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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR013086 | 13,086 | Sodium:neurotransmitter symporter, serotonin, N-terminal | Na/ntran_symport_serotonin_N | Domain | 643 | false | false | The serotonin (5-HT) neurotransmitter transporter is known to be expressed in the brain and also in the periphery: on platelet, placental and pulmonary cell membranes. The brain 5-HT transporter is thought to be the principal site of action of therapeutic anti-depressants (which inhibit this transporter), and it may al... | [
"GO:0005335",
"GO:0006836",
"GO:0005886"
] | [
"serotonin:sodium:chloride symporter activity",
"neurotransmitter transport",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS"
] | [
"PF03491",
"PR01203"
] | [
"5HT_transport_N",
"5HTTRANSPORT"
] | [
641,
262
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-380615",
"R-HSA-380615",
"R-MMU-380615",
"R-RNO-380615"
] | [
"REACTOME:R-BTA-380615",
"REACTOME:R-HSA-380615",
"REACTOME:R-MMU-380615",
"REACTOME:R-RNO-380615"
] | 4 | [
"6vrh",
"6vrk",
"6vrl",
"9hco",
"9iy7"
] | 5 | [
"PUB00001020",
"PUB00006006",
"PUB00006007",
"PUB00006008",
"PUB00006042"
] | [
"15336049",
"8811182",
"8103691",
"7823024",
"7681602"
] | [
"Cloners quick on the uptake.",
"Molecular biology of mammalian amino acid transporters.",
"Neurotransmitter transporters: three distinct gene families.",
"Neurotransmitter transporters: three important gene families for neuronal function.",
"Antidepressant- and cocaine-sensitive human serotonin transporter... | [
1992,
1996,
1993,
1994,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
643
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
3,
2
] | 3 | true | Domain | Sodium:neurotransmitter symporter, serotonin, N-terminal | Sodium:neurotransmitter symporter, serotonin, N-terminal | Na/ntran_symport_serotonin_N | 6 |
IPR013087 | 13,087 | Zinc finger C2H2-type | Znf_C2H2_type | Domain | 1,056,533 | false | false | This entry represents the classical C2H2 zinc finger domain. C2H2-type (classical) zinc fingers (Znf) were the first class to be characterised. They contain a short β-hairpin and an α-helix (β/β/α structure), where a single zinc atom is held in place by Cys(2)His(2) (C2H2) residues in a tetrahedral array. C2H2 Znf's ca... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PFAM",
"PFAM",
"PROSITE",
"PROFILE",
"SMART"
] | [
"PF00096",
"PF12874",
"PF13912",
"PF25420",
"PS00028",
"PS50157",
"SM00355"
] | [
"zf-C2H2",
"zf-met",
"zf-C2H2_6",
"zf-C2H2_ZN292",
"ZINC_FINGER_C2H2_1",
"ZINC_FINGER_C2H2_2",
"ZnF_C2H2"
] | [
632441,
73442,
102414,
2494,
978028,
905560,
865486
] | 7 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-113418",
"R-BTA-212300",
"R-BTA-212436",
"R-BTA-3214841",
"R-BTA-5689896",
"R-BTA-5696395",
"R-BTA-5696400",
"R-BTA-674695",
"R-BTA-6781823",
"R-BTA-6782135",
"R-BTA-6782210",
"R-BTA-6796648",
"R-BTA-6807505",
"R-BTA-72086",
"R-BTA-72163",
"R-BTA-73762",
"R-BTA-73772",
"R-BT... | [
"REACTOME:R-BTA-113418",
"REACTOME:R-BTA-212300",
"REACTOME:R-BTA-212436",
"REACTOME:R-BTA-3214841",
"REACTOME:R-BTA-5689896",
"REACTOME:R-BTA-5696395",
"REACTOME:R-BTA-5696400",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6781823",
"REACTOME:R-BTA-6782135",
"REACTOME:R-BTA-6782210",
"REACTOME:R-... | 427 | [
"1a1f",
"1a1g",
"1a1h",
"1a1i",
"1a1j",
"1a1k",
"1a1l",
"1aay",
"1ard",
"1are",
"1arf",
"1bbo",
"1bhi",
"1e39",
"1ej6",
"1f2i",
"1fv5",
"1g2d",
"1g2f",
"1jk1",
"1jk2",
"1jn7",
"1jrx",
"1jry",
"1jrz",
"1klr",
"1kls",
"1kss",
"1ksu",
"1lj1",
"1llm",
"1m64"... | 735 | [
"PUB00014077",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035808",
"PUB00035809",
"PUB00035811",
"PUB00035812",
"PUB00043274",
"PUB00155326",
"PUB00155327",
"PUB00160210"
] | [
"12665246",
"17210253",
"15963892",
"15718139",
"10529348",
"11361095",
"10664601",
"10940247",
"11179890",
"18253864",
"15933716",
"17525732",
"31723249"
] | [
"Zinc fingers--folds for many occasions.",
"Sticky fingers: zinc-fingers as protein-recognition motifs.",
"Multiple modes of RNA recognition by zinc finger proteins.",
"Zinc finger proteins: getting a grip on RNA.",
"Zinc finger peptides for the regulation of gene expression.",
"Three classes of C2H2 zinc... | [
2002,
2007,
2005,
2005,
1999,
2001,
2000,
2000,
2001,
2008,
2005,
2007,
2020
] | 13 | [] | [
"IPR003604",
"IPR022755",
"IPR031514",
"IPR034729",
"IPR034731",
"IPR041057",
"IPR048403",
"IPR048414",
"IPR048420",
"IPR049009",
"IPR054177",
"IPR055186",
"IPR055187",
"IPR056380",
"IPR056436",
"IPR056438",
"IPR056545",
"IPR057829",
"IPR059009",
"IPR059042",
"IPR059058",
"... | 0 | 26 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2234,
3995,
1048001,
1035,
1268
] | 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... | [
734,
288,
4028,
837,
2499,
2057,
97,
487,
2164,
51,
30,
916
] | 12 | true | Domain | Zinc finger C2H2-type | Zinc finger C2H2-type | Znf_C2H2_type | 8 |
IPR013088 | 13,088 | Zinc finger, NHR/GATA-type | Znf_NHR/GATA | Homologous_superfamily | 149,069 | false | false | This entry represents a zinc finger motif found in nuclear hormone receptors and in erythroid transcription factor GATA-1. Nuclear hormone receptors usually have two copies of this motif, while GATA-1 has one copy. The zinc fingers in nuclear receptors are generally regarded as DNA-binding domains [ ], while those in G... | [
"GO:0008270",
"GO:0006355"
] | [
"zinc ion binding",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"CATHGENE3D"
] | [
"G3DSA:3.30.50.10"
] | [
""
] | [
149069
] | 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-1251985",
"R-BTA-1257604",
"R-BTA-381340",
