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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR013591 | 13,591 | Brevis radix (BRX) domain | Brevis_radix_dom | Domain | 7,377 | false | false | This is a short domain, approximately 35 residues in length that is found near the C terminus in a number of plant proteins, being repeated in some members. It is found in Brevis radix-like proteins. These may act as a regulator of cell proliferation and elongation in the root [ ]. It is also found in proteins annotate... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08381",
"PS51514"
] | [
"BRX",
"BRX"
] | [
7334,
7300
] | 2 | [] | [] | [] | 0 | [
"6l0v",
"6l0w"
] | 2 | [
"PUB00054173"
] | [
"16514016"
] | [
"Characterization of the plant-specific BREVIS RADIX gene family reveals limited genetic redundancy despite high sequence conservation."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Candidatus Daviesbacteria bacterium GW2011_GWC2_40_12",
"Eukaryota",
"viral metagenome"
] | [
1,
7375,
1
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
94,
39,
106
] | 3 | true | Domain | Brevis radix (BRX) domain | Brevis radix (BRX) domain | Brevis_radix_dom | 5 |
IPR013593 | 13,593 | Pro-opiomelanocortin N-terminal | Melanocortin_N | Domain | 2,547 | false | false | This domain represents the N-terminal peptide of pro-opiomelanocortin (NPP). It is thought to represent an important pituitary peptide, given its high yield from pituitary glands, and exhibits a potent in vitro aldosterone-stimulating activity [ ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08384",
"SM01364"
] | [
"NPP",
"NPP"
] | [
2547,
1090
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-111885",
"R-BTA-193048",
"R-BTA-194002",
"R-BTA-202040",
"R-BTA-209952",
"R-BTA-211976",
"R-BTA-375276",
"R-BTA-418555",
"R-BTA-418594",
"R-HSA-111885",
"R-HSA-193048",
"R-HSA-194002",
"R-HSA-202040",
"R-HSA-209952",
"R-HSA-211976",
"R-HSA-375276",
"R-HSA-418555",
"R-HSA-418... | [
"REACTOME:R-BTA-111885",
"REACTOME:R-BTA-193048",
"REACTOME:R-BTA-194002",
"REACTOME:R-BTA-202040",
"REACTOME:R-BTA-209952",
"REACTOME:R-BTA-211976",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-418555",
"REACTOME:R-BTA-418594",
"REACTOME:R-HSA-111885",
"REACTOME:R-HSA-193048",
"REACTOME:R-HSA-194... | 39 | [] | 0 | [
"PUB00020897"
] | [
"6945581"
] | [
"Complete amino acid sequence of a human pituitary glycopeptide: an important maturation product of pro-opiomelanocortin."
] | [
1981
] | 1 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
2547
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
9,
3,
4
] | 4 | true | Domain | Pro-opiomelanocortin N-terminal | Pro-opiomelanocortin N-terminal | Melanocortin_N | 1 |
IPR013594 | 13,594 | Dynein heavy chain, tail | Dynein_heavy_tail | Domain | 18,879 | false | false | Dyneins are motor proteins of eukaryotic cells that convert energy from ATP hydrolysis into force and movement along microtubules. They generally contain one to three heavy chains (each >500kDa), which belong to the AAA+ superfamily of mechanochemical enzymes, along with several accessory subunits ranging from light to... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08385"
] | [
"DHC_N1"
] | [
18879
] | 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-CEL-5620924",
"R-CEL-6798695",
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-9646399",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9646399",
"R-DME-3371497",
"R-DME-6798695",
"R-DME-6807878",
"R-DME-6811436",
"R-DME-9646399",
"R-HSA-141444",
"R-HSA-2132295",
"R-HSA-2467813",
"R-HSA-250025... | [
"REACTOME:R-CEL-5620924",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-9646399",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-9646399",
"REACTOME:R-DME-3371497",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-6807878",
"REACTOM... | 82 | [
"5afr",
"5nug",
"6f1t",
"6f1u",
"6f1v",
"6f38",
"6f3a",
"6rla",
"6rlb",
"6sc2",
"6zyw",
"6zyx",
"6zyy",
"7k58",
"7k5b",
"7kek",
"7kzm",
"7kzn",
"7kzo",
"7moq",
"7z8f",
"7z8g",
"7z8h",
"7z8i",
"7z8j",
"7z8k",
"7z8l",
"8bwy",
"8bx8",
"8glv",
"8j07",
"8pqv"... | 111 | [
"PUB00005841",
"PUB00020863",
"PUB00020905",
"PUB00033356",
"PUB00061850",
"PUB00062447",
"PUB00097475",
"PUB00097476",
"PUB00097477",
"PUB00097478",
"PUB00097479",
"PUB00163363",
"PUB00163364"
] | [
"9927482",
"10336435",
"10862709",
"15661525",
"8666668",
"22398446",
"9242627",
"15880123",
"9403697",
"12610617",
"19203583",
"16061793",
"16229832"
] | [
"AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.",
"Interaction mapping of a dynein heavy chain. Identification of dimerization and intermediate-chain binding domains.",
"AAA domains and organization of the dynein motor unit.",
"Recent pro... | [
1999,
1999,
2000,
2005,
1996,
2012,
1997,
2005,
1997,
2003,
2009,
2005,
2005
] | 13 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"mine drainage metagenome"
] | [
18878,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
2,
23,
27,
53,
19,
1,
29,
1,
1
] | 9 | true | Domain | Dynein heavy chain, tail | Dynein heavy chain, tail | Dynein_heavy_tail | 9 |
IPR013595 | 13,595 | Peptidase S33 tripeptidyl aminopeptidase-like, C-terminal | Pept_S33_TAP-like_C | Domain | 27,889 | false | false | This entry represents a C-terminal domain associated with putative hydrolases and bacterial peptidases that belong to MEROPS peptidase family S33 (clan SC). They are related to a tripeptidyl aminopeptidase from Streptomyces lividans ( ). A member of this family ( ) is thought to be involved in the C-terminal processing... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08386"
] | [
"Abhydrolase_4"
] | [
27889
] | 1 | [] | [] | [] | 0 | [
"2wtm",
"2wtn",
"8g5t",
"8g5u"
] | 4 | [
"PUB00020911"
] | [
"15574930"
] | [
"Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
16,
20405,
7272,
196
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica"
] | [
2,
1,
5
] | 3 | true | Domain | Peptidase S33 tripeptidyl aminopeptidase-like, C-terminal | Peptidase S33 tripeptidyl aminopeptidase-like, C-terminal | Pept_S33_TAP-like_C | 3 |
IPR013598 | 13,598 | Exportin-1/Importin-beta-like | Exportin-1/Importin-b-like | Domain | 24,938 | false | false | The exchange of macromolecules between the nucleus and cytoplasm takes place through nuclear pore complexes within the nuclear membrane. Active transport of large molecules through these pore complexes require carrier proteins, called karyopherins (importins and exportins), which shuttle between the two compartments. T... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08389"
] | [
"Xpo1"
] | [
24938
] | 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-DDI-5687128",
"R-DME-3769402",
"R-DME-450520",
"R-DME-69273",
"R-DME-9634638",
"R-DME-9707616",
"R-DME-9856649",
"R-HSA-141444",
"R-HSA-165054",
"R-HSA-168333",
"R-HSA-203927",
"R-HSA-2173788",
"R-HSA-2467813",
"R-HSA-2500257",
"R-HSA-3769402",
"R-HSA-450520",
"R-HSA-5663220",
"... | [
"REACTOME:R-DDI-5687128",
"REACTOME:R-DME-3769402",
"REACTOME:R-DME-450520",
"REACTOME:R-DME-69273",
"REACTOME:R-DME-9634638",
"REACTOME:R-DME-9707616",
"REACTOME:R-DME-9856649",
"REACTOME:R-HSA-141444",
"REACTOME:R-HSA-165054",
"REACTOME:R-HSA-168333",
"REACTOME:R-HSA-203927",
"REACTOME:R-HSA... | 56 | [
"2x19",
"2x1g",
"2xwu",
"3a6p",
"3gb8",
"3gjx",
"3ibv",
"3icq",
"3m1i",
"3nby",
"3nbz",
"3nc0",
"3nc1",
"3vyc",
"3wyf",
"3wyg",
"3zjy",
"3zkv",
"4bsm",
"4bsn",
"4c0o",
"4c0p",
"4c0q",
"4fgv",
"4gmx",
"4gpt",
"4hat",
"4hau",
"4hav",
"4haw",
"4hax",
"4hay"... | 110 | [
"PUB00019254",
"PUB00020894",
"PUB00034676"
] | [
"9323123",
"9323132",
"17170104"
] | [
"Nuclear export receptors: from importin to exportin.",
"Exportin 1 (Crm1p) is an essential nuclear export factor.",
"Classical nuclear localization signals: definition, function, and interaction with importin alpha."
] | [
1997,
1997,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA)",
"Eukaryota"
] | [
1,
24937
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
27,
4,
18,
14,
31,
13,
6,
15,
37,
3,
5,
86
] | 12 | true | Domain | Exportin-1/Importin-beta-like | Exportin-1/Importin-beta-like | Exportin-1/Importin-b-like | 9 |
IPR013600 | 13,600 | Ly49-like, N-terminal | Ly49_N | Domain | 678 | false | false | The sequences making up this entry are annotated as, or are similar to, Ly49 receptors (e.g. ). These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell functio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08391"
] | [
"Ly49"
] | [
678
] | 1 | [] | [] | [] | 0 | [
"1qo3",
"3c8j",
"3g8l",
"4jo8"
] | 4 | [
"PUB00020827",
"PUB00020929"
] | [
"15607796",
"10925254"
] | [
"Mouse Ly49 NK receptors: balancing activation and inhibition.",
"Ly-49P activates NK-mediated lysis by recognizing H-2Dd."
] | [
2005,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
678
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
102,
57
] | 3 | true | Domain | Ly49-like, N-terminal | Ly49-like, N-terminal | Ly49_N | 8 |
IPR013601 | 13,601 | FAE1/Type III polyketide synthase-like protein | FAE1_typ3_polyketide_synth | Domain | 13,755 | false | false | This domain is found in proteins that are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region contains the active site residues, as well as motifs involved in sub... | [
"GO:0016747",
"GO:0006633",
"GO:0016020"
] | [
"acyltransferase activity, transferring groups other than amino-acyl groups",
"fatty acid biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF08392"
] | [
"FAE1_CUT1_RppA"
] | [
13755
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.199",
"GenProp1569",
"PWY-5080",
"PWY-5972",
"PWY-6433",
"PWY-6598",
"PWY-7035",
"PWY-7036",
"PWY-7601",
"PWY-7602",
"PWY-7619",
"PWY-7724",
"PWY-7725",
"PWY-8041"
] | [
"EC:2.3.1.199",
"GP:GenProp1569",
"METACYC:PWY-5080",
"METACYC:PWY-5972",
"METACYC:PWY-6433",
"METACYC:PWY-6598",
"METACYC:PWY-7035",
"METACYC:PWY-7036",
"METACYC:PWY-7601",
"METACYC:PWY-7602",
"METACYC:PWY-7619",
"METACYC:PWY-7724",
"METACYC:PWY-7725",
"METACYC:PWY-8041"
] | 14 | [
"8ysp",
"8yst",
"8yt0",
"8yw7",
"9uu3",
"9uu4",
"9uu5"
] | 7 | [
"PUB00020820"
] | [
"12139488"
] | [
"Alteration of reaction and substrate specificity of a bacterial type III polyketide synthase by site-directed mutagenesis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Yasminevirus sp. GU-2018",
"metagenomes"
] | [
449,
13296,
1,
9
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
84,
78,
100
] | 3 | true | Domain | FAE1/Type III polyketide synthase-like protein | FAE1/Type III polyketide synthase-like protein | FAE1_typ3_polyketide_synth | 9 |
IPR013602 | 13,602 | Dynein heavy chain, linker | Dhc_linker | Domain | 30,258 | false | false | This entry represents the linker of the dynein heavy chain motor domain. Dyneins are motor proteins of eukaryotic cells that convert energy from ATP hydrolysis into force and movement along microtubules. They generally contain one to three heavy chains (each >500kDa), which belong to the AAA+ superfamily of mechanochem... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08393"
] | [
"DHC_N2"
] | [
30258
] | 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-CEL-5620924",
"R-CEL-6798695",
"R-CEL-6807878",
"R-CEL-6811436",
"R-CEL-9646399",
"R-DDI-6798695",
"R-DDI-6807878",
"R-DDI-9646399",
"R-DME-3371497",
"R-DME-6798695",
"R-DME-6807878",
"R-DME-6811436",
"R-DME-9646399",
"R-HSA-141444",
"R-HSA-2132295",
"R-HSA-2467813",
"R-HSA-250025... | [
"REACTOME:R-CEL-5620924",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811436",
"REACTOME:R-CEL-9646399",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-9646399",
"REACTOME:R-DME-3371497",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-6807878",
"REACTOM... | 82 | [
"3qmz",
"3vkg",
"3vkh",
"4ai6",
"4akg",
"4akh",
"4aki",
"4rh7",
"4w8f",
"5nug",
"5vh9",
"5vlj",
"6f38",
"6f3a",
"6rla",
"6rlb",
"6sc2",
"6zyw",
"6zyx",
"6zyy",
"7k58",
"7k5b",
"7kek",
"7kzm",
"7kzn",
"7kzo",
"7mgm",
"7mi1",
"7mi3",
"7mi6",
"7mi8",
"7moq"... | 151 | [
"PUB00005841",
"PUB00033356",
"PUB00061850",
"PUB00062447",
"PUB00097475",
"PUB00097476",
"PUB00097477",
"PUB00097478",
"PUB00097479",
"PUB00163363",
"PUB00163364"
] | [
"9927482",
"15661525",
"8666668",
"22398446",
"9242627",
"15880123",
"9403697",
"12610617",
"19203583",
"16061793",
"16229832"
] | [
"AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.",
"Recent progress in dynein structure and mechanism.",
"Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.",
"The 2.8 A cryst... | [
1999,
2005,
1996,
2012,
1997,
2005,
1997,
2003,
2009,
2005,
2005
] | 11 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"mine drainage metagenome"
] | [
30257,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strai... | [
5,
33,
33,
64,
32,
1,
57,
1,
1
] | 9 | true | Domain | Dynein heavy chain, linker | Dynein heavy chain, linker | Dhc_linker | 8 |
IPR013603 | 13,603 | TRASH transcription regulator C-terminal, prokaryotic | TRASH_TR_C_prok | Domain | 176 | false | false | This region is found in the C terminus of a number of prokaryotic transcriptional regulators. It is thought to function as a metal-sensing regulatory module [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08394"
] | [
"Arc_trans_TRASH"
] | [
176
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014222"
] | [
"12713899"
] | [
"TRASH: a novel metal-binding domain predicted to be involved in heavy-metal sensing, trafficking and resistance."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"marine sediment metagenome"
] | [
171,
3,
2
] | 3 | [] | [] | 0 | true | Domain | TRASH transcription regulator C-terminal, prokaryotic | TRASH transcription regulator C-terminal, prokaryotic | TRASH_TR_C_prok | 7 |
IPR013604 | 13,604 | 7TM chemosensory receptor | 7TM_chemorcpt | Family | 12,305 | false | false | This family includes a number of insect chemosensory receptors encoded by gustatory receptor (GR) and odorant receptor (OR) genes across the insect tree of life. They are seven-transmembrane ligand-gated ion channels, showing high sequence divergence, consistent with an ancient origin for the family [ , , , , ]. This e... | [
"GO:0050909",
"GO:0016020"
] | [
"sensory perception of taste",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF08395"
] | [
"7tm_7"
] | [
12305
] | 1 | [] | [] | [] | 0 | [
"8jm9",
"8jma",
"8uvt",
"8uvu",
"8vc1",
"8vc2",
"8vv3",
"8x82",
"8x83",
"8x84",
"8zdz",
"8ze3"
] | 12 | [
"PUB00020817",
"PUB00020866",
"PUB00152147",
"PUB00152148",
"PUB00152149",
"PUB00154497"
] | [
"12364795",
"14608037",
"18408712",
"30111839",
"21709218",
"15456826"
] | [
"G protein-coupled receptors in Anopheles gambiae.",
"Molecular evolution of the insect chemoreceptor gene superfamily in Drosophila melanogaster.",
"Insect olfactory receptors are heteromeric ligand-gated ion channels.",
"Cryo-EM structure of the insect olfactory receptor Orco.",
"Sugar-regulated cation ch... | [
2002,
2003,
2008,
2018,
2011,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
12305
] | 1 | [
"Caenorhabditis elegans",
"Drosophila melanogaster"
] | [
3,
197
] | 2 | true | Family | 7TM chemosensory receptor | 7TM chemosensory receptor | 7TM_chemorcpt | 1 |
IPR013605 | 13,605 | Spider toxin omega agotoxin/Tx1 family | Toxin_34 | Family | 128 | false | false | The Tx1 family lethal spider neurotoxin induces excitatory symptoms in mice [ , ]. This family also includes type I, II and III omega-agatoxins [ ]. | [
"GO:0090729"
] | [
"toxin activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08396"
] | [
"Toxin_34"
] | [
128
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020839",
"PUB00085764",
"PUB00097933"
] | [
"8340362",
"1339015",
"33597864"
] | [
"Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the Brazilian \"armed\" spider Phoneutria nigriventer predicts the synthesis and processing of a preprotoxin.",
