmk",
"7pmn",
"8b9a",
"8b9b",
"8b9c",
"8b9d",
"8kg6",
"8ouw",
"8xgc",
"9e2w",
"9e2x"
] | 15 | [
"PUB00016387",
"PUB00066967",
"PUB00077532"
] | [
"15367656",
"22842922",
"17116885"
] | [
"Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.",
"Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.",
"Tipin and Timeless form a mutually protective complex required for genotoxic stress resist... | [
2004,
2012,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3984
] | 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... | [
5,
1,
3,
2,
5,
4,
1,
3,
7,
1,
1,
4
] | 12 | true | Domain | Chromosome segregation in meiosis protein 3 | Chromosome segregation in meiosis protein 3 | Csm3 | 8 |
IPR012924 | 12,924 | TfuA-like, core | TfuA_core | Domain | 1,686 | false | false | This domain consists of a group of sequences that are similar to the core of TfuA protein ( ). TfuA plays a crucial dual role in peptide backbone thioamidation, functioning as both a hydrolase and a protein interaction mediator. It catalyses the hydrolysis of ThiS-COSH using a Ser/Lys catalytic pair to generate sulfide... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07812"
] | [
"TfuA"
] | [
1686
] | 1 | [] | [] | [] | 0 | [
"6xp8"
] | 1 | [
"PUB00016421",
"PUB00093716",
"PUB00158997"
] | [
"8763943",
"28880150",
"33707784"
] | [
"A newly discovered gene, tfuA, involved in the production of the ribosomally synthesized peptide antibiotic trifolitoxin.",
"Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea.",
"Functional elucidation of TfuA in peptide backbone thioamidat... | [
1996,
2017,
2021
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Sordariales",
"ecological metagenomes",
"uncultured Caudovirales phage"
] | [
212,
1463,
2,
8,
1
] | 5 | [] | [] | 0 | true | Domain | TfuA-like, core | TfuA-like, core | TfuA_core | 3 |
IPR012925 | 12,925 | TipAS antibiotic-recognition domain | TipAS_dom | Domain | 10,416 | false | false | TipAL is a bacterial transcriptional regulator of the MerR family. The tipA gene can be expressed as a long form, TipAL, and a short form, TipAS, which constitutes the C-terminal part of TipAL. TipAS forms the antibiotic-recognition domain [ ]. This domain, which has an α-helical globin-like fold, is also found at the ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07739"
] | [
"TipAS"
] | [
10416
] | 1 | [] | [] | [] | 0 | [
"1ny9",
"2mbz",
"2mc0",
"3qao",
"6et8",
"6h95",
"6h96",
"6h97",
"6hai",
"7cla",
"8rky"
] | 11 | [
"PUB00015229",
"PUB00055552",
"PUB00055553"
] | [
"12682015",
"10200972",
"10498730"
] | [
"Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators.",
"Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters.",
"Identification of a regulator that controls stationary-phase expression of catalase-peroxidase in Cau... | [
2003,
1999,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes",
"unclassified Caudoviricetes"
] | [
10283,
8,
7,
116,
2
] | 5 | [] | [] | 0 | true | Domain | TipAS antibiotic-recognition domain | TipAS antibiotic-recognition domain | TipAS_dom | 4 |
IPR012926 | 12,926 | TMEM120A/B | TMEM120A/B | Family | 5,183 | false | false | This entry represents a group of transmembrane proteins including TACAN (also known as TMEM120A) and TMEM120B. TMEM120A is involved in mechanosensation and plays an essential role in lipid metabolism and adipocyte differentiation [ , ]. It was first described as an ion channel that contributes to sensing mechanical pai... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF07851",
"PTHR21433"
] | [
"TMEM120A-B",
""
] | [
5183,
5082
] | 2 | [] | [] | [] | 0 | [
"7cxr",
"7f3t",
"7f3u",
"7f6v",
"7f73",
"7n0k",
"7n0l",
"7n7p"
] | 8 | [
"PUB00094219",
"PUB00094220",
"PUB00158954",
"PUB00158955",
"PUB00158956",
"PUB00158957"
] | [
"32084332",
"26024229",
"36420836",
"34374645",
"34409941",
"34465718"
] | [
"TACAN Is an Ion Channel Involved in Sensing Mechanical Pain.",
"TMEM120A and B: Nuclear Envelope Transmembrane Proteins Important for Adipocyte Differentiation.",
"Regulation of PKD2 channel function by TACAN.",
"TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty ac... | [
2020,
2015,
2023,
2021,
2021,
2021
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
5183
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
21,
1,
8,
3,
8,
5,
6,
8,
15
] | 9 | true | Family | TMEM120A/B | TMEM120A/B | TMEM120A/B | 6 |
IPR012927 | 12,927 | Effector protease OspD3-like, N-terminal | Toxin_15_N | Domain | 528 | false | false | This domain is present in the N-terminal region of the ShET2 enterotoxin and the Effector protease OspD3 from Shigella flexneri, Ankyrin repeat protein A (ARPA) from Escherichia coli and related sequences from bacteria. OspD3 is an effector protease that disrupts necroptosis in host cells by mediating proteolytic cleav... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07906"
] | [
"Toxin_15"
] | [
528
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00084320",
"PUB00162553"
] | [
"28085133",
"32657447"
] | [
"EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation.",
"A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase-8."