"R-BTA-383280",
"R-BTA-4090294",
"R-BTA-5362517",
"R-BTA-5689896",
"R-BTA-6811558",
"R-BTA-8866427",
"R-BTA-8866910",
"R-BTA-8931987",
"R-BTA-8939211",
"R-BTA-9009391",
"R-BTA-9018519",
"R-BTA-9029569",
"R-BTA-9623433",
"R-BTA-983231"... | [
"REACTOME:R-BTA-1251985",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-381340",
"REACTOME:R-BTA-383280",
"REACTOME:R-BTA-4090294",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-5689896",
"REACTOME:R-BTA-6811558",
"REACTOME:R-BTA-8866427",
"REACTOME:R-BTA-8866910",
"REACTOME:R-BTA-8931987",
"REACTOME:... | 283 | [
"1a6y",
"1by4",
"1cit",
"1dsz",
"1ga5",
"1gat",
"1gau",
"1gdc",
"1glu",
"1gnf",
"1hcp",
"1hcq",
"1hlz",
"1hra",
"1kb2",
"1kb4",
"1kb6",
"1lat",
"1lo1",
"1lv3",
"1r0n",
"1r0o",
"1r4i",
"1r4o",
"1r4r",
"1rgd",
"1rxr",
"1y0j",
"1ynw",
"2a66",
"2c7a",
"2ebl"... | 146 | [
"PUB00014077",
"PUB00021440",
"PUB00021697",
"PUB00032561",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"12665246",
"10698945",
"10212985",
"15644435",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"Zinc fingers--folds for many occasions.",
"Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1.",
"The solution structure of the N-terminal zinc finger of GATA-1 reveals a specific binding face for the transcriptional co-factor FOG.",
"Zinc fingers as protein recognition mo... | [
2002,
2000,
1999,
2005,
2007,
2005,
2005,
1999,
2001
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
8001,
140996,
6,
66
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
117,
402,
382,
87,
1,
431,
226,
8,
85,
288,
10,
5,
161
] | 13 | true | Homologous_superfamily | Zinc finger, NHR/GATA-type | Zinc finger, NHR/GATA-type | Znf_NHR/GATA | 8 |
IPR013094 | 13,094 | Alpha/beta hydrolase fold-3 | AB_hydrolase_3 | Domain | 116,854 | false | false | This entry represents the catalytic domain fold-3 of α/β hydrolase. The α/β hydrolase fold [ ] is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an α/β-sheet (rather than a barrel), containing 8 strands connected by helices [ ]. The en... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF07859"
] | [
"Abhydrolase_3"
] | [
116854
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.1",
"GenProp1503",
"R-BTA-8964038",
"R-HSA-163560",
"R-HSA-211945",
"R-HSA-71240",
"R-HSA-8964038",
"R-HSA-9841922",
"R-MMU-211945",
"R-MMU-8964038",
"R-RNO-211945",
"R-RNO-8964038",
"R-SPO-211945",
"R-SPO-8964038"
] | [
"EC:3.1.1",
"GP:GenProp1503",
"REACTOME:R-BTA-8964038",
"REACTOME:R-HSA-163560",
"REACTOME:R-HSA-211945",
"REACTOME:R-HSA-71240",
"REACTOME:R-HSA-8964038",
"REACTOME:R-HSA-9841922",
"REACTOME:R-MMU-211945",
"REACTOME:R-MMU-8964038",
"REACTOME:R-RNO-211945",
"REACTOME:R-RNO-8964038",
"REACTOM... | 14 | [
"1evq",
"1jji",
"1jkm",
"1lzk",
"1lzl",
"1qz3",
"1u4n",
"1vkh",
"2c7b",
"2hm7",
"2o7r",
"2o7v",
"2pbl",
"2qru",
"2yh2",
"2zsh",
"2zsi",
"3aik",
"3ail",
"3aim",
"3ain",
"3aio",
"3d7r",
"3dnm",
"3ebl",
"3ed1",
"3fak",
"3g9t",
"3g9u",
"3g9z",
"3ga7",
"3h17"... | 170 | [
"PUB00004958",
"PUB00038968",
"PUB00043472"
] | [
"1409539",
"16321951",
"14681380"
] | [
"The alpha/beta hydrolase fold.",
"Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis.",
"ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins."
] | [
1992,
2005,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"Viruses",
"unclassified sequences"
] | [
613,
51200,
64338,
1,
44,
658
] | 6 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
73,
9,
34,
4,
1,
13,
21,
12,
179,
33,
1,
4,
180
] | 13 | true | Domain | Alpha/beta hydrolase fold-3 | Alpha/beta hydrolase fold-3 | AB_hydrolase_3 | 1 |
IPR013095 | 13,095 | Type III secretion system chaperone | T3SS_chaperone | Family | 448 | false | false | Type III secretion chaperones are involved in delivering virulence effector proteins from bacterial pathogens directly into eukaryotic cells. The chaperones may prevent aggregation and degradation of their substrates, may target the effector to the secretion apparatus, and may ensure a secretion-component unfolded conf... | [] | [] | [] | 0 | [
"NCBIFAM",
"PFAM",
"PIRSF",
"CDD"
] | [
"NF011749",
"PF07824",
"PIRSF034754",
"cd17022"
] | [
"PRK15202.1",
"Chaperone_III",
"T3SS_chaperone",
"T3SC_IA_SigE-like"
] | [
411,
444,
335,
438
] | 4 | [] | [] | [] | 0 | [
"1k3s"
] | 1 | [
"PUB00016448"
] | [
"11685226"
] | [
"Structural and biochemical characterization of the type III secretion chaperones CesT and SigE."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
448
] | 1 | [] | [] | 0 | true | Family | Type III secretion system chaperone | Type III secretion system chaperone | T3SS_chaperone | 8 |
IPR013096 | 13,096 | Cupin 2, conserved barrel | Cupin_2 | Domain | 167,684 | false | false | This entry represents the conserved barrel domain of the cupin superfamily [ ] (cupa is the Latin term for a small barrel). The cupin domain found in gentisate 1,2-dioxygenase, H2HPP isomerase, (S)-ureidoglycine aminohydrolase and related proteins. This domain is a conserved β-barrel scaffold that supports diverse cata... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07883"
] | [
"Cupin_2"
] | [
167684
] | 1 | [
"GP"
] | [
"GenProp1393"
] | [
"GP:GenProp1393"
] | 1 | [
"1o4t",
"1rc6",
"1sef",
"1sq4",
"1uij",
"1v70",
"1vj2",
"1y3t",
"1y9q",
"1yhf",
"1zz6",
"1zz7",
"1zz8",
"1zz9",
"1zzb",
"1zzc",
"2bnm",
"2bnn",
"2bno",
"2d40",
"2dct",
"2f4p",
"2fqp",
"2gu9",
"2h0v",
"2i45",
"2o8q",
"2oa2",
"2opk",
"2pfw",
"2phd",
"2q30"... | 132 | [
"PUB00005817",
"PUB00102112"
] | [
"9573603",
"11133965"
] | [
"Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins.",
"nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism."