"Omega-agatoxins differentially block calcium channels in locust, chick and rat synaptosomes.",
"A Novel Insecticidal Spider Peptide tha... | [
1993,
1992,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"RTA clade"
] | [
128
] | 1 | [] | [] | 0 | true | Family | Spider toxin omega agotoxin/Tx1 family | Spider toxin omega agotoxin/Tx1 family | Toxin_34 | 4 |
IPR013606 | 13,606 | IMD/I-BAR domain | I-BAR_dom | Domain | 12,593 | false | false | The I-BAR domain (also known as IMD domain, IRSp53 and MIM homology domain) is a BAR-like domain of approximately 250 amino acids found at the N-terminal in the IRSp53 (insulin receptor tyrosine kinase substrate p53) and in the evolutionarily related IRSp53/MIM family. The BAR domain forms an anti-parallel all-helical ... | [
"GO:0007009"
] | [
"plasma membrane organization"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF08397",
"PS51338"
] | [
"IMD",
"IMD"
] | [
12516,
12218
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-2029482",
"R-BTA-4420097",
"R-BTA-5663213",
"R-BTA-9013149",
"R-BTA-9013423",
"R-DRE-9035034",
"R-HSA-2029482",
"R-HSA-4420097",
"R-HSA-5663213",
"R-HSA-9013148",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013423",
"R-HSA-9035034",
"R-HSA-9664422",
"R-MMU-2029482",
"R-MMU-44200... | [
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5663213",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013423",
"REACTOME:R-DRE-9035034",
"REACTOME:R-HSA-2029482",
"REACTOME:R-HSA-4420097",
"REACTOME:R-HSA-5663213",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013149",
"REACTOM... | 28 | [
"1wdz",
"1y2o",
"2d1l",
"2ykt",
"3ok8",
"4nqi"
] | 6 | [
"PUB00020898",
"PUB00035722",
"PUB00035723",
"PUB00043717",
"PUB00071724",
"PUB00071727",
"PUB00071728",
"PUB00153744"
] | [
"14752106",
"17430976",
"14980512",
"17497115",
"21743456",
"21093245",
"17371834",
"22921828"
] | [
"A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein.",
"Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties.",
"Extracellular fragment of brain-specific angioge... | [
2004,
2007,
2004,
2007,
2011,
2011,
2007,
2012
] | 8 | [] | [
"IPR030060",
"IPR030128"
] | 0 | 2 | 0 | [
"Eukaryota"
] | [
12593
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
103,
21,
34,
14,
32
] | 6 | true | Domain | IMD/I-BAR domain | IMD/I-BAR domain | I-BAR_dom | 9 |
IPR013607 | 13,607 | Phospholipase A2-like domain | Phospholipase_A2-like | Domain | 4,407 | false | false | This entry represents a domain that is likely to be a phospholipase A2-like enzyme. It is found in a variety of contexts across the tree of life. This domain can be found in the N-terminal region of the Parvovirus VP1 coat protein [ ]; its function is not known. Parvoviruses are some of the smallest viruses containing ... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08398"
] | [
"Phospholip_A2_4"
] | [
4407
] | 1 | [] | [] | [] | 0 | [
"3j1q",
"3kic",
"3kie",
"3ng9",
"3ntt",
"4g0r",
"4gbt",
"4iov",
"4rso",
"5ipi",
"5ipk",
"6cbe",
"6e9d",
"6ihb",
"6nz0",
"6u3q",
"6u95",
"7kp3",
"7kpn",
"7rk8",
"7rk9",
"7rwl",
"7rwt",
"7thr",
"7ti4",
"7ti5",
"7ud4",
"8fyw",
"8fz0",
"9b7s",
"9b7t",
"9b7u"... | 47 | [
"PUB00028082",
"PUB00054921",
"PUB00096898"
] | [
"9927584",
"20097398",
"12050365"
] | [
"Controlled conformational transitions in the MVM virion expose the VP1 N-terminus and viral genome without particle disassembly.",
"Determination and analysis of the full-length chicken parvovirus genome.",
"Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA... | [
1999,
2010,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
247,
1040,
3117,
3
] | 4 | [] | [] | 0 | true | Domain | Phospholipase A2-like domain | Phospholipase A2-like domain | Phospholipase_A2-like | 1 |
IPR013608 | 13,608 | VWA N-terminal | VWA_N | Domain | 9,178 | false | false | This domain is found at the N terminus of proteins containing von Willebrand factor type A (VWA, ) and Cache ( ) domains. It has been found in vertebrates, Drosophila melanogaster (Fruit fly) and Caenorhabditis elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08399"
] | [
"VWA_N"
] | [
9178
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-112308",
"R-CEL-422356",
"R-CEL-5576892",
"R-CEL-5576893",
"R-HSA-112308",
"R-HSA-400042",
"R-HSA-422356",
"R-HSA-5576892",
"R-HSA-5576893",
"R-HSA-9662360",
"R-HSA-9856532",
"R-MMU-112308",
"R-MMU-422356",
"R-MMU-5576892",
"R-MMU-5576893",
"R-RNO-112308",
"R-RNO-422356",
"R... | [
"REACTOME:R-CEL-112308",
"REACTOME:R-CEL-422356",
"REACTOME:R-CEL-5576892",
"REACTOME:R-CEL-5576893",
"REACTOME:R-HSA-112308",
"REACTOME:R-HSA-400042",
"REACTOME:R-HSA-422356",
"REACTOME:R-HSA-5576892",
"REACTOME:R-HSA-5576893",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9856532",
"REACTOME:R-M... | 19 | [
"3jbr",
"5gjv",
"5gjw",
"6jp5",
"6jp8",
"6jpa",
"6jpb",
"7jpk",
"7jpl",
"7jpv",
"7jpw",
"7jpx",
"7mix",
"7miy",
"7uhf",
"7uhg",
"7vfs",
"7vfu",
"7vfv",
"7vfw",
"7xlq",
"7yg5",
"8e56",
"8e57",
"8e58",
"8e59",
"8e5a",
"8e5b",
"8eog",
"8epl",
"8epm",
"8fd7"... | 46 | [
"PUB00020868"
] | [
"11487633"
] | [
"Ducky mouse phenotype of epilepsy and ataxia is associated with mutations in the Cacna2d2 gene and decreased calcium channel current in cerebellar Purkinje cells."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Candidatus Lokiarchaeum ossiferum",
"Eukaryota"
] | [
1,
9177
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
48,
6,
18,
12,
24
] | 6 | true | Domain | VWA N-terminal | VWA N-terminal | VWA_N | 5 |
IPR013609 | 13,609 | Lambda-like tail fibre protein, N-terminal | Stf-like_N | Domain | 2,841 | false | false | This domain is found at the N terminus of Lambda-like phage and prophage tail fibre proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08400"
] | [
"phage_tail_N"
] | [
2841
] | 1 | [] | [] | [] | 0 | [
"9e7m"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ecdysozoa",
"Viruses",
"metagenomes"
] | [
2792,
4,
42,
3
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Lambda-like tail fibre protein, N-terminal | Lambda-like tail fibre protein, N-terminal | Stf-like_N | 6 |
IPR013610 | 13,610 | ArdC, N-terminal ssDNA binding domain | ArdC_N | Domain | 11,090 | false | false | This is the α-helical ssDNA binding domain of anti-restriction factor ArdC deployed by plasmids and phages in polyvalent proteins related to the BHD domains of XPC/Rad4 and the Tc-38 domain found in kinetoplastid minicircle binding proteins [ , , ]. The structure of this domain is composed of three α-helices and a thre... | [
"GO:0003697"
] | [
"single-stranded DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08401"
] | [
"ArdcN"
] | [
11090
] | 1 | [] | [] | [] | 0 | [
"6i89",
"6sna"
] | 2 | [
"PUB00043496",
"PUB00091133",
"PUB00098071",
"PUB00098072"
] | [
"10686096",
"28559295",
"30396152",
"32348296"
] | [
"Antirestriction protein Ard (Type C) encoded by IncW plasmid pSa has a high similarity to the \"protein transport\" domain of TraC1 primase of promiscuous plasmid RP4.",
"Polyvalent Proteins, a Pervasive Theme in the Intergenomic Biological Conflicts of Bacteriophages and Conjugative Elements.",
"Unexpected Ev... | [
2000,
2017,
2018,
2020
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes",
"plasmids"
] | [
316,
10544,
35,
40,
144,
11
] | 6 | [] | [] | 0 | true | Domain | ArdC, N-terminal ssDNA binding domain | ArdC, N-terminal ssDNA binding domain | ArdC_N | 9 |
IPR013611 | 13,611 | Transport-associated OB, type 2 | Transp-assoc_OB_typ2 | Domain | 87,778 | false | false | The TOBE domain [ ] (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum (e.g. ) and sulphate ( ). Found in ABC transporters immediately after the ATPase domain. A strong RPE motif ... | [
"GO:0005524",
"GO:0022857",
"GO:0055085",
"GO:0043190"
] | [
"ATP binding",
"transmembrane transporter activity",
"transmembrane transport",
"ATP-binding cassette (ABC) transporter complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF08402"
] | [
"TOBE_2"
] | [
87778
] | 1 | [
"EC"
] | [
"7.6.2.11"
] | [
"EC:7.6.2.11"
] | 1 | [
"1q12",
"1q1b",
"1q1e",
"2awn",
"2awo",
"2r6g",
"2yyz",
"3fh6",
"3gd7",
"3puv",
"3puw",
"3pux",
"3puy",
"3puz",
"3pv0",
"3rlf",
"4jbw",
"4khz",
"4ki0",
"8y5f",
"8y5g",
"8y5h",
"8y5i",
"8zx1",
"9bcr",
"9j4r",
"9nqj",
"9nxc"
] | 28 | [
"PUB00007673"
] | [
"10829230"
] | [
"Protein fold recognition using sequence profiles and its application in structural genomics."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2321,
84282,
157,
1018
] | 4 | [
"Escherichia coli (strain K12)"
] | [
5
] | 1 | true | Domain | Transport-associated OB, type 2 | Transport-associated OB, type 2 | Transp-assoc_OB_typ2 | 6 |
IPR013612 | 13,612 | Amino acid permease, N-terminal | AA_permease_N | Domain | 5,378 | false | false | Amino acid permeases are integral membrane proteins involved in the transport of amino acids into the cell. A number of such proteins have been found to be evolutionary related [ , , ]. These proteins appear to contain up to 12 transmembrane segments. The best conserved region in this family is located in the second tr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08403"
] | [
"AA_permease_N"
] | [
5378
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DRE-426117",
"R-HSA-426117",
"R-HSA-5619087",
"R-HSA-5619104",
"R-MMU-426117",
"R-RNO-426117"
] | [
"REACTOME:R-DRE-426117",
"REACTOME:R-HSA-426117",
"REACTOME:R-HSA-5619087",
"REACTOME:R-HSA-5619104",
"REACTOME:R-MMU-426117",
"REACTOME:R-RNO-426117"
] | 6 | [
"6pzt",
"7d10",
"7n3n",
"7s1x",
"7s1y",
"7s1z",
"7y6i",
"7yg0",
"7yg1",
"7zgo",
"8fhn",
"8fho",
"8fhp",
"8fhq",
"8fhr",
"8fht",
"8vpn",
"8vpp",
"9bwt",
"9c0e",
"9c0g",
"9c0h"
] | 22 | [
"PUB00001779",
"PUB00003402",
"PUB00005006"
] | [
"2687114",
"3146645",
"8382989"
] | [
"Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases.",
"Evolutionary relationship and secondary structure predictions in four transport proteins of Saccharomyces cerevisiae.",
"Mammalian integral membrane receptors are homo... | [
1989,
1988,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
5378
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
2,
12,
10,
22
] | 5 | true | Domain | Amino acid permease, N-terminal | Amino acid permease, N-terminal | AA_permease_N | 8 |
IPR013613 | 13,613 | Baculoviridae p74 N-terminal | Baculo_p74_N | Domain | 256 | false | false | This domain is found at the N terminus of P74 occlusion-derived virus (ODV) envelope proteins which are required for oral infectivity. The envelope proteins are found in baculoviruses which are insect pathogens. The C terminus of P74 is anchored to the membrane whereas the N terminus is exposed to the virion surface. F... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08404"
] | [
"Baculo_p74_N"
] | [
256
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020928"
] | [
"15914841"
] | [
"Evidence for proteolytic cleavage of the baculovirus occlusion-derived virion envelope protein P74."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Arthropoda",
"Viruses"
] | [
37,
219
] | 2 | [] | [] | 0 | true | Domain | Baculoviridae p74 N-terminal | Baculoviridae p74 N-terminal | Baculo_p74_N | 7 |
IPR013614 | 13,614 | Viral polyprotein, Caliciviridae N-terminal | Viral_PP_Calicivir_N | Domain | 2,341 | false | false | This domain is found at the N terminus of non-structural viral polyproteins of the Caliciviridae subfamily. | [
"GO:0003968",
"GO:0004197",
"GO:0017111",
"GO:0044419"
] | [
"RNA-directed RNA polymerase activity",
"cysteine-type endopeptidase activity",
"ribonucleoside triphosphate phosphatase activity",
"biological process involved in interspecies interaction between organisms"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF08405"
] | [
"Calici_PP_N"
] | [
2341
] | 1 | [
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.22.66",
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:2.7.7.48",
"EC:3.4.22.66",
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 8 | [
"9r34"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
2341
] | 1 | [] | [] | 0 | true | Domain | Viral polyprotein, Caliciviridae N-terminal | Viral polyprotein, Caliciviridae N-terminal | Viral_PP_Calicivir_N | 5 |
IPR013615 | 13,615 | CbbQ/NirQ/NorQ, C-terminal | CbbQ_C | Domain | 4,886 | false | false | This domain is found at the C terminus of proteins of the CbbQ/NirQ/NorQ family of proteins which play a role in the post-translational activation of Rubisco [ ]. It is also found in the Thauera aromaticaTutH protein which is similar to the CbbQ/NirQ/NorQ family [ ], as well as in putative chaperones. The ATPase domain... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08406"
] | [
"CbbQ_C"
] | [
4886
] | 1 | [] | [] | [] | 0 | [
"5c3c",
"6l1q"
] | 2 | [
"PUB00017121",
"PUB00020976"
] | [
"10698784",
"10548510"
] | [
"Transcriptional analysis of the tutE tutFDGH gene cluster from Thauera aromatica strain T1.",
"The cbbQ genes, located downstream of the form I and form II RubisCO genes, affect the activity of both RubisCOs."
] | [
2000,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
74,
4456,
144,
19,
193
] | 5 | [] | [] | 0 | true | Domain | CbbQ/NirQ/NorQ, C-terminal | CbbQ/NirQ/NorQ, C-terminal | CbbQ_C | 5 |
IPR013616 | 13,616 | Chitin synthase N-terminal | Chitin_synth_N | Domain | 6,778 | false | false | This is the N-terminal domain of Chitin synthase. | [
"GO:0004100"
] | [
"chitin synthase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08407"
] | [
"Chitin_synth_1N"
] | [
6778
] | 1 | [
"EC",
"METACYC"
] | [
"2.4.1.16",
"PWY-6981"
] | [
"EC:2.4.1.16",
"METACYC:PWY-6981"
] | 2 | [
"7stl",
"7stm",
"7stn",
"7sto",
"7xs6",
"7xs7",
"8k3p",
"8k3q",
"8k3r",
"8k3t",
"8k3u",
"8k3v",
"8k3w",
"8k3x"
] | 14 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bifidobacterium callitrichidarum",
"Eukaryota"
] | [
1,
6777
] | 2 | [
"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)"
] | [
3,
2,
2
] | 3 | true | Domain | Chitin synthase N-terminal | Chitin synthase N-terminal | Chitin_synth_N | 4 |
IPR013617 | 13,617 | DNA-directed DNA polymerase, family B, viral insert domain | DNA-dir_DNA_pol_B_vir_insert | Domain | 212 | false | false | This viral domain is found between the exonuclease domain of the DNA polymerase family B ( ) and the domain, connecting the two. | [
"GO:0003887"
] | [
"DNA-directed DNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08408"
] | [
"DNA_pol_B_3"
] | [
212
] | 1 | [
"EC"
] | [
"2.7.7.7"
] | [
"EC:2.7.7.7"
] | 1 | [
"5n2e",
"5n2g",
"5n2h",
"8hdz",
"8hg1",
"8hlz",
"8hm0",
"8hoy",
"8hpa",
"8j86",
"8j8f",
"8j8g",
"8k8s",
"8k8u",
"8q3r",
"8wpe",
"8wpf",
"8wpk",
"8wpp",
"9k9r",
"9k9s",
"9k9t",
"9k9u",
"9k9v"
] | 24 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Nucleocytoviricota"
] | [
212
] | 1 | [] | [] | 0 | true | Domain | DNA-directed DNA polymerase, family B, viral insert domain | DNA-directed DNA polymerase, family B, viral insert domain | DNA-dir_DNA_pol_B_vir_insert | 4 |
IPR013618 | 13,618 | Protein O-mannosyl-transferase TMTC, DUF1736 | TMTC_DUF1736 | Domain | 7,827 | false | false | This domain of unknown function is found in O-mannosyl-transferases TMTC1-4, and constitutes a loop between TM7 and TM8 located in the ER lumen that contains a small hydrophobic, but not membrane-embedded helix. This loop is critical for catalysis and binding of ligands, especially the lipid-linked sugar moiety [ ]. TM... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08409"
] | [
"TMTC_DUF1736"
] | [
7827
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.4.1.109",
"PWY-7921",
"PWY-7922",
"PWY-7979"
] | [
"EC:2.4.1.109",
"METACYC:PWY-7921",
"METACYC:PWY-7922",
"METACYC:PWY-7979"
] | 4 | [] | 0 | [
"PUB00098068",
"PUB00098069"
] | [
"33436046",
"28973932"
] | [
"Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites.",
"Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins."
