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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR015196 | 15,196 | Peptide-N-glycosidase F, N-terminal | PngaseF_N | Domain | 1,378 | false | false | This domain adopts an eight-stranded antiparallel β jelly roll configuration, with the β strands arranged into two sheets. It is similar in topology to many viral capsid proteins, as well as lectins and several glucanases. This domain allows the protein to bind sugars and catalyses the complete removal of N-linked olig... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF09112",
"SM01290"
] | [
"N-glycanase_N",
"N-glycanase_N"
] | [
1261,
1343
] | 2 | [] | [] | [] | 0 | [
"3ks7",
"4qhb",
"4r4x",
"4r4z",
"7zgn"
] | 5 | [
"PUB00035451"
] | [
"7881905"
] | [
"The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
990,
373,
2,
13
] | 4 | [
"Danio rerio"
] | [
1
] | 1 | true | Domain | Peptide-N-glycosidase F, N-terminal | Peptide-N-glycosidase F, N-terminal | PngaseF_N | 3 |
IPR015197 | 15,197 | Peptide-N-glycosidase F, C-terminal | PngaseF_C | Domain | 1,674 | false | false | This domain adopts an eight-stranded antiparallel β jelly roll configuration, with the β strands arranged into two sheets. It is similar in topology to many viral capsid proteins, as well as lectins and several glucanases. This domain allows the protein to bind sugars and catalyses the complete removal of N-linked olig... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09113"
] | [
"N-glycanase_C"
] | [
1674
] | 1 | [] | [] | [] | 0 | [
"1pgs",
"1pnf",
"1png",
"3ks7",
"3pms",
"4qhb",
"4r4x",
"4r4z",
"7zgn"
] | 9 | [
"PUB00035451"
] | [
"7881905"
] | [
"The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
1247,
389,
6,
32
] | 4 | [
"Danio rerio"
] | [
1
] | 1 | true | Domain | Peptide-N-glycosidase F, C-terminal | Peptide-N-glycosidase F, C-terminal | PngaseF_C | 2 |
IPR015198 | 15,198 | Bacteriophage T4, MotA, transcription regulator N-terminal | Phage_T4_MotA_Tscrpt_reg_N | Domain | 241 | false | false | Transcription factor MotA is required for the activation of middle promoters in Bacteriophage T4, in addition to phage T4 co-activator AsiA, and sigma-70-containing Escherichia coli RNA polymerase. Phage T4 middle promoters have the sigma70 -10 DNA element, but not the -35 element; instead, they have a MotA box at -30 ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09114"
] | [
"MotA_activ"
] | [
241
] | 1 | [] | [] | [] | 0 | [
"1bja",
"1i1s",
"6k4y"
] | 3 | [
"PUB00023643",
"PUB00035545"
] | [
"9155025",
"16996538"
] | [
"The activation domain of the MotA transcription factor from bacteriophage T4.",
"Mutational analysis of sigma70 region 4 needed for appropriation by the bacteriophage T4 transcription factors AsiA and MotA."
] | [
1997,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Propionigenium maris DSM 9537",
"Viruses"
] | [
1,
240
] | 2 | [] | [] | 0 | true | Domain | Bacteriophage T4, MotA, transcription regulator N-terminal | Bacteriophage T4, MotA, transcription regulator N-terminal | Phage_T4_MotA_Tscrpt_reg_N | 1 |
IPR015199 | 15,199 | DNA polymerase III, delta subunit, C-terminal | DNA_pol_III_delta_C | Domain | 7,771 | false | false | This entry represents a domain which is predominantly found in prokaryotic DNA polymerase III, assuming an α helical structure with a core of five α helices and an additional small helix. This domain is essential for the formation of the polymerase clamp loader [ ]. | [
"GO:0003677",
"GO:0003887",
"GO:0006260",
"GO:0009360"
] | [
"DNA binding",
"DNA-directed DNA polymerase activity",
"DNA replication",
"DNA polymerase III complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF09115"
] | [
"DNApol3-delta_C"
] | [
7771
] | 1 | [
"EC"
] | [
"2.7.7.7"
] | [
"EC:2.7.7.7"
] | 1 | [
"1a5t",
"1jr3",
"1xxh",
"1xxi",
"3glf",
"3glg",
"3glh",
"3gli",
"8giy",
"8giz",
"8gj0",
"8gj1",
"8gj2",
"8gj3",
"8val",
"8vam",
"8van",
"8vap",
"8vaq",
"8var",
"8vas",
"8vat"
] | 22 | [
"PUB00006060"
] | [
"9363942"
] | [
"Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
7660,
3,
108
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DNA polymerase III, delta subunit, C-terminal | DNA polymerase III, delta subunit, C-terminal | DNA_pol_III_delta_C | 9 |
IPR015200 | 15,200 | Sliding clamp, C-terminal | Sliding_clamp_C | Domain | 463 | false | false | This domain is essential for the interaction of the sliding clamp (also known as gp45) with the corresponding polymerase. It adopts a DNA clamp fold, consisting of two α-helices and two β-sheets - the fold is duplicated and has internal pseudo two-fold symmetry [ , ]. | [
"GO:0039693"
] | [
"viral DNA genome replication"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF09116"
] | [
"gp45-slide_C"
] | [
463
] | 1 | [] | [] | [] | 0 | [
"1b77",
"1b8h",
"1czd",
"3u5z",
"3u60",
"3u61",
"6drt",
"7d7d",
"8uh7",
"8uk9",
"8unf",
"8unh"
] | 12 | [
"PUB00007415",
"PUB00100539"
] | [
"10535734",
"33602900"
] | [
"Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex.",
"Transcription activation by a sliding clamp."
] | [
1999,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Pseudomonadati",
"Viruses",
"metagenomes"
] | [
7,
2,
435,
19
] | 4 | [] | [] | 0 | true | Domain | Sliding clamp, C-terminal | Sliding clamp, C-terminal | Sliding_clamp_C | 8 |
IPR015201 | 15,201 | Antimicrobial protein MiAMP1 | Antimicrobial_MiAMP1 | Family | 399 | false | false | MiAMP1 is a highly basic protein from the nut kernel of Macadamia integrifolia (Macadamia nut), which inhibits the growth of several microbial plant pathogens in vitro while having no effect on mammalian or plant cells. It consists of eight β-strands which are arranged in two Greek key motifs. These Greek key motifs th... | [
"GO:0006952",
"GO:0045926"
] | [
"defense response",
"negative regulation of growth"
] | [
"biological_process",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09117"
] | [
"MiAMP1"
] | [
399
] | 1 | [] | [] | [] | 0 | [
"1c01"
] | 1 | [
"PUB00023800"
] | [
"10543955"
] | [
"MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Eukaryota"
] | [
58,
341
] | 2 | [
"Zea mays"
] | [
4
] | 1 | true | Family | Antimicrobial protein MiAMP1 | Antimicrobial protein MiAMP1 | Antimicrobial_MiAMP1 | 8 |
IPR015202 | 15,202 | Galactose oxidase-like, Early set domain | GO-like_E_set | Domain | 12,637 | false | false | E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for c... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09118",
"cd02851"
] | [
"GO-like_E_set",
"E_set_GO_C"
] | [
12617,
12082
] | 2 | [] | [] | [] | 0 | [
"1gof",
"1gog",
"1goh",
"1k3i",
"1t2x",
"2eib",
"2eic",
"2eid",
"2eie",
"2jkx",
"2vz1",
"2vz3",
"2wq8",
"4unm",
"5c86",
"5c92",
"5lqi",
"5lxz",
"6ryv",
"6ryw",
"6ryx",
"6stx",
"6xlr",
"6xls",
"6xlt",
"8tx5",
"8tx6",
"9g43",
"9g8h"
] | 29 | [
"PUB00003324",
"PUB00028414",
"PUB00044942",
"PUB00080765",
"PUB00080766"
] | [
"8182749",
"11923309",
"10825529",
"12530525",
"15239382"
] | [
"Crystal structure of a free radical enzyme, galactose oxidase.",
"Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.",
"Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.",
"Oligo-1,6-glucosi... | [
1994,
2002,
2000,
2002,
2004
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
2667,
9957,
8
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
28,
2,
10,
17
] | 4 | true | Domain | Galactose oxidase-like, Early set domain | Galactose oxidase-like, Early set domain | GO-like_E_set | 9 |
IPR015203 | 15,203 | Secreted effector protein SptP, N-terminal domain | SptP_N | Domain | 724 | false | false | The domain is found in the Salmonella effector protein SptP, which interacts with SicP chaperone dimers mainly through four regions of its chaperone-binding domain. The structure of the SptP-SicP complex contains four molecules of SicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers th... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF09119"
] | [
"SicP-binding"
] | [
724
] | 1 | [] | [] | [] | 0 | [
"1jyo"
] | 1 | [
"PUB00014306"
] | [
"11689946"
] | [
"Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
724
] | 1 | [] | [] | 0 | true | Domain | Secreted effector protein SptP, N-terminal domain | Secreted effector protein SptP, N-terminal domain | SptP_N | 8 |
IPR015206 | 15,206 | 3-mercaptopyruvate sulfurtransferase, C-terminal domain | SulfurTase_C | Domain | 47 | false | false | This entry represents a domain found in putative 3-mercaptopyruvate sulphurtransferases from Trypanosomatida (kinetoplastids). This domain adopts a structure consisting of a four-stranded antiparallel β-sheet and an α-helix, arranged in a β(2)-α-β(2) fashion, and bearing a remarkable structural similarity to the FK506-... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09122"
] | [
"DUF1930"
] | [
47
] | 1 | [] | [] | [] | 0 | [
"1okg"
] | 1 | [
"PUB00029481",
"PUB00088236"
] | [
"12952945",
"12419809"
] | [
"The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active site.",
"3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolis... | [
2003,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Trypanosomatidae"
] | [
47
] | 1 | [] | [] | 0 | true | Domain | 3-mercaptopyruvate sulfurtransferase, C-terminal domain | 3-mercaptopyruvate sulfurtransferase, C-terminal domain | SulfurTase_C | 7 |
IPR015207 | 15,207 | Protein of unknown function DUF1931 | DUF1931 | Family | 679 | false | false | This entry represents a set of hypothetical bacterial proteins containing a core of six α-helices, where one central helix is surrounded by the other five. The exact function of this family has not, as yet, been determined [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09123"
] | [
"DUF1931"
] | [
679
] | 1 | [] | [] | [] | 0 | [
"1r4v",
"1wwi",
"1wws"
] | 3 | [
"PUB00035390"
] | [
"16287087"
] | [
"The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
242,
435,
2
] | 3 | [] | [] | 0 | true | Family | Protein of unknown function DUF1931 | Protein of unknown function DUF1931 | DUF1931 | 6 |
IPR015208 | 15,208 | T4 recombination endonuclease VII, dimerisation | T4_recomb_endonuclease_dimer | Domain | 336 | false | false | This entry represents a dimerisation domain predominantly found in Bacteriophage T4 recombination endonuclease VII. It adopts a helical secondary structure, with three α helices oriented parallel to each other. As well as mediating dimerisation of the protein, this domain is also involved in binding to the DNA major gr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09124"
] | [
"Endonuc-dimeris"
] | [
336
] | 1 | [] | [] | [] | 0 | [
"1e7d",
"1e7l",
"1en7",
"2qnc",
"2qnf"
] | 5 | [
"PUB00024458"
] | [
"11327769"
] | [
"Conformational flexibility in T4 endonuclease VII revealed by crystallography: implications for substrate binding and cleavage."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
23,
4,
309
] | 3 | [] | [] | 0 | true | Domain | T4 recombination endonuclease VII, dimerisation | T4 recombination endonuclease VII, dimerisation | T4_recomb_endonuclease_dimer | 2 |
IPR015209 | 15,209 | Cytochrome C oxidase subunit IIa, transmembrane domain | Cyt_c_oxidase_su2a_TM_dom | Domain | 47 | false | false | This N-terminal domain forms the transmembrane region in subunit II of cytochrome c oxidase from Thermus thermophilus. This domain adopts a tertiary structure consisting of two antiparallel transmembrane helices, in a transmembrane helix hairpin fold [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09125"
] | [
"COX2-transmemb"
] | [
47
] | 1 | [] | [] | [] | 0 | [
"1ehk",
"1xme",
"2qpd",
"2qpe",
"3bvd",
"3eh3",
"3eh4",
"3eh5",
"3qjq",
"3qjr",
"3qjs",
"3qjt",
"3qju",
"3qjv",
"3s33",
"3s38",
"3s39",
"3s3a",
"3s3b",
"3s3c",
"3s3d",
"3s8f",
"3s8g",
"4fa7",
"4faa",
"4g70",
"4g71",
"4g72",
"4g7q",
"4g7r",
"4g7s",
"4gp4"... | 41 | [
"PUB00024563"
] | [
"10775261"
] | [
"Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Deinococcota",
"Haloferax mucosum ATCC BAA-1512"
] | [
46,
1
] | 2 | [] | [] | 0 | true | Domain | Cytochrome C oxidase subunit IIa, transmembrane domain | Cytochrome C oxidase subunit IIa, transmembrane domain | Cyt_c_oxidase_su2a_TM_dom | 1 |
IPR015210 | 15,210 | Type II restriction enzyme NaeI | NaeI | Domain | 544 | false | false | This restriction endonuclease NaeI domain adopts a secondary structure consisting of nine α-helices, six 3-10 helices and 13 β-strands. NaeI binds two GCC-CGG recognition sequences to cleave DNA into blunt-ended products [ ]. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enz... | [
"GO:0009036",
"GO:0009307"
] | [
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF09126",
"cd22338"
] | [
"NaeI",
"NaeI-like"
] | [
544,
467
] | 2 | [] | [] | [] | 0 | [
"1ev7",
"1iaw"
] | 2 | [
"PUB00028462",
"PUB00028667",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707",
"PUB00110634",
"PUB00110635"
] | [
"10856254",
"11473254",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693",
"10654258",
"14529527"
] | [
"Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase.",
"Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases th... | [
2000,
2001,
2005,
2003,
2002,
2001,
2004,
2003,
2000,
2003
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"marine sediment metagenome"
] | [
543,
1
] | 2 | [] | [] | 0 | true | Domain | Type II restriction enzyme NaeI | Type II restriction enzyme NaeI | NaeI | 9 |
IPR015211 | 15,211 | Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal | Peptidase_M1_C | Domain | 9,754 | false | false | This C-terminal domain is found in peptidases belonging to MEROPS peptidase family M1, particularly: aminopeptidase-1 of Caenorhabditis elegans, aminopeptidase O, aminopeptidase B and the bifunctional leukotriene A4 (LTA-4) hydrolase/aminopeptidase. | [
"GO:0008237",
"GO:0008270"
] | [
"metallopeptidase activity",
"zinc ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF09127",
"SM01263"
] | [
"Leuk-A4-hydro_C",
"Leuk-A4-hydro_C"
] | [
9706,
9703
] | 2 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"3.3.2.10",
"3.4.11",
"3.4.11.-",
"PWY-6423",
"PWY-6710",
"PWY-7694",
"PWY-7778",
"PWY-7954",
"PWY-8356",
"PWY-8395",
"PWY-8397",
"PWY-8399",
"PWY-8400",
"R-BTA-2142691",
"R-BTA-6798695",
"R-BTA-9018676",
"R-BTA-9018681",
"R-BTA-9018896",
"R-BTA-9020265",
"R-BTA-9023661",
"R-... | [
"EC:3.3.2.10",
"EC:3.4.11",
"EC:3.4.11.-",
"METACYC:PWY-6423",
"METACYC:PWY-6710",
"METACYC:PWY-7694",
"METACYC:PWY-7778",
"METACYC:PWY-7954",
"METACYC:PWY-8356",
"METACYC:PWY-8395",
"METACYC:PWY-8397",
"METACYC:PWY-8399",
"METACYC:PWY-8400",
"REACTOME:R-BTA-2142691",
"REACTOME:R-BTA-679... | 69 | [
"1gw6",
"1h19",
"1hs6",
"1sqm",
"2r59",
"2vj8",
"2xpy",
"2xpz",
"2xq0",
"3b7r",
"3b7s",
"3b7t",
"3b7u",
"3cho",
"3chp",
"3chq",
"3chr",
"3chs",
"3cia",
"3fh5",
"3fh7",
"3fh8",
"3fhe",
"3fts",
"3ftu",
"3ftv",
"3ftw",
"3ftx",
"3fty",
"3ftz",
"3fu0",
"3fu3"... | 82 | [
"PUB00025776"
] | [
"11175901"
] | [
"Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
1746,
7999,
9
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
3,
8,
2,
13,
16,
1,
1,
17,
1,
1,
3
] | 12 | true | Domain | Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal | Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal | Peptidase_M1_C | 3 |
IPR015212 | 15,212 | Regulator of G protein signalling-like domain | RGS-like_dom | Domain | 6,415 | false | false | This entry represents a domain consisting of twelve helices that fold into a compact structure that contains the overall structural scaffold observed in other regulator of G protein signalling (RGS) proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS fold, in which helic... | [
"GO:0005085",
"GO:0005737"
] | [
"guanyl-nucleotide exchange factor activity",
"cytoplasm"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF09128"
] | [
"RGS-like"
] | [
6415
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CFA-193648",
"R-CFA-416482",
"R-CFA-416572",
"R-CFA-8980692",
"R-CFA-9013026",
"R-CFA-9013106",
"R-CFA-9013148",
"R-HSA-193648",
"R-HSA-416482",
"R-HSA-416572",
"R-HSA-8980692",
"R-HSA-9013026",
"R-HSA-9013106",
"R-HSA-9013148",
"R-HSA-9013149",
"R-MMU-193648",
"R-MMU-416482",
"... | [
"REACTOME:R-CFA-193648",
"REACTOME:R-CFA-416482",
"REACTOME:R-CFA-416572",
"REACTOME:R-CFA-8980692",
"REACTOME:R-CFA-9013026",
"REACTOME:R-CFA-9013106",
"REACTOME:R-CFA-9013148",
"REACTOME:R-HSA-193648",
"REACTOME:R-HSA-416482",
"REACTOME:R-HSA-416572",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HS... | 29 | [
"1htj",
"1iap",
"1shz",
"3ab3",
"3cx6",
"3cx7",
"3cx8"
] | 7 | [
"PUB00025791",
"PUB00028666"
] | [
"11470431",
"11524686"
] | [
"Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases.",
"Structure of the rgRGS domain of p115RhoGEF."