] | [
1998,
2001
] | 2 | [] | [
"IPR044697",
"IPR047263"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"plasmids",
"unclassified sequences"
] | [
5408,
149461,
10971,
74,
2,
1768
] | 6 | [
"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",
"Zea mays"
] | [
6,
16,
4,
4,
7
] | 5 | true | Domain | Cupin 2, conserved barrel | Cupin 2, conserved barrel | Cupin_2 | 4 |
IPR013097 | 13,097 | Stress responsive alpha+beta-barrel | Dabb | Domain | 20,253 | false | false | The stress-response A/B barrel domain is found in a class of stress-response proteins in plants. It is also found in some bacterial fructose-bisphosphate aldolase such as at the C terminus of a fructose 1,6-bisphosphate aldolase from Hydrogenophilus thermoluteolus ( ) [ ]. is found in the pA01 plasmid, which encodes ge... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF07876",
"PS51502",
"SM00886"
] | [
"Dabb",
"S_R_A_B_BARREL",
"Dabb"
] | [
19867,
20196,
19289
] | 3 | [] | [] | [] | 0 | [
"1q4r",
"1q53",
"1rjj",
"1si9",
"1tr0",
"2q3p",
"2qyc",
"3bb5",
"3bde",
"3bgu",
"3bn7",
"3fmb",
"5b08",
"5b09",
"5b0a",
"5b0b",
"5b0c",
"5b0d",
"5b0e",
"5b0f",
"5b0g",
"5xzq",
"5xzt",
"5y02",
"7w6d",
"7w6e",
"7w6f",
"8oz4",
"8ozo",
"8ozs",
"8s4e"
] | 31 | [
"PUB00016419",
"PUB00016433",
"PUB00016501",
"PUB00022615",
"PUB00031070",
"PUB00031274"
] | [
"14704136",
"14872131",
"10705449",
"15213437",
"15371455",
"15364906"
] | [
"Transcript identification and profiling during salt stress and recovery of Populus euphratica.",
"Structure of the hypothetical protein At3g17210 from Arabidopsis thaliana.",
"Structure of ribulose 1,5-bisphosphate carboxylase/oxygenase gene cluster from a thermophilic hydrogen-oxidizing bacterium, Hydrogenoph... | [
2004,
2004,
2000,
2004,
2004,
2004
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
64,
11763,
8263,
163
] | 4 | [
"Arabidopsis thaliana",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
25,
3,
21,
27
] | 4 | true | Domain | Stress responsive alpha+beta-barrel | Stress responsive alpha+beta-barrel | Dabb | 7 |
IPR013098 | 13,098 | Immunoglobulin I-set | Ig_I-set | Domain | 275,591 | false | false | This entry represents I-set domains, which are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein fa... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07679"
] | [
"I-set"
] | [
275591
] | 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-114608",
"R-BTA-163125",
"R-BTA-388844",
"R-BTA-445355",
"R-BTA-5627123",
"R-BTA-77387",
"R-BTA-8849932",
"R-CEL-1257604",
"R-CEL-1307965",
"R-CEL-1474228",
"R-CEL-177929",
"R-CEL-190322",
"R-CEL-190370",
"R-CEL-190371",
"R-CEL-190372",
"R-CEL-190373",
"R-CEL-190374",
"R-CEL... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-163125",
"REACTOME:R-BTA-388844",
"REACTOME:R-BTA-445355",
"REACTOME:R-BTA-5627123",
"REACTOME:R-BTA-77387",
"REACTOME:R-BTA-8849932",
"REACTOME:R-CEL-1257604",
"REACTOME:R-CEL-1307965",
"REACTOME:R-CEL-1474228",
"REACTOME:R-CEL-177929",
"REACTOME:R-CEL... | 606 | [
"1bih",
"1cs6",
"1cvs",
"1djs",
"1e0o",
"1epf",
"1ev2",
"1evt",
"1fhg",
"1fq9",
"1g1c",
"1gxe",
"1hcf",
"1he7",
"1ie5",
"1ii4",
"1iil",
"1ij9",
"1koa",
"1nct",
"1ncu",
"1nun",
"1pd6",
"1qz1",
"1rhf",
"1ry7",
"1tit",
"1tiu",
"1tlk",
"1tnm",
"1tnn",
"1u2h"... | 327 | [
"PUB00010610",
"PUB00014840",
"PUB00015110",
"PUB00024043",
"PUB00027656",
"PUB00027657",
"PUB00086969",
"PUB00094313"
] | [
"11377196",
"9417933",
"15327963",
"10830169",
"10698639",
"16369100",
"22829780",
"11809975"
] | [
"Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state.",
"Sequence profiles of immunoglobulin and immunoglobulin-like domains.",
"Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and ot... | [
2001,
1997,
2004,
2000,
2000,
2006,
2012,
2002
] | 8 | [
"IPR007110"
] | [
"IPR034828",
"IPR047018",
"IPR047100",
"IPR057911"
] | 1 | 4 | 0 | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"Viruses",
"metagenomes"
] | [
784,
274718,
5,
45,
39
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
112,
1626,
370,
574,
476,
697
] | 6 | true | Domain | Immunoglobulin I-set | Immunoglobulin I-set | Ig_I-set | 2 |
IPR013099 | 13,099 | Potassium channel domain | K_chnl_dom | Domain | 82,239 | false | false | This domain is found in a variety of potassium channel proteins, including the two membrane helix type ion channels found in bacteria [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07885"
] | [
"Ion_trans_2"
] | [
82239
] | 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-1299308",
"R-BTA-5576886",
"R-CEL-1296052",
"R-CEL-1299316",
"R-CEL-1299503",
"R-CEL-5576886",
"R-DME-1296052",
"R-HSA-1296052",
"R-HSA-1299287",
"R-HSA-1299308",
"R-HSA-1299316",
"R-HSA-1299344",
"R-HSA-1299361",
"R-HSA-1299503",
"R-HSA-5576886",
"R-HSA-9667769",
"R-MMU-12960... | [
"REACTOME:R-BTA-1299308",
"REACTOME:R-BTA-5576886",
"REACTOME:R-CEL-1296052",
"REACTOME:R-CEL-1299316",
"REACTOME:R-CEL-1299503",
"REACTOME:R-CEL-5576886",
"REACTOME:R-DME-1296052",
"REACTOME:R-HSA-1296052",
"REACTOME:R-HSA-1299287",
"REACTOME:R-HSA-1299308",
"REACTOME:R-HSA-1299316",
"REACTOM... | 41 | [
"1bl8",
"1f6g",
"1j95",
"1jvm",
"1k4c",
"1k4d",
"1lnq",
"1p7b",
"1r3i",
"1r3j",
"1r3k",
"1r3l",
"1s5h",
"1xl4",
"1xl6",
"1zwi",
"2a9h",
"2ahy",
"2ahz",
"2atk",
"2bob",
"2boc",
"2dwd",
"2dwe",
"2h8p",
"2hfe",
"2hg5",
"2hjf",
"2hvj",
"2hvk",
"2ih1",
"2ih3"... | 349 | [
"PUB00016572"
] | [
"11836519"
] | [
"Potassium channel structures."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1289,
27863,
52547,
58,
482
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
21,
121,
116,
43,
1,
76,
61,
2,
13,
90,
1,
16
] | 12 | true | Domain | Potassium channel domain | Potassium channel domain | K_chnl_dom | 3 |
IPR013100 | 13,100 | Limonene-1,2-epoxide hydrolase | LEH | Domain | 1,649 | false | false | Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold c... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07858"
] | [
"LEH"
] | [
1649
] | 1 | [] | [] | [] | 0 | [
"1nu3",
"1nww",
"2bng",
"4r9k",
"4r9l",
"4xbt",
"4xbx",
"4xby",
"4xdv",
"4xdw",
"5aih",
"5aii",
"5cf1",
"5cf2",
"5ck6",
"5clk",
"5gkw",
"5jpp",
"5jpu",
"5yao",
"5yng",
"5yqt",
"7vwd",
"7vwm",
"7vx2",
"7xee",
"7xef"
] | 27 | [
"PUB00016459"
] | [
"12773375"
] | [
"Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1581,
4,
64
] | 3 | [] | [] | 0 | true | Domain | Limonene-1,2-epoxide hydrolase | Limonene-1,2-epoxide hydrolase | LEH | 6 |
IPR013101 | 13,101 | Phosphate response ubiquitin E3 ligase 1-like, LRR | LRR_PRU1-like | Repeat | 1,294 | false | false | This entry represents a short segment of LRRs found in plant proteins such as Phosphate response ubiquitin E3 ligase 1, PRU1 (also known as Putative F-box/LRR-repeat protein At3g42770). PRU1 is a E3 ligase involved in phosphate homeostasis. Under low Pi stress it targets WRKY6 (AT1G62300) for degradation which in turn ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07723"
] | [
"LRR_2"
] | [
1294
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00001625",
"PUB00001898",
"PUB00004163",
"PUB00005426",
"PUB00007147",
"PUB00007148",
"PUB00017058",
"PUB00094376",
"PUB00155967"
] | [
"1657640",
"2176636",
"8264799",
"7817399",
"11751054",
"11967365",
"14747988",
"21606681",
"29567663"
] | [
"A leucine-rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a beta-sheet structure.",
"slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains.",
"Crystal structure of porcine ribonuclease... | [
1991,
1990,
1993,
1994,
2001,
2002,
2004,
2011,
2018
] | 9 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"viral metagenome"
] | [
10,
1283,
1
] | 3 | [
"Arabidopsis thaliana"
] | [
79
] | 1 | true | Repeat | Phosphate response ubiquitin E3 ligase 1-like, LRR | Phosphate response ubiquitin E3 ligase 1-like, LRR | LRR_PRU1-like | 7 |
IPR013102 | 13,102 | Pyrimidine nucleoside phosphorylase, C-terminal | PYNP_C | Domain | 16,773 | false | false | This domain is found at the C-terminal end of the large α/β domain making up various pyrimidine nucleoside phosphorylases [ , ]. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP, ) there is an added three-stranded anti-parallel β shee... | [
"GO:0016763",
"GO:0006213"
] | [
"pentosyltransferase activity",
"pyrimidine nucleoside metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF07831",
"SM00941"
] | [
"PYNP_C",
"PYNP_C"
] | [
16526,
16717
] | 2 | [
"EC",
"EC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.4.2",
"2.4.2.4",
"PWY-7181",
"R-HSA-73614",
"R-HSA-73621",
"R-MMU-73614",
"R-MMU-73621",
"R-RNO-73614",
"R-RNO-73621"
] | [
"EC:2.4.2",
"EC:2.4.2.4",
"METACYC:PWY-7181",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-73621",
"REACTOME:R-MMU-73614",
"REACTOME:R-MMU-73621",
"REACTOME:R-RNO-73614",
"REACTOME:R-RNO-73621"
] | 9 | [
"1azy",
"1brw",
"1otp",
"1tpt",
"1uou",
"2dsj",
"2j0f",
"2tpt",
"2wk5",
"2wk6",
"3h5q",
"4ead",
"4eaf",
"4ga4",
"4ga5",
"4ga6",
"4lhm",
"4x46",
"4xr5",
"4yek",
"4yyy",
"5ep8",
"5ey3",
"5oln",
"7m7k"
] | 25 | [
"PUB00002573",
"PUB00010724"
] | [
"2199449",
"9817849"
] | [
"Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.",
"The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation."
] | [
1990,
1998
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
439,
15247,
803,
284
] | 4 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
5,
1,
2
] | 5 | true | Domain | Pyrimidine nucleoside phosphorylase, C-terminal | Pyrimidine nucleoside phosphorylase, C-terminal | PYNP_C | 7 |
IPR013103 | 13,103 | Reverse transcriptase, RNA-dependent DNA polymerase | RVT_2 | Domain | 130,855 | false | false | A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses. This entry includes reverse tran... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07727"
] | [
"RVT_2"
] | [
130855
] | 1 | [
"EC",
"EC",
"EC",
"EC"
] | [
"2.7.7.49",
"2.7.7.7",
"3.1.26.4",
"3.4.23.-"
] | [
"EC:2.7.7.49",
"EC:2.7.7.7",
"EC:3.1.26.4",
"EC:3.4.23.-"
] | 4 | [] | 0 | [
"PUB00001193"
] | [
"1698615"
] | [
"Origin and evolution of retroelements based upon their reverse transcriptase sequences."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"ecological metagenomes"
] | [
73,
130777,
3,
2
] | 4 | [
"Arabidopsis thaliana",
"Drosophila melanogaster",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Zea mays"
] | [
181,
6,
865,
47,
84
] | 5 | true | Domain | Reverse transcriptase, RNA-dependent DNA polymerase | Reverse transcriptase, RNA-dependent DNA polymerase | RVT_2 | 4 |
IPR013104 | 13,104 | Clostridium neurotoxin, receptor-binding C-terminal | Toxin_rcpt-bd_C | Domain | 189 | false | false | The Clostridium neurotoxin family is composed of tetanus neurotoxins and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain ( ), the central translocation domains and two receptor-binding domains [ ]. This domain is the C-ter... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07951"
] | [
"Toxin_R_bind_C"
] | [
189
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.4.24.69",
"GenProp0707",
"R-HSA-5250955",
"R-HSA-5250958",
"R-HSA-5250968",
"R-HSA-5250971",
"R-HSA-5250981",
"R-HSA-5250982",
"R-HSA-5250989",
"R-HSA-5250992"
] | [
"EC:3.4.24.69",
"GP:GenProp0707",
"REACTOME:R-HSA-5250955",
"REACTOME:R-HSA-5250958",
"REACTOME:R-HSA-5250968",
"REACTOME:R-HSA-5250971",
"REACTOME:R-HSA-5250981",
"REACTOME:R-HSA-5250982",
"REACTOME:R-HSA-5250989",
"REACTOME:R-HSA-5250992"
] | 10 | [
"1a8d",
"1af9",
"1d0h",
"1dfq",
"1diw",
"1dll",
"1epw",
"1f31",
"1fv2",
"1fv3",
"1g9a",
"1g9b",
"1g9c",
"1g9d",
"1i1e",
"1s0b",
"1s0c",
"1s0d",
"1s0e",
"1s0f",
"1s0g",
"1yxw",
"1yyn",
"1z0h",
"2nm1",
"2np0",
"2nyy",
"2nz9",
"2vu9",
"2vua",
"2vxr",
"3azv"... | 141 | [
"PUB00016466"
] | [
"9783750"
] | [
"Crystal structure of botulinum neurotoxin type A and implications for toxicity."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Clostridium",
"unclassified Caudoviricetes"
] | [
186,
3
] | 2 | [] | [] | 0 | true | Domain | Clostridium neurotoxin, receptor-binding C-terminal | Clostridium neurotoxin, receptor-binding C-terminal | Toxin_rcpt-bd_C | 9 |
IPR013105 | 13,105 | Tetratricopeptide repeat 2 | TPR_2 | Repeat | 46,953 | false | false | This repeat includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by . The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins [ , , ]. It mediates protein-protein interactions and the assembly of multiprotein complexes [ ]. The TPR motif consists of 3-16 tand... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07719"
] | [
"TPR_2"
] | [
46953