] | [
2021,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
22,
7805
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
12,
7,
13,
7,
19
] | 6 | true | Domain | Protein O-mannosyl-transferase TMTC, DUF1736 | Protein O-mannosyl-transferase TMTC, DUF1736 | TMTC_DUF1736 | 3 |
IPR013619 | 13,619 | Domain of unknown function DUF1737 | DUF1737 | Domain | 3,018 | false | false | This domain of unknown function is found at the N terminus of bacterial and viral hypothetical proteins. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08410"
] | [
"DUF1737"
] | [
3018
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriati",
"Viruses",
"metagenomes"
] | [
2905,
2,
82,
29
] | 4 | [] | [] | 0 | true | Domain | Domain of unknown function DUF1737 | Domain of unknown function DUF1737 | DUF1737 | 4 |
IPR013621 | 13,621 | Ion transport N-terminal | Ion_trans_N | Domain | 4,633 | false | false | This domain is found to the N terminus of in voltage- and cyclic nucleotide-gated K/Na ion channels. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08412"
] | [
"Ion_trans_N"
] | [
4633
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1296061",
"R-MMU-1296061",
"R-RNO-1296061"
] | [
"REACTOME:R-HSA-1296061",
"REACTOME:R-MMU-1296061",
"REACTOME:R-RNO-1296061"
] | 3 | [
"5u6o",
"5u6p",
"6gyn",
"6gyo",
"6uqf",
"6uqg",
"7nmn",
"7np3",
"7np4",
"8inz",
"8io0",
"8io3",
"8ofi",
"8t4m",
"8t4y",
"8t50",
"8uc7",
"8uc8",
"8y60",
"9bc6",
"9bc7"
] | 21 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
4633
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
14,
9,
6,
9
] | 5 | true | Domain | Ion transport N-terminal | Ion transport N-terminal | Ion_trans_N | 1 |
IPR013623 | 13,623 | NADPH oxidase Respiratory burst | NADPH_Ox | Domain | 4,864 | false | false | This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N terminus of an EF-hand ( ), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants [ ]. | [
"GO:0004601",
"GO:0050664"
] | [
"peroxidase activity",
"oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08414"
] | [
"NADPH_Ox"
] | [
4864
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"1.11.1.-",
"1.6.3.-",
"PWY-5292"
] | [
"EC:1.11.1.-",
"EC:1.6.3.-",
"METACYC:PWY-5292"
] | 3 | [
"3a8r"
] | 1 | [
"PUB00020945"
] | [
"9628030"
] | [
"Six Arabidopsis thaliana homologues of the human respiratory burst oxidase (gp91phox)."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
4864
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
44,
26,
83
] | 3 | true | Domain | NADPH oxidase Respiratory burst | NADPH oxidase Respiratory burst | NADPH_Ox | 6 |
IPR013625 | 13,625 | Tensin/EPS8 phosphotyrosine-binding domain | PTB | Domain | 13,322 | false | false | The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) of tensin tends to be found at the C terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to t... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08416"
] | [
"PTB"
] | [
13322
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8875513",
"R-CEL-8875513",
"R-HSA-8875513",
"R-HSA-9662360",
"R-HSA-9662361",
"R-MMU-8875513",
"R-RNO-8875513"
] | [
"REACTOME:R-BTA-8875513",
"REACTOME:R-CEL-8875513",
"REACTOME:R-HSA-8875513",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9662361",
"REACTOME:R-MMU-8875513",
"REACTOME:R-RNO-8875513"
] | 7 | [
"1wvh",
"2cy4",
"2cy5",
"2dkq",
"2gjy",
"2loz",
"3hqc"
] | 7 | [
"PUB00018031",
"PUB00020856",
"PUB00020924",
"PUB00081239",
"PUB00081240",
"PUB00081241"
] | [
"15567406",
"11023826",
"14592531",
"11911882",
"10610414",
"11994738"
] | [
"Structural and evolutionary division of phosphotyrosine binding (PTB) domains.",
"Molecular characterization of human tensin.",
"Tensin.",
"PTB or not PTB -- that is the question.",
"The function of PTB domain proteins.",
"Phosphotyrosine-binding domains in signal transduction."
] | [
2005,
2000,
2004,
2002,
1999,
2002
] | 6 | [] | [
"IPR033928",
"IPR033929"
] | 0 | 2 | 0 | [
"Metazoa"
] | [
13322
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
182,
9,
51,
32,
41
] | 6 | true | Domain | Tensin/EPS8 phosphotyrosine-binding domain | Tensin/EPS8 phosphotyrosine-binding domain | PTB | 2 |
IPR013626 | 13,626 | Pheophorbide a oxygenase | PaO | Domain | 4,082 | false | false | This domain is found in bacterial and plant proteins to the C terminus of a Rieske 2Fe-2S domain ( ). One of the proteins the domain is found in is Pheophorbide a oxygenase (PaO) which seems to be a key regulator of chlorophyll catabolism. Arabidopsis PaO (AtPaO) is a Rieske-type 2Fe-2S enzyme that is identical to Arab... | [
"GO:0010277"
] | [
"chlorophyllide a oxygenase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08417"
] | [
"PaO"
] | [
4082
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020931"
] | [
"14657372"
] | [
"Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"viral metagenome"
] | [
415,
3665,
2
] | 3 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
15,
31,
27
] | 3 | true | Domain | Pheophorbide a oxygenase | Pheophorbide a oxygenase | PaO | 4 |
IPR013627 | 13,627 | DNA polymerase alpha, subunit B, N-terminal | Pol_alpha_B_N | Domain | 1,849 | false | false | This entry represents the N-terminal domain of subunit B of DNA polymerase alpha-primase, an enzyme which is essential for DNA replication in higher eukaryotes as it initiates synthesis on both leading and lagging strand single-stranded DNA templates. It consists of a primase heterodimer that synthesises RNA primers, a... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08418"
] | [
"Pol_alpha_B_N"
] | [
1849
] | 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-CEL-113501",
"R-CEL-68952",
"R-CEL-68962",
"R-CEL-69091",
"R-CEL-69166",
"R-CEL-69183",
"R-DME-113501",
"R-DME-68952",
"R-DME-68962",
"R-DME-69091",
"R-DME-69166",
"R-DME-69183",
"R-HSA-113501",
"R-HSA-174411",
"R-HSA-174430",
"R-HSA-68952",
"R-HSA-68962",
"R-HSA-69091",
"R-HS... | [
"REACTOME:R-CEL-113501",
"REACTOME:R-CEL-68952",
"REACTOME:R-CEL-68962",
"REACTOME:R-CEL-69091",
"REACTOME:R-CEL-69166",
"REACTOME:R-CEL-69183",
"REACTOME:R-DME-113501",
"REACTOME:R-DME-68952",
"REACTOME:R-DME-68962",
"REACTOME:R-DME-69091",
"REACTOME:R-DME-69166",
"REACTOME:R-DME-69183",
"R... | 37 | [
"2keb",
"4e2i",
"4y97",
"5exr",
"7u5c",
"8b9d",
"8d0k",
"8g99",
"8g9f",
"8qj7",
"8v5m",
"8v5n",
"8v5o",
"8v6g",
"8v6h",
"8v6i",
"8v6j"
] | 17 | [
"PUB00052915",
"PUB00093651"
] | [
"19494830",
"20234039"
] | [
"3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases.",
"Structure of a DNA polymerase alpha-primase domain that docks on the SV40 helicase and activates the viral primosome."
] | [
2009,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1849
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
1,
2,
2,
7,
7,
6
] | 7 | true | Domain | DNA polymerase alpha, subunit B, N-terminal | DNA polymerase alpha, subunit B, N-terminal | Pol_alpha_B_N | 9 |
IPR013630 | 13,630 | Methyltransferase putative zinc binding domain | Methyltransf_Zn-bd_dom_put | Domain | 4,851 | false | false | This domain is found at the N terminus of bacterial methyltransferases and contains four conserved cysteines suggesting a potential role in zinc binding. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08421"
] | [
"Methyltransf_13"
] | [
4851
] | 1 | [] | [] | [] | 0 | [
"3ndi",
"3ndj",
"4e2w",
"4e2x",
"4e2y",
"4e2z",
"4e30",
"4e31",
"4e32",
"4e33",
"4rv9",
"4rvd",
"4rvf",
"4rvg",
"4rvh",
"5t64",
"5t67",
"5t6b"
] | 18 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
34,
4532,
68,
15,
202
] | 5 | [] | [] | 0 | true | Domain | Methyltransferase putative zinc binding domain | Methyltransferase putative zinc binding domain | Methyltransf_Zn-bd_dom_put | 1 |
IPR013632 | 13,632 | Rad51-like, C-terminal | Rad51_C | Domain | 23,791 | false | false | This domain is found at the C-terminal of DNA repair and recombination protein Rad51, and eukaryotic and archaeal Rad51-like proteins. It is critical for DNA binding [ ]. Rad51 is a homologue of the bacterial RecA protein. Rad51 and RecA share a core ATPase domain. RAD51 is a key protein involved in the homologous reco... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08423"
] | [
"Rad51"
] | [
23791
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-5685938",
"R-BTA-5685942",
"R-BTA-5693568",
"R-BTA-5693579",
"R-BTA-5693616",
"R-BTA-912446",
"R-CFA-5685938",
"R-CFA-5685942",
"R-CFA-5693568",
"R-CFA-5693579",
"R-CFA-5693616",
"R-CFA-912446",
"R-DME-5693616",
"R-GGA-265976",
"R-GGA-351433",
"R-GGA-5685938",
"R-GGA-5685942",... | [
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5685942",
"REACTOME:R-BTA-5693568",
"REACTOME:R-BTA-5693579",
"REACTOME:R-BTA-5693616",
"REACTOME:R-BTA-912446",
"REACTOME:R-CFA-5685938",
"REACTOME:R-CFA-5685942",
"REACTOME:R-CFA-5693568",
"REACTOME:R-CFA-5693579",
"REACTOME:R-CFA-5693616",
"REACTOME... | 45 | [
"1n0w",
"1pzn",
"1szp",
"1t4g",
"1v5w",
"1xu4",
"2b21",
"2bke",
"2cvf",
"2cvh",
"2dfl",
"2f1h",
"2f1i",
"2f1j",
"2fpk",
"2fpl",
"2fpm",
"2gdj",
"2i1q",
"2z43",
"2zjb",
"2zub",
"2zuc",
"2zud",
"3etl",
"3ew9",
"3ewa",
"3fyh",
"3lda",
"3ntu",
"4a6p",
"4a6x"... | 157 | [
"PUB00020893",
"PUB00073165",
"PUB00081849",
"PUB00161266"
] | [
"15908697",
"11751635",
"16798872",
"11751636"
] | [
"Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding.",
"Identification and purification of two distinct complexes containing the five RAD51 paralogs.",
"Origins and evolution of the recA/RAD51 gene family: evidence for ancient gene duplication and endosymbioti... | [
2005,
2001,
2006,
2001
] | 4 | [] | [
"IPR047323",
"IPR047348"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
2100,
12,
3,
21497,
179
] | 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... | [
33,
3,
15,
40,
35,
21,
2,
25,
34,
3,
3,
62
] | 12 | true | Domain | Rad51-like, C-terminal | Rad51-like, C-terminal | Rad51_C | 4 |
IPR013633 | 13,633 | siRNA-mediated silencing protein NRDE-2 | NRDE-2 | Family | 4,417 | false | false | Eukaryotic cells express a wide variety of endogenous small regulatory RNAs that regulate heterochromatin formation, developmental timing, defence against parasitic nucleic acids, and genome rearrangement. Many small regulatory RNAs are thought to function in nuclei, and in plants and fungi small interfering RNAs (siRN... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08424",
"PTHR13471"
] | [
"NRDE-2",
""
] | [
3802,
4371
] | 2 | [] | [] | [] | 0 | [
"6ieh"
] | 1 | [
"PUB00057435"
] | [
"20543824"
] | [
"Small regulatory RNAs inhibit RNA polymerase II during the elongation phase of transcription."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4417
] | 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",
"Schizosaccharomyces pombe (stra... | [
13,
1,
2,
3,
5,
2,
1,
2,
3,
1,
14
] | 11 | true | Family | siRNA-mediated silencing protein NRDE-2 | siRNA-mediated silencing protein NRDE-2 | NRDE-2 | 7 |
IPR013636 | 13,636 | Armadillo-like helical domain-containing protein 3, C-terminal | ARMH3_C | Domain | 3,440 | false | false | This is the C-terminal domain of Armadillo-like helical domain-containing protein 3 (ARMH3), the previously uncharacterised peripheral Golgi protein C10orf76. ARMH3 interacts with and is involved in GBF1 recruitment, Golgi maintenance and protein secretion [ , ]. C10orf76 associates with the lipid kinase PI4KB that inc... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08427",
"SM01158"
] | [
"ARMH3_C",
"DUF1741"
] | [
3428,
3362
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00098076",
"PUB00098077"
] | [
"31519766",
"31829496"
] | [
"BioID Performed on Golgi Enriched Fractions Identify C10orf76 as a GBF1 Binding Protein Essential for Golgi Maintenance and Secretion.",
"Characterization of the c10orf76-PI4KB complex and its necessity for Golgi PI4P levels and enterovirus replication."