] | [
2001,
2001
] | 2 | [
"IPR016137"
] | [
"IPR037884",
"IPR037887",
"IPR037889"
] | 1 | 3 | 0 | [
"Opisthokonta"
] | [
6415
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
57,
8,
18,
13,
18
] | 6 | true | Domain | Regulator of G protein signalling-like domain | Regulator of G protein signalling-like domain | RGS-like_dom | 5 |
IPR015213 | 15,213 | Cholesterol oxidase, substrate-binding | Cholesterol_OX_subst-bd | Domain | 679 | false | false | The substrate-binding domain found in cholesterol oxidase is composed of an eight-stranded mixed β-pleated sheet and six α-helices. This domain is positioned over the isoalloxazine ring system of the FAD cofactor bound by the FAD-binding domain ( ) and forms the roof of the active site cavity, allowing for catalysis of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09129"
] | [
"Chol_subst-bind"
] | [
679
] | 1 | [] | [] | [] | 0 | [
"1i19",
"2i0k",
"3js8"
] | 3 | [
"PUB00025871"
] | [
"11397813"
] | [
"Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
641,
38
] | 2 | [] | [] | 0 | true | Domain | Cholesterol oxidase, substrate-binding | Cholesterol oxidase, substrate-binding | Cholesterol_OX_subst-bd | 2 |
IPR015214 | 15,214 | Pesticidal crystal protein, central domain, Cry2A/18 | Pest_cryst_cen_dom_Cry2A/18 | Domain | 156 | false | false | The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production [ ]. When an insect ingests these proteins, they are activated by proteolytic cleavage. The N terminus is cleaved in all of the proteins and a C-terminal extens... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09131"
] | [
"Endotoxin_mid"
] | [
156
] | 1 | [] | [] | [] | 0 | [
"1i5p"
] | 1 | [
"PUB00015089",
"PUB00015090",
"PUB00025909",
"PUB00083810"
] | [
"7490762",
"11468393",
"11377201",
"9729610"
] | [
"Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation.",
"Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis.",
"Structure of Cry2Aa suggests an unexpected receptor binding epitope.",
"Revision of the nomenclature for the Bacillus t... | [
1995,
2001,
2001,
1998
] | 4 | [] | [] | 0 | 0 | null | [
"Bacillales",
"Phytophthora nicotianae"
] | [
154,
2
] | 2 | [] | [] | 0 | true | Domain | Pesticidal crystal protein, central domain, Cry2A/18 | Pesticidal crystal protein, central domain, Cry2A/18 | Pest_cryst_cen_dom_Cry2A/18 | 4 |
IPR015215 | 15,215 | BmKX domain | BmKX_dom | Domain | 14 | false | false | This entry represents a domain that is often, thought not exclusively, found in short-chain scorpion toxins. It forms a structure consisting of a cysteine-stabilised α/β scaffold consisting of a short 3-10-helix and a two-stranded antiparallel β-sheet. The biological method of action of the toxins has not yet been defi... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09132"
] | [
"BmKX"
] | [
14
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00030690"
] | [
"15683869"
] | [
"A novel short-chain peptide BmKX from the Chinese scorpion Buthus martensi Karsch, sequencing, gene cloning and structure determination."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Giardia intestinalis"
] | [
14
] | 1 | [] | [] | 0 | true | Domain | BmKX domain | BmKX domain | BmKX_dom | 3 |
IPR015216 | 15,216 | SANT associated | SANTA | Domain | 2,580 | false | false | The SANTA domain (SANT associated) is approximately 90 amino acids in length and is conserved in eukaryotes. It is sometimes found in association with the SANT domain ( , also known as the Myb-like DNA-binding domain) implying a putative function in regulating chromatin remodelling. Sequence analysis has showed that th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09133"
] | [
"SANTA"
] | [
2580
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-69273",
"R-HSA-606279",
"R-HSA-69273",
"R-MMU-606279",
"R-MMU-69273"
] | [
"REACTOME:R-CEL-69273",
"REACTOME:R-HSA-606279",
"REACTOME:R-HSA-69273",
"REACTOME:R-MMU-606279",
"REACTOME:R-MMU-69273"
] | 5 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2580
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
13,
1,
16,
2,
3,
6,
3,
6
] | 8 | true | Domain | SANT associated | SANT associated | SANTA | 7 |
IPR015217 | 15,217 | Invasin, domain 3 | Invasin_dom_3 | Domain | 1,625 | false | false | This domain adopts a structure consisting of an immunoglobulin-like β-sandwich, with seven strands in two β-sheets, arranged in a Greek-key topology. It forms part of the extracellular region of the protein, which can be expressed as a soluble protein (Inv497) that binds integrins and promotes subsequent uptake by cell... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09134"
] | [
"Invasin_D3"
] | [
1625
] | 1 | [] | [] | [] | 0 | [
"1cwv",
"4e9l",
"5ldy",
"5n40"
] | 4 | [
"PUB00018560"
] | [
"10514372"
] | [
"Crystal structure of invasin: a bacterial integrin-binding protein."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Erwinia phage pEp_SNUABM_08",
"Eukaryota",
"metagenomes"
] | [
16,
1585,
1,
8,
15
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Invasin, domain 3 | Invasin, domain 3 | Invasin_dom_3 | 6 |
IPR015220 | 15,220 | Glucodextranase, N-terminal | Glucodextranase_N | Domain | 1,600 | false | false | This domain is found in bacterial and archaeal glucoamylases and glucodextranases, and adopts a structure consisting of 17 antiparallel β-strands [ , ]. These β-strands are divided into two β-sheets, and one of the β-sheets is wrapped by an extended polypeptide, which appears to stabilise the domain. This domain, toget... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09137",
"cd07430"
] | [
"Glucodextran_N",
"GH15_N"
] | [
1600,
1132
] | 2 | [] | [] | [] | 0 | [
"1lf6",
"1lf9",
"1ug9",
"1ulv"
] | 4 | [
"PUB00027010",
"PUB00031762"
] | [
"12614608",
"14660574"
] | [
"Crystal structure and evolution of a prokaryotic glucoamylase.",
"Structural insights into substrate specificity and function of glucodextranase."
] | [
2003,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"metagenomes"
] | [
1313,
4,
250,
33
] | 4 | [] | [] | 0 | true | Domain | Glucodextranase, N-terminal | Glucodextranase, N-terminal | Glucodextranase_N | 8 |
IPR015221 | 15,221 | Ubiquitin-related modifier 1 | Urm1 | Family | 3,971 | false | false | Ubiquitin related modifier 1 (Urm1) is a ubiquitin related protein that modifies proteins in the yeast ubiquitin-like urmylation pathway [ ]. Structural comparisons and phylogenetic analysis of the ubiquitin superfamily has indicated that Urm1 has the most conserved structural and sequence features of the common ancest... | [
"GO:0034227",
"GO:0005737"
] | [
"tRNA thio-modification",
"cytoplasm"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER",
"CDD"
] | [
"MF_03048",
"PF09138",
"PIRSF037379",
"PTHR14986",
"cd01764"
] | [
"Urm1",
"Urm1",
"Ubiquitin-related_modifier_1",
"",
"Ubl_Urm1"
] | [
3627,
3969,
2912,
3772,
3529
] | 5 | [
"REACTOME"
] | [
"R-HSA-6782315"
] | [
"REACTOME:R-HSA-6782315"
] | 1 | [
"1wgk",
"1xo3",
"2ax5",
"2k9x",
"2pko",
"2qjl",
"4idi",
"4wwm",
"6yuc",
"6z6s",
"7q5n"
] | 11 | [
"PUB00035477",
"PUB00035478",
"PUB00070178"
] | [
"16864801",
"14551258",
"21209336"
] | [
"Solution structure of Urm1 and its implications for the origin of protein modifiers.",
"Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast.",
"Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier."
] | [
2006,
2003,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota"
] | [
64,
5,
3902
] | 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... | [
7,
1,
1,
2,
1,
1,
1,
1,
4,
1,
1,
4
] | 12 | true | Family | Ubiquitin-related modifier 1 | Ubiquitin-related modifier 1 | Urm1 | 2 |
IPR015222 | 15,222 | Phosphatidate cytidylyltransferase, mitochondrial | Tam41 | Family | 4,913 | false | false | Tam41 is a mitochondrial phosphatidate cytidylyltransferase (CDP-DAG synthase) that catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. It is required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the... | [
"GO:0004605",
"GO:0032049"
] | [
"phosphatidate cytidylyltransferase activity",
"cardiolipin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF09139",
"PIRSF028840",
"PTHR13619"
] | [
"Tam41_Mmp37",
"Mmp37",
""
] | [
4913,
3355,
4801
] | 3 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.41",
"PWY-5667",
"PWY-5981",
"PWY-7817"
] | [
"EC:2.7.7.41",
"METACYC:PWY-5667",
"METACYC:PWY-5981",
"METACYC:PWY-7817"
] | 4 | [
"6ig2",
"6ig4",
"7ecd"
] | 3 | [
"PUB00084968",
"PUB00084969"
] | [
"19114592",
"23623749"
] | [
"The translocator maintenance protein Tam41 is required for mitochondrial cardiolipin biosynthesis.",
"Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria."