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DDI-2559580",
"R-DDI-3214842",
"R-HSA-1169408",
"R-HSA-3371497",
"R-HSA-3371568",
"R-HSA-8939211",
"R-HSA-9018519",
"R-HSA-909733",
"R-HSA-9679191",
"R-HSA-9696273",
"R-MMU-3371497",
"R-MMU-3371568",
"R-MMU-8939211",
"R-MMU-9018519",
"R-PFA-3371497",
"R-RNO-3371497",
"R-RNO-337156... | [
"REACTOME:R-DDI-2559580",
"REACTOME:R-DDI-3214842",
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-3371497",
"REACTOME:R-HSA-3371568",
"REACTOME:R-HSA-8939211",
"REACTOME:R-HSA-9018519",
"REACTOME:R-HSA-909733",
"REACTOME:R-HSA-9679191",
"REACTOME:R-HSA-9696273",
"REACTOME:R-MMU-3371497",
"REACTOME... | 20 | [
"1e96",
"1hh8",
"1p5q",
"1qz2",
"1w3b",
"1wm5",
"3u4t",
"3zgq",
"4hoq",
"4hor",
"4hos",
"4hot",
"4j0u",
"5w5h",
"5w5i",
"6c6k",
"6vfj",
"6vl6",
"7kw7",
"7mnl",
"7mnm",
"7mnn",
"7mno",
"7tbl",
"7tbm",
"8a3t",
"8a5y",
"8a61",
"8ffv",
"8ur5",
"8ur7"
] | 31 | [
"PUB00001313",
"PUB00005443",
"PUB00005695",
"PUB00014195",
"PUB00094363"
] | [
"9482716",
"7667876",
"1882418",
"14659697",
"22404999"
] | [
"The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.",
"Tetratrico peptide repeat interactions: to TPR or not to TPR?",
"The TPR snap helix: a novel protein repeat motif from mitosis to transcription.",
"TPR proteins: the versati... | [
1998,
1995,
1991,
2003,
2012
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
592,
20006,
25844,
4,
507
] | 5 | [
"Arabidopsis thaliana",
"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",
"Saccharomyces cerevisiae... | [
38,
48,
14,
1,
27,
15,
4,
35,
20,
1,
1,
94
] | 12 | true | Repeat | Tetratricopeptide repeat 2 | Tetratricopeptide repeat 2 | TPR_2 | 7 |
IPR013106 | 13,106 | Immunoglobulin V-set domain | Ig_V-set | Domain | 265,789 | false | false | This entry represents the V-set domains, which are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families, including immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2), CD4, CD80, and CD86; in myelin membran... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"SMART"
] | [
"PF07686",
"PF15910",
"SM00406"
] | [
"V-set",
"V-set_2",
"IGv"
] | [
236316,
1019,
157637
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-1257604",
"R-BTA-1971475",
"R-BTA-198933",
"R-BTA-2022870",
"R-BTA-2022923",
"R-BTA-2024101",
"R-BTA-202733",
"R-BTA-216083",
"R-BTA-2173791",
"R-BTA-3000178",
"R-BTA-381426",
"R-BTA-420029",
"R-BTA-5576892",
"R-BTA-6811558",
"R-BTA-8957275",
"R-BTA-9927354",
"R-CEL-1474228",
... | [
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-1971475",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-2022870",
"REACTOME:R-BTA-2022923",
"REACTOME:R-BTA-2024101",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173791",
"REACTOME:R-BTA-3000178",
"REACTOME:R-BTA-381426",
"REACTOME:R-... | 320 | [
"12e8",
"15c8",
"1a0q",
"1a14",
"1a2y",
"1a3l",
"1a3r",
"1a4j",
"1a4k",
"1a5f",
"1a64",
"1a6p",
"1a6t",
"1a6u",
"1a6v",
"1a6w",
"1a7b",
"1a7n",
"1a7o",
"1a7p",
"1a7q",
"1a7r",
"1a8j",
"1ac6",
"1acy",
"1ad0",
"1ad9",
"1adq",
"1ae6",
"1afv",
"1ah1",
"1ahw"... | 11,789 | [
"PUB00010610",
"PUB00014840",
"PUB00015110",
"PUB00027656"
] | [
"11377196",
"9417933",
"15327963",
"10698639"
] | [
"Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state.",
"Sequence profiles of immunoglobulin and immunoglobulin-like domains.",
"Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and ot... | [
2001,
1997,
2004,
2000
] | 4 | [
"IPR003599"
] | [
"IPR029863",
"IPR033319",
"IPR037677",
"IPR039944",
"IPR041849",
"IPR042711",
"IPR047014",
"IPR047318"
] | 1 | 8 | 0 | [
"Bacteria",
"Metazoa",
"Viruses",
"bird metagenome"
] | [
31,
265348,
408,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
26,
1270,
137,
18512,
2255,
1480
] | 6 | true | Domain | Immunoglobulin V-set domain | Immunoglobulin V-set domain | Ig_V-set | 4 |
IPR013107 | 13,107 | Acyl-CoA dehydrogenase, C-terminal domain | Acyl-CoA_DH_C | Domain | 28,558 | false | false | Acyl Co-A dehydrogenases ( ) are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases [ , , ] catalyse the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concomitant reduction of enzyme-bound FAD. Reoxidat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08028"
] | [
"Acyl-CoA_dh_2"
] | [
28558
] | 1 | [
"EC"
] | [
"1.14.14"
] | [
"EC:1.14.14"
] | 1 | [
"2jbr",
"2jbs",
"2jbt",
"2or0",
"2rfq",
"3afe",
"3aff",
"3x0x",
"3x0y",
"4doy",
"4jek",
"4nxl",
"5lvu",
"5lvw",
"5mr6",
"5xb8",
"5xdb",
"5xdc",
"5xdd",
"5xde",
"5xdg",
"6u76",
"6uug",
"7f70",
"7f72",
"7f74",
"8cda"
] | 27 | [
"PUB00001328",
"PUB00002511",
"PUB00002861",
"PUB00007933"
] | [
"3326738",
"2777793",
"8034667",
"8356049"
] | [
"Molecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency.",
"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of t... | [
1987,
1989,
1994,
1993
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
27546,
763,
249
] | 3 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Domain | Acyl-CoA dehydrogenase, C-terminal domain | Acyl-CoA dehydrogenase, C-terminal domain | Acyl-CoA_DH_C | 9 |
IPR013108 | 13,108 | Amidohydrolase 3 | Amidohydro_3 | Domain | 74,626 | false | false | This entry represents a subset of amidohydrolase domains that participate in different functions including cytosine degradation, atrazine degradation and other metabolic processes. The structure of the domain from Escherichia coli has been studied, and like other amidohydrolases, it forms a classical α-β TIM-barrel fol... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07969"
] | [
"Amidohydro_3"
] | [
74626
] | 1 | [
"EC",
"GP",
"GP"
] | [
"3.5.2",
"GenProp1361",
"GenProp1540"
] | [
"EC:3.5.2",
"GP:GenProp1361",
"GP:GenProp1540"
] | 3 | [
"1k6w",
"1k70",
"1m7j",
"1r9x",
"1r9y",
"1r9z",
"1ra0",
"1ra5",
"1rak",
"1rjp",
"1rjq",
"1rjr",
"1rk5",
"1rk6",
"1v4y",
"1v51",
"1xrf",
"1xrt",
"2qt3",
"3d6n",
"3g77",
"3gip",
"3giq",
"3icj",
"3igh",
"3mpg",
"3o7u",
"3r0d",
"3rn6",
"4bjh",
"4cqb",
"4cqc"... | 54 | [
"PUB00004994",
"PUB00014255",
"PUB00028135"
] | [
"9144792",
"11812140",
"11395407"
] | [
"An evolutionary treasure: unification of a broad set of amidohydrolases related to urease.",
"The structure of Escherichia coli cytosine deaminase.",
"Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies."