] | [
2019,
2020
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3440
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
2,
1,
1,
8,
1
] | 7 | true | Domain | Armadillo-like helical domain-containing protein 3, C-terminal | Armadillo-like helical domain-containing protein 3, C-terminal | ARMH3_C | 9 |
IPR013637 | 13,637 | Lysine-specific demethylase-like domain | Lys_sp_deMease-like_dom | Domain | 9,202 | false | false | This domain is found in the central region of lysine-specific demethylases, which are nuclear proteins that may have a role in DNA-binding and transcription, and are associated with malignant cancer phenotypes [ ]. The domain is also found in various other Jumonji/ARID domain-containing proteins (see , ). | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08429"
] | [
"PLU-1"
] | [
9202
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.11.67",
"R-CEL-3214842",
"R-DME-8866911",
"R-DRE-8866911",
"R-GGA-8866911",
"R-HSA-3214842",
"R-HSA-8866911",
"R-HSA-9821002",
"R-MMU-3214842",
"R-MMU-8866911",
"R-SPO-3214842"
] | [
"EC:1.14.11.67",
"REACTOME:R-CEL-3214842",
"REACTOME:R-DME-8866911",
"REACTOME:R-DRE-8866911",
"REACTOME:R-GGA-8866911",
"REACTOME:R-HSA-3214842",
"REACTOME:R-HSA-8866911",
"REACTOME:R-HSA-9821002",
"REACTOME:R-MMU-3214842",
"REACTOME:R-MMU-8866911",
"REACTOME:R-SPO-3214842"
] | 11 | [
"5ceh",
"5k4l",
"5v9p",
"5v9t"
] | 4 | [
"PUB00020834"
] | [
"10336460"
] | [
"A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Paenibacillus larvae subsp. larvae"
] | [
9201,
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",
"Schizosaccharomyces pombe (stra... | [
8,
2,
23,
2,
35,
7,
1,
2,
19,
2,
34
] | 11 | true | Domain | Lysine-specific demethylase-like domain | Lysine-specific demethylase-like domain | Lys_sp_deMease-like_dom | 8 |
IPR013638 | 13,638 | Fork-head N-terminal | Fork-head_N | Domain | 2,530 | false | false | The region described in this entry is found towards the N terminus of various eukaryotic fork head/HNF-3-related transcription factors (which contain the domain). These proteins play key roles in embryogenesis, maintenance of differentiated cell states, and tumorigenesis [ ]. | [
"GO:0008134",
"GO:0019904"
] | [
"transcription factor binding",
"protein domain specific binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08430"
] | [
"Forkhead_N"
] | [
2530
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-9018519",
"R-HSA-210745",
"R-HSA-9018519",
"R-HSA-9764790",
"R-HSA-9796292",
"R-HSA-9823730",
"R-HSA-9925561",
"R-HSA-9925563",
"R-HSA-9937080",
"R-MMU-9018519",
"R-RNO-9018519"
] | [
"REACTOME:R-DME-9018519",
"REACTOME:R-HSA-210745",
"REACTOME:R-HSA-9018519",
"REACTOME:R-HSA-9764790",
"REACTOME:R-HSA-9796292",
"REACTOME:R-HSA-9823730",
"REACTOME:R-HSA-9925561",
"REACTOME:R-HSA-9925563",
"REACTOME:R-HSA-9937080",
"REACTOME:R-MMU-9018519",
"REACTOME:R-RNO-9018519"
] | 11 | [
"5a5u",
"6fec",
"8vfy",
"8vfz",
"8vg1",
"8vg2"
] | 6 | [
"PUB00020873"
] | [
"8817449"
] | [
"Five years on the wings of fork head."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
5,
2525
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
6,
7,
6,
16
] | 5 | true | Domain | Fork-head N-terminal | Fork-head N-terminal | Fork-head_N | 8 |
IPR013640 | 13,640 | VPS4-associated protein 1 | Vfa1 | Family | 1,604 | false | false | Vps Four-Associated 1, Vfa1, in yeast, is an endosomal protein that interacts with the AAA-ATPase Vps4. It would seem to be involved in regulating the trafficking of other proteins to the endocytic vacuole [ ]. There is a CCCH zinc finger at the N terminus. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08432",
"PTHR28218"
] | [
"Vfa1",
""
] | [
1604,
1567
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00066734"
] | [
"21777356"
] | [
"An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1604
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Family | VPS4-associated protein 1 | VPS4-associated protein 1 | Vfa1 | 6 |
IPR013641 | 13,641 | Protein KTI12/L-seryl-tRNA(Sec) kinase | KTI12/PSTK | Family | 5,587 | false | false | Kti12 associates with Elongator complex, a six-subunit histone acetytransferase complex that functions with the elongating form of RNA polymerase II during transcription [ ]. It is not a structural subunit but may play a regulatory role in Elongator function [ ]. It has been shown that Kti12 is associated with chromati... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08433"
] | [
"KTI12"
] | [
5587
] | 1 | [
"REACTOME"
] | [
"R-HSA-2408557"
] | [
"REACTOME:R-HSA-2408557"
] | 1 | [
"3a4l",
"3a4m",
"3a4n",
"3adb",
"3adc",
"3add",
"3am1",
"6qp0"
] | 8 | [
"PUB00020941",
"PUB00043578",
"PUB00045475",
"PUB00098046"
] | [
"15772087",
"15769872",
"15317934",
"11929532"
] | [
"Physical and functional interaction between Elongator and the chromatin-associated Kti12 protein.",
"An early step in wobble uridine tRNA modification requires the Elongator complex.",
"Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase.",
"Molecular analysis of KTI12/TOT4, a Saccharomyc... | [
2005,
2005,
2004,
2002
] | 4 | [] | [
"IPR020024",
"IPR020028"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
46,
97,
5430,
4,
10
] | 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... | [
3,
2,
3,
2,
6,
4,
1,
2,
8,
1,
1,
7
] | 12 | true | Family | Protein KTI12/L-seryl-tRNA(Sec) kinase | Protein KTI12/L-seryl-tRNA(Sec) kinase | KTI12/PSTK | 2 |
IPR013642 | 13,642 | Calcium-activated chloride channel, N-terminal | CLCA_N | Domain | 3,507 | false | false | The CLCA family of calcium-activated chloride channels has been identified in many epithelial and endothelial cell types as well as in smooth muscle cells [ ] and has four or five putative transmembrane regions. Additionally to their role as chloride channels some CLCA proteins function as adhesion molecules and may al... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08434"
] | [
"CLCA"
] | [
3507
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-2672351",
"R-MMU-2672351"
] | [
"REACTOME:R-HSA-2672351",
"REACTOME:R-MMU-2672351"
] | 2 | [] | 0 | [
"PUB00020852",
"PUB00020930",
"PUB00085070",
"PUB00085071"
] | [
"15284223",
"11896056",
"22350745",
"23112050"
] | [
"Molecular and functional analyses of two new calcium-activated chloride channel family members from mouse eye and intestine.",
"Molecular and functional characterization of a murine calcium-activated chloride channel expressed in smooth muscle.",
"Impaired autoproteolytic cleavage of mCLCA6, a murine integral ... | [
2004,
2002,
2012,
2012
] | 4 | [] | [] | 0 | 0 | null | [
"Eumetazoa",
"Oscillospiraceae"
] | [
3505,
2
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
5,
14,
16
] | 4 | true | Domain | Calcium-activated chloride channel, N-terminal | Calcium-activated chloride channel, N-terminal | CLCA_N | 4 |
IPR013643 | 13,643 | Calicivirus coat protein C-terminal | Calicivirus_coat_C | Domain | 9,112 | false | false | This is the calicivirus coat protein ( ) C-terminal region. Bovine calicivirus is a positive-stranded ssRNA viruses that cause gastroenteritis [ ]. The calicivirus genome contains two open reading frames, ORF1 and ORF2 [ , ]. ORF1 encodes a non-structural polypeptide, which has RNA helicase, cysteine protease and RNA p... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08435"
] | [
"Calici_coat_C"
] | [
9112
] | 1 | [] | [] | [] | 0 | [
"1ihm",
"2obr",
"2obs",
"2obt",
"2zl5",
"2zl6",
"2zl7",
"3asp",
"3asq",
"3asr",
"3ass",
"3ast",
"3bqj",
"3by1",
"3by2",
"3d26",
"3lq6",
"3lqe",
"3onu",
"3ony",
"3pa1",
"3pa2",
"3pum",
"3pun",
"3pvd",
"3q38",
"3q39",
"3q3a",
"3q6q",
"3q6r",
"3r6j",
"3r6k"... | 228 | [
"PUB00001630",
"PUB00003519",
"PUB00003528",
"PUB00005577",
"PUB00044072"
] | [
"1551442",
"8642693",
"8892921",
"1840711",
"16733562"
] | [
"An insect picornavirus may have genome organization similar to that of caliciviruses.",
"Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.",
"Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translatio... | [
1992,
1996,
1996,
1991,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
9112
] | 1 | [] | [] | 0 | true | Domain | Calicivirus coat protein C-terminal | Calicivirus coat protein C-terminal | Calicivirus_coat_C | 7 |
IPR013645 | 13,645 | Glycosyl transferase, family 8, C-terminal | Glyco_transf_8N | Domain | 3,002 | false | false | This domain is found at the C terminus of bacterial glucosyltransferase and galactosyltransferase proteins. | [
"GO:0008918",
"GO:0009103"
] | [
"lipopolysaccharide 3-alpha-galactosyltransferase activity",
"lipopolysaccharide biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08437"
] | [
"Glyco_transf_8C"
] | [
3002
] | 1 | [
"EC"
] | [
"2.4.1.58"
] | [
"EC:2.4.1.58"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Rhodnius prolixus",
"metagenomes"
] | [
2995,
1,
6
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | Glycosyl transferase, family 8, C-terminal | Glycosyl transferase, family 8, C-terminal | Glyco_transf_8N | 5 |
IPR013646 | 13,646 | Obg-like GTPase YGR210-like, G4 motif-containing domain | YGR210-like_G4 | Domain | 2,921 | false | false | This domain is part of the G domain found at the C-terminal of in archaeal and eukaryotic GTPases. Members of this entry form a subfamily within the Obg family of GTPases, and includes YGR210 from yeasts and its homologues from archaea [ ]. This domain contains the NKxD motif, known as the G4 motif [ ]. The P-loop guan... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08438"
] | [
"YGR210-like_G4"
] | [
2921
] | 1 | [] | [] | [] | 0 | [
"1wxq"
] | 1 | [
"PUB00013952",
"PUB00016351",
"PUB00022779",
"PUB00027072",
"PUB00036769",
"PUB00074840"
] | [
"11916378",
"12837776",
"15019792",
"12429099",
"17430889",
"14644502"
] | [
"Classification and evolution of P-loop GTPases and related ATPases.",
"Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.",
"Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8.",
"Structural and biochemical analysis of the Obg GTP binding protein... | [
2002,
2003,
2004,
2002,
2007,
2003
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"ecological metagenomes"
] | [
1328,
1556,
37
] | 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)"
] | [
1,
1,
1
] | 3 | true | Domain | Obg-like GTPase YGR210-like, G4 motif-containing domain | Obg-like GTPase YGR210-like, G4 motif-containing domain | YGR210-like_G4 | 1 |
IPR013647 | 13,647 | Oligopeptidase F, N-terminal domain | OligopepF_N_dom | Domain | 13,979 | false | false | This domain is found towards the N terminus of oligoendopeptidase F proteins. An example protein is Lactococcus lactis PepF, [ ]. The function of this N-terminal domain is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08439"
] | [
"Peptidase_M3_N"
] | [
13979
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.24.-",
"PWY-8119"
] | [
"EC:3.4.24.-",
"METACYC:PWY-8119"
] | 2 | [
"2qr4",
"3ce2"
] | 2 | [
"PUB00017380"
] | [
"7798200"
] | [
"Biochemical and genetic characterization of PepF, an oligopeptidase from Lactococcus lactis."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
385,
13408,
74,
112
] | 4 | [] | [] | 0 | true | Domain | Oligopeptidase F, N-terminal domain | Oligopeptidase F, N-terminal domain | OligopepF_N_dom | 8 |
IPR013648 | 13,648 | Polyprotein, Potyviridae | PP_Potyviridae | Domain | 4,329 | false | false | This domain is found in polyproteins of the viral Potyviridae taxon. | [
"GO:0003968",
"GO:0005198",
"GO:0016818",
"GO:0018144"
] | [
"RNA-directed RNA polymerase activity",
"structural molecule activity",
"hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides",
"RNA-protein covalent cross-linking"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"PFAM"
] | [
"PF08440"
] | [
"Poty_PP"
] | [
4329
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.21.-",
"3.4.22.44",
"3.4.22.45",
"3.6.4.-",
"PWY-7250",
"PWY-7884"
] | [
"EC:2.7.7.48",
"EC:3.4.21.-",
"EC:3.4.22.44",
"EC:3.4.22.45",
"EC:3.6.4.-",
"METACYC:PWY-7250",
"METACYC:PWY-7884"
] | 7 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Orthornavirae"
] | [
4329
] | 1 | [] | [] | 0 | true | Domain | Polyprotein, Potyviridae | Polyprotein, Potyviridae | PP_Potyviridae | 3 |
IPR013649 | 13,649 | Integrin alpha, first immunoglubulin-like domain | Integrin_alpha_Ig-like_1 | Domain | 20,381 | false | false | This entry represents the first immunoglobulin-like domain of the three found in integrin alpha and integrin alpha precursors to the C terminus of a number of FG-GAP repeats ( ) and to the N terminus of the cytoplasmic region . | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08441"
] | [
"Integrin_A_Ig_1"
] | [
20381
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1566948",
"R-BTA-1566977",
"R-BTA-198933",
"R-BTA-202733",
"R-BTA-210991",
"R-BTA-216083",
"R-BTA-3000157",
"R-BTA-6798695",
"R-BTA-8874081",
"R-BTA-9634597",
"R-BTA-9860927",
"R-CEL-114608",
"R-CEL-1236973",
"R-CEL-1566977",
"R-CEL-198933",
"R-CEL-202733",
"R-CEL-210991",
"... | [
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-1566977",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-210991",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-3000157",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8874081",
"REACTOME:R-BTA-9634597",
"REACTOME:R-BTA-9860927",
"REACTOME:R-... | 127 | [
"1jv2",
"1l5g",
"1m1x",
"1u8c",
"3fcs",
"3ije",
"3k6s",
"3k71",
"3k72",
"3v4p",
"3v4v",
"3vi3",
"3vi4",
"4cak",
"4g1e",
"4g1m",
"4irz",
"4mmx",
"4mmy",
"4mmz",
"4neh",
"4nen",
"4o02",
"4um8",
"4um9",
"5e6r",
"5e6s",
"5e6u",
"5es4",
"5ffg",
"5ffo",
"5nem"... | 100 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Metazoa",
"bird metagenome"
] | [
20380,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
64,
7,
58,
75,
78
] | 6 | true | Domain | Integrin alpha, first immunoglubulin-like domain | Integrin alpha, first immunoglubulin-like domain | Integrin_alpha_Ig-like_1 | 8 |
IPR013651 | 13,651 | ATP-grasp fold, RimK-type | ATP-grasp_RimK-type | Domain | 24,866 | false | false | This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK [ ]. It has an unusual nucleotide-binding fold referred to as palmate, or ATP-grasp fold. This domain is found in a number of enzymes of known structure as well as in urea amidolyase, tubulin-tyrosine ligase, and three enzymes of purine biosynt... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08443"
] | [
"RimK"
] | [
24866
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"6.3.2",
"6.3.2.-",
"PWY-6289",
"PWY-6374",
"PWY-6378",
"PWY-6379",
"PWY-6409",
"PWY-6574",
"PWY-7510",
"PWY-7533",
"PWY-7542",
"PWY-7543",
"PWY-7549",
"PWY-7555",
"PWY-7556",
"PWY-7561",
"PWY-7563",
"PWY-7565",
"PWY-7569",
"PWY-7570",
"PWY-7571",
"PWY-7577",
"PWY-7600",
... | [
"EC:6.3.2",
"EC:6.3.2.-",
"METACYC:PWY-6289",
"METACYC:PWY-6374",
"METACYC:PWY-6378",
"METACYC:PWY-6379",
"METACYC:PWY-6409",
"METACYC:PWY-6574",
"METACYC:PWY-7510",
"METACYC:PWY-7533",
"METACYC:PWY-7542",
"METACYC:PWY-7543",
"METACYC:PWY-7549",
"METACYC:PWY-7555",
"METACYC:PWY-7556",
... | 49 | [
"1uc8",
"1uc9",
"3vpb",
"3vpc",
"3vpd",
"4iwx",
"4iwy",
"5i47",
"5k2m",
"5zct",
"5zk6",
"7drm",
"7drn",
"7dro",
"7drp",
"7lg5",
"7lgj",
"7lgn",
"7lgq",
"7qyr",
"7qys",
"7txu",
"7txv",
"7wac",
"7wad",
"7wae",
"7waf",
"8e1h",
"8e1i",
"8e1j",
"8e1s",
"8e1t"... | 34 | [
"PUB00020972"
] | [
"9416615"
] | [
"A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity."
] | [
1997
] | 1 | [
"IPR011761"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1943,
19348,
3264,
31,
280
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
2,
1,
3,
2,
2,
6,
1,
1
] | 8 | true | Domain | ATP-grasp fold, RimK-type | ATP-grasp fold, RimK-type | ATP-grasp_RimK-type | 8 |
IPR013652 | 13,652 | Glycine N-acyltransferase, C-terminal | Glycine_N-acyltransferase_C | Domain | 1,629 | false | false | This entry represents mammalian-specific glycine N-acyltransferase (also called aralkyl acyl-CoA:amino acid N-acyltransferase; ). Mitochondrial acyltransferases catalyse the transfer of an acyl group from acyl-CoA to the N terminus of glycine to produce N-acylglycine. These enzymes can conjugate a multitude of substrat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08444"
] | [
"Gly_acyl_tr_C"
] | [
1629
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.3.1.13",
"R-HSA-177128",
"R-HSA-177135",
"R-HSA-9749641",
"R-MMU-177128",
"R-MMU-177135",
"R-MMU-9749641",
"R-RNO-177128",
"R-RNO-177135",
"R-RNO-9749641"
] | [
"EC:2.3.1.13",
"REACTOME:R-HSA-177128",
"REACTOME:R-HSA-177135",
"REACTOME:R-HSA-9749641",
"REACTOME:R-MMU-177128",
"REACTOME:R-MMU-177135",
"REACTOME:R-MMU-9749641",
"REACTOME:R-RNO-177128",
"REACTOME:R-RNO-177135",
"REACTOME:R-RNO-9749641"
] | 10 | [
"7pk0",
"7pk1",
"7pk2"
] | 3 | [
"PUB00036032",
"PUB00036033"
] | [
"10630424",
"8660675"
] | [
"The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase.",
"Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase."