] | [
2008,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
22,
4889,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
2,
1,
4,
5,
1,
10,
3,
1,
2,
4
] | 12 | true | Family | Phosphatidate cytidylyltransferase, mitochondrial | Phosphatidate cytidylyltransferase, mitochondrial | Tam41 | 9 |
IPR015223 | 15,223 | ATPase MipZ | MipZ | Family | 2,668 | false | false | Cell division in bacteria is facilitated by a polymeric ring structure, the Z ring, composed of tubulin-like FtsZ protofilaments. Correct positioning of the division plane is a prerequisite for the generation of daughter cells with a normal chromosome complement. In Caulobacter crescentus MipZ, an essential protein, co... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09140"
] | [
"MipZ"
] | [
2668
] | 1 | [] | [] | [] | 0 | [
"2xit",
"2xj4",
"2xj9"
] | 3 | [
"PUB00035421"
] | [
"16839883"
] | [
"MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Metallosphaera yellowstonensis MK1",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
2607,
5,
1,
54,
1
] | 5 | [] | [] | 0 | true | Family | ATPase MipZ | ATPase MipZ | MipZ | 1 |
IPR015224 | 15,224 | Talin, central | Talin_cent | Domain | 4,697 | false | false | This domain adopts a structure consisting of five α-helices that fold into a bundle. It contains a vinculin binding site (VBS) composed of a hydrophobic surface spanning five turns of helix four. Activation of the VBS causes subsequent recruitment of vinculin, which enables maturation of small integrin/talin complexes ... | [
"GO:0005200",
"GO:0001726",
"GO:0005925"
] | [
"structural constituent of cytoskeleton",
"ruffle",
"focal adhesion"
] | [
"molecular_function",
"cellular_component",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF09141"
] | [
"Talin_middle"
] | [
4697
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-114608",
"R-HSA-354192",
"R-HSA-354194",
"R-HSA-372708",
"R-HSA-381038",
"R-HSA-399955",
"R-HSA-445355",
"R-HSA-5674135",
"R-HSA-6802946",
"R-HSA-6802948",
"R-HSA-6802952",
"R-HSA-6802955",
"R-HSA-9649948",
"R-HSA-9656223",
"R-HSA-9856530",
"R-MMU-114608",
"R-MMU-354192",
"R... | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-354192",
"REACTOME:R-HSA-354194",
"REACTOME:R-HSA-372708",
"REACTOME:R-HSA-381038",
"REACTOME:R-HSA-399955",
"REACTOME:R-HSA-445355",
"REACTOME:R-HSA-5674135",
"REACTOME:R-HSA-6802946",
"REACTOME:R-HSA-6802948",
"REACTOME:R-HSA-6802952",
"REACTOME:R-HSA... | 22 | [
"1sj7",
"1sj8",
"5nl1",
"6r9t",
"8vdo",
"8vdp",
"8vdq",
"8vdr"
] | 8 | [
"PUB00031077"
] | [
"15272303"
] | [
"Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4697
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
17,
4,
2,
10,
10
] | 6 | true | Domain | Talin, central | Talin, central | Talin_cent | 3 |
IPR015225 | 15,225 | tRNA pseudouridine synthase II, TruB, subfamily 2, C-terminal | tRNA_psdUridine_synth_fam2_C | Domain | 4,350 | false | false | Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF09142"
] | [
"TruB_C"
] | [
4350
] | 1 | [
"EC"
] | [
"5.4.99.25"
] | [
"EC:5.4.99.25"
] | 1 | [
"1sgv"
] | 1 | [
"PUB00026665",
"PUB00031055",
"PUB00045922",
"PUB00092579"
] | [
"11779468",
"15028724",
"10529181",
"19664587"
] | [
"Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.",
"Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft.",
"Role of cysteine residues in pseudouridine synt... | [
2001,
2004,
1999,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Geodia barretti",
"metagenomes"
] | [
4242,
4,
104
] | 3 | [] | [] | 0 | true | Domain | tRNA pseudouridine synthase II, TruB, subfamily 2, C-terminal | tRNA pseudouridine synthase II, TruB, subfamily 2, C-terminal | tRNA_psdUridine_synth_fam2_C | 1 |
IPR015226 | 15,226 | Type III effector HopF2 | T3_effector_HopF2 | Family | 182 | false | false | Many Gram-negative pathogenic bacteria directly translocate effector proteins into eukaryotic host cells via a type III secretion system. Type III effector proteins are determinants of virulence on susceptible plant hosts; they are also the proteins that trigger specific disease resistance in resistant plant hosts. Evo... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09143"
] | [
"AvrPphF-ORF-2"
] | [
182
] | 1 | [] | [] | [] | 0 | [
"1s21"
] | 1 | [
"PUB00030874"
] | [
"15341731"
] | [
"Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
182
] | 1 | [] | [] | 0 | true | Family | Type III effector HopF2 | Type III effector HopF2 | T3_effector_HopF2 | 2 |
IPR015227 | 15,227 | Mitogen, Yersinia pseudotuberculosis | Mitogen_YERPS | Family | 5 | false | false | Members of this family of Yersinia pseudotuberculosis mitogens adopt a sandwich structure consisting of nine strands in two β sheets, in a jelly-roll topology. As with other superantigens, they are able to excessively activate T cells by binding to the T cell receptor [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09144"
] | [
"YpM"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"1pm4",
"1poq"
] | 2 | [
"PUB00029905"
] | [
"14725774"
] | [
"Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Yersinia pseudotuberculosis complex"
] | [
5
] | 1 | [] | [] | 0 | true | Family | Mitogen, Yersinia pseudotuberculosis | Mitogen, Yersinia pseudotuberculosis | Mitogen_YERPS | 2 |
IPR015228 | 15,228 | SWA2-like, ubiquitin-associated domain | SWA2_UBA | Domain | 57 | false | false | Ubiquitin-associated (UBA) domains contain approximately 40 residues and bind ubiquitin non-covalently. They adopt a secondary structure consisting of three α-helices, and have been identified in various modular proteins involved in protein trafficking, clathrin assembly/disassembly, DNA repair, proteasomal degradation... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09145",
"cd14329"
] | [
"Ubiq-assoc",
"UBA_SWA2p_like"
] | [
57,
53
] | 2 | [] | [] | [] | 0 | [
"1pgy"
] | 1 | [
"PUB00029852",
"PUB00080329"
] | [
"14997574",
"11084334"
] | [
"Solution structure of the ubiquitin-binding domain in Swa2p from Saccharomyces cerevisiae.",
"The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast."
] | [
2004,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomycetes"
] | [
57
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | SWA2-like, ubiquitin-associated domain | SWA2-like, ubiquitin-associated domain | SWA2_UBA | 3 |
IPR015230 | 15,230 | Carbapenam-3-carboxylate synthase, N-terminal | CarA_N | Domain | 50 | false | false | This domain is found in the N-terminal of carbapenam-3-carboxylate synthase (carA), and is composed of two antiparallel six-stranded β-sheets that form a sandwich, flanked on each side by two α-helices [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09147"
] | [
"CarA_N"
] | [
50
] | 1 | [] | [] | [] | 0 | [
"1q15",
"1q19"
] | 2 | [
"PUB00022497",
"PUB00069787",
"PUB00069788",
"PUB00069789"
] | [
"12890666",
"12820893",
"17658887",
"19371088"
] | [
"Crystal structure of carbapenam synthetase (CarA).",
"Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora.",
"Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase.",
"A conserved tyrosyl-glutamyl catalytic dyad i... | [
2003,
2003,
2007,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
50
] | 1 | [] | [] | 0 | true | Domain | Carbapenam-3-carboxylate synthase, N-terminal | Carbapenam-3-carboxylate synthase, N-terminal | CarA_N | 4 |
IPR015231 | 15,231 | Protein of unknown function DUF1934 | DUF1934 | Family | 4,644 | false | false | This entry represents a family of hypothetical bacterial proteins. Their precise function has not, as yet, been defined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09148"
] | [
"DUF1934"
] | [
4644
] | 1 | [] | [] | [] | 0 | [
"1r0u"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Mytilus edulis",
"Podoviridae sp. ct0dB2",
"metagenomes"
] | [
4617,
1,
1,
25
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF1934 | Protein of unknown function DUF1934 | DUF1934 | 3 |
IPR015232 | 15,232 | Domain of unknown function DUF1935 | DUF1935 | Domain | 921 | false | false | This entry represents a conserved region found in various eukaryotic hypothetical proteins, as well as in homologues of the cysteine protease calpain. Its function has not, as yet, been defined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09149"
] | [
"DUF1935"
] | [
921
] | 1 | [] | [] | [] | 0 | [
"1r75",
"2fe0"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
921
] | 1 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1935 | Domain of unknown function DUF1935 | DUF1935 | 1 |
IPR015233 | 15,233 | Orange carotenoid-binding protein, N-terminal | Orange_carotenoid-bd_N | Domain | 800 | false | false | Carotenoids such as beta-carotene, lycopene, lutein and beta-cryptoxanthine are produced in plants and certain bacteria, algae and fungi, where they function as accessory photosynthetic pigments and as scavengers of oxygen radicals for photoprotection. They are also essential dietary nutrients in animals. Orange carote... | [
"GO:0031404",
"GO:0016037",
"GO:0030089"
] | [
"chloride ion binding",
"light absorption",
"phycobilisome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PROFILE"
] | [
"PF09150",
"PS51773"
] | [
"Carot_N",
"OCP_N"
] | [
799,
800
] | 2 | [] | [] | [] | 0 | [
"3mg1",
"3mg2",
"3mg3",
"4xb4",
"4xb5",
"5fcx",
"5fcy",
"5hgr",
"5tuw",
"5tux",
"5tv0",
"5ui2",
"6mcj",
"6pq1",
"6t6k",
"6t6m",
"6t6o",
"7ekr",
"7qcz",
"7qd0",
"7qd1",
"7qd2",
"7sc9",
"7scb",
"7scc",
"7ytf",
"7yth",
"7zsf",
"7zsg",
"7zsh",
"7zsi",
"7zsj"... | 40 | [
"PUB00027263",
"PUB00035631",
"PUB00035632",
"PUB00035633"
] | [
"12517340",
"17307930",
"16531492",
"16034528"
] | [
"The crystal structure of a cyanobacterial water-soluble carotenoid binding protein.",
"Light-induced energy dissipation in iron-starved cyanobacteria: roles of OCP and IsiA proteins.",
"A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria.",
"Structure and functi... | [
2003,
2007,
2006,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
800
] | 1 | [] | [] | 0 | true | Domain | Orange carotenoid-binding protein, N-terminal | Orange carotenoid-binding protein, N-terminal | Orange_carotenoid-bd_N | 3 |
IPR015234 | 15,234 | Domain of unknown function DUF1936 | DUF1936 | Domain | 5 | false | false | This domain is predominantly found in various hypothetical archaeal proteins. Its exact function has not been defined yet. It possesses a zinc ribbon fold [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09151"
] | [
"DUF1936"
] | [
5
] | 1 | [] | [] | [] | 0 | [
"1pvm",
"2qh1"
] | 2 | [
"PUB00046549"
] | [
"18021800"
] | [
"Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Aspergillus taichungensis",
"Thermoplasmatales"
] | [
1,
4
] | 2 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1936 | Domain of unknown function DUF1936 | DUF1936 | 5 |
IPR015235 | 15,235 | Domain of unknown function DUF1937 | DUF1937 | Domain | 288 | false | false | This entry represents a domain whose exact function has not, as yet, been described. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09152"
] | [
"DUF1937"
] | [
288
] | 1 | [] | [] | [] | 0 | [
"1t1j"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Cryptomonas curvata",
"Viruses",
"metagenomes"
] | [
221,
1,
16,
50
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1937 | Domain of unknown function DUF1937 | DUF1937 | 1 |
IPR015236 | 15,236 | Methylated DNA-protein cysteine methyltransferase, ribonuclease H-like domain | MGMT_N | Domain | 46 | false | false | This domain, found in the archaeal protein O6-alkylguanine-DNA alkyltransferase (also known as Methylated-DNA--protein-cysteine methyltransferase, MGMT), adopts a secondary structure consisting of a three stranded antiparallel β-sheet and three α helices. This entry represents the N-terminal ribonuclease H-like domain ... | [
"GO:0005737"
] | [
"cytoplasm"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF09153"
] | [
"MGMT_N"
] | [
46
] | 1 | [
"EC"
] | [
"2.1.1.63"
] | [
"EC:2.1.1.63"
] | 1 | [
"1mgt"
] | 1 | [
"PUB00027330"
] | [
"10497033"
] | [
"Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Thermococcaceae"
] | [
46
] | 1 | [] | [] | 0 | true | Domain | Methylated DNA-protein cysteine methyltransferase, ribonuclease H-like domain | Methylated DNA-protein cysteine methyltransferase, ribonuclease H-like domain | MGMT_N | 1 |
IPR015237 | 15,237 | Alpha-amylase C-terminal, prokaryotic | Alpha-amylase_C_pro | Domain | 2,838 | false | false | This entry represents a C-terminal domain associated with prokaryotic alpha-amylases. It adopts a secondary structure consisting of an eight-stranded antiparallel β-sheet containing a Greek key motif [ ]. The function of this domain was studied in the Alpha-amylase from Geobacillus thermoleovorans ( ), showing this reg... | [
"GO:0004553"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09154"
] | [
"Alpha-amy_C_pro"
] | [
2838
] | 1 | [
"EC"
] | [
"3.2.1.1"
] | [
"EC:3.2.1.1"
] | 1 | [
"1bli",
"1bpl",
"1e3x",
"1e3z",
"1e40",
"1e43",
"1hvx",
"1mwo",
"1mxd",
"1mxg",
"1ob0",
"1ud2",
"1ud3",
"1ud4",
"1ud5",
"1ud6",
"1ud8",
"1vjs",
"1w9x",
"1wp6",
"1wpc",
"2d3l",
"2d3n",
"2die",
"2gjp",
"2gjr",
"3bc9",
"3bcd",
"3bcf",
"3bh4",
"3qgv",
"4uzu"... | 44 | [
"PUB00027474",
"PUB00099859"
] | [
"12482867",
"32257525"
] | [
"Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc.",
"Functional study of C-terminal domain of the thermoacidophilic raw starch-hydrolyzing α-amylase Gt-amy."
] | [
2003,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Siphoviridae sp. ctYaH2",
"unclassified sequences"
] | [
2258,
463,
108,
1,
8
] | 5 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Alpha-amylase C-terminal, prokaryotic | Alpha-amylase C-terminal, prokaryotic | Alpha-amylase_C_pro | 5 |
IPR015238 | 15,238 | Protein of unknown function DUF1940 | DUF1940 | Family | 13 | false | false | This family adopts a secondary structure consisting of six α helices, with four long helices forming a left-handed, antiparallel α helical bundle. The function of this family of archaeal hypothetical proteins has not, as yet, been defined [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09155"
] | [
"DUF1940"
] | [
13
] | 1 | [] | [] | [] | 0 | [
"1nig"
] | 1 | [
"PUB00035391"
] | [
"15704011"
] | [
"Crystal structure of the hypothetical protein TA1238 from Thermoplasma acidophilum: a new type of helical super-bundle."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Thermoplasmatales",
"mine drainage metagenome"
] | [
11,
2
] | 2 | [] | [] | 0 | true | Family | Protein of unknown function DUF1940 | Protein of unknown function DUF1940 | DUF1940 | 8 |
IPR015239 | 15,239 | Anthrax toxin lethal factor, central domain | Anthrax_LF_cen | Domain | 18 | false | false | Anthrax toxin is a plasmid-encoded toxin complex produced by the Gram-positive, spore-forming bacteria, Bacillus anthracis. The toxin consists of three non-toxic proteins: the protective antigen (PA), the lethal factor (LF) and the edema factor (EF) [ ]. These component proteins self-assemble at the surface of host cel... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09156"
] | [
"Anthrax-tox_M"
] | [
18
] | 1 | [
"REACTOME"
] | [
"R-HSA-5210891"
] | [
"REACTOME:R-HSA-5210891"
] | 1 | [
"1j7n",
"1jky",
"1pwp",
"1pwq",
"1pwu",
"1pwv",
"1pww",
"1yqy",
"1zxv",
"4dv8",
"4pkq",
"4pkr",
"4pks",
"4pkt",
"4pku",
"4pkv",
"4pkw",
"4wf6",
"4xm6",
"4xm7",
"4xm8",
"5d1s",
"5d1t",
"5d1u",
"6psn",
"6wjj",
"6zxj",
"6zxk",
"6zxl"
] | 29 | [
"PUB00026280",
"PUB00031089",
"PUB00035784",
"PUB00035785",
"PUB00035786",
"PUB00035787"
] | [
"11700563",
"15131111",
"14570563",
"17335404",
"17381430",
"14616089"
] | [
"Crystal structure of the anthrax lethal factor.",
"Structural and kinetic analyses of the interaction of anthrax adenylyl cyclase toxin with reaction products cAMP and pyrophosphate.",
"Anthrax toxin.",
"Anthrax toxin: receptor binding, internalization, pore formation, and translocation.",
"Characterizatio... | [
2001,
2004,
2003,
2007,
2007,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Bacillus"
] | [
18
] | 1 | [] | [] | 0 | true | Domain | Anthrax toxin lethal factor, central domain | Anthrax toxin lethal factor, central domain | Anthrax_LF_cen | 7 |
IPR015240 | 15,240 | tRNA pseudouridine synthase II, TruB, subfamily 1, C-terminal | tRNA_sdUridine_synth_fam1_C | Domain | 7,070 | false | false | Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ... | [
"GO:0003723",
"GO:0009982",
"GO:0001522",
"GO:0009451"
] | [
"RNA binding",
"pseudouridine synthase activity",
"pseudouridine synthesis",
"RNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF09157"
] | [
"TruB-C_2"
] | [
7070
] | 1 | [
"EC"
] | [
"5.4.99.25"
] | [
"EC:5.4.99.25"
] | 1 | [
"1k8w",
"1r3f",
"1zl3"
] | 3 | [
"PUB00026665",
"PUB00031055",
"PUB00045922",
"PUB00092579"
] | [
"11779468",
"15028724",
"10529181",
"19664587"
] | [
"Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.",
"Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft.",
"Role of cysteine residues in pseudouridine synt... | [
2001,
2004,
1999,
2009
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6956,
17,
97
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | tRNA pseudouridine synthase II, TruB, subfamily 1, C-terminal | tRNA pseudouridine synthase II, TruB, subfamily 1, C-terminal | tRNA_sdUridine_synth_fam1_C | 7 |
IPR015241 | 15,241 | Transcription regulator MotA, C-terminal | MotA_Tscrpt_reg_C | Domain | 259 | false | false | Transcription factor MotA is required for the activation of middle promoters in Bacteriophage T4, in addition to phage T4 co-activator AsiA, and sigma-70-containing Escherichia coli RNA polymerase. Phage T4 middle promoters have the sigma70 -10 DNA element, but not the -35 element; instead, they have a MotA box at -30 ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09158"
] | [
"MotCF"
] | [
259
] | 1 | [] | [] | [] | 0 | [
"1kaf",
"5jlt",
"6k4y"
] | 3 | [
"PUB00028817",
"PUB00035545"
] | [
"11918797",
"16996538"
] | [
"The MotA transcription factor from bacteriophage T4 contains a novel DNA-binding domain: the 'double wing' motif.",
"Mutational analysis of sigma70 region 4 needed for appropriation by the bacteriophage T4 transcription factors AsiA and MotA."