] | [
1997,
2002,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudovirales sp. ctTVN2",
"Eukaryota",
"unclassified sequences"
] | [
1231,
65863,
1,
5859,
1672
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
8,
3,
3,
3,
1,
12
] | 6 | true | Domain | Amidohydrolase 3 | Amidohydrolase 3 | Amidohydro_3 | 5 |
IPR013111 | 13,111 | Epidermal growth factor-like domain, extracellular | EGF_extracell | Domain | 22,498 | false | false | This entry contains EGF domains found in a variety of extracellular and membrane proteins, including integrin beta-1-3, tenascin, multiple epidermal growth factor-like domains (protein 10 and disintegrin), and metalloproteinase domain-containing protein 22/23, among others. In integrin beta subunits, this domain is ref... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07974"
] | [
"EGF_2"
] | [
22498
] | 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-166016",
"R-BTA-198933",
"R-BTA-202733",
"R-BTA-2129379",
"R-BTA-216083",
"R-BTA-2173789",
"R-BTA-3000178",
"R-BTA-6798695",
"R-CEL-114608",
"R-CEL-1236973",
"R-CEL-1912420",
"R-CEL-2129379",
"R-CEL-216083",
"R-CEL-2173789",
"R-CEL-3000157",
"R-CEL-3000170",
... | [
"REACTOME:R-BTA-1566948",
"REACTOME:R-BTA-166016",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-202733",
"REACTOME:R-BTA-2129379",
"REACTOME:R-BTA-216083",
"REACTOME:R-BTA-2173789",
"REACTOME:R-BTA-3000178",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-114608",
"REACTOME:R-CEL-1236973",
"REACTOME:R-C... | 173 | [
"1jv2",
"1l5g",
"1m1x",
"1u8c",
"2e26",
"2wft",
"2wfx",
"2wg3",
"2wg4",
"2ygq",
"3a7q",
"3fcs",
"3g5c",
"3ho3",
"3ho4",
"3ho5",
"3ije",
"4cak",
"4g1e",
"4g1m",
"4mmx",
"4mmy",
"4mmz",
"4o02",
"4um8",
"5b4x",
"5y2z",
"5y31",
"6avq",
"6avr",
"6avu",
"6bxj"... | 85 | [
"PUB00001555",
"PUB00003983",
"PUB00004321",
"PUB00004609",
"PUB00152567"
] | [
"3282918",
"6607417",
"2288911",
"6334307",
"19704023"
] | [
"Structure and function of epidermal growth factor-like regions in proteins.",
"Computer-based characterization of epidermal growth factor precursor.",
"The many faces of epidermal growth factor repeats.",
"Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth ... | [
1988,
1984,
1990,
1984,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified dsDNA viruses"
] | [
5,
22488,
5
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
62,
13,
54,
40,
97
] | 6 | true | Domain | Epidermal growth factor-like domain, extracellular | Epidermal growth factor-like domain, extracellular | EGF_extracell | 4 |
IPR013112 | 13,112 | FAD-binding 8 | FAD-bd_8 | Domain | 39,949 | false | false | This entry represents FAD binding domain that is associated with ferric reductase NAD binding proteins and the heavy chain of Cytochrome b-245. Members of this group are predominantly found in eukaryotes and bacteria. | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08022"
] | [
"FAD_binding_8"
] | [
39949
] | 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-1222556",
"R-BTA-1236973",
"R-BTA-3299685",
"R-BTA-4420097",
"R-BTA-5668599",
"R-BTA-6798695",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013423",
"R-CEL-209968",
"R-CFA-209968",
"R-DDI-209968",
"R-DDI-3299685",
"R-DDI-6798695",
"R-DME-209968",
"R-HSA-1222556",
"R-HSA-1236973",... | [
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1236973",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013404",
"REACTOME:R-BTA-9013423",
"REACTOME:R-CEL-209968",
"REACTOME:R-CFA-209968",
"REACTOME:... | 55 | [
"5o0x",
"6sz5",
"6wxr",
"6wxu",
"6wxv",
"7d3e",
"7d3f",
"7u8g",
"8cak",
"8cal",
"8cao",
"8cap",
"8cb0",
"8gz3",
"8kei",
"8qq1",
"8qq5",
"8qq7",
"8qt6",
"8qt7",
"8qt9",
"8qta",
"8u7y",
"8u85",
"8u86",
"8u87",
"8wej",
"8x2l"
] | 28 | [] | [] | [] | [] | 0 | [
"IPR017927"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"unclassified sequences"
] | [
3779,
36086,
3,
81
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
94,
2,
20,
6,
27,
15,
9,
40,
28,
8,
2,
105
] | 12 | true | Domain | FAD-binding 8 | FAD-binding 8 | FAD-bd_8 | 1 |
IPR013113 | 13,113 | Siderophore-interacting, FAD-binding | SIP_FAD-bd | Domain | 19,447 | false | false | This entry describes the FAD-binding domain found in siderophore-interacting proteins (SIP), mostly found in bacteria. This domain is also found in Mycobactin import ATP-binding/permease protein IrtA. Siderophore-interacting proteins (SIPs) are flavin-dependent enzymes that catalyse the release of iron from the siderop... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08021"
] | [
"FAD_binding_9"
] | [
19447
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-1222449",
"R-HSA-9638334"
] | [
"REACTOME:R-HSA-1222449",
"REACTOME:R-HSA-9638334"
] | 2 | [
"2gpj",
"4yhb",
"6geh",
"6k2l",
"6tej",
"6tek",
"7lrn",
"7wiu",
"7wiv",
"7wiw",
"7wix",
"7xlz",
"8c4l",
"9fxc",
"9g2k",
"9g2l",
"9g2m"
] | 17 | [
"PUB00160336",
"PUB00160337",
"PUB00160338"
] | [
"34308084",
"19948799",
"32296173"
] | [
"Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from <i>Acinetobacter baumannii</i>.",
"The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain.",
"The ABC exporter IrtAB imports and reduces mycobacterial siderophores.... | [
2021,
2010,
2020
] | 3 | [
"IPR017927"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
19391,
13,
43
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Siderophore-interacting, FAD-binding | Siderophore-interacting, FAD-binding | SIP_FAD-bd | 6 |