] | [
2000,
1996
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
1629
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
6,
9
] | 3 | true | Domain | Glycine N-acyltransferase, C-terminal | Glycine N-acyltransferase, C-terminal | Glycine_N-acyltransferase_C | 3 |
IPR013653 | 13,653 | GCN5-related N-acetyltransferase Rv2170-like domain | GCN5-like_dom | Domain | 10,154 | false | false | This entry represents a domain found towards the C-terminal end of GCN5-like protein acetyltransferase Rv2170 from Mycobacterium tuberculosis, which is involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation [ ]. Proteins in this entry... | [
"GO:0016747"
] | [
"acyltransferase activity, transferring groups other than amino-acyl groups"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08445"
] | [
"FR47"
] | [
10154
] | 1 | [] | [] | [] | 0 | [
"1sqh",
"3ec4"
] | 2 | [
"PUB00103909",
"PUB00155478"
] | [
"32633465",
"28250431"
] | [
"Dual lysine and N-terminal acetyltransferases reveal the complexity underpinning protein acetylation.",
"Novel protein acetyltransferase, Rv2170, modulates carbon and energy metabolism in Mycobacterium tuberculosis."
] | [
2020,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
30,
7296,
2764,
64
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
4,
14,
1
] | 3 | true | Domain | GCN5-related N-acetyltransferase Rv2170-like domain | GCN5-related N-acetyltransferase Rv2170-like domain | GCN5-like_dom | 5 |
IPR013654 | 13,654 | PAS fold-2 | PAS_2 | Domain | 11,792 | false | false | The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [1]. The PAS fold appears in archaea, eubacteria and eukarya. | [
"GO:0006355"
] | [
"regulation of DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08446"
] | [
"PAS_2"
] | [
11792
] | 1 | [] | [] | [] | 0 | [
"1ztu",
"2o9b",
"2o9c",
"2ool",
"2vea",
"3c2w",
"3g6o",
"3ibr",
"3nhq",
"3nop",
"3not",
"3nou",
"3s7n",
"3s7o",
"3s7p",
"3s7q",
"3zq5",
"4cqh",
"4e04",
"4gw9",
"4ijg",
"4o01",
"4o0p",
"4o8g",
"4our",
"4q0h",
"4q0i",
"4q0j",
"4r6l",
"4r70",
"4rq9",
"4s21"... | 170 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5926,
5856,
10
] | 3 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
77,
1,
36,
45
] | 4 | true | Domain | PAS fold-2 | PAS fold-2 | PAS_2 | 9 |
IPR013655 | 13,655 | PAS fold 3 | PAS_fold_3 | Domain | 146,887 | false | false | The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [ ]. The PAS fold appears in archaea, eubacteria and eukarya, and is involved in a variety of functions within sensory proteins promoting protein-protein interactions, signal transfer or as a stimuli sensor [ ]. The... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08447"
] | [
"PAS_3"
] | [
146887
] | 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-DME-1234158",
"R-DME-1234176",
"R-DME-8951664",
"R-HSA-1234158",
"R-HSA-1234174",
"R-HSA-1234176",
"R-HSA-1989781",
"R-HSA-211945",
"R-HSA-211976",
"R-HSA-211981",
"R-HSA-2122947",
"R-HSA-5689880",
"R-HSA-6785807",
"R-HSA-8849473",
"R-HSA-8857538",
"R-HSA-8937144",
"R-HSA-8951664"... | [
"REACTOME:R-DME-1234158",
"REACTOME:R-DME-1234176",
"REACTOME:R-DME-8951664",
"REACTOME:R-HSA-1234158",
"REACTOME:R-HSA-1234174",
"REACTOME:R-HSA-1234176",
"REACTOME:R-HSA-1989781",
"REACTOME:R-HSA-211945",
"REACTOME:R-HSA-211976",
"REACTOME:R-HSA-211981",
"REACTOME:R-HSA-2122947",
"REACTOME:R... | 48 | [
"2vlg",
"3eeh",
"3gdi",
"3h9w",
"3icy",
"3lyx",
"3mr0",
"3nja",
"4dj2",
"4dj3",
"4h6j",
"4zpr",
"5sy5",
"5sy7",
"6ph3",
"6ph4",
"6pps",
"7vna",
"7vnh",
"7vni",
"7xi3",
"7xi4",
"7y04",
"7zub",
"8dik",
"8h77",
"8qmo",
"8xs6",
"8xs7",
"8xs8",
"8xs9",
"8xsa"... | 34 | [
"PUB00005472",
"PUB00014500",
"PUB00014501",
"PUB00015791",
"PUB00033218",
"PUB00033219",
"PUB00033220",
"PUB00033221",
"PUB00094320"
] | [
"9301332",
"15009198",
"12377121",
"10357859",
"16681374",
"16417511",
"14979724",
"16537433",
"21663441"
] | [
"PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.",
"The PAS fold. A redefinition of the PAS domain based upon structural prediction.",
"Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.",
"PAS domains: internal sensors of oxyg... | [
1997,
2004,
2002,
1999,
2006,
2006,
2004,
2006,
2011
] | 9 | [
"IPR000014"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4553,
118750,
22297,
12,
1275
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces po... | [
1,
55,
19,
2,
44,
42,
6,
1,
46,
2
] | 10 | true | Domain | PAS fold 3 | PAS fold 3 | PAS_fold_3 | 3 |
IPR013656 | 13,656 | PAS fold 4 | PAS_4 | Domain | 148,470 | false | false | The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [ ]. The PAS fold appears in archaea, eubacteria and eukarya, and is involved in a variety of functions within sensory proteins promoting protein-protein interactions, signal transfer or as a stimuli sensor [ ]. The... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08448"
] | [
"PAS_4"
] | [
148470
] | 1 | [] | [] | [] | 0 | [
"2r78",
"3fc7",
"3fg8",
"3k3c",
"3k3d",
"3kx0",
"3luq",
"3mxq",
"5hwt",
"5hwv",
"5hww",
"6ide",
"6kju",
"6ugl",
"7dwm"
] | 15 | [
"PUB00005472",
"PUB00014500",
"PUB00014501",
"PUB00015791",
"PUB00033218",
"PUB00033219",
"PUB00033220",
"PUB00094320",
"PUB00099685"
] | [
"9301332",
"15009198",
"12377121",
"10357859",
"16681374",
"16417511",
"14979724",
"21663441",
"34424339"
] | [
"PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.",
"The PAS fold. A redefinition of the PAS domain based upon structural prediction.",
"Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.",
"PAS domains: internal sensors of oxyg... | [
1997,
2004,
2002,
1999,
2006,
2006,
2004,
2011,
2021
] | 9 | [
"IPR000014"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
8800,
136943,
4,
1374,
1349
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Domain | PAS fold 4 | PAS fold 4 | PAS_4 | 3 |
IPR013657 | 13,657 | HUT1 | HUT1 | Family | 17,491 | false | false | This family represents a group of nucleotide sugar transporters (NSTs) that belong to the SLC35 family of solute carriers, and their function is highly conserved from simple eukaryotes, fungi and parasites to plants and mammals, including the nucleotide sugar transporters SLC35B1-4 from humans and HUT1 and YEA4 from ye... | [
"GO:0055085"
] | [
"transmembrane transport"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF08449",
"PTHR10778"
] | [
"UAA",
""
] | [
17343,
15928
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-174362",
"R-CEL-727802",
"R-DDI-174362",
"R-DDI-727802",
"R-DME-174362",
"R-DME-727802",
"R-DRE-727802",
"R-HSA-174362",
"R-HSA-727802",
"R-MMU-174362",
"R-MMU-727802",
"R-SCE-727802",
"R-SPO-727802"
] | [
"REACTOME:R-CEL-174362",
"REACTOME:R-CEL-727802",
"REACTOME:R-DDI-174362",
"REACTOME:R-DDI-727802",
"REACTOME:R-DME-174362",
"REACTOME:R-DME-727802",
"REACTOME:R-DRE-727802",
"REACTOME:R-HSA-174362",
"REACTOME:R-HSA-727802",
"REACTOME:R-MMU-174362",
"REACTOME:R-MMU-727802",
"REACTOME:R-SCE-727... | 13 | [
"5oge",
"5ogk",
"6qsk",
"9gry",
"9grz",
"9gs3",
"9gs5",
"9gs7",
"9gsl",
"9i20"
] | 10 | [
"PUB00020858",
"PUB00070623",
"PUB00103678",
"PUB00103679",
"PUB00103680",
"PUB00103681",
"PUB00103682",
"PUB00103683",
"PUB00103684"
] | [
"11432728",
"12759756",
"10788474",
"31604945",
"16965264",
"29143814",
"35041824",
"30154480",
"11284010"
] | [
"The drug/metabolite transporter superfamily.",
"Molecular physiology and pathology of the nucleotide sugar transporter family (SLC35).",
"Characterization of Yeast Yea4p, a uridine diphosphate-N-acetylglucosamine transporter localized in the endoplasmic reticulum and required for chitin synthesis.",
"Structu... | [
2001,
2004,
2000,
2019,
2006,
2017,
2022,
2018,
2001
] | 9 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Micavibrio aeruginosavorus"
] | [
17489,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
25,
9,
6,
7,
18,
15,
2,
8,
17,
5,
2,
40
] | 12 | true | Family | HUT1 | HUT1 | HUT1 | 8 |
IPR013658 | 13,658 | SMP-30/Gluconolactonase/LRE-like region | SGL | Domain | 43,295 | false | false | This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30, also known as regucalcin ), gluconolactonase ( ) and luciferin-regenerating enzyme (LRE, ). SMP-30 is a gluconolact... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08450"
] | [
"SGL"
] | [
43295
] | 1 | [
"EC"
] | [
"3.1.1"
] | [
"EC:3.1.1"
] | 1 | [
"1e1a",
"1pjx",
"2dg0",
"2dg1",
"2dso",
"2ghs",
"2gvu",
"2gvv",
"2gvw",
"2gvx",
"2iao",
"2iap",
"2iaq",
"2iar",
"2ias",
"2iat",
"2iau",
"2iav",
"2iaw",
"2iax",
"3byc",
"3dr2",
"3e5z",
"3g4e",
"3g4h",
"3hlh",
"3hli",
"3i1c",
"3kgg",
"3li3",
"3li4",
"3li5"... | 67 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
241,
31249,
11219,
586
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
4,
1,
3,
28,
2,
1,
2,
3,
1
] | 9 | true | Domain | SMP-30/Gluconolactonase/LRE-like region | SMP-30/Gluconolactonase/LRE-like region | SGL | 2 |
IPR013659 | 13,659 | Adenosine/AMP deaminase N-terminal | A_deaminase_N | Domain | 2,132 | false | false | This domain is found toward the N terminus of the Adenosine/AMP deaminase domain ( ) in metazoan proteins such as the Cat eye syndrome critical region protein 1 and its homologues. | [
"GO:0005615"
] | [
"extracellular space"
] | [
"cellular_component"
] | 1 | [
"PFAM"
] | [
"PF08451"
] | [
"A_deaminase_N"
] | [
2132
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.5.4.4",
"PWY-6609",
"PWY-6611",
"PWY-7179",
"R-DDI-5683826",
"R-DDI-6798695",
"R-DRE-5683826",
"R-DRE-6798695",
"R-HSA-5683826",
"R-HSA-6798695"
] | [
"EC:3.5.4.4",
"METACYC:PWY-6609",
"METACYC:PWY-6611",
"METACYC:PWY-7179",
"REACTOME:R-DDI-5683826",
"REACTOME:R-DDI-6798695",
"REACTOME:R-DRE-5683826",
"REACTOME:R-DRE-6798695",
"REACTOME:R-HSA-5683826",
"REACTOME:R-HSA-6798695"
] | 10 | [
"3lgd",
"3lgg",
"9nte",
"9ntf",
"9ntg",
"9nth",
"9nti",
"9ntj",
"9ntk"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteroidota",
"Eukaryota"
] | [
9,
2123
] | 2 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens"
] | [
4,
11,
7
] | 3 | true | Domain | Adenosine/AMP deaminase N-terminal | Adenosine/AMP deaminase N-terminal | A_deaminase_N | 8 |
IPR013660 | 13,660 | DNA polymerase B exonuclease, N-terminal | DNApol_B_exo_N | Domain | 192 | false | false | This domain is found in viral DNA polymerases to the N terminus of DNA polymerase family B exonuclease domains ( ). | [
"GO:0003887"
] | [
"DNA-directed DNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08452"
] | [
"DNAP_B_exo_N"
] | [
192
] | 1 | [
"EC",
"EC"
] | [
"2.7.7.7",
"3.1.11.-"
] | [
"EC:2.7.7.7",
"EC:3.1.11.-"
] | 2 | [
"5n2e",
"5n2g",
"5n2h",
"8hdz",
"8hg1",
"8hlz",
"8hm0",
"8hoy",
"8hpa",
"8j86",
"8j8f",
"8j8g",
"8k8s",
"8k8u",
"8q3r",
"8wpe",
"8wpf",
"8wpk",
"8wpp",
"9k9r",
"9k9s",
"9k9t",
"9k9u",
"9k9v"
] | 24 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Poxviridae"
] | [
192
] | 1 | [] | [] | 0 | true | Domain | DNA polymerase B exonuclease, N-terminal | DNA polymerase B exonuclease, N-terminal | DNApol_B_exo_N | 6 |
IPR013661 | 13,661 | Peptidase M9, collagenase, N-terminal domain | Peptidase_M9_N_dom | Domain | 2,450 | false | false | Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08453"
] | [
"Peptidase_M9_N"
] | [
2450
] | 1 | [
"EC"
] | [
"3.4.24.3"
] | [
"EC:3.4.24.3"
] | 1 | [
"2y3u",
"2y50",
"2y6i",
"4are",
"7esi",
"7vlz",
"7wss",
"7xeb",
"8jt1",
"9l5o"
] | 10 | [
"PUB00003579"
] | [
"7674922"
] | [
"Evolutionary families of metallopeptidases."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Naiadarchaeum limnaeum",
"Eukaryota",
"ecological metagenomes"
] | [
2436,
1,
10,
3
] | 4 | [] | [] | 0 | true | Domain | Peptidase M9, collagenase, N-terminal domain | Peptidase M9, collagenase, N-terminal domain | Peptidase_M9_N_dom | 4 |
IPR013662 | 13,662 | RyR/IP3R Homology associated domain | RIH_assoc-dom | Domain | 13,521 | false | false | This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1, 4, 5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels [ ]. There seems to be no known function for this domain [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08454"
] | [
"RIH_assoc"
] | [
13521
] | 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-CEL-114508",
"R-CEL-139853",
"R-CEL-381676",
"R-CEL-5578775",
"R-CEL-9717207",
"R-CEL-983695",
"R-DDI-114508",
"R-DDI-139853",
"R-DDI-5578775",
"R-DDI-9717207",
"R-DME-114508",
"R-DME-139853",
"R-DME-381676",
"R-DME-5578775",
"R-DME-9717207",
"R-DME-983695",
"R-HSA-112043",
"R-H... | [
"REACTOME:R-CEL-114508",
"REACTOME:R-CEL-139853",
"REACTOME:R-CEL-381676",
"REACTOME:R-CEL-5578775",
"REACTOME:R-CEL-9717207",
"REACTOME:R-CEL-983695",
"REACTOME:R-DDI-114508",
"REACTOME:R-DDI-139853",
"REACTOME:R-DDI-5578775",
"REACTOME:R-DDI-9717207",
"REACTOME:R-DME-114508",
"REACTOME:R-DME... | 49 | [
"3j8h",
"3jav",
"5gky",
"5gkz",
"5gl0",
"5gl1",
"5go9",
"5goa",
"5gug",
"5j8v",
"5l1d",
"5t15",
"5t9m",
"5t9n",
"5t9r",
"5t9s",
"5t9v",
"5ta3",
"5tal",
"5tam",
"5tan",
"5tap",
"5taq",
"5tas",
"5tat",
"5tau",
"5tav",
"5taw",
"5tax",
"5tay",
"5taz",
"5tb0"... | 210 | [
"PUB00006473",
"PUB00020904"
] | [
"10664581",
"14516409"
] | [
"Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases.",
"What we don't know about the structure of ryanodine receptor calcium release channels."