] | [
2002,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
259
] | 1 | [] | [] | 0 | true | Domain | Transcription regulator MotA, C-terminal | Transcription regulator MotA, C-terminal | MotA_Tscrpt_reg_C | 8 |
IPR015242 | 15,242 | Mitochondrial resolvase Ydc2, catalytic | Ydc2_cat | Domain | 1,140 | false | false | This domain forms a ribonuclease H fold consisting of two β sheets and one α helix, arranged as a β-α-β motif. Each β sheet has five strands, arranged in a 32145 order, with the second strand being antiparallel to the rest. They are capable of resolving Holliday junctions and cleave DNA after 5'-CT-3, and 5'-TT-3, sequ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09159"
] | [
"Ydc2-catalyt"
] | [
1140
] | 1 | [] | [] | [] | 0 | [
"1kcf"
] | 1 | [
"PUB00026683",
"PUB00055559",
"PUB00055561"
] | [
"11726496",
"2834089",
"20064926"
] | [
"Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.",
"Cloning of a nuclear gene MRS1 involved in the excision of a single group I intron (bI3) from the mitochondrial COB transcript in S. cerevisiae.",
"Splicing of yeast aI5beta group I intron requires SUV3 to recycle MRS1 vi... | [
2001,
1986,
2010
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Megaviricetes",
"metagenomes"
] | [
1057,
6,
77
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
2,
1
] | 3 | true | Domain | Mitochondrial resolvase Ydc2, catalytic | Mitochondrial resolvase Ydc2, catalytic | Ydc2_cat | 6 |
IPR015243 | 15,243 | FimH, mannose-binding domain | FimH_man-bd | Domain | 1,058 | false | false | This domain adopts a secondary structure consisting of a β-sandwich, with nine strands arranged in two sheets in a Greek key topology. It is found in FimH, a mannose-specific adhesin of uropathogenic Escherichia coli strains. The domain appears to bind specifically to D-mannose and mediates cellular adhesion to mannosy... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09160",
"cd10466"
] | [
"FimH_man-bind",
"FimH_man-bind"
] | [
1057,
788
] | 2 | [
"REACTOME"
] | [
"R-HSA-9638630"
] | [
"REACTOME:R-HSA-9638630"
] | 1 | [
"1kiu",
"1klf",
"1qun",
"1tr7",
"1uwf",
"2vco",
"3jwn",
"3mcy",
"3rfz",
"3zl1",
"3zl2",
"3zpd",
"4att",
"4auj",
"4auu",
"4auy",
"4av0",
"4av4",
"4av5",
"4avh",
"4avi",
"4avj",
"4avk",
"4buq",
"4ca4",
"4css",
"4cst",
"4j3o",
"4lov",
"4x50",
"4x5p",
"4x5q"... | 105 | [
"PUB00021998",
"PUB00079629"
] | [
"12010488",
"20507142"
] | [
"Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection.",
"Structure-based drug design and optimization of mannoside bacterial FimH antagonists."
] | [
2002,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"human gut metagenome"
] | [
1055,
1,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Domain | FimH, mannose-binding domain | FimH, mannose-binding domain | FimH_man-bd | 1 |
IPR015245 | 15,245 | Nuclear RNA export factor Tap, RNA-binding domain | Tap_RNA-bd | Domain | 2,657 | false | false | This domain adopts a structure consisting of an α+β sandwich with an antiparallel β-sheet, arranged in a 2(β-α-β) motif. It is mainly found in mRNA export factors, which mediate the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive... | [
"GO:0003723",
"GO:0006406",
"GO:0005737"
] | [
"RNA binding",
"mRNA export from nucleus",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF09162"
] | [
"Tap-RNA_bind"
] | [
2657
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-159227",
"R-BTA-159230",
"R-BTA-159231",
"R-BTA-159236",
"R-CEL-159236",
"R-DME-159227",
"R-DME-159230",
"R-DME-159231",
"R-DME-159236",
"R-HSA-159227",
"R-HSA-159230",
"R-HSA-159231",
"R-HSA-159236",
"R-MMU-159227",
"R-MMU-159230",
"R-MMU-159231",
"R-MMU-159236",
"R-RNO-159... | [
"REACTOME:R-BTA-159227",
"REACTOME:R-BTA-159230",
"REACTOME:R-BTA-159231",
"REACTOME:R-BTA-159236",
"REACTOME:R-CEL-159236",
"REACTOME:R-DME-159227",
"REACTOME:R-DME-159230",
"REACTOME:R-DME-159231",
"REACTOME:R-DME-159236",
"REACTOME:R-HSA-159227",
"REACTOME:R-HSA-159230",
"REACTOME:R-HSA-159... | 21 | [
"1fo1",
"1ft8",
"1koh",
"1koo",
"3rw6",
"3rw7",
"4wyk",
"6e5u"
] | 8 | [
"PUB00026786"
] | [
"11854490"
] | [
"The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
2657
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
9,
1,
11,
14,
15
] | 6 | true | Domain | Nuclear RNA export factor Tap, RNA-binding domain | Nuclear RNA export factor Tap, RNA-binding domain | Tap_RNA-bd | 2 |
IPR015246 | 15,246 | Formate dehydrogenase, transmembrane | Formate_DH_TM | Domain | 4,087 | false | false | The transmembrane domain of the beta subunit of formate dehydrogenase consists of a single transmembrane helix. This domain acts as a transmembrane anchor, allowing the conduction of electrons within the protein [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09163"
] | [
"Form-deh_trans"
] | [
4087
] | 1 | [] | [] | [] | 0 | [
"1kqf",
"1kqg"
] | 2 | [
"PUB00009871"
] | [
"11884747"
] | [
"Molecular basis of proton motive force generation: structure of formate dehydrogenase-N."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4056,
11,
20
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Formate dehydrogenase, transmembrane | Formate dehydrogenase, transmembrane | Formate_DH_TM | 5 |
IPR015247 | 15,247 | Vitamin D binding protein, domain III | VitD-bind_III | Domain | 649 | false | false | This domain is predominantly found in Vitamin D binding proteins, and adopts a multihelical structure. It is required for formation of an actin 'clamp', allowing the protein to bind to actin [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09164"
] | [
"VitD-bind_III"
] | [
649
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-196791",
"R-MMU-196791",
"R-RNO-196791"
] | [
"REACTOME:R-HSA-196791",
"REACTOME:R-MMU-196791",
"REACTOME:R-RNO-196791"
] | 3 | [
"1j78",
"1j7e",
"1kw2",
"1kxp",
"1lot",
"1ma9"
] | 6 | [
"PUB00026841"
] | [
"12048248"
] | [
"Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
649
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
2,
4
] | 3 | true | Domain | Vitamin D binding protein, domain III | Vitamin D binding protein, domain III | VitD-bind_III | 5 |
IPR015248 | 15,248 | Ubiquinol-cytochrome c reductase iron-sulphur subunit, N-terminal | UQCRFS1_N | Domain | 962 | false | false | This entry represents the N-terminal domain of human Cytochrome b-c1 complex subunit Rieske, mitochondrial, also known as Ubiquinol-cytochrome c reductase iron-sulphur subunit (UQCRFS1), and similar sequences mainly from chordates and arthropods. UQCRFS1 adopts a structure consisting of many antiparallel β-sheets, with... | [
"GO:0008121"
] | [
"quinol-cytochrome-c reductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09165"
] | [
"Ubiq-Cytc-red_N"
] | [
962
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"7.1.1.8",
"PWY-3781",
"PWY-6692",
"PWY-7279",
"R-BTA-611105",
"R-BTA-9865881",
"R-CEL-9865881",
"R-DME-9865881",
"R-DRE-9865881",
"R-GGA-611105",
"R-GGA-9865881",
"R-HSA-611105",
"R-HSA-9865881",
"R-MMU-611105",
"R-MMU-9865881",
"R-RNO-611105",
"R-RNO-9865881",
"R-SSC-9865881"
] | [
"EC:7.1.1.8",
"METACYC:PWY-3781",
"METACYC:PWY-6692",
"METACYC:PWY-7279",
"REACTOME:R-BTA-611105",
"REACTOME:R-BTA-9865881",
"REACTOME:R-CEL-9865881",
"REACTOME:R-DME-9865881",
"REACTOME:R-DRE-9865881",
"REACTOME:R-GGA-611105",
"REACTOME:R-GGA-9865881",
"REACTOME:R-HSA-611105",
"REACTOME:R-H... | 18 | [
"1be3",
"1bgy",
"1l0l",
"1l0n",
"1ntk",
"1ntm",
"1ntz",
"1nu1",
"1pp9",
"1ppj",
"1sqb",
"1sqp",
"1sqq",
"1sqv",
"1sqx",
"2a06",
"2fyu",
"2ybb",
"3cwb",
"3h1h",
"3h1i",
"3h1j",
"3h1k",
"3h1l",
"3l70",
"3l71",
"3l72",
"3l73",
"3l74",
"3l75",
"3tgu",
"4d6t"... | 104 | [
"PUB00014307"
] | [
"12269811"
] | [
"The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
962
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
4,
1,
4
] | 4 | true | Domain | Ubiquinol-cytochrome c reductase iron-sulphur subunit, N-terminal | Ubiquinol-cytochrome c reductase iron-sulphur subunit, N-terminal | UQCRFS1_N | 7 |
IPR015249 | 15,249 | Biliverdin reductase, catalytic | Biliverdin_Rdtase_cat | Domain | 1,048 | false | false | This entry represents the biliverdin reductase, catalytic domain, which adopts a structure ccontaining a six-stranded β-sheet that is flanked on one face by several α-helices. This domain contains the catalytic active site which reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubi... | [
"GO:0004074",
"GO:0008270",
"GO:0042167"
] | [
"biliverdin reductase [NAD(P)H] activity",
"zinc ion binding",
"heme catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF09166"
] | [
"Biliv-reduc_cat"
] | [
1048
] | 1 | [
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.3.1.24",
"GenProp1591",
"PWY-5874",
"R-HSA-189483",
"R-HSA-9707564",
"R-MMU-189483",
"R-MMU-9707564",
"R-RNO-189483",
"R-RNO-9707564"
] | [
"EC:1.3.1.24",
"GP:GenProp1591",
"METACYC:PWY-5874",
"REACTOME:R-HSA-189483",
"REACTOME:R-HSA-9707564",
"REACTOME:R-MMU-189483",
"REACTOME:R-MMU-9707564",
"REACTOME:R-RNO-189483",
"REACTOME:R-RNO-9707564"
] | 9 | [
"1gcu",
"1lc0",
"1lc3",
"2h63"
] | 4 | [
"PUB00026979"
] | [
"12079357"
] | [
"Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
1048
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
2,
1,
3
] | 4 | true | Domain | Biliverdin reductase, catalytic | Biliverdin reductase, catalytic | Biliverdin_Rdtase_cat | 6 |
IPR015250 | 15,250 | MPT63-like | MPT63-like | Domain | 848 | false | false | MPT63 is a secreted protein of unknown function that is specific to Mycobacterium tuberculosis. MPT63 assumes a β-sandwich structure consisting of two antiparallel β-sheets (similar to an immunoglobulin-like fold), and an additional small, antiparallel β-sheet. The longer-stranded β-sheet is made up of four antiparalle... | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF09167"
] | [
"DUF1942"
] | [
848
] | 1 | [] | [] | [] | 0 | [
"1lmi"
] | 1 | [
"PUB00028893"
] | [
"12441386"
] | [
"Crystal structure of a major secreted protein of Mycobacterium tuberculosis-MPT63 at 1.5-A resolution."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
848
] | 1 | [] | [] | 0 | true | Domain | MPT63-like | MPT63-like | MPT63-like | 7 |
IPR015251 | 15,251 | X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain | PepX_N_dom | Domain | 1,457 | false | false | This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight α helices and three β strands, with the last α helix connecting to the first strand of the catalytic domain. The first strand of the N terminus also forms a small parallel β sheet with strand five of the catalytic domain. This d... | [
"GO:0008239",
"GO:0006508"
] | [
"dipeptidyl-peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF09168",
"SM00940"
] | [
"PepX_N",
"PepX_N"
] | [
1457,
1396
] | 2 | [
"EC"
] | [
"3.4.14.11"
] | [
"EC:3.4.14.11"
] | 1 | [
"1lns",
"6nff"
] | 2 | [
"PUB00027070"
] | [
"12377124"
] | [
"The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
1457
] | 1 | [] | [] | 0 | true | Domain | X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain | X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain | PepX_N_dom | 4 |
IPR015252 | 15,252 | Breast cancer type 2 susceptibility protein, helical domain | BRCA2_hlx | Domain | 2,832 | false | false | This entry represents a domain found in BRCA2 proteins. This domain adopts a helical structure, consisting of a four-helix cluster core (α1, α8, α9, α10) and two successive β-hairpins (β1 to β4). An approximately 50-amino acid segment that contains four short helices (α2 to α4), meanders around the surface of the core ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09169"
] | [
"BRCA-2_helical"
] | [
2832
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-HSA-5685939",
"R-HSA-5685942",
"R-HSA-5693554",
"R-HSA-5693568",
"R-HSA-5693579",
"R-HSA-5693616",
"R-HSA-912446",
"R-HSA-9701192",
"R-HSA-9704331",
"R-HSA-9704646",
"R-HSA-9709275",
"R-HSA-9709570",
"R-HSA-9709603",
"R-HSA-9763198",
"R-MMU-5685939",
"R-MMU-5685942",
"R-MMU-569356... | [
"REACTOME:R-HSA-5685939",