IPR013114 | 13,114 | Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ | FabA_FabZ | Family | 31,417 | false | false | Fatty acids biosynthesis occurs by two distinct pathways: in fungi, mammals and mycobacteria, type I or associative fatty-acid biosynthesis (type I FAS) is accomplished by multifunctional proteins in which distinct domains catalyse specific reactions; in plants and most bacteria, type II or dissociative fatty-acid bios... | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF07977",
"PTHR30272"
] | [
"FabA",
""
] | [
30968,
27937
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.59",
"PWY-5971",
"PWY-5973",
"PWY-5989",
"PWY-6282",
"PWY-6519",
"PWY-7388",
"PWY-7663",
"PWY-7664",
"PWY-7858",
"PWY-8173",
"PWY-8174",
"PWY-8175",
"PWY-8203",
"PWY-8279",
"PWY-8280",
"PWY-8427",
"PWYG-321"
] | [
"EC:4.2.1.59",
"METACYC:PWY-5971",
"METACYC:PWY-5973",
"METACYC:PWY-5989",
"METACYC:PWY-6282",
"METACYC:PWY-6519",
"METACYC:PWY-7388",
"METACYC:PWY-7663",
"METACYC:PWY-7664",
"METACYC:PWY-7858",
"METACYC:PWY-8173",
"METACYC:PWY-8174",
"METACYC:PWY-8175",
"METACYC:PWY-8203",
"METACYC:PWY-... | 18 | [
"1mka",
"1mkb",
"1u1z",
"1z6b",
"1zhg",
"2cf2",
"2gll",
"2glm",
"2glp",
"2glv",
"2okh",
"2oki",
"3az8",
"3az9",
"3aza",
"3azb",
"3b7j",
"3cf8",
"3cf9",
"3d04",
"3d6x",
"3doy",
"3doz",
"3dp0",
"3dp1",
"3dp2",
"3dp3",
"3ed0",
"3q62",
"4b0b",
"4b0c",
"4b0i"... | 59 | [
"PUB00014939"
] | [
"14684903"
] | [
"Crystallization and preliminary crystallographic analysis of beta-hydroxyacyl ACP dehydratase (FabZ) from Plasmodium falciparum."
] | [
2004
] | 1 | [] | [
"IPR010083",
"IPR010084"
] | 0 | 2 | 0 | [
"Bacteria",
"Eukaryota",
"Halorubrum tibetense",
"unclassified sequences"
] | [
29580,
1238,
1,
598
] | 4 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
2,
6,
8
] | 4 | true | Family | Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ | Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ | FabA_FabZ | 4 |
IPR013115 | 13,115 | Histidine biosynthesis HisG, C-terminal | HisG_C | Domain | 14,545 | false | false | ATP phosphoribosyltransferase ( ) is the enzyme that catalyzes the first step in the biosynthesis of histidine in bacteria, fungi and plants as shown below. It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate with nitrog... | [
"GO:0000287",
"GO:0003879",
"GO:0000105",
"GO:0005737"
] | [
"magnesium ion binding",
"ATP phosphoribosyltransferase activity",
"L-histidine biosynthetic process",
"cytoplasm"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM",
"NCBIFAM"
] | [
"PF08029",
"TIGR03455"
] | [
"HisG_C",
"HisG_C-term"
] | [
14427,
14339
] | 2 | [
"EC",
"GP"
] | [
"2.4.2.17",
"GenProp0109"
] | [
"EC:2.4.2.17",
"GP:GenProp0109"
] | 2 | [
"1h3d",
"1nh7",
"1nh8",
"1q1k",
"2vd3",
"4yb5",
"4yb6",
"4yb7",
"5lht",
"5lhu",
"5u99",
"6czl",
"6czm",
"7dah",
"7dam"
] | 15 | [
"PUB00022501",
"PUB00028083",
"PUB00028134"
] | [
"14741209",
"11751055",
"12511575"
] | [
"The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.",
"The PRT protein family.",
"Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis."
] | [
2004,
2001,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
770,
10637,
2823,
315
] | 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"
] | [
8,
1,
1,
1,
1,
1,
8
] | 7 | true | Domain | Histidine biosynthesis HisG, C-terminal | Histidine biosynthesis HisG, C-terminal | HisG_C | 1 |
IPR013116 | 13,116 | Ketol-acid reductoisomerase, N-terminal | KARI_N | Domain | 27,139 | false | false | Ketol-acid reductoisomerase (KARI; ( )), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyzes the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essential branched-chain amino acids valine, leucine, and isoleucine. KARI catalyses a... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF07991",
"PS51850"
] | [
"KARI_N",
"KARI_N"
] | [
27124,
26619
] | 2 | [
"EC",
"EC",
"METACYC",
"METACYC"
] | [
"1.1.1",
"1.1.1.86",
"PWY-5103",
"PWY-7111"
] | [
"EC:1.1.1",
"EC:1.1.1.86",
"METACYC:PWY-5103",
"METACYC:PWY-7111"
] | 4 | [
"1np3",
"1qmg",
"1yrl",
"1yve",
"3fr7",
"3fr8",
"3ulk",
"4kqw",
"4kqx",
"4tsk",
"4xdy",
"4xdz",
"4xeh",
"4xiy",
"4ypo",
"5e4r",
"5w3k",
"5yeq",
"6aqj",
"6bul",
"6c55",
"6c5n",
"6jcv",
"6jcw",
"6jcz",
"6jd1",
"6jd2",
"6jx2",
"6kou",
"6kpa",
"6kpe",
"6kph"... | 75 | [
"PUB00001302",
"PUB00029172",
"PUB00034453",
"PUB00052029",
"PUB00088660",
"PUB00088661",
"PUB00088662"
] | [
"9218783",
"12691757",
"16322583",
"19362563",
"11352718",
"25849365",
"26644020"
] | [
"The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.",
"Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa.",
"The crystal structure of a bact... | [
1997,
2003,
2005,
2009,
2001,
2015,
2016
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Imitervirales",
"unclassified sequences"
] | [
872,
22298,
3413,
3,
553
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
4,
1,
1,
10,
1,
1,
12
] | 7 | true | Domain | Ketol-acid reductoisomerase, N-terminal | Ketol-acid reductoisomerase, N-terminal | KARI_N | 3 |
IPR013117 | 13,117 | Intimin, C-terminal | Intimin_C | Domain | 434 | false | false | This domain is found at the C terminus of intimin. Its structure has been solved and shown to have a C-lectin type of structure [ ]. Intimin is a bacterial adhesion molecule involved in intimate attachment of enteropathogenic and enterohemorrhagic Escherichia coli to mammalian host cells. Intimin targets the translocat... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07979"