] | [
2000,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"bird metagenome"
] | [
13520,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
108,
11,
30,
12,
35
] | 6 | true | Domain | RyR/IP3R Homology associated domain | RyR/IP3R Homology associated domain | RIH_assoc-dom | 8 |
IPR013663 | 13,663 | Helicase, SWF/SNF/SWI type, bacterial | Helicase_SWF/SNF/SWI_bac | Domain | 4,967 | false | false | This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N terminus of the SNF2 family N-terminal domain ( ) and together with the Helicase conserved C-terminal domain ( ). The function of the domain is not clear [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08455"
] | [
"SNF2_assoc"
] | [
4967
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020850"
] | [
"9025290"
] | [
"A Bacillus cereus member of the SNF2 family."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4941,
3,
23
] | 3 | [] | [] | 0 | true | Domain | Helicase, SWF/SNF/SWI type, bacterial | Helicase, SWF/SNF/SWI type, bacterial | Helicase_SWF/SNF/SWI_bac | 5 |
IPR013664 | 13,664 | Viral methyltransferase, C-terminal domain | Virgavirus_MeTrfase_C | Domain | 119 | false | false | This domain is found to the C terminus of the viral methyltransferase domain ( ) in single-stranded-RNA positive-strand viruses with no DNA stage in the Virgaviridae family. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08456"
] | [
"Vmethyltransf_C"
] | [
119
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
... | [
"2.1.1.-",
"2.7.7.-",
"2.7.7.48",
"3.6.4.13",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975"... | [
"EC:2.1.1.-",
"EC:2.7.7.-",
"EC:2.7.7.48",
"EC:3.6.4.13",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC... | 163 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"NPAAA clade",
"Virgaviridae"
] | [
2,
117
] | 2 | [] | [] | 0 | true | Domain | Viral methyltransferase, C-terminal domain | Viral methyltransferase, C-terminal domain | Virgavirus_MeTrfase_C | 7 |
IPR013665 | 13,665 | Sfi1 spindle body | Sfi1_dom | Domain | 1,823 | false | false | This is a domain of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins [ ] which are present in microtubule-organising centres. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08457"
] | [
"Sfi1"
] | [
1823
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020821"
] | [
"14504268"
] | [
"Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1823
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
1
] | 3 | true | Domain | Sfi1 spindle body | Sfi1 spindle body | Sfi1_dom | 8 |
IPR013666 | 13,666 | Pleckstrin-like, plant | PH_pln | Domain | 3,939 | false | false | This domain describes a pleckstrin homology (PH)-like region found in several plant proteins, including VAN3-binding protein from Arabidopsis thaliana (also known as FORKED1), a component of the auto-regulatory loop which enables auxin canalisation by recruitment of the PIN1 auxin efflux protein to the cell membrane [ ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08458"
] | [
"PH_2"
] | [
3939
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00090780"
] | [
"20626652"
] | [
"FORKED1 encodes a PH domain protein that is required for PIN1 localization in developing leaf veins."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3939
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
57,
29,
40
] | 3 | true | Domain | Pleckstrin-like, plant | Pleckstrin-like, plant | PH_pln | 3 |
IPR013668 | 13,668 | Ribonuclease R winged-helix domain | RNase_R_HTH_12 | Domain | 4,716 | false | false | This domain is found at the amino terminus of Ribonuclease R and a number of presumed transcriptional regulatory proteins from archaea. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08461"
] | [
"WHD_RNase_R"
] | [
4716
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Halorubrum tailed virus 25",
"Trichuris trichiura",
"unclassified sequences"
] | [
409,
4258,
1,
1,
47
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Ribonuclease R winged-helix domain | Ribonuclease R winged-helix domain | RNase_R_HTH_12 | 6 |
IPR013669 | 13,669 | Coat protein, C-terminal, Carmoviral | Coat_prot_C_Carmovir | Domain | 71 | false | false | This domain is found to the C terminus of the domain in Carmoviruses. The coat protein of the Turnip crinkle virus (TCV; Tombusviridae) is a suppressor of RNA silencing and is required for cell to cell movement in its host [ ]. The plant cellular trafficking machinery could hijack functional viral proteins to permit ce... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08462"
] | [
"Carmo_coat_C"
] | [
71
] | 1 | [] | [] | [] | 0 | [
"1opo"
] | 1 | [
"PUB00044095",
"PUB00044096",
"PUB00044097"
] | [
"18533829",
"18515824",
"17657600"
] | [
"A versatile assay for the identification of RNA silencing suppressors based on complementation of viral movement.",
"Influence of viral genes on the cell-to-cell spread of RNA silencing.",
"Complete nucleotide sequence of Nootka lupine vein-clearing virus."
] | [
2008,
2008,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Alphacarmovirus"
] | [
71
] | 1 | [] | [] | 0 | true | Domain | Coat protein, C-terminal, Carmoviral | Coat protein, C-terminal, Carmoviral | Coat_prot_C_Carmovir | 9 |
IPR013670 | 13,670 | EcoEI R protein C-terminal domain | EcoEI_R_C_dom | Domain | 7,616 | 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:0003824",
"GO:0006304"
] | [
"DNA binding",
"catalytic activity",
"DNA modification"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08463"
] | [
"EcoEI_R_C"
] | [
7616
] | 1 | [
"EC"
] | [
"3.1.21.3"
] | [
"EC:3.1.21.3"
] | 1 | [] | 0 | [
"PUB00019722",
"PUB00020851",
"PUB00035705",
"PUB00035707"
] | [
"10449767",
"8412658",
"15121719",
"12665693"
] | [
"Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes.",
"Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes.",
"S-Adenosyl-L-methionine-dependent restriction ... | [
1999,
1993,
2004,
2003
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctVJE9",
"unclassified sequences"
] | [
227,
7281,
10,
1,
97
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | EcoEI R protein C-terminal domain | EcoEI R protein C-terminal domain | EcoEI_R_C_dom | 4 |
IPR013671 | 13,671 | Geminivirus AC4/5, conserved domain | Gemini_AC4/5_cons-dom | Domain | 563 | false | false | This domain is found in replication initiator (Rep) associated proteins such as AC5 in the Geminivirus/Begomovirus. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08464"
] | [
"Gemini_AC4_5_2"
] | [
563
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Begomovirus"
] | [
563
] | 1 | [] | [] | 0 | true | Domain | Geminivirus AC4/5, conserved domain | Geminivirus AC4/5, conserved domain | Gemini_AC4/5_cons-dom | 5 |
IPR013672 | 13,672 | Herpesvirus thymidine kinase, C-terminal | Herpes_TK_C | Domain | 125 | false | false | This domain is found towards the C terminus in Herpesvirus Thymidine kinases. | [
"GO:0004797",
"GO:0005524"
] | [
"thymidine kinase activity",
"ATP binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08465"
] | [
"Herpes_TK_C"
] | [
125
] | 1 | [
"EC",
"METACYC"
] | [
"2.7.1.21",
"PWY-7199"
] | [
"EC:2.7.1.21",
"METACYC:PWY-7199"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Herpesvirales",
"Nocardia panacis"
] | [
124,
1
] | 2 | [] | [] | 0 | true | Domain | Herpesvirus thymidine kinase, C-terminal | Herpesvirus thymidine kinase, C-terminal | Herpes_TK_C | 9 |
IPR013673 | 13,673 | Potassium channel, inwardly rectifying, Kir, N-terminal | K_chnl_inward-rec_Kir_N | Domain | 2,030 | false | false | Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08466"
] | [
"IRK_N"
] | [
2030
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1296041",
"R-BTA-1296053",
"R-BTA-5576886",
"R-BTA-997272",
"R-CFA-1296041",
"R-CFA-1296053",
"R-CFA-5576886",
"R-CFA-997272",
"R-GGA-1296041",
"R-GGA-1296053",
"R-GGA-5576886",
"R-GGA-997272",
"R-HSA-1296041",
"R-HSA-1296053",
"R-HSA-5576886",
"R-HSA-9729555",
"R-HSA-997272",... | [
"REACTOME:R-BTA-1296041",
"REACTOME:R-BTA-1296053",
"REACTOME:R-BTA-5576886",
"REACTOME:R-BTA-997272",
"REACTOME:R-CFA-1296041",
"REACTOME:R-CFA-1296053",
"REACTOME:R-CFA-5576886",
"REACTOME:R-CFA-997272",
"REACTOME:R-GGA-1296041",
"REACTOME:R-GGA-1296053",
"REACTOME:R-GGA-5576886",
"REACTOME:... | 29 | [
"2xky",
"7zdz"
] | 2 | [
"PUB00001055",
"PUB00001069",
"PUB00001622",
"PUB00002771",
"PUB00004011",
"PUB00004020",
"PUB00006577",
"PUB00009378",
"PUB00009410",
"PUB00009411"
] | [
"1772658",
"7580148",
"1879548",
"1373731",
"2448635",
"2451788",
"2555158",
"11178249",
"10102275",
"10449331"
] | [
"The molecular biology of K+ channels.",
"The inward rectifier potassium channel family.",
"Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"Multiple potassium-channel components are produced ... | [
1991,
1995,
1991,
1992,
1988,
1988,
1989,
2000,
1999,
1999
] | 10 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
2030
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
6,
5,
6
] | 4 | true | Domain | Potassium channel, inwardly rectifying, Kir, N-terminal | Potassium channel, inwardly rectifying, Kir, N-terminal | K_chnl_inward-rec_Kir_N | 3 |
IPR013674 | 13,674 | Luteovirus RNA polymerase P1-P2/replicase | Luteo_Rpol_P1-P2 | Domain | 299 | false | false | This domain is found in RNA-dependent RNA polymerase P1-P2 fusion/replicase proteins in plant Luteoviruses. | [
"GO:0003968"
] | [
"RNA-directed RNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08467"
] | [
"Luteo_P1-P2"
] | [
299
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Tolivirales"
] | [
299
] | 1 | [] | [] | 0 | true | Domain | Luteovirus RNA polymerase P1-P2/replicase | Luteovirus RNA polymerase P1-P2/replicase | Luteo_Rpol_P1-P2 | 7 |
IPR013675 | 13,675 | Methyltransferase small, N-terminal | Mtase_sm_N | Domain | 4,517 | false | false | This domain is found to the N terminus of the methyltransferase small domain ( ) in bacterial proteins [ ]. | [
"GO:0008990",
"GO:0006364"
] | [
"rRNA (guanine-N2-)-methyltransferase activity",
"rRNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08468"
] | [
"MTS_N"
] | [
4517
] | 1 | [
"EC"
] | [
"2.1.1.172"
] | [
"EC:2.1.1.172"
] | 1 | [
"2pjd"
] | 1 | [
"PUB00020947"
] | [
"9873033"
] | [
"Purification, cloning, and characterization of the 16 S RNA m2G1207 methyltransferase from Escherichia coli."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ecdysozoa",
"ecological metagenomes"
] | [
4499,
4,
14
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Methyltransferase small, N-terminal | Methyltransferase small, N-terminal | Mtase_sm_N | 8 |
IPR013676 | 13,676 | Nucleoside triphosphatase I, C-terminal | NPHI_C | Domain | 153 | false | false | This entry represents the C-terminal domain of Nucleoside triphosphatase I (NPH1), specific to the family Poxviridae [ ]. It is usually found associated with the helicase conserved C-terminal domain ( ). NPH1 serves two roles in transcription. It is a DNA-dependent ATPase required for providing the needed energy to ach... | [
"GO:0005524",
"GO:0017111",
"GO:0006351"
] | [
"ATP binding",
"ribonucleoside triphosphate phosphatase activity",
"DNA-templated transcription"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08469"
] | [
"NPHI_C"
] | [
153
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 6 | [
"6rfl",
"7aoh",
"8c8h",
"8rqk",
"9fpy",
"9fq6"
] | 6 | [
"PUB00020994",
"PUB00099860",
"PUB00099861",
"PUB00099862"
] | [
"1850911",
"27189950",
"22069335",
"34556871"
] | [
"DNA sequence of the nucleoside triphosphate phosphohydrolase I (NPH I) of the Choristoneura biennis entomopoxvirus.",
"Nucleoside Triphosphate Phosphohydrolase I (NPH I) Functions as a 5' to 3' Translocase in Transcription Termination of Vaccinia Early Genes.",
"Role of forward translocation in nucleoside trip... | [
1991,
2016,
2011,
2021
] | 4 | [] | [] | 0 | 0 | null | [
"Nucleocytoviricota",
"metagenomes"
] | [
151,
2
] | 2 | [] | [] | 0 | true | Domain | Nucleoside triphosphatase I, C-terminal | Nucleoside triphosphatase I, C-terminal | NPHI_C | 4 |
IPR013677 | 13,677 | Non-toxic nonhaemagglutinin, C-terminal | NTNH_C | Domain | 115 | false | false | The domain described here is found at the C-terminal of the NTNH component. Bacteria of the Clostridium genus produce protein neurotoxins, which are complexes consisting of neurotoxin (NT), haemagglutinin (HA), non-toxic nonhaemagglutinin (NTNH), and RNA [ , ]. BoNT is always encoded together with associated non-toxic ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08470"
] | [
"NTNH_C"
] | [
115
] | 1 | [
"GP"
] | [
"GenProp0707"
] | [
"GP:GenProp0707"
] | 1 | [
"3v0a",
"3v0b",
"3vuo",
"4zkt",
"9arj",
"9ark",
"9arl",
"9ea9",
"9qc7",
"9qc8",
"9qcm",
"9qco"
] | 12 | [
"PUB00020995",
"PUB00020996",
"PUB00062647",
"PUB00105422"
] | [
"11233171",
"11595633",
"22363010",
"25592073"
] | [
"Characterization of nicking of the nontoxic-nonhemagglutinin components of Clostridium botulinum types C and D progenitor toxin.",
"Clostridium botulinum and its neurotoxins: a metabolic and cellular perspective.",
"Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.",
"Two-component systems... | [
2000,
2001,
2012,
2015
] | 4 | [] | [] | 0 | 0 | null | [
"Clostridia",
"unclassified Caudoviricetes"
] | [
111,
4
] | 2 | [] | [] | 0 | true | Domain | Non-toxic nonhaemagglutinin, C-terminal | Non-toxic nonhaemagglutinin, C-terminal | NTNH_C | 2 |
IPR013678 | 13,678 | Ribonucleotide reductase class II vitamin B12-dependent, N-terminal domain | RNR_2_N | Domain | 5,567 | false | false | This domain is found to the N terminus of the ribonucleotide reductase barrel domain ( ). It occurs in bacterial class II ribonucleotide reductase proteins which depend upon coenzyme B12 (deoxyadenosylcobalamine) [ ]. | [
"GO:0004748",
"GO:0050897"
] | [
"ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor",
"cobalt ion binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08471"
] | [
"Ribonuc_red_2_N"
] | [
5567
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.17.4.1",
"PWY-6545",
"PWY-7184",
"PWY-7198",
"PWY-7210",
"PWY-7220",
"PWY-7222",
"PWY-7226",
"PWY-7227"
] | [
"EC:1.17.4.1",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"METACYC:PWY-7220",
"METACYC:PWY-7222",
"METACYC:PWY-7226",
"METACYC:PWY-7227"
] | 9 | [
"7b9p",
"7b9q"
] | 2 | [
"PUB00020887"
] | [
"11832503"
] | [
"Streptomyces spp. contain class Ia and class II ribonucleotide reductases: expression analysis of the genes in vegetative growth."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
22,
5362,
6,
177
] | 4 | [] | [] | 0 | true | Domain | Ribonucleotide reductase class II vitamin B12-dependent, N-terminal domain | Ribonucleotide reductase class II vitamin B12-dependent, N-terminal domain | RNR_2_N | 3 |
IPR013679 | 13,679 | Sucrose-phosphatase, C-terminal | SPP_C | Domain | 1,532 | false | false | This is the sucrose-phosphatase (S6PP or SPP) C-terminal domain [ ] as found in plant sucrose phosphatases. These enzymes irreversibly catalyse the last step in sucrose synthesis following the formation of Sucrose-6-Phosphate via sucrose-phosphate synthase (SPS). | [
"GO:0050307",
"GO:0005986"
] | [
"sucrose-phosphate phosphatase activity",
"sucrose biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08472"
] | [
"S6PP_C"
] | [
1532
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.1.3.24",
"PWY-7238",
"PWY-7347"
] | [
"EC:3.1.3.24",
"METACYC:PWY-7238",
"METACYC:PWY-7347"
] | 3 | [] | 0 | [
"PUB00010220"
] | [
"11050182"
] | [
"Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"marine sediment metagenome"
] | [
40,
1479,
12,
1
] | 4 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
18,
6,
39
] | 3 | true | Domain | Sucrose-phosphatase, C-terminal | Sucrose-phosphatase, C-terminal | SPP_C | 4 |
IPR013680 | 13,680 | Voltage-dependent calcium channel, alpha-2/delta subunit, conserved region | VDCC_a2/dsu | Domain | 8,861 | false | false | Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by d... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08473"
] | [
"VGCC_alpha2"
] | [
8861
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-112308",
"R-HSA-400042",
"R-HSA-422356",
"R-HSA-5576892",
"R-HSA-5576893",
"R-HSA-9662360",
"R-HSA-9856532",
"R-MMU-112308",
"R-MMU-422356",
"R-MMU-5576892",
"R-MMU-5576893",
"R-RNO-112308",
"R-RNO-422356",
"R-RNO-5576892",
"R-RNO-5576893"
] | [
"REACTOME:R-HSA-112308",
"REACTOME:R-HSA-400042",
"REACTOME:R-HSA-422356",
"REACTOME:R-HSA-5576892",
"REACTOME:R-HSA-5576893",
"REACTOME:R-HSA-9662360",
"REACTOME:R-HSA-9856532",
"REACTOME:R-MMU-112308",
"REACTOME:R-MMU-422356",
"REACTOME:R-MMU-5576892",
"REACTOME:R-MMU-5576893",
"REACTOME:R-R... | 15 | [
"3jbr",
"5gjv",
"5gjw",
"6jp5",
"6jp8",
"6jpa",
"6jpb",
"7jpk",
"7jpl",
"7jpv",
"7jpw",
"7jpx",
"7mix",
"7miy",
"7uhf",
"7uhg",
"7vfs",
"7vfu",
"7vfv",
"7vfw",
"7xlq",
"7yg5",
"8e56",
"8e57",
"8e58",
"8e59",
"8e5a",
"8e5b",
"8eog",
"8epl",
"8epm",
"8fd7"... | 46 | [
"PUB00036034"
] | [
"14657414"
] | [
"International Union of Pharmacology. XL. Compendium of voltage-gated ion channels: calcium channels."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
8861
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
40,
7,
19,
15,
24
] | 5 | true | Domain | Voltage-dependent calcium channel, alpha-2/delta subunit, conserved region | Voltage-dependent calcium channel, alpha-2/delta subunit, conserved region | VDCC_a2/dsu | 7 |
IPR013681 | 13,681 | Myelin transcription factor 1 | Myelin_TF | Domain | 4,858 | false | false | This domain is found in the myelin transcription factor 1 (MYT1) of chordates. MYT1 contains C2HC zinc finger domains ( ) and is expressed in developing neurons of the central nervous system [ ] where it is involved in the selection of neuronal precursor cells [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08474"
] | [
"MYT1"
] | [
4858
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020867",
"PUB00020907"
] | [
"8980226",
"9373037"
] | [
"X-MyT1, a Xenopus C2HC-type zinc finger protein with a regulatory function in neuronal differentiation.",
"Myelin transcription factor 1 (Myt1) of the oligodendrocyte lineage, along with a closely related CCHC zinc finger, is expressed in developing neurons in the mammalian central nervous system."