"REACTOME:R-HSA-5685942",
"REACTOME:R-HSA-5693554",
"REACTOME:R-HSA-5693568",
"REACTOME:R-HSA-5693579",
"REACTOME:R-HSA-5693616",
"REACTOME:R-HSA-912446",
"REACTOME:R-HSA-9701192",
"REACTOME:R-HSA-9704331",
"REACTOME:R-HSA-9704646",
"REACTOME:R-HSA-9709275",
"REACTOME... | 24 | [
"1iyj",
"1miu",
"1mje"
] | 3 | [
"PUB00021040"
] | [
"12228710"
] | [
"BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
2832
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
14,
3,
32,
4,
3,
6,
26
] | 7 | true | Domain | Breast cancer type 2 susceptibility protein, helical domain | Breast cancer type 2 susceptibility protein, helical domain | BRCA2_hlx | 4 |
IPR015253 | 15,253 | Stn1, C-terminal | CST_STN1_C | Domain | 1,265 | false | false | Stn1 is a component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to t... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09170"
] | [
"STN1_2"
] | [
1265
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-174411",
"R-BTA-174430",
"R-HSA-174411",
"R-HSA-174430",
"R-MMU-174411",
"R-MMU-174430",
"R-RNO-174411",
"R-RNO-174430"
] | [
"REACTOME:R-BTA-174411",
"REACTOME:R-BTA-174430",
"REACTOME:R-HSA-174411",
"REACTOME:R-HSA-174430",
"REACTOME:R-MMU-174411",
"REACTOME:R-MMU-174430",
"REACTOME:R-RNO-174411",
"REACTOME:R-RNO-174430"
] | 8 | [
"1wj5",
"4jqf",
"6w6w",
"7u5c",
"8d0b",
"8d0k",
"8soj",
"8sok"
] | 8 | [
"PUB00053884",
"PUB00053885",
"PUB00057805",
"PUB00097419",
"PUB00153024"
] | [
"19854130",
"19648609",
"20008938",
"23826127",
"25483097"
] | [
"RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway.",
"OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, associates with TPP1 and is implicated in telomere length regulation.",
"Stn1-Ten1 is an Rpa2-Rpa3-like comple... | [
2009,
2009,
2009,
2013,
2014
] | 5 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
1265
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
8,
3,
6
] | 4 | true | Domain | Stn1, C-terminal | Stn1, C-terminal | CST_STN1_C | 7 |
IPR015255 | 15,255 | Vitellinogen, open beta-sheet | Vitellinogen_open_b-sht | Domain | 8,361 | false | false | This entry represents the open β-sheet domain found in vitellinogen, which generally corresponds to a domain within the lipovitellin-1 peptide product. This domain adopts a structure consisting of several large open β-sheets [ ]. Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients... | [
"GO:0005319",
"GO:0006869"
] | [
"lipid transporter activity",
"lipid transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF09172",
"SM01169"
] | [
"Vit_open_b-sht",
"DUF1943"
] | [
8191,
7666
] | 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-HSA-202733",
"R-HSA-3000471",
"R-HSA-3000480",
"R-HSA-3000484",
"R-HSA-3000497",
"R-HSA-381426",
"R-HSA-432142",
"R-HSA-5686938",
"R-HSA-8856825",
"R-HSA-8856828",
"R-HSA-8866423",
"R-HSA-8957275",
"R-HSA-8963888",
"R-HSA-8963901",
"R-HSA-8964026",
"R-HSA-8964038",
"R-HSA-8964041"... | [
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-3000471",
"REACTOME:R-HSA-3000480",
"REACTOME:R-HSA-3000484",
"REACTOME:R-HSA-3000497",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-432142",
"REACTOME:R-HSA-5686938",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-HSA-8866423",
"REACTOME:R... | 56 | [
"1lsh",
"9bd1",
"9bd8",
"9bde",
"9bdt",
"9coo",
"9e9r",
"9ea7",
"9eag",
"9enr",
"9ens"
] | 11 | [
"PUB00005307",
"PUB00007158",
"PUB00035546",
"PUB00035547",
"PUB00035548",
"PUB00035549"
] | [
"9687371",
"12135361",
"17314313",
"9692232",
"17189915",
"8838584"
] | [
"The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein.",
"Lipid-protein interactions in lipovitellin.",
"Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.",
"Molecular characteristics of insect vitellogenins and vitellog... | [
1998,
2002,
2007,
1998,
2006,
1996
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8361
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
26,
5,
9,
2,
4
] | 6 | true | Domain | Vitellinogen, open beta-sheet | Vitellinogen, open beta-sheet | Vitellinogen_open_b-sht | 5 |
IPR015256 | 15,256 | Initiation factor eIF2 gamma, C-terminal | eIF2g_C | Domain | 5,933 | false | false | In eukaryotes and archaea, the e/aIF2 factor is involved in the initiation of protein biosynthesis. In its GTP bound form, e/aIF2 delivers methionylated initiator tRNA to the small subunit of the ribosome. After the pairing between the AUG initiation codon on mRNA and the CAU anticodon of the initiator tRNA, GTP is hyd... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09173",
"cd15490"
] | [
"eIF2_C",
"eIF2_gamma_III"
] | [
5932,
5541
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.6.5.3",
"R-BTA-156827",
"R-BTA-381042",
"R-BTA-382556",
"R-BTA-72649",
"R-BTA-72695",
"R-BTA-72702",
"R-BTA-72731",
"R-BTA-9840373",
"R-DDI-156827",
"R-DDI-382556",
"R-DDI-72695",
"R-DDI-72702",
"R-DDI-72731",
"R-DDI-9840373",
"R-DME-156827",
"R-DME-381042",
"R-DME-382556",
"R... | [
"EC:3.6.5.3",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-381042",
"REACTOME:R-BTA-382556",
"REACTOME:R-BTA-72649",
"REACTOME:R-BTA-72695",
"REACTOME:R-BTA-72702",
"REACTOME:R-BTA-72731",
"REACTOME:R-BTA-9840373",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-382556",
"REACTOME:R-DDI-72695",
"REACTO... | 73 | [
"1kjz",
"1kk0",
"1kk1",
"1kk2",
"1kk3",
"1s0u",
"2aho",
"2d74",
"2dcu",
"2plf",
"2pmd",
"2qmu",
"2qn6",
"3cw2",
"3i1f",
"3j81",
"3jap",
"3pen",
"3qsy",
"3sjz",
"3v11",
"4m0l",
"4m2l",
"4m4s",
"4m53",
"4nbs",
"4qfm",
"4qhy",
"4rcy",
"4rcz",
"4rd0",
"4rd1"... | 99 | [
"PUB00011835",
"PUB00039286"
] | [
"11927566",
"16407071"
] | [
"The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.",
"Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer."
] | [
2002,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
940,
2,
4920,
16,
55
] | 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... | [
17,
1,
3,
3,
2,
9,
1,
7,
4,
1,
1,
10
] | 12 | true | Domain | Initiation factor eIF2 gamma, C-terminal | Initiation factor eIF2 gamma, C-terminal | eIF2g_C | 1 |
IPR015257 | 15,257 | Repressor of RNA polymerase III transcription Maf1 | Maf1 | Family | 4,736 | false | false | Maf1 is a negative regulator of RNA polymerase III [ , ]. It inhibits the de novo assembly of TFIIIB onto DNA [ ]. Maf1 represses Pol III in response to DNA damage, oxidative stress, growth to stationary phase, treatment with rapamycin or chlorpromazine, and blocking of the secretory pathway [ ]. It targets the initiat... | [
"GO:0016480"
] | [
"negative regulation of transcription by RNA polymerase III"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF09174",
"PIRSF037240",
"PTHR22504"
] | [
"Maf1",
"RNA_polIII_Trep_MAF1",
""
] | [
4699,
3145,
4619
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8943724",
"R-DDI-8943724",
"R-HSA-8943724",
"R-MMU-8943724",
"R-RNO-8943724",
"R-SCE-8943724",
"R-SPO-8943724"
] | [
"REACTOME:R-BTA-8943724",
"REACTOME:R-DDI-8943724",
"REACTOME:R-HSA-8943724",
"REACTOME:R-MMU-8943724",
"REACTOME:R-RNO-8943724",
"REACTOME:R-SCE-8943724",
"REACTOME:R-SPO-8943724"
] | 7 | [
"3nr5",
"5u4z",
"5u50",
"6tut"
] | 4 | [
"PUB00035415",
"PUB00035416",
"PUB00035417",
"PUB00042710",
"PUB00067982",
"PUB00067983"
] | [
"11438659",
"16762835",
"12504022",
"17785443",
"15196897",
"20887893"
] | [
"Maf1p, a negative effector of RNA polymerase III in Saccharomyces cerevisiae.",
"General repression of RNA polymerase III transcription is triggered by protein phosphatase type 2A-mediated dephosphorylation of Maf1.",
"Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcripti... | [
2001,
2006,
2002,
2007,
2004,
2010
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
4735,
1
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
9,
1,
2,
2,
5,
3,
1,
3,
5,
1,
1,
9
] | 12 | true | Family | Repressor of RNA polymerase III transcription Maf1 | Repressor of RNA polymerase III transcription Maf1 | Maf1 | 9 |
IPR015258 | 15,258 | Vitellinogen, beta-sheet shell | Vitellinogen_b-sht_shell | Domain | 2,899 | false | false | This entry represents the β-sheet shell domain found in vitellinogen, which generally corresponds to the lipovitellin-2 peptide product. This domain consists of several large open β-sheets [ ]. It is often found C-terminal to and . Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrien... | [
"GO:0005319",
"GO:0006869"
] | [
"lipid transporter activity",
"lipid transport"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF09175",
"SM01170"
] | [
"Vit_b-sht_shell",
"DUF1944"
] | [
2899,
2874
] | 2 | [] | [] | [] | 0 | [
"1lsh"
] | 1 | [
"PUB00005307",
"PUB00007158",
"PUB00035546",
"PUB00035547",
"PUB00035548",
"PUB00035549"
] | [
"9687371",
"12135361",
"17314313",
"9692232",
"17189915",
"8838584"
] | [
"The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein.",
"Lipid-protein interactions in lipovitellin.",
"Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.",
"Molecular characteristics of insect vitellogenins and vitellog... | [
1998,
2002,
2007,
1998,
2006,
1996
] | 6 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
2899
] | 1 | [
"Danio rerio"
] | [
18
] | 1 | true | Domain | Vitellinogen, beta-sheet shell | Vitellinogen, beta-sheet shell | Vitellinogen_b-sht_shell | 3 |
IPR015259 | 15,259 | Methylene-tetrahydromethanopterin dehydrogenase, N-terminal | Methyl-teptahyd_DH_N | Domain | 1,007 | false | false | Prokaryotic methylene-tetrahydromethanopterin dehydrogenase catalyses the dehydrogenation of methylene-tetrahydromethanopterin during growth on one-carbon compounds such as methanol. It can also catalyse the reversible dehydrogenation of methylene-tetrahydrofolate, though at much lower efficiency [ ]. The pterin domain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09176"
] | [
"Mpt_N"
] | [
1007
] | 1 | [] | [] | [] | 0 | [
"1lu9",
"1lua",
"6tge",
"6tlk",
"6tm3"
] | 5 | [
"PUB00022108"
] | [
"12176390"
] | [
"Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Cladocopium goreaui",
"ecological metagenomes"
] | [
23,
965,
1,
18
] | 4 | [] | [] | 0 | true | Domain | Methylene-tetrahydromethanopterin dehydrogenase, N-terminal | Methylene-tetrahydromethanopterin dehydrogenase, N-terminal | Methyl-teptahyd_DH_N | 8 |
IPR015260 | 15,260 | Syntaxin 6/10/61, N-terminal | Syntaxin-6/10/61_N | Domain | 6,991 | false | false | This domain is found in the N-terminal of various SNARE proteins, including Syntaxin 6/10/61, adopt a structure consisting of an antiparallel three-helix bundle. Its exact function has not been determined, though it is known that it regulates the SNARE motif, as well as mediate various protein-protein interactions invo... | [
"GO:0048193",
"GO:0016020"
] | [
"Golgi vesicle transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF09177"
] | [
"STX6_10_61_N"
] | [
6991
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-GGA-6811438",
"R-GGA-6811440",
"R-HSA-6811438",
"R-HSA-6811440",
"R-MMU-6811438",
"R-MMU-6811440",
"R-RNO-6811438",
"R-RNO-6811440",
"R-SPO-6811440"
] | [
"REACTOME:R-GGA-6811438",
"REACTOME:R-GGA-6811440",
"REACTOME:R-HSA-6811438",
"REACTOME:R-HSA-6811440",
"REACTOME:R-MMU-6811438",
"REACTOME:R-MMU-6811440",
"REACTOME:R-RNO-6811438",
"REACTOME:R-RNO-6811440",
"REACTOME:R-SPO-6811440"
] | 9 | [
"1lvf",
"2c5i",
"2c5j",
"2c5k",
"4dnd",
"4j2c"
] | 6 | [
"PUB00014055",
"PUB00146863",
"PUB00159934",
"PUB00159935",
"PUB00159936",
"PUB00159937",
"PUB00159938",
"PUB00159939",
"PUB00159940"
] | [
"12082176",
"10397773",
"3462080",
"2576542",
"16154903",
"5765772",
"21826108",
"25535279",
"15919093"
] | [
"Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog.",
"A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.",
"The resected edentulous mandible--prosthetic treatment with implant-fixed prosthesis: a new clinical technique... | [
2002,
1999,
1986,
1989,
2005,
1969,
2012,
2015,
2005
] | 9 | [] | [
"IPR048036"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
6991
] | 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",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Ze... | [