] | [
2017,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
521,
7
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Effector protease OspD3-like, N-terminal | Effector protease OspD3-like, N-terminal | Toxin_15_N | 4 |
IPR012928 | 12,928 | Clostridium neurotoxin, receptor binding N-terminal | Toxin_rcpt-bd_N | Domain | 372 | false | false | The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. These toxins act as inhibitors of neurotransmitter release [ , ]. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain ( ), the central translocation domai... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF07953"
] | [
"Toxin_R_bind_N"
] | [
372
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24.69",
"R-HSA-5250955",
"R-HSA-5250958",
"R-HSA-5250968",
"R-HSA-5250971",
"R-HSA-5250981",
"R-HSA-5250982",
"R-HSA-5250989",
"R-HSA-5250992"
] | [
"EC:3.4.24.69",
"REACTOME:R-HSA-5250955",
"REACTOME:R-HSA-5250958",
"REACTOME:R-HSA-5250968",
"REACTOME:R-HSA-5250971",
"REACTOME:R-HSA-5250981",
"REACTOME:R-HSA-5250982",
"REACTOME:R-HSA-5250989",
"REACTOME:R-HSA-5250992"
] | 9 | [
"1a8d",
"1af9",
"1d0h",
"1dfq",
"1diw",
"1dll",
"1epw",
"1f31",
"1fv2",
"1fv3",
"1g9a",
"1g9b",
"1g9c",
"1g9d",
"1i1e",
"1s0b",
"1s0c",
"1s0d",
"1s0e",
"1s0f",
"1s0g",
"1yxw",
"1yyn",
"1z0h",
"2nm1",
"2np0",
"2nyy",
"2nz9",
"2vu9",
"2vua",
"2vxr",
"3azv"... | 150 | [
"PUB00016466",
"PUB00088575",
"PUB00088576"
] | [
"9783750",
"1328520",
"23435179"
] | [
"Crystal structure of botulinum neurotoxin type A and implications for toxicity.",
"Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation.",
"Botulinum toxins: mechanisms of action, antinociception and clinic... | [
1998,
1992,
2013
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
332,
8,
27,
5
] | 4 | [] | [] | 0 | true | Domain | Clostridium neurotoxin, receptor binding N-terminal | Clostridium neurotoxin, receptor binding N-terminal | Toxin_rcpt-bd_N | 7 |
IPR012929 | 12,929 | Nucleoprotein, TPR/MLP1-2 domain | Nucleoprot-TPR/MLP1-2_dom | Domain | 4,575 | false | false | This domain is found in several proteins, including TPR protein and yeast myosin-like protein 1 (MLP1) and MPL2. TPR and MLP1/2 share several features; for example, they have coiled-coil regions and are associated with nuclear pores [ , , ]. TPR is thought to be a component of nuclear pore complex-attached intranuclear... | [
"GO:0006606"
] | [
"protein import into nucleus"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF07926"
] | [
"TPR_MLP1_2"
] | [
4575
] | 1 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"GenProp2036",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-DME-170822",
"R-DME-3108214",
"R-DME-3301854",
"R-DME-4085377",
"R-DME-4551638",
"R-DME-4615885",
"R-DME-5578749",
"R-HSA-1169408",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-H... | [
"GP:GenProp2036",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-DME-170822",
"REACTOME:R-DME-3108214",
"REACTOME:R-DME-3301854",
"REACTOME:R-DME-4085377",
"REACTOME:R-DME-4551638",
"REACTOME:R-DME-4615885",
"REACTOME:R-DME-55787... | 86 | [] | 0 | [
"PUB00016402",
"PUB00016576",
"PUB00075590",
"PUB00075591"
] | [
"9024684",
"7798308",
"10085285",
"12531921"
] | [
"Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments.",
"Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex.",
"Proteins c... | [
1997,
1994,
1999,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4575
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"... | [
4,
9,
2,
1,
3,
1,
1,
4,
1,
1,
38
] | 11 | true | Domain | Nucleoprotein, TPR/MLP1-2 domain | Nucleoprotein, TPR/MLP1-2 domain | Nucleoprot-TPR/MLP1-2_dom | 1 |
IPR012930 | 12,930 | TraC-like | TraC | Family | 740 | false | false | The members of this family are sequences that are similar to TraC ( ) from Rhizobium etli. The gene encoding this protein is one of a group of genes found on plasmid p42a of Rhizobium etli (strain CFN 42/ATCC 51251) that are thought to be involved in the process of plasmid self-transmission. Mobilisation of plasmid p42... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07820"
] | [
"TraC"
] | [
740
] | 1 | [
"GP"
] | [
"GenProp0490"
] | [
"GP:GenProp0490"
] | 1 | [] | 0 | [
"PUB00016590"
] | [
"12591886"
] | [
"Conjugative transfer of p42a from rhizobium etli CFN42, which is required for mobilization of the symbiotic plasmid, is regulated by quorum sensing."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"marine sediment metagenome"
] | [
739,
1
] | 2 | [] | [] | 0 | true | Family | TraC-like | TraC-like | TraC | 2 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.