] | [
1996,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bilateria"
] | [
4858
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
71,
32,
10,
19
] | 4 | true | Domain | Myelin transcription factor 1 | Myelin transcription factor 1 | Myelin_TF | 6 |
IPR013682 | 13,682 | Baculovirus Vp91, capsid protein, N-terminal | BaculoV_Vp91_N | Domain | 206 | false | false | This domain is a C2HC BV-type zinc finger found at the N terminus of the viral capsid protein 91 (VP91) from baculoviruses such as nucleopolyhedrovirus [ ]. Vp91 plays multiple roles in the baculovirus life cycle and is essential for nucleocapsid assembly and for efficient establishment of per os infection. It contains... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08475",
"PS51807"
] | [
"Baculo_VP91_N",
"ZF_C2HC_BV"
] | [
201,
206
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00010528",
"PUB00084235"
] | [
"11602755",
"23864639"
] | [
"Genome sequence of a baculovirus pathogenic for Culex nigripalpus.",
"The baculovirus core gene ac83 is required for nucleocapsid assembly and per os infectivity of Autographa californica nucleopolyhedrovirus."
] | [
2001,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Baculoviridae",
"Bilateria"
] | [
202,
4
] | 2 | [] | [] | 0 | true | Domain | Baculovirus Vp91, capsid protein, N-terminal | Baculovirus Vp91, capsid protein, N-terminal | BaculoV_Vp91_N | 1 |
IPR013683 | 13,683 | Vaccinia virus D10, N-terminal | Vaccinia_D10_N | Domain | 101 | false | false | This domain is found at the N-terminal end of Protein D10 from Vaccinia virus, also known as mRNA-decapping protein OPG122, and similar sequences from poxvirus. The VD10 protein is probably essential for virus replication [ ] and is often found to the N terminus of a NUDIX hydrolase domain. Previous studies indicated t... | [
"GO:0016791"
] | [
"phosphatase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08476"
] | [
"VD10_N"
] | [
101
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"3.1.3.-",
"PWY-4702",
"PWY-5491",
"PWY-6148",
"PWY-6352",
"PWY-6365",
"PWY-6366",
"PWY-6368",
"PWY-6456",
"PWY-6575",
"PWY-6627",
"PWY-6664",
"PWY-6686",
"PWY-6720",
"PWY-6724",
"PWY-6955",
"PWY-6990",
"PWY-6991",
"PWY-7018",
"PWY-7119",
"PWY-7321",
"PWY-7531",
"PWY-7771... | [
"EC:3.1.3.-",
"METACYC:PWY-4702",
"METACYC:PWY-5491",
"METACYC:PWY-6148",
"METACYC:PWY-6352",
"METACYC:PWY-6365",
"METACYC:PWY-6366",
"METACYC:PWY-6368",
"METACYC:PWY-6456",
"METACYC:PWY-6575",
"METACYC:PWY-6627",
"METACYC:PWY-6664",
"METACYC:PWY-6686",
"METACYC:PWY-6720",
"METACYC:PWY-6... | 36 | [] | 0 | [
"PUB00008085",
"PUB00020910",
"PUB00055937",
"PUB00103713",
"PUB00103714",
"PUB00103715"
] | [
"2177083",
"9847390",
"17283339",
"35202449",
"24155373",
"35435699"
] | [
"Analysis of the fowlpox virus genome region corresponding to the vaccinia virus D6 to A1 region: location of, and variation in, non-essential genes in poxviruses.",
"Down regulation of gene expression by the vaccinia virus D10 protein.",
"Vaccinia virus D10 protein has mRNA decapping activity, providing a mech... | [
1990,
1999,
2007,
2022,
2014,
2022
] | 6 | [] | [] | 0 | 0 | null | [
"Chordopoxvirinae"
] | [
101
] | 1 | [] | [] | 0 | true | Domain | Vaccinia virus D10, N-terminal | Vaccinia virus D10, N-terminal | Vaccinia_D10_N | 9 |
IPR013685 | 13,685 | POTRA domain, FtsQ-type | POTRA_FtsQ_type | Domain | 20,154 | false | false | FtsQ/DivIB bacterial division proteins ( ) contain an N-terminal POTRA domain (for polypeptide-transport-associated domain). This is found in different types of proteins, usually associated with a transmembrane β-barrel. FtsQ/DivIB may have chaperone-like roles, which has also been postulated for the POTRA domain in ot... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08478"
] | [
"POTRA_1"
] | [
20154
] | 1 | [] | [] | [] | 0 | [
"2vh1",
"2vh2",
"5z2w",
"6h9n",
"6h9o",
"8bh1",
"8hhf",
"8hhg",
"8hhh",
"8p1u"
] | 10 | [
"PUB00020825"
] | [
"14559180"
] | [
"POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins."
] | [
2003
] | 1 | [
"IPR034746"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
19735,
30,
389
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | POTRA domain, FtsQ-type | POTRA domain, FtsQ-type | POTRA_FtsQ_type | 6 |
IPR013686 | 13,686 | Polypeptide-transport-associated, ShlB-type | Polypept-transport_assoc_ShlB | Domain | 12,559 | false | false | The POTRA domain (for polypeptide-transport-associated domain) is found towards the N terminus of ShlB family proteins ( ). ShlB is important in the secretion and activation of the haemolysin ShlA. It has been postulated that the POTRA domain has a chaperone-like function over ShlA; it may fold back into the C-terminal... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08479"
] | [
"POTRA_2"
] | [
12559
] | 1 | [] | [] | [] | 0 | [
"2mhj",
"2x8x",
"3mc8",
"3mc9",
"3njt",
"4qky",
"4ql0",
"6wil",
"6wim",
"8xnb"
] | 10 | [
"PUB00020825"
] | [
"14559180"
] | [
"POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctvyM23",
"unclassified sequences"
] | [
12418,
46,
1,
94
] | 4 | [] | [] | 0 | true | Domain | Polypeptide-transport-associated, ShlB-type | Polypeptide-transport-associated, ShlB-type | Polypept-transport_assoc_ShlB | 6 |
IPR013688 | 13,688 | GBS Bsp-like | GBS_Bsp-like | Repeat | 1,217 | false | false | This repeat is found in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08481"
] | [
"GBS_Bsp-like"
] | [
1217
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00020919"
] | [
"12368458"
] | [
"Influence of proteins Bsp and FemH on cell shape and peptidoglycan composition in group B streptococcus."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes",
"unclassified Caudoviricetes"
] | [
1210,
4,
3
] | 3 | [] | [] | 0 | true | Repeat | GBS Bsp-like | GBS Bsp-like | GBS_Bsp-like | 2 |
IPR013689 | 13,689 | ATP-dependent RNA helicase HrpB, C-terminal | RNA_helicase_ATP-dep_HrpB_C | Domain | 11,895 | false | false | This domain is found near the C terminus of bacterial ATP-dependent helicases such as HrpB. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08482"
] | [
"HrpB_C"
] | [
11895
] | 1 | [] | [] | [] | 0 | [
"6eud",
"6heg"
] | 2 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11727,
87,
81
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | ATP-dependent RNA helicase HrpB, C-terminal | ATP-dependent RNA helicase HrpB, C-terminal | RNA_helicase_ATP-dep_HrpB_C | 4 |
IPR013692 | 13,692 | UDP-glucose 4-epimerase CapD, C-terminal domain | CapD_C | Domain | 3,062 | false | false | This domain is found to the C terminus of the domain in the polysaccharide biosynthesis enzyme CapD from some bacteria. CapD epimerises UDP-galactose to UDP-glucose [ ]. | [
"GO:0003978",
"GO:0009103"
] | [
"UDP-glucose 4-epimerase activity",
"lipopolysaccharide biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08485"
] | [
"Polysacc_syn_2C"
] | [
3062
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.1.3.2",
"PWY-3821",
"PWY-6317",
"PWY-6397",
"PWY-6527",
"PWY-7328",
"PWY-7344"
] | [
"EC:5.1.3.2",
"METACYC:PWY-3821",
"METACYC:PWY-6317",
"METACYC:PWY-6397",
"METACYC:PWY-6527",
"METACYC:PWY-7328",
"METACYC:PWY-7344"
] | 7 | [
"3vvb",
"3vvc",
"3w1v",
"4g5h",
"4j2o"
] | 5 | [
"PUB00070293"
] | [
"16386381"
] | [
"Characterization of RP 333, a gene encoding CapD of Rickettsia prowazekii with UDP-glucose 4-epimerase activity."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomicrobiales",
"Opisthokonta",
"Siphoviridae sp. ctPAi1",
"unclassified sequences"
] | [
2984,
3,
6,
1,
68
] | 5 | [] | [] | 0 | true | Domain | UDP-glucose 4-epimerase CapD, C-terminal domain | UDP-glucose 4-epimerase CapD, C-terminal domain | CapD_C | 3 |
IPR013693 | 13,693 | Sporulation stage II protein D, amidase enhancer LytB N-terminal | SpoIID/LytB_N | Domain | 10,131 | false | false | This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation [ ]. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08486"
] | [
"SpoIID"
] | [
10131
] | 1 | [] | [] | [] | 0 | [
"4rwr",
"5i1t",
"5txu"
] | 3 | [
"PUB00020841",
"PUB00020927"
] | [
"12502745",
"10961456"
] | [
"A cytoskeleton-like role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore.",
"Biological roles of two new murein hydrolases of Streptococcus pneumoniae representing examples of module shuffling."
] | [
2002,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
8,
9795,
8,
4,
316
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Sporulation stage II protein D, amidase enhancer LytB N-terminal | Sporulation stage II protein D, amidase enhancer LytB N-terminal | SpoIID/LytB_N | 8 |
IPR013694 | 13,694 | VIT domain | VIT | Domain | 19,768 | false | false | The inter-alpha-trypsin inhibitor (ITI) family is composed of protease inhibitors that are assembled from two precursor proteins: a light chain and different homologous heavy chains (ITIHs). Originally identified as plasma inhibitors, recent data indicate that ITI plays a role in extracellular matrix stabilisation and ... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART"
] | [
"PF08487",
"PF13757",
"PS51468",
"SM00609"
] | [
"VIT",
"VIT_2",
"VIT",
"VIT"
] | [
17904,
1601,
19404,
16335
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-114608",
"R-HSA-114608",
"R-HSA-196807",
"R-HSA-381426",
"R-HSA-8957275",
"R-HSA-9683610",
"R-HSA-9694631",
"R-MMU-114608",
"R-MMU-381426",
"R-MMU-8957275",
"R-RNO-114608",
"R-SSC-381426",
"R-SSC-8957275"
] | [
"REACTOME:R-BTA-114608",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-196807",
"REACTOME:R-HSA-381426",
"REACTOME:R-HSA-8957275",
"REACTOME:R-HSA-9683610",
"REACTOME:R-HSA-9694631",
"REACTOME:R-MMU-114608",
"REACTOME:R-MMU-381426",
"REACTOME:R-MMU-8957275",
"REACTOME:R-RNO-114608",
"REACTOME:R-SSC... | 13 | [
"6fpy",
"6fpz",
"9bw6",
"9bw7",
"9c4f",
"9c4n"
] | 6 | [
"PUB00020822"
] | [
"14744536"
] | [
"ITIH5, a novel member of the inter-alpha-trypsin inhibitor heavy chain family is downregulated in breast cancer."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"unclassified sequences"
] | [
16,
3565,
16081,
14,
92
] | 5 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Rattus norvegicus"
] | [
42,
35,
33,
2,
42
] | 5 | true | Domain | VIT domain | VIT domain | VIT | 1 |
IPR013695 | 13,695 | Wall-associated receptor kinase | WAK | Domain | 2,356 | false | false | This domain is found together with the eukaryotic protein kinase domain in plant wall-associated receptor kinases (WAKs) and related proteins. WAKs are serine-threonine kinases which might be involved in signalling to the cytoplasm and are required for cell expansion [ ]. | [
"GO:0004674",
"GO:0016020"
] | [
"protein serine/threonine kinase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF08488"
] | [
"WAK"
] | [
2356
] | 1 | [
"EC"
] | [
"2.7.11.-"
] | [
"EC:2.7.11.-"
] | 1 | [] | 0 | [
"PUB00020864"
] | [
"11544019"
] | [
"WAKs; cell wall associated kinases."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Magnoliopsida"
] | [
2356
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica"
] | [
62,
4
] | 2 | true | Domain | Wall-associated receptor kinase | Wall-associated receptor kinase | WAK | 6 |
IPR013696 | 13,696 | TiaS, FLD domain | TiaS_FLD | Domain | 938 | false | false | This is the FLD domain found in tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS [ ]. TiaS is an ATP-dependent agmatine transferase that catalyses the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2) [ , ]. This modified base specifically recognises AUA codons. TiaS consists of four dom... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08489"
] | [
"TiaS_FLD"
] | [
938
] | 1 | [
"EC"
] | [
"6.3.4.22"
] | [
"EC:6.3.4.22"
] | 1 | [
"3amt",
"3amu",
"3au7",
"3u02",
"4rvz",
"5xob",
"6agg"
] | 7 | [
"PUB00056803",
"PUB00106019",
"PUB00154283"
] | [
"20139989",
"30121296",
"22002223"
] | [
"Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea.",
"Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon.",
"Structural basis of tRNA agmatinylation essential for AUA codon decoding."