24,
3,
3,
8,
5,
1,
17,
4,
1,
18
] | 10 | true | Domain | Syntaxin 6/10/61, N-terminal | Syntaxin 6/10/61, N-terminal | Syntaxin-6/10/61_N | 4 |
IPR015261 | 15,261 | 4-alpha-glucanotransferase, C-terminal | 4-alpha-glucanotransf_C | Domain | 9 | false | false | Members of this entry, which are predominantly found in prokaryotic 4-alpha-glucanotransferase, adopt a structure composed of six antiparallel β-strands, four of which form a β-sheet and another two form a type I, β-hairpin. The role of this family of domains, has not, as yet, been defined [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09178"
] | [
"MGTA_C"
] | [
9
] | 1 | [] | [] | [] | 0 | [
"1lwh",
"1lwj"
] | 2 | [
"PUB00027143"
] | [
"12139940"
] | [
"Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Thermotogales"
] | [
9
] | 1 | [] | [] | 0 | true | Domain | 4-alpha-glucanotransferase, C-terminal | 4-alpha-glucanotransferase, C-terminal | 4-alpha-glucanotransf_C | 8 |
IPR015262 | 15,262 | tRNA(Ile)-lysidine synthase, substrate-binding domain | tRNA_Ile_lys_synt_subst-bd | Domain | 13,159 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0005524",
"GO:0016879",
"GO:0008033",
"GO:0005737"
] | [
"nucleotide binding",
"ATP binding",
"ligase activity, forming carbon-nitrogen bonds",
"tRNA processing",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM"
] | [
"PF09179"
] | [
"TilS"
] | [
13159
] | 1 | [
"EC"
] | [
"6.3.4.19"
] | [
"EC:6.3.4.19"
] | 1 | [
"1ni5",
"3a2k"
] | 2 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00014303",
"PUB00016132",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"7731953",
"12012333",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
1994,
2002,
2000,
2002
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
12840,
17,
302
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | tRNA(Ile)-lysidine synthase, substrate-binding domain | tRNA(Ile)-lysidine synthase, substrate-binding domain | tRNA_Ile_lys_synt_subst-bd | 3 |
IPR015265 | 15,265 | Bacterial purine repressor, N-terminal | PuR_N | Domain | 3,620 | false | false | The N-terminal domain of the bacterial purine repressor PuR is a winged-helix domain, a subdivision of the HTH structural family. It consists of a canonical arrangement of secondary structures: a1-b1-a2-T-a3-b2-W-b3, where a2-T-a3 is the HTH motif, a3 is the recognition helix, and W is the wing. The domain allows for r... | [
"GO:0003677",
"GO:0006355"
] | [
"DNA binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09182"
] | [
"PuR_N"
] | [
3620
] | 1 | [] | [] | [] | 0 | [
"1o57",
"1p4a",
"7rmw"
] | 3 | [
"PUB00029324"
] | [
"12837783"
] | [
"The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Phytophthora kernoviae 00238/432",
"metagenomes"
] | [
3604,
1,
15
] | 3 | [] | [] | 0 | true | Domain | Bacterial purine repressor, N-terminal | Bacterial purine repressor, N-terminal | PuR_N | 8 |
IPR015266 | 15,266 | Domain of unknown function DUF1947 | DUF1947 | Domain | 336 | false | false | Members of this entry are a set of hypothetical archaeal proteins. Their exact function has not, as yet, been defined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09183"
] | [
"DUF1947"
] | [
336
] | 1 | [] | [] | [] | 0 | [
"1q7h",
"1zs7",
"2cx0",
"2cx1"
] | 4 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
330,
3,
3
] | 3 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1947 | Domain of unknown function DUF1947 | DUF1947 | 7 |
IPR015267 | 15,267 | Protein phosphatase 4 core regulatory subunit R2 | PPP4R2 | Family | 4,619 | false | false | Protein phosphatase 4 core regulatory subunit R2 (PPP4R2), also known as Psy4 in budding yeast, is the regulatory subunit of the histone H2A phosphatase complex. The histone H2A phosphatase complex dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break ... | [
"GO:0019888",
"GO:0030289"
] | [
"protein phosphatase regulator activity",
"protein phosphatase 4 complex"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF09184",
"PTHR16487"
] | [
"PPP4R2",
""
] | [
4284,
4463
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-5693607",
"R-DRE-5693607",
"R-GGA-5693607",
"R-HSA-5693607",
"R-MMU-5693607",
"R-XTR-5693607"
] | [
"REACTOME:R-DME-5693607",
"REACTOME:R-DRE-5693607",
"REACTOME:R-GGA-5693607",
"REACTOME:R-HSA-5693607",
"REACTOME:R-MMU-5693607",
"REACTOME:R-XTR-5693607"
] | 6 | [] | 0 | [
"PUB00078845"
] | [
"16299494"
] | [
"A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4619
] | 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... | [
7,
1,
3,
2,
6,
6,
1,
2,
4,
1,
6
] | 11 | true | Family | Protein phosphatase 4 core regulatory subunit R2 | Protein phosphatase 4 core regulatory subunit R2 | PPP4R2 | 2 |
IPR015268 | 15,268 | Protein of unknown function DUF1948 | DUF1948 | Family | 7 | false | false | Members of this family of Mycoplasma hypothetical proteins adopt a helical structure, with one central α-helix surrounded by five others, in a NusB-like fold. Their function has not, as yet, been determined [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09185"
] | [
"DUF1948"
] | [
7
] | 1 | [] | [] | [] | 0 | [
"1q8c"
] | 1 | [
"PUB00030162"
] | [
"15146506"
] | [
"A conserved hypothetical protein from Mycoplasma genitalium shows structural homology to nusb proteins."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
7
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF1948 | Protein of unknown function DUF1948 | DUF1948 | 3 |
IPR015269 | 15,269 | Uncharacterised domain UPF0029, Impact, C-terminal | UPF0029_Impact_C | Domain | 13,488 | false | false | Members of this entry are a set of functionally uncharacterised hypothetical bacterial proteins. They adopt a ferredoxin-like fold, with a β-α-β-β-α-β arrangement [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09186"
] | [
"DUF1949"
] | [
13488
] | 1 | [] | [] | [] | 0 | [
"1vi7",
"3lh2"
] | 2 | [
"PUB00032088",
"PUB00046141"
] | [
"15103642",
"11116084"
] | [
"Crystal structure of YIGZ, a conserved hypothetical protein from Escherichia coli k12 with a novel fold.",
"Comparative genome analysis of the mouse imprinted gene impact and its nonimprinted human homolog IMPACT: toward the structural basis for species-specific imprinting."
] | [
2004,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
12931,
64,
435,
58
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Uncharacterised domain UPF0029, Impact, C-terminal | Uncharacterised domain UPF0029, Impact, C-terminal | UPF0029_Impact_C | 6 |
IPR015270 | 15,270 | Protein RDM1, plant | RDM1_plant | Family | 757 | false | false | This family includes protein RDM1 from Arabidopsis, which is a a small protein that binds single-stranded methyl DNA, and associates and co-localises with RNA polymerase II, AGO4 and DRM2 in the nucleus. RDM1 is a component of the RNA-directed DNA methylation effector complex and may have a role in linking siRNA produc... | [
"GO:0080188",
"GO:0005634"
] | [
"gene silencing by siRNA-directed DNA methylation",
"nucleus"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF09187",
"PTHR36366"
] | [
"RdDM_RDM1",
""
] | [
757,
741
] | 2 | [] | [] | [] | 0 | [
"1vk5",
"2q3t",
"3gan",
"6ois",
"6oit"
] | 5 | [
"PUB00057309"
] | [
"20410883"
] | [
"An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Magnoliopsida"
] | [
757
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
3,
2,
5
] | 3 | true | Family | Protein RDM1, plant | Protein RDM1, plant | RDM1_plant | 1 |
IPR015271 | 15,271 | Protein of unknown function DUF1951 | DUF1951 | Family | 14 | false | false | This entry consists of Mycoplasma hypothetical proteins that adopt a multi-helical structure containing a buried central helix. Their function has not been determined yet. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09188"
] | [
"DUF1951"
] | [
14
] | 1 | [] | [] | [] | 0 | [
"1tm9"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
14
] | 1 | [] | [] | 0 | true | Family | Protein of unknown function DUF1951 | Protein of unknown function DUF1951 | DUF1951 | 4 |
IPR015272 | 15,272 | Molybdopterin cofactor biosynthesis MoaD-related, C-terminal | MoadD_C | Domain | 436 | false | false | In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis. Proteins are found in Thermus thermophilus, including threonine synthase ( ), which catalyses the conversion of O-phospho-L-homoserine to L-threonine and phosphate.... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09189"
] | [
"MoaD_arch"
] | [
436
] | 1 | [] | [] | [] | 0 | [
"1v8c"
] | 1 | [
"PUB00035630"
] | [
"17223713"
] | [
"Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
267,
167,
2
] | 3 | [] | [] | 0 | true | Domain | Molybdopterin cofactor biosynthesis MoaD-related, C-terminal | Molybdopterin cofactor biosynthesis MoaD-related, C-terminal | MoadD_C | 7 |
IPR015273 | 15,273 | Cysteinyl-tRNA synthetase, class Ia, DALR | Cys-tRNA-synt_Ia_DALR | Domain | 26,465 | false | false | Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth... | [
"GO:0000166",
"GO:0004817",
"GO:0005524",
"GO:0006423",
"GO:0005737"
] | [
"nucleotide binding",
"cysteine-tRNA ligase activity",
"ATP binding",
"cysteinyl-tRNA aminoacylation",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PFAM",
"SMART"
] | [
"PF09190",
"SM00840"
] | [
"DALR_2",
"DALR_2"
] | [
25437,
25115
] | 2 | [
"EC"
] | [
"6.1.1.16"
] | [
"EC:6.1.1.16"
] | 1 | [
"1li5",
"1li7",
"1u0b",
"3tqo",
"6ujd",
"8qhp"
] | 6 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
796,
23656,
1488,
525
] | 4 | [
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
1,
1,
12
] | 3 | true | Domain | Cysteinyl-tRNA synthetase, class Ia, DALR | Cysteinyl-tRNA synthetase, class Ia, DALR | Cys-tRNA-synt_Ia_DALR | 4 |
IPR015274 | 15,274 | CD4, extracellular | CD4-extracel | Domain | 515 | false | false | This domain adopts an immunoglobulin-like β-sandwich with seven strands in 2 β sheets, in a Greek key topology. It is predominantly found in the extracellular portion of CD4 proteins, where it enables interaction with major histocompatibility complex class II antigens [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09191"
] | [
"CD4-extracel"
] | [
515
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-CFA-202424",
"R-CFA-202427",
"R-CFA-202430",
"R-CFA-202433",
"R-CFA-389948",
"R-CFA-449836",
"R-CFA-8856825",
"R-CFA-8856828",
"R-HSA-1462054",
"R-HSA-167590",
"R-HSA-173107",
"R-HSA-180534",
"R-HSA-202424",
"R-HSA-202427",
"R-HSA-202430",
"R-HSA-202433",
"R-HSA-389948",
"R-HSA-... | [
"REACTOME:R-CFA-202424",
"REACTOME:R-CFA-202427",
"REACTOME:R-CFA-202430",
"REACTOME:R-CFA-202433",
"REACTOME:R-CFA-389948",
"REACTOME:R-CFA-449836",
"REACTOME:R-CFA-8856825",
"REACTOME:R-CFA-8856828",
"REACTOME:R-HSA-1462054",
"REACTOME:R-HSA-167590",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-... | 38 | [
"1cid",
"1wio",
"1wip",
"1wiq",
"3t0e",
"5u1f",
"6met",
"7t0o",
"7t0r",
"8fyi",
"8fyj",
"8z7n"
] | 12 | [
"PUB00035368"
] | [
"8493535"
] | [
"Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Amniota"
] | [
515
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
4
] | 3 | true | Domain | CD4, extracellular | CD4, extracellular | CD4-extracel | 7 |
IPR015275 | 15,275 | Actin-fragmin kinase, catalytic domain | Actin-fragmin_kin_cat_dom | Domain | 1,198 | false | false | This domain assumes a secondary structure consisting of eight β strands and 11 α-helices, organised in two lobes. It is predominantly found in actin-fragmin kinase. It is the catalytic domain that mediates the phosphorylation of actin [ ]. An atypical actin-fragmin kinase domain is also found at the N terminus of dual-... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09192",
"cd05124"
] | [
"Act-Frag_cataly",
"AFK"
] | [
1198,
92
] | 2 | [] | [] | [] | 0 | [
"1cja"
] | 1 | [
"PUB00014026",
"PUB00095636"
] | [
"10357805",
"26721646"
] | [
"The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain.",
"The mitogen-activated protein kinase phosphatase PHS1 regulates flowering in Arabidopsis thaliana."
] | [
1999,
2016
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
10,
1188
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
5,
19
] | 3 | true | Domain | Actin-fragmin kinase, catalytic domain | Actin-fragmin kinase, catalytic domain | Actin-fragmin_kin_cat_dom | 4 |
IPR015276 | 15,276 | Cholecystokinin A receptor, N-terminal | CholecystokininA_recpt_N | Domain | 566 | false | false | This entry represents the extracellular N-terminal domain of the cholecystokinin A receptor. This domain adopts a tertiary structure consisting of a few helical turns and a disulphide-cross linked loop. It is required for interaction of the cholecystokinin A receptor with its corresponding hormonal ligand [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09193"
] | [
"CholecysA-Rec_N"
] | [
566
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-375276",
"R-HSA-416476",
"R-MMU-375276",
"R-MMU-416476",
"R-RNO-375276",
"R-RNO-416476"
] | [
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-375276",
"REACTOME:R-RNO-416476"
] | 6 | [
"1d6g",
"7ezh",
"7ezk",
"7ezm",
"7f8u",
"7f8x",
"7f8y",
"7mbx",
"7mby",
"7xou",
"7xov",
"9bkj",
"9bkk"
] | 13 | [
"PUB00028327"
] | [
"10555959"
] | [
"Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Tetrapoda"
] | [
566
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
3
] | 3 | true | Domain | Cholecystokinin A receptor, N-terminal | Cholecystokinin A receptor, N-terminal | CholecystokininA_recpt_N | 2 |
IPR015277 | 15,277 | Restriction endonuclease, type II, AvaI/BsoBI | Restrct_endonuc_II_AvaI/BsoBI | Family | 142 | false | false | This entry represent AvaI and BsoBI restriction endonucleases, both of which recognise the double-stranded sequence CYCGRG (where Y = T/C, and R = A/G) and cleave after C-1 [ ]. There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and ... | [
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF09194"
] | [
"Endonuc-BsobI"
] | [
142
] | 1 | [
"EC"
] | [
"3.1.21.4"
] | [
"EC:3.1.21.4"
] | 1 | [
"1dc1"
] | 1 | [
"PUB00028340",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"11250198",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of degenerate DNA sequences and potential histidine catalysis.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship b... | [
2001,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomicrobia",
"termite gut metagenome"
] | [
139,
2,
1
] | 3 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, AvaI/BsoBI | Restriction endonuclease, type II, AvaI/BsoBI | Restrct_endonuc_II_AvaI/BsoBI | 8 |
IPR015278 | 15,278 | Type-2 restriction enzyme BglII-like | BglII-like | Family | 740 | false | false | This entry represents BglII restriction endonucleases, which recognise AGATCT and cleaves after A-1 [ , ]. BglII adopts a structure consisting of an α/β core containing a six-stranded β-sheet surrounded by five α-helices, two of which are involved in homodimerisation of the endonuclease. It also includes the BstYI "int... | [
"GO:0009036",
"GO:0009307"
] | [
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09195"
] | [
"Endonuc-BglII"
] | [
740
] | 1 | [] | [] | [] | 0 | [
"1d2i",
"1dfm",
"1es8",
"1sdo",
"1vrr",
"2p0j"
] | 6 | [
"PUB00028319",
"PUB00028457",
"PUB00031005",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"10655616",
"11175900",
"15099740",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolution.",
"Structure of free BglII reveals an unprecedented scissor-like motion for opening an endonuclease.",
"Crystal structure of BstYI at 1.85A resolution: a thermophilic restriction endonuc... | [
2000,
2001,
2004,
2005,
2003,
2002,
2001,
2004,
2003
] | 9 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Opisthokonta",
"metagenomes"
] | [
18,
692,
3,
2,
25
] | 5 | [] | [] | 0 | true | Family | Type-2 restriction enzyme BglII-like | Type-2 restriction enzyme BglII-like | BglII-like | 3 |
IPR015279 | 15,279 | Malto-oligosyltrehalose synthase, C-terminal | Trehalose_TreY_C | Domain | 10 | false | false | This domain is found in the Archaeal protein maltooligosyl trehalose synthase produced by Sulfolobus spp [ ]. Its function has not, as yet, been defined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09196"
] | [
"DUF1953"
] | [
10
] | 1 | [] | [] | [] | 0 | [
"1iv8",
"3hje"
] | 2 | [
"PUB00066695"
] | [
"8980629"
] | [
"Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Sulfolobaceae"
] | [
10
] | 1 | [] | [] | 0 | true | Domain | Malto-oligosyltrehalose synthase, C-terminal | Malto-oligosyltrehalose synthase, C-terminal | Trehalose_TreY_C | 6 |
IPR015280 | 15,280 | Rap1, DNA-binding domain | Rap1_DNA-bd | Domain | 198 | false | false | Members of this entry, which are predominantly found in the yeast protein Rap1, assume a secondary structure consisting of a three-helix bundle and an N-terminal arm. They contain an Arg-Asp-Arg-Lys sequence that interacts with an ACAregion in the 3, region of the DNA-binding site [ ]. | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09197"
] | [
"Rap1-DNA-bind"
] | [
198
] | 1 | [
"REACTOME"
] | [
"R-SPO-174437"
] | [
"REACTOME:R-SPO-174437"
] | 1 | [
"1ign",
"3ukg",
"4gfb",
"6ldm",
"8s8p"
] | 5 | [
"PUB00026022"
] | [
"8620531"
] | [
"The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Dikarya",
"Mesosutterella faecium"
] | [
197,
1
] | 2 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1
] | 2 | true | Domain | Rap1, DNA-binding domain | Rap1, DNA-binding domain | Rap1_DNA-bd | 1 |
IPR015281 | 15,281 | DNA beta-glucosyltransferase, bacteriophage | Phage_Bgt | Family | 25 | false | false | Members of this family include DNA-modifying enzymes encoded by bacteriophage T4 that catalyses the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA [ ]. It is involved in a DNA modification process to protect the phage genome against its own nu... | [
"GO:0033821",
"GO:0099018"
] | [
"DNA beta-glucosyltransferase activity",
"symbiont-mediated evasion of host restriction-modification system"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09198"
] | [
"T4-Gluco-transf"
] | [
25
] | 1 | [] | [] | [] | 0 | [
"1bgt",
"1bgu",
"1c3j",
"1ixy",
"1j39",
"1jej",
"1jg6",
"1jg7",
"1jiu",
"1jiv",
"1jix",
"1m5r",
"1nvk",
"1nzd",
"1nzf",
"1qkj",
"1sxp",
"1sxq",
"2bgt",
"2bgu"
] | 20 | [
"PUB00028739",
"PUB00074885"
] | [
"11493010",
"22229759"
] | [
"High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.",
"Biochemical characterization of recombinant β-glucosyltransferase and analysis of global 5-hydroxymethylcytosine in unique genomes."
] | [
2001,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Caudoviricetes"
] | [
25
] | 1 | [] | [] | 0 | true | Family | DNA beta-glucosyltransferase, bacteriophage | DNA beta-glucosyltransferase, bacteriophage | Phage_Bgt | 1 |
IPR015282 | 15,282 | Staphylococcal superantigen-like OB-fold domain | SSL_OB | Domain | 376 | false | false | This OB-fold domain folds into a five-stranded β-barrel [ ]. Proteins containing this domain are found in various staphylococcal toxins described as staphylococcal superantigen-like (SSL) proteins that are related to the staphylococcal enterotoxins (SEs) or superantigens. These SSL proteins of which 11 have so far been... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09199"
] | [
"SSL_OB"
] | [
376
] | 1 | [] | [] | [] | 0 | [
"1m4v",
"1v1o",
"1v1p",
"2qej",
"2r61",
"2rdg",
"2rdh",
"2z8l",
"3kls",
"3o13",
"3prx",
"3r2i",
"3r2t",
"3ury",
"3v05",
"4dxf",
"4dxg",
"4o1n",
"4rco",
"4rfb",
"4rgt",
"4rh6",
"4zys",
"5d3d",
"5d3i",
"5i4d",
"6lwt",
"6ucd",
"7ttz",
"9c65",
"9c6z"
] | 31 | [
"PUB00018994",
"PUB00031971",
"PUB00048974",
"PUB00049265",
"PUB00049331",
"PUB00065773",
"PUB00075648",
"PUB00075649"
] | [
"12082105",
"15213171",
"17848512",
"17996251",
"18045383",
"22949551",
"20133685",
"2121764"
] | [
"The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome.",
"Structural relationships and cellular tropism of staphylococcal superantigen-like proteins.",
"Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed... | [
2002,
2004,
2007,
2007,
2007,
2012,
2010,
1990
] | 8 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
376
] | 1 | [] | [] | 0 | true | Domain | Staphylococcal superantigen-like OB-fold domain | Staphylococcal superantigen-like OB-fold domain | SSL_OB | 8 |
IPR015283 | 15,283 | Monellin | Monellin | Family | 2 | false | false | Monellin, a protein produced by the West African plant Dioscoreophyllum cumminsii (Serendipity berry), is approximately 70,000 times sweeter than sucrose on a molar basis. The protein adopts an α-β structure, with a cystatin-like fold, where each helix packs against a coiled antiparallel β-sheet [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09200"
] | [
"Monellin"
] | [
2
] | 1 | [] | [] | [] | 0 | [
"1fa3",
"1fuw",
"1iv7",
"1iv9",
"1krl",
"1m9g",
"1mnl",
"1mol",
"2o9u",
"2q33",
"3mon",
"3pxm",
"3pyj",
"3q2p",
"4mon",
"5lc6",
"5lc7",
"5o7k",
"5o7l",
"5o7q",
"5o7r",
"5o7s",
"5xfu",
"5yct",
"5ycu",
"5ycw",
"5z1p",
"6l44",
"6l4i",
"6l4j",
"6l4n",
"6lay"... | 49 | [
"PUB00028970"
] | [
"8230222"
] | [
"Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution."
] | [
1993
] | 1 | [] | [
"IPR000828",
"IPR002095"
] | 0 | 2 | 0 | [
"Dioscoreophyllum cumminsii"
] | [
2
] | 1 | [] | [] | 0 | true | Family | Monellin | Monellin | Monellin | 7 |
IPR015284 | 15,284 | Signal recognition particle (SRP) receptor alpha subunit, N-terminal | SRX_dom | Domain | 61 | false | false | This domain (SRX domain) is found in the signal recognition particle receptor (SR) subunit alpha, also known as Srp101 in budding yeast, which consist of a central six-stranded anti-parallel β-sheet sandwiched by helix alpha1 on one side and helices alpha2-alpha4 on the other. The SRX domain of SRalpha can bind SRbeta,... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09201"
] | [
"SRX"
] | [
61
] | 1 | [] | [] | [] | 0 | [
"1nrj"
] | 1 | [
"PUB00022264",
"PUB00075370"
] | [
"12654246",
"9679135"
] | [
"Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.",
"A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit."
] | [
2003,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Saccharomycetes"
] | [
61
] | 1 | [
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1
] | 1 | true | Domain | Signal recognition particle (SRP) receptor alpha subunit, N-terminal | Signal recognition particle (SRP) receptor alpha subunit, N-terminal | SRX_dom | 3 |
IPR015285 | 15,285 | RIO2 kinase winged helix domain, N-terminal | RIO2_wHTH_N | Domain | 5,252 | false | false | This N-terminal domain is found in RIO2 kinases, and is structurally homologous to the winged helix (wHTH) domain. It adopts a structure consisting of four α helices followed by two β strands and a fifth α helix. The domain confers DNA binding properties to the protein, as per other winged helix domains [ ]. | [
"GO:0004674",
"GO:0005524",
"GO:0006468"
] | [
"protein serine/threonine kinase activity",
"ATP binding",
"protein phosphorylation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF09202"
] | [
"Rio2_N"
] | [
5252
] | 1 | [
"EC",
"REACTOME",
"REACTOME"
] | [
"2.7.11.1",
"R-HSA-6791226",
"R-MMU-6791226"
] | [
"EC:2.7.11.1",
"REACTOME:R-HSA-6791226",
"REACTOME:R-MMU-6791226"
] | 3 | [
"1tqi",
"1tqm",
"1tqp",
"1zao",
"1zar",
"4gyg",
"4gyi",
"6eml",
"6fai",
"6fdm",
"6fdn",
"6fdo",
"6g18",
"6g51",
"6hk6",
"6rbd",
"6y7c",
"7vbt",
"7wu0",
"8c00",
"8c01",
"8cbj",
"9f81"
] | 23 | [
"PUB00031542"
] | [
"15341724"
] | [
"Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"unclassified sequences"
] | [
656,
4583,
13
] | 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... | [
6,
1,
2,
2,
1,
3,
1,
3,
3,
1,
1,
15
] | 12 | true | Domain | RIO2 kinase winged helix domain, N-terminal | RIO2 kinase winged helix domain, N-terminal | RIO2_wHTH_N | 2 |
IPR015286 | 15,286 | Porin family, mycobacterial-type | Porin_fam_mycobact-type | Family | 2,854 | false | false | MspA is a membrane porin produced by Mycobacteria, allowing hydrophilic nutrients to enter the bacterium. The protein forms a tightly interconnected octamer with eightfold rotation symmetry that resembles a goblet and contains a central channel. Each subunit fold contains a β-sandwich of Ig-like topology and a β-ribbon... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09203"
] | [
"MspA"
] | [
2854
] | 1 | [] | [] | [] | 0 | [
"1uun",
"2v9u"
] | 2 | [
"PUB00031908"
] | [
"14976314"
] | [
"The structure of a mycobacterial outer-membrane channel."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mycobacteriales"
] | [
2,
2852
] | 2 | [] | [] | 0 | true | Family | Porin family, mycobacterial-type | Porin family, mycobacterial-type | Porin_fam_mycobact-type | 6 |
IPR015287 | 15,287 | Colicin D immunity protein domain | Colicin_D_immunity_dom | Domain | 489 | false | false | Colicin D is a bacteriocin that kills target cells by cleaving tRNA(Arg). Colicin D immunity protein (ImmD) inhibits the bactericidal activity of colicin D by binding to its tRNase catalytic domain [ ]. | [
"GO:0015643",
"GO:0030153"
] | [
"toxic substance binding",
"bacteriocin immunity"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09204"
] | [
"Colicin_immun"
] | [
489
] | 1 | [] | [] | [] | 0 | [
"1tfk",
"1tfo",
"1v74"
] | 3 | [
"PUB00032009"
] | [
"15014439"
] | [
"Structural inhibition of the colicin D tRNase by the tRNA-mimicking immunity protein."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"hydrothermal vent metagenome"
] | [
465,
5,
18,
1
] | 4 | [] | [] | 0 | true | Domain | Colicin D immunity protein domain | Colicin D immunity protein domain | Colicin_D_immunity_dom | 2 |
IPR015289 | 15,289 | Alpha-L-arabinofuranosidase B, catalytic | A-L-arabinofuranosidase_B_cat | Domain | 2,584 | false | false | This domain, found in fungal alpha-L-arabinofuranosidase B, adopts a β-sandwich fold similar to that of concanavalin A-like lectins/glucanase. The β-sandwich fold consists of two anti-parallel β-sheets with seven and six strands, respectively. In addition, there are four helices outside of the β-strands. The β-sandwich... | [
"GO:0046556",
"GO:0031221"
] | [
"alpha-L-arabinofuranosidase activity",
"arabinan metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF09206"
] | [
"ArabFuran-catal"
] | [
2584
] | 1 | [
"EC"
] | [
"3.2.1.55"
] | [
"EC:3.2.1.55"
] | 1 | [
"1wd3",
"1wd4",
"2d43",
"2d44",
"6sxr",
"6sxs",
"6sxt"
] | 7 | [
"PUB00035358"
] | [
"15292273"
] | [
"Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"marine sediment metagenome"
] | [
1417,
6,
1160,
1
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Alpha-L-arabinofuranosidase B, catalytic | Alpha-L-arabinofuranosidase B, catalytic | A-L-arabinofuranosidase_B_cat | 5 |
IPR015291 | 15,291 | Restriction endonuclease, type II, MspI | Restrct_endonuc_II_MspI | Family | 37 | false | false | This entry represents type II restriction endonucleases such as MspI, which recognises the palindromic tetranucleotide sequence 5'-CCGG and cleave between the first and second nucleotides, leaving 2 base 5' overhangs. They fold into an α/β architecture, with a five-stranded mixed β-sheet sandwiched on both sides by α-h... | [