] | [
2010,
2018,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"unclassified sequences"
] | [
896,
2,
40
] | 3 | [] | [] | 0 | true | Domain | TiaS, FLD domain | TiaS, FLD domain | TiaS_FLD | 6 |
IPR013697 | 13,697 | DNA polymerase epsilon, catalytic subunit A, C-terminal | DNA_pol_e_suA_C | Domain | 4,805 | false | false | This domain is found on the catalytic subunit of DNA polymerase epsilon. It is found C-terminal to and . | [
"GO:0003887",
"GO:0008270",
"GO:0006260",
"GO:0005634"
] | [
"DNA-directed DNA polymerase activity",
"zinc ion binding",
"DNA replication",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"SMART"
] | [
"PF08490",
"SM01159"
] | [
"DUF1744",
"DUF1744"
] | [
4739,
4640
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.7.7",
"R-DDI-110314",
"R-DDI-5651801",
"R-DDI-5656169",
"R-DDI-5696397",
"R-DDI-6782135",
"R-DDI-6782210",
"R-DDI-68952",
"R-DDI-68962",
"R-DME-110314",
"R-DME-5651801",
"R-DME-5656169",
"R-DME-5696400",
"R-DME-6782135",
"R-DME-68952",
"R-DME-68962",
"R-HSA-110314",
"R-HSA-565... | [
"EC:2.7.7.7",
"REACTOME:R-DDI-110314",
"REACTOME:R-DDI-5651801",
"REACTOME:R-DDI-5656169",
"REACTOME:R-DDI-5696397",
"REACTOME:R-DDI-6782135",
"REACTOME:R-DDI-6782210",
"REACTOME:R-DDI-68952",
"REACTOME:R-DDI-68962",
"REACTOME:R-DME-110314",
"REACTOME:R-DME-5651801",
"REACTOME:R-DME-5656169",
... | 49 | [
"6hv8",
"6hv9",
"6wjv",
"7pfo",
"7plo",
"7pmk",
"7pmn",
"7qhs",
"7z13",
"8kg6",
"8kg8",
"8kg9",
"8p5e",
"8p62",
"8p63",
"8tw9",
"8twa",
"8xgc",
"9b8s",
"9b8t",
"9nea"
] | 21 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4805
] | 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... | [
13,
1,
1,
3,
8,
6,
1,
4,
3,
1,
1,
17
] | 12 | true | Domain | DNA polymerase epsilon, catalytic subunit A, C-terminal | DNA polymerase epsilon, catalytic subunit A, C-terminal | DNA_pol_e_suA_C | 2 |
IPR013698 | 13,698 | Squalene epoxidase | Squalene_epoxidase | Domain | 6,536 | false | false | This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae (Baker's yeast) where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol bi... | [
"GO:0004506",
"GO:0050660",
"GO:0016020"
] | [
"squalene monooxygenase activity",
"flavin adenine dinucleotide binding",
"membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF08491"
] | [
"SE"
] | [
6536
] | 1 | [
"EC",
"GP",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"1.14.14.17",
"GenProp1594",
"GenProp1683",
"PWY-5670",
"R-HSA-191273",
"R-HSA-2426168",
"R-MMU-191273",
"R-RNO-191273",
"R-SCE-191273",
"R-SPO-191273"
] | [
"EC:1.14.14.17",
"GP:GenProp1594",
"GP:GenProp1683",
"METACYC:PWY-5670",
"REACTOME:R-HSA-191273",
"REACTOME:R-HSA-2426168",
"REACTOME:R-MMU-191273",
"REACTOME:R-RNO-191273",
"REACTOME:R-SCE-191273",
"REACTOME:R-SPO-191273"
] | 10 | [
"6c6n",
"6c6p",
"6c6r"
] | 3 | [
"PUB00020824"
] | [
"9161422"
] | [
"Cloning and expression of squalene epoxidase from the pathogenic yeast Candida albicans."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
264,
6267,
5
] | 3 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (st... | [
38,
6,
6,
3,
1,
12,
4,
1,
1,
16
] | 10 | true | Domain | Squalene epoxidase | Squalene epoxidase | Squalene_epoxidase | 1 |
IPR013699 | 13,699 | Signal recognition particle, SRP72 subunit, RNA-binding | Signal_recog_part_SRP72_RNA-bd | Domain | 4,424 | false | false | The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ , , ]. SRP recognises the signal sequence of the nascent po... | [
"GO:0008312",
"GO:0006614",
"GO:0048500"
] | [
"7S RNA binding",
"SRP-dependent cotranslational protein targeting to membrane",
"signal recognition particle"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF08492"
] | [
"SRP72"
] | [
4424
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CEL-1799339",
"R-CFA-1799339",
"R-DDI-1799339",
"R-HSA-1799339",
"R-SCE-1799339",
"R-SPO-1799339"
] | [
"REACTOME:R-CEL-1799339",
"REACTOME:R-CFA-1799339",
"REACTOME:R-DDI-1799339",
"REACTOME:R-HSA-1799339",
"REACTOME:R-SCE-1799339",
"REACTOME:R-SPO-1799339"
] | 6 | [
"5m73",
"6frk",
"7nfx",
"7obq",
"7obr",
"8qvw",
"8qvx"
] | 7 | [
"PUB00020940",
"PUB00028143",
"PUB00035998",
"PUB00035999",
"PUB00053948",
"PUB00063486",
"PUB00100261"
] | [
"15588816",
"16469117",
"17622352",
"17507650",
"12364595",
"12605305",
"34020957"
] | [
"Identification of an RNA-binding domain in human SRP72.",
"Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.",
"X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.",
"The signal recognition part... | [
2005,
2006,
2007,
2007,
2002,
2003,
2021
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine sediment metagenome"
] | [
4423,
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... | [
10,
1,
1,
3,
3,
3,
1,
3,
8,
1,
1,
5
] | 12 | true | Domain | Signal recognition particle, SRP72 subunit, RNA-binding | Signal recognition particle, SRP72 subunit, RNA-binding | Signal_recog_part_SRP72_RNA-bd | 1 |
IPR013700 | 13,700 | Aflatoxin regulatory protein | AflR | Domain | 1,907 | false | false | This domain is found in the aflatoxin regulatory protein (AflR) and related fungal sequences. AflR is involved in the regulation of the biosynthesis of aflatoxin in the fungal genus Aspergillus [ ]. It occurs together with the fungal Zn(2)-Cys(6) binuclear cluster domain ( ). Aflatoxins belong to a family of decaketide... | [
"GO:0003677",
"GO:0006355",
"GO:0045122",
"GO:0005634"
] | [
"DNA binding",
"regulation of DNA-templated transcription",
"aflatoxin biosynthetic process",
"nucleus"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF08493"
] | [
"AflR"
] | [
1907
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000143",
"PUB00004117",
"PUB00004702",
"PUB00020861",
"PUB00053494"
] | [
"8074521",
"1557122",
"2107541",
"9758790",
"8662194"
] | [
"Molecular characterization of aflR, a regulatory locus for aflatoxin biosynthesis.",
"DNA recognition by GAL4: structure of a protein-DNA complex.",
"GAL4 transcription factor is not a \"zinc finger\" but forms a Zn(II)2Cys6 binuclear cluster.",
"Regulation of aflR and its product, AflR, associated with afla... | [
1994,
1992,
1990,
1998,
1996
] | 5 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1907
] | 1 | [] | [] | 0 | true | Domain | Aflatoxin regulatory protein | Aflatoxin regulatory protein | AflR | 1 |
IPR013701 | 13,701 | Lhr-like, DEAD/H associated domain | Lhr-like_DEAD/DEAH_assoc | Domain | 13,254 | false | false | This domain is found in Lhr DEAD-box RNA helicase and ATP-dependent helicases. This domain is associated with ( ) and ( ). It can be found C-terminal in some Lhr proteins. Lhr is a DNA helicase that translocates in a 3'-to-5' direction on single-stranded DNA and is likely involved in DNA repair. It is most active on th... | [
"GO:0005524",
"GO:0016818"
] | [
"ATP binding",
"hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08494"
] | [
"DEAD_assoc"
] | [
13254
] | 1 | [
"EC",
"EC"
] | [
"5.6.2.-",
"5.6.2.4"
] | [
"EC:5.6.2.-",
"EC:5.6.2.4"
] | 2 | [
"5v9x",
"7lhl"
] | 2 | [
"PUB00160772"
] | [
"32706021"
] | [
"Mechanistic insights into Lhr helicase function in DNA repair."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1494,
11635,
11,
114
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Lhr-like, DEAD/H associated domain | Lhr-like, DEAD/H associated domain | Lhr-like_DEAD/DEAH_assoc | 1 |
IPR013702 | 13,702 | FIST domain, N-terminal | FIST_domain_N | Domain | 9,010 | false | false | The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids [ ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08495",
"SM00897"
] | [
"FIST",
"FIST"
] | [
8986,
8238
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044261"
] | [
"17855421"
] | [
"FIST: a sensory domain for diverse signal transduction pathways in prokaryotes and ubiquitin signaling in eukaryotes."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
196,
7784,
856,
174
] | 4 | [] | [] | 0 | true | Domain | FIST domain, N-terminal | FIST domain, N-terminal | FIST_domain_N | 9 |
IPR013703 | 13,703 | Peptidase S49, N-terminal proteobacteria | Peptidase_S49_N_proteobac | Domain | 4,769 | false | false | Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif... | [
"GO:0004252",
"GO:0005886"
] | [
"serine-type endopeptidase activity",
"plasma membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF08496"
] | [
"Peptidase_S49_N"
] | [
4769
] | 1 | [
"EC",
"METACYC"
] | [
"3.4.21.-",
"PWY-7884"
] | [
"EC:3.4.21.-",
"METACYC:PWY-7884"
] | 2 | [] | 0 | [
"PUB00000522",
"PUB00003576",
"PUB00020845",
"PUB00020899"
] | [
"8439290",
"7845208",
"15611110",
"15205439"
] | [
"Evolutionary families of peptidases.",
"Families of serine peptidases.",
"A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii.",
"Displacements of prohead protease genes in the late operons of double-stranded-DNA ba... | [
1993,
1994,
2005,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halorubrum tibetense",
"unclassified sequences"
] | [
4567,
163,
1,
38
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Peptidase S49, N-terminal proteobacteria | Peptidase S49, N-terminal proteobacteria | Peptidase_S49_N_proteobac | 4 |
IPR013704 | 13,704 | UPF0313, N-terminal | UPF0313_N | Domain | 7,886 | false | false | This domain tends to occur to the N terminus of radical SAM domain in hypothetical bacterial proteins. Proteins in this entry are radical SAM proteins, they catalyse diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. Ev... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08497"
] | [
"Radical_SAM_N"
] | [
7886
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00010539",
"PUB00015124"
] | [
"11222759",
"15317939"
] | [
"Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.",
"Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybd... | [
2001,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
148,
7596,
7,
1,
134
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | UPF0313, N-terminal | UPF0313, N-terminal | UPF0313_N | 9 |
IPR013705 | 13,705 | Sterol methyltransferase C-terminal | Sterol_MeTrfase_C | Domain | 4,815 | false | false | This domain is found to the C terminus of a methyltransferase domain ( ) in fungal and plant sterol methyltransferases [ ]. | [
"GO:0008168",
"GO:0006694"
] | [
"methyltransferase activity",
"steroid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08498"
] | [
"Sterol_MT_C"
] | [
4815
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.1.1",
"GenProp1594",
"GenProp1609"
] | [
"EC:2.1.1",
"GP:GenProp1594",
"GP:GenProp1609"
] | 3 | [] | 0 | [
"PUB00020885"
] | [
"9746350"
] | [
"Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Streptomyces"
] | [
4813,
2
] | 2 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
9,
1,
15,
1,
1,
43
] | 6 | true | Domain | Sterol methyltransferase C-terminal | Sterol methyltransferase C-terminal | Sterol_MeTrfase_C | 5 |
IPR013706 | 13,706 | PDE1, N-terminal domain | PDE1_N | Domain | 5,924 | false | false | This domain is found at the N terminus of PDE1 predominantly from vertebrates. This domain adopts an all α-helical structure. It is found next to the catalytic domain ( ). The cyclic nucleotide phosphodiesterases (PDE) comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cA... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08499"
] | [
"PDEase_I_N"
] | [
5924
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.4.17",
"R-BTA-111957",
"R-BTA-418457",
"R-BTA-418555",
"R-CEL-111957",
"R-CEL-418457",
"R-CEL-418555",
"R-DME-111957",
"R-DME-418457",
"R-DME-418555",
"R-HSA-111957",
"R-HSA-418457",
"R-HSA-418555",
"R-MMU-111957",
"R-MMU-418457",
"R-MMU-418555",
"R-RNO-111957",
"R-RNO-418457"... | [
"EC:3.1.4.17",
"REACTOME:R-BTA-111957",
"REACTOME:R-BTA-418457",
"REACTOME:R-BTA-418555",
"REACTOME:R-CEL-111957",
"REACTOME:R-CEL-418457",
"REACTOME:R-CEL-418555",
"REACTOME:R-DME-111957",
"REACTOME:R-DME-418457",
"REACTOME:R-DME-418555",
"REACTOME:R-HSA-111957",
"REACTOME:R-HSA-418457",
"R... | 19 | [] | 0 | [
"PUB00043423",
"PUB00043424",
"PUB00043425",
"PUB00154469"
] | [
"18447606",
"18367027",
"18436153",
"34170501"
] | [
"Roflumilast: an oral, once-daily selective PDE-4 inhibitor for the management of COPD and asthma.",
"Phosphodiesterase 5 inhibition in essential hypertension.",
"Type 3 phosphodiesterase inhibitors may be protective against cerebrovascular events in patients with claudication.",
"Photoreceptor Phosphodiester... | [
2008,
2008,
2008,
2022
] | 4 | [] | [] | 0 | 0 | null | [
"Metazoa"
] | [
5924
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
34,
8,
14,
16,
31
] | 6 | true | Domain | PDE1, N-terminal domain | PDE1, N-terminal domain | PDE1_N | 2 |
IPR013707 | 13,707 | Tombusvirus p33 | Tombusvirus_p33 | Domain | 421 | false | false | Tombusviruses, which replicate in a wide range of plant hosts, replicate with the help of viral replicase protein including the overlapping p33 and p92 proteins which contain the domain described here [ ]. | [
"GO:0003968"
] | [
"RNA-directed RNA polymerase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08500"
] | [
"Tombus_P33"
] | [
421
] | 1 | [
"EC"
] | [
"2.7.7.48"
] | [
"EC:2.7.7.48"
] | 1 | [] | 0 | [
"PUB00020914"
] | [
"15936051"
] | [
"The role of the p33:p33/p92 interaction domain in RNA replication and intracellular localization of p33 and p92 proteins of Cucumber necrosis tombusvirus."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Viruses"
] | [
421
] | 1 | [] | [] | 0 | true | Domain | Tombusvirus p33 | Tombusvirus p33 | Tombusvirus_p33 | 4 |
IPR013708 | 13,708 | Shikimate dehydrogenase substrate binding, N-terminal | Shikimate_DH-bd_N | Domain | 44,707 | false | false | This domain is the substrate binding domain of shikimate dehydrogenase [ ]. Shikimate dehydrogenase catalyses the fourth step of the mycobacterial Shikimate pathway, which results in the biosynthesis of chorismate. Chorismate is a precursor of aromatic amino acids, naphthoquinones, menaquinones and mycobactins [ , ]. T... | [
"GO:0004764"
] | [
"shikimate 3-dehydrogenase (NADP+) activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08501"
] | [
"Shikimate_dh_N"
] | [
44707
] | 1 | [
"EC",
"EC",
"GP",
"METACYC"
] | [
"1.1.1",
"1.1.1.25",
"GenProp1478",
"PWY-6163"
] | [
"EC:1.1.1",
"EC:1.1.1.25",
"GP:GenProp1478",
"METACYC:PWY-6163"
] | 4 | [
"1npd",
"1npy",
"1nvt",
"1nyt",
"1o9b",
"1p74",
"1p77",
"1vi2",
"1wxd",
"2cy0",
"2d5c",
"2egg",
"2ev9",
"2gpt",
"2hk7",
"2hk8",
"2hk9",
"2nlo",
"2o7q",
"2o7s",
"3don",
"3doo",
"3fbt",
"3jyo",
"3jyp",
"3jyq",
"3o8q",
"3pgj",
"3phg",
"3phh",
"3phi",
"3phj"... | 61 | [
"PUB00020926",
"PUB00027835",
"PUB00043322"
] | [
"15735308",
"12637497",
"18260104"
] | [
"Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae.",
"Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.",
"Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis."
] | [
2005,
2003,
2008
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
841,
35541,
7682,
643
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
2,
4,
7,
1,
1,
26
] | 7 | true | Domain | Shikimate dehydrogenase substrate binding, N-terminal | Shikimate dehydrogenase substrate binding, N-terminal | Shikimate_DH-bd_N | 6 |
IPR013709 | 13,709 | 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain | 2-isopropylmalate_synth_dimer | Domain | 36,894 | false | false | This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway [ ]. This domain, is an internally duplicated structure with a novel fold [ ]. It comprises two similar units that are arranged such that the two helices pack toge... | [
"GO:0003852",
"GO:0009098"
] | [
"2-isopropylmalate synthase activity",
"L-leucine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF08502",
"SM00917"
] | [
"LeuA_dimer",
"LeuA_dimer"
] | [
36415,
36479
] | 2 | [
"EC",
"METACYC"
] | [
"2.3.3.13",
"PWY-6871"
] | [
"EC:2.3.3.13",
"METACYC:PWY-6871"
] | 2 | [
"1sr9",
"3f6g",
"3f6h",
"3fig",
"3hps",
"3hpz",
"3hq1"
] | 7 | [
"PUB00020847"
] | [
"15159544"
] | [
"Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1027,
31678,
3277,
912
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
10,
1,
1,
5,
2,
1,
18
] | 7 | true | Domain | 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain | 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain | 2-isopropylmalate_synth_dimer | 2 |
IPR013710 | 13,710 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase, N-terminal | DapH_N | Domain | 3,120 | false | false | This domain is found at the N terminus of t2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase (DapH) which catalyses the acylation of L-2-amino-6-oxopimelate to 2-N-acetyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants [ ]. The N-terminal do... | [
"GO:0047200"
] | [
"tetrahydrodipicolinate N-acetyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08503"
] | [
"DapH_N"
] | [
3120
] | 1 | [
"EC",
"METACYC"
] | [
"2.3.1.89",
"PWY-2941"
] | [
"EC:2.3.1.89",
"METACYC:PWY-2941"
] | 2 | [
"3bv8",
"3cj8",
"3r8y"
] | 3 | [
"PUB00013971",
"PUB00020828"
] | [
"11910040",
"9012664"
] | [
"Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase.",
"Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase."
] | [
2002,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanopyrus kandleri",
"ecological metagenomes"
] | [
3107,
2,
2,
9
] | 4 | [] | [] | 0 | true | Domain | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase, N-terminal | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase, N-terminal | DapH_N | 6 |
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