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF09208"
] | [
"Endonuc-MspI"
] | [
37
] | 1 | [] | [] | [] | 0 | [
"1sa3",
"1yfi"
] | 2 | [
"PUB00030968",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"15341737",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"An asymmetric complex of restriction endonuclease MspI on its palindromic DNA recognition site.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between different subgroups of ... | [
2004,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
36,
1
] | 2 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, MspI | Restriction endonuclease, type II, MspI | Restrct_endonuc_II_MspI | 6 |
IPR015292 | 15,292 | Transcription regulator YbiH, C-terminal | Tscrpt_reg_YbiH_C | Domain | 3,402 | false | false | This entry represents the C-terminal domain found in the hypothetical transcriptional regulator YbiH from bacteria such as Salmonella typhimurium and Escherichia coli. YbiH is a member of the TetR (tetracycline resistance) transcriptional regulator family of proteins. The C-terminal domains of YbiH and TetR share a mul... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09209"
] | [
"CecR_C"
] | [
3402
] | 1 | [] | [] | [] | 0 | [
"1t33",
"7e1l",
"7e1n"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3381,
3,
18
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Transcription regulator YbiH, C-terminal | Transcription regulator YbiH, C-terminal | Tscrpt_reg_YbiH_C | 6 |
IPR015293 | 15,293 | 1,4-alpha-glucan branching enzyme, C-terminal | BE_C | Domain | 2,430 | false | false | This entry represents the C-terminal domain found in bacterial 1,4-alpha-glucan branching enzymes ( ), such as TTHA1902 from Thermus thermophilus and TK1436 from Thermococcus kodakarensis, which belong to the glycoside hydrolase family 57 . These enzymes catalyse the formation of branch points in alpha-glucans by cleav... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09210"
] | [
"BE_C"
] | [
2430
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.1.18",
"PWY-5067",
"PWY-622",
"PWY-7900"
] | [
"EC:2.4.1.18",
"METACYC:PWY-5067",
"METACYC:PWY-622",
"METACYC:PWY-7900"
] | 4 | [
"1ufa",
"2b5d",
"3n8t",
"3n92",
"3n98",
"3p0b",
"5wu7"
] | 7 | [
"PUB00058786",
"PUB00090452"
] | [
"21104698",
"21097495"
] | [
"Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.",
"Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of... | [
2011,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Menopon gallinae",
"metagenomes"
] | [
46,
2331,
1,
52
] | 4 | [] | [] | 0 | true | Domain | 1,4-alpha-glucan branching enzyme, C-terminal | 1,4-alpha-glucan branching enzyme, C-terminal | BE_C | 2 |
IPR015294 | 15,294 | Penicillin-binding protein 4, C-terminal domain | Pen-bd_prot4_C_dom | Domain | 545 | false | false | This domain is found towards the C terminus of prokaryotic penicillin-binding protein 4. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09211"
] | [
"DUF1958"
] | [
545
] | 1 | [] | [] | [] | 0 | [
"1tvf",
"3hum",
"3hun",
"5tw4",
"5tw8",
"5tx9",
"5txi",
"5ty2",
"5ty7",
"6c39",
"6c3k",
"6dz8",
"7kcv",
"7kcw",
"7kcx",
"7kcy"
] | 16 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota"
] | [
545
] | 1 | [] | [] | 0 | true | Domain | Penicillin-binding protein 4, C-terminal domain | Penicillin-binding protein 4, C-terminal domain | Pen-bd_prot4_C_dom | 9 |
IPR015295 | 15,295 | Carbohydrate binding module 27 | CBM27 | Domain | 187 | false | false | This domain is found in carbohydrate binding proteins that bind to beta-1, 4-mannooligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. The region adopts a β sandwich structure comprising 13 β strands with a single, small α-helix and a si... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09212"
] | [
"CBM27"
] | [
187
] | 1 | [] | [] | [] | 0 | [
"1of3",
"1of4",
"1oh4",
"1pmh",
"1pmj",
"6tn6"
] | 6 | [
"PUB00029410"
] | [
"12791255"
] | [
"Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ceratitis capitata"
] | [
186,
1
] | 2 | [] | [] | 0 | true | Domain | Carbohydrate binding module 27 | Carbohydrate binding module 27 | CBM27 | 4 |
IPR015296 | 15,296 | Chemokine-binding M3, viral | Chemokine-bd_M3_vir | Family | 8 | false | false | This entry represents a group of viral chemokine binding proteins, which bind with CC-chemokine MCP-1, acting as cytokine decoy receptors [ ]. For example, the murine herpesvirus decoy receptor M3 acts as an immune system saboteur by altering host anti-viral inflammatory repsonses. M3 adopts a structure consisting of t... | [
"GO:0019956"
] | [
"chemokine binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09213"
] | [
"M3"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"1mkf",
"1ml0",
"2nyz",
"2nz1"
] | 4 | [
"PUB00027380"
] | [
"12419245"
] | [
"Structural basis of chemokine sequestration by a herpesvirus decoy receptor."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Rhadinovirus"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Chemokine-binding M3, viral | Chemokine-binding M3, viral | Chemokine-bd_M3_vir | 2 |
IPR015297 | 15,297 | Bacteriophage PRD1, P2, absorption protein | Phage_PRD1_P2 | Family | 8 | false | false | This entry represents absorption protein P2 (synonym: receptor-binding protein P2) from the bacteriophage PRD1. Absorption protein P2 is a multi-β-sheet protein whose complicated topology forms an elongated seahorse-shaped molecule with a distinct head, containing a pseudo-β propeller structure with approximate six-fol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09214"
] | [
"Prd1-P2"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"1n7u",
"1n7v"
] | 2 | [
"PUB00029009"
] | [
"12623018"
] | [
"The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Alphatectivirus"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Bacteriophage PRD1, P2, absorption protein | Bacteriophage PRD1, P2, absorption protein | Phage_PRD1_P2 | 6 |
IPR015298 | 15,298 | Bacteriophage T4, Gp8 | Phage_T4_Gp8 | Domain | 439 | false | false | Members of this family of viral baseplate structural proteins adopt a structure consisting of a three-layer β-sandwich with two finger-like loops containing an α-helix at the opposite sides of the sandwich. The two peripheral, five-stranded, antiparallel β-sheets are stacked against the middle, four-stranded, antiparal... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09215"
] | [
"Phage-Gp8"
] | [
439
] | 1 | [] | [] | [] | 0 | [
"1n7z",
"1n80",
"1n8b",
"1pdm",
"1tja",
"5hx2",
"5iv5",
"5iv7",
"9f4a",
"9f4b"
] | 10 | [
"PUB00029011"
] | [
"12729757"
] | [
"Structure and location of gene product 8 in the bacteriophage T4 baseplate."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Marine Group I thaumarchaeote",
"Pseudomonadati",
"Viruses",
"marine metagenome"
] | [
3,
3,
406,
27
] | 4 | [] | [] | 0 | true | Domain | Bacteriophage T4, Gp8 | Bacteriophage T4, Gp8 | Phage_T4_Gp8 | 9 |
IPR015299 | 15,299 | Gamete antigen, Plasmodium | Gamete_antigen_PLAspp | Family | 149 | false | false | Members of this family are essential for gametocytogenesis in Plasmodium falciparum. They contain a fold composed of two pseudo dyad-related repeats of the helix-turn-helix motif, serving as a platform for RNA and Src homology-3 (SH3) binding [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09216"
] | [
"Pfg27"
] | [
149
] | 1 | [] | [] | [] | 0 | [
"1n81"
] | 1 | [
"PUB00029012"
] | [
"12577051"
] | [
"Structure of a gametocyte protein essential for sexual development in Plasmodium falciparum."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Plasmodium"
] | [
149
] | 1 | [] | [] | 0 | true | Family | Gamete antigen, Plasmodium | Gamete antigen, Plasmodium | Gamete_antigen_PLAspp | 2 |
IPR015300 | 15,300 | DNA-binding pseudobarrel domain superfamily | DNA-bd_pseudobarrel_sf | Homologous_superfamily | 62,715 | false | false | This superfamily represents a DNA recognition domain found in the restriction endonuclease EcoRII and numerous transcription factors. The EcoRII structure has been studied and forms an eight-stranded β-sheet with the strands in the order of b2, b5, b4, b3, b7, b6, b1 and b8. The strands are mostly antiparallel to each ... | [] | [] | [] | 0 | [
"CATHGENE3D",
"SSF"
] | [
"G3DSA:2.40.330.10",
"SSF101936"
] | [
"",
""
] | [
61621,
61476
] | 2 | [] | [] | [] | 0 | [
"1na6",
"1wid",
"1yel",
"3hqf",
"4i1k",
"4ldu",
"4ldv",
"4ldw",
"4ldx",
"4ldy",
"5o63",
"5os9",
"5yzy",
"5yzz",
"5z00",
"6fas",
"6j9a",
"6j9b",
"6j9c",
"6sdg",
"6ycq",
"7et6",
"8oj1",
"8oj2"
] | 24 | [
"PUB00029018"
] | [
"14659759"
] | [
"Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanohalophilus portucalensis",
"metagenomes"
] | [
808,
61898,
2,
7
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
635,
239,
587
] | 3 | true | Homologous_superfamily | DNA-binding pseudobarrel domain superfamily | DNA-binding pseudobarrel domain superfamily | DNA-bd_pseudobarrel_sf | 9 |
IPR015302 | 15,302 | Major coat protein, L-A virus | Major_coat_LA-virus | Domain | 190 | false | false | Members of this entry include the major coat protein of the Saccharomyces cerevisiae virus L-A (ScV-L-A) [ ]. The major coat protein is a large polypeptide without apparent domain division. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09220"
] | [
"LA-virus_coat"
] | [
190
] | 1 | [] | [] | [] | 0 | [
"1m1c",
"7qwx",
"7qwz",
"7zts",
"7zuf",
"8a5t",
"8pe4"
] | 7 | [
"PUB00028919"
] | [
"12244300"
] | [
"L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Viruses",
"viral metagenome"
] | [
22,
165,
3
] | 3 | [
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1
] | 1 | true | Domain | Major coat protein, L-A virus | Major coat protein, L-A virus | Major_coat_LA-virus | 4 |
IPR015303 | 15,303 | Fimbrial adhesin F17-AG, lectin domain | Fimbrial_adhesin_lectin_dom | Domain | 32 | false | false | This entry represents the carbohydrate-specific lectin domain found in bacterial fimbrial adhesins F17-G. It adopts a compact, elongated structure consisting of a β-sandwich with two major sheets: one consisting of five long strands in mixed orientations, and a front sheet with four antiparallel strands, forming an imm... | [
"GO:0044406",
"GO:0009289"
] | [
"adhesion of symbiont to host",
"pilus"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF09222"
] | [
"Fim-adh_lectin"
] | [
32
] | 1 | [] | [] | [] | 0 | [
"1o9v",
"1o9w",
"1o9z",
"1oio",
"1zk5",
"1zpl",
"2bs7",
"2bs8",
"2bsb",
"2bsc",
"3f64",
"3f6j",
"3ffo",
"4k0o"
] | 14 | [
"PUB00029365"
] | [
"12864853"
] | [
"The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
32
] | 1 | [] | [] | 0 | true | Domain | Fimbrial adhesin F17-AG, lectin domain | Fimbrial adhesin F17-AG, lectin domain | Fimbrial_adhesin_lectin_dom | 8 |
IPR015304 | 15,304 | ZinT domain | ZinT_dom | Domain | 3,089 | false | false | This domain is found in prokaryotic proteins that were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium and ensure its subsequent elimination [ ]. Previously known YodA, these proteins have been renamed as ZinT, and have been shown ... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF09223"
] | [
"ZinT"
] | [
3089
] | 1 | [] | [] | [] | 0 | [
"1oee",
"1oej",
"1oek",
"1s7d",
"1txl",
"4arh",
"4aw8",
"4ayh",
"4tnn",
"5aq6",
"5xm5",
"5yxc",
"6lm2",
"7jj9",
"7jja",
"7jjb"
] | 16 | [
"PUB00015733",
"PUB00070803"
] | [
"12909634",
"17931600"
] | [
"YodA from Escherichia coli is a metal-binding, lipocalin-like protein.",
"Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT."
] | [
2003,
2007
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Fungi",
"Methanomicrobia",
"metagenomes"
] | [
3075,
10,
2,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | ZinT domain | ZinT domain | ZinT_dom | 6 |
IPR015305 | 15,305 | Protein of unknown function DUF1961 | DUF1961 | Family | 705 | false | false | Members of this family are found in a set of hypothetical bacterial proteins. Their exact function has not, as yet, been determined. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF09224"
] | [
"DUF1961"
] | [
705
] | 1 | [] | [] | [] | 0 | [
"1oq1"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales",
"ecological metagenomes",
"leotiomyceta"
] | [
505,
4,
7,
189
] | 4 | [] | [] | 0 | true | Family | Protein of unknown function DUF1961 | Protein of unknown function DUF1961 | DUF1961 | 2 |
IPR015306 | 15,306 | Restriction endonuclease, type II, PvuII | Restrct_endonuc_II_PvuII | Family | 103 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [] | [] | [] | 0 | [
"PFAM",
"CDD"
] | [
"PF09225",
"cd22351"
] | [
"Endonuc-PvuII",
"PvuII-like"
] | [
103,
78
] | 2 | [] | [] | [] | 0 | [
"1eyu",
"1f0o",
"1h56",
"1k0z",
"1ni0",
"1pvi",
"1pvu",
"2pvi",
"3ksk",
"3pvi"
] | 10 | [
"PUB00032997",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"9878366",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"Asp34 of PvuII endonuclease is directly involved in DNA minor groove recognition and indirectly involved in catalysis.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between ... | [
1998,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Trichonephila clavata"
] | [
102,
1
] | 2 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, PvuII | Restriction endonuclease, type II, PvuII | Restrct_endonuc_II_PvuII | 4 |
IPR015307 | 15,307 | Restriction endonuclease, type II, HincII | Restrct_endonuc_II_HincII | Family | 35 | false | false | There are four classes of restriction endonucleases: types I, II, III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit compositi... | [
"GO:0003677",
"GO:0009036",
"GO:0009307"
] | [
"DNA binding",
"type II site-specific deoxyribonuclease activity",
"DNA restriction-modification system"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM",
"CDD"
] | [
"PF09226",
"cd22329"
] | [
"Endonuc-HincII",
"HincII-like"
] | [
35,
29
] | 2 | [] | [] | [] | 0 | [
"1kc6",
"1tw8",
"1tx3",
"1xhu",
"1xhv",
"2aud",
"2gie",
"2gig",
"2gih",
"2gii",
"2gij",
"3e3y",
"3e40",
"3e41",
"3e42",
"3e43",
"3e44",
"3e45",
"3ebc"
] | 19 | [
"PUB00032428",
"PUB00035691",
"PUB00035692",
"PUB00035693",
"PUB00035694",
"PUB00035705",
"PUB00035707"
] | [
"15476804",
"15770420",
"14576294",
"11827971",
"11557805",
"15121719",
"12665693"
] | [
"Mechanistic insights from the structures of HincII bound to cognate DNA cleaved from addition of Mg2+ and Mn2+.",
"Type II restriction endonucleases: structure and mechanism.",
"Diversity of type II restriction endonucleases that require two DNA recognition sites.",
"Evolutionary relationship between differe... | [
2004,
2005,
2003,
2002,
2001,
2004,
2003
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"metagenomes"
] | [
31,
2,
2
] | 3 | [] | [] | 0 | true | Family | Restriction endonuclease, type II, HincII | Restriction endonuclease, type II, HincII | Restrct_endonuc_II_HincII | 5 |
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