] | [
"Intimin_C"
] | [
434
] | 1 | [] | [] | [] | 0 | [
"1cwv",
"1e5u",
"1f00",
"1f02",
"2zqk",
"2zwk",
"3ncw",
"3ncx"
] | 8 | [
"PUB00006621"
] | [
"10835344"
] | [
"Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
434
] | 1 | [] | [] | 0 | true | Domain | Intimin, C-terminal | Intimin, C-terminal | Intimin_C | 6 |
IPR013118 | 13,118 | Mannitol dehydrogenase, C-terminal | Mannitol_DH_C | Domain | 26,450 | false | false | Long-chain mannitol dehydrogenases are a group of secondary alcohol dehydrogenases that differ from other alcohol or polyol dehydrogenases in that they do not utilise Zn(2+) or other metal cofactors and do not contain a conserved catalytic tyrosine residue. The proteins in this family that have been studied are monomer... | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08125"
] | [
"Mannitol_dh_C"
] | [
26450
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"METACYC"
] | [
"1.1.1",
"1.1.1.17",
"GenProp1387",
"GenProp1449",
"GenProp1636",
"PWY-6531"
] | [
"EC:1.1.1",
"EC:1.1.1.17",
"GP:GenProp1387",
"GP:GenProp1449",
"GP:GenProp1636",
"METACYC:PWY-6531"
] | 6 | [
"1lj8",
"1m2w",
"3h2z",
"4im7",
"5itg",
"5jnm",
"7ocn",
"7ocp",
"7ocq",
"7ocr",
"7ocs",
"7oct",
"7ocu",
"7rk4",
"7rk5"
] | 15 | [
"PUB00003120",
"PUB00007926",
"PUB00027206",
"PUB00028133"
] | [
"8254318",
"9639934",
"12196534",
"11160802"
] | [
"Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodobacter sphaeroides.",
"Genes for D-arabinitol and ribitol catabolism from Klebsiella pneumoniae.",
"Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and ... | [
1993,
1998,
2002,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"Viruses",
"unclassified sequences"
] | [
24302,
1972,
5,
5,
166
] | 5 | [
"Escherichia coli (strain K12)",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
5,
1,
2
] | 3 | true | Domain | Mannitol dehydrogenase, C-terminal | Mannitol dehydrogenase, C-terminal | Mannitol_DH_C | 4 |
IPR013120 | 13,120 | Fatty acyl-CoA reductase-like, NAD-binding domain | FAR_NAD-bd | Domain | 48,134 | false | false | This entry represents the C-terminal NAD-binding region of the fatty acyl-coenzyme A reductases (FARs) from plants and animals. FARs catalyse the reduction of fatty acyl-CoA to fatty alcohols [ , ]. Proteins containing this domain also include funagal non-ribosomal peptide synthetases and non-reducing polyketide syntha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF07993"
] | [
"NAD_binding_4"
] | [
48134
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.3.1.-",
"PWY-3602",
"PWY-361",
"PWY-4801",
"PWY-4922",
"PWY-5048",
"PWY-5139",
"PWY-5268",
"PWY-5284",
"PWY-5292",
"PWY-5307",
"PWY-5313",
"PWY-5317",
"PWY-5318",
"PWY-5353",
"PWY-5400",
"PWY-5473",
"PWY-5475",
"PWY-5477",
"PWY-5660",
"PWY-5679",
"PWY-5710",
"PWY-5794"... | [
"EC:2.3.1.-",
"METACYC:PWY-3602",
"METACYC:PWY-361",
"METACYC:PWY-4801",
"METACYC:PWY-4922",
"METACYC:PWY-5048",
"METACYC:PWY-5139",
"METACYC:PWY-5268",
"METACYC:PWY-5284",
"METACYC:PWY-5292",
"METACYC:PWY-5307",
"METACYC:PWY-5313",
"METACYC:PWY-5317",
"METACYC:PWY-5318",
"METACYC:PWY-53... | 225 | [
"4dqv",
"4f6c",
"4f6l",
"4u5q",
"4u7w",
"4w4t",
"5msc",
"5msd",
"5mso",
"5msp",
"5msq",
"5msr",
"5mss",
"5mst",
"5msu",
"5msv",
"5msw",
"6nki",
"6vtj",
"6vtz",
"7eoz",
"8aep",
"8v1x"
] | 23 | [
"PUB00013838",
"PUB00082323",
"PUB00095129",
"PUB00095145",
"PUB00095146",
"PUB00095147",
"PUB00095148",
"PUB00095586",
"PUB00151132"
] | [
"10320345",
"26662839",
"22510154",
"20571114",
"24108123",
"27416025",
"17102130",
"19182784",
"28634299"
] | [
"Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5.",
"Two separate key enzymes and two pathway-specific transcription factors are involved in fusaric acid biosynthesis in Fusarium fujikuroi.",
"Illuminat... | [
1999,
2016,
2012,
2010,
2013,
2016,
2007,
2009,
2017
] | 9 | [] | [
"IPR010080"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Yasminevirus sp. GU-2018",
"unclassified sequences"
] | [
125,
12832,
35084,
1,
92
] | 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... | [
55,
1,
6,
33,
25,
5,
2,
38,
9,
1,
2,
29
] | 12 | true | Domain | Fatty acyl-CoA reductase-like, NAD-binding domain | Fatty acyl-CoA reductase-like, NAD-binding domain | FAR_NAD-bd | 7 |
IPR013121 | 13,121 | Ferric reductase, NAD binding domain | Fe_red_NAD-bd_6 | Domain | 36,995 | false | false | This entry contains ferric reductase NAD binding proteins. | [
"GO:0016491"
] | [
"oxidoreductase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08030"
] | [
"NAD_binding_6"
] | [
36995
] | 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-1222556",
"R-BTA-1236973",
"R-BTA-3299685",
"R-BTA-4420097",
"R-BTA-5668599",
"R-BTA-6798695",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013423",
"R-CEL-209968",
"R-CFA-209968",
"R-DDI-209968",
"R-DDI-3299685",
"R-DDI-6798695",
"R-DME-209968",
"R-HSA-1222556",
"R-HSA-1236973",... | [
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1236973",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013404",
"REACTOME:R-BTA-9013423",
"REACTOME:R-CEL-209968",
"REACTOME:R-CFA-209968",
"REACTOME:... | 55 | [
"3a1f",
"5o0x",
"6sz5",
"6wxr",
"6wxu",
"6wxv",
"7d3e",
"7d3f",
"7u8g",
"8cak",
"8cal",
"8cao",
"8cap",
"8cb0",
"8gz3",
"8kei",
"8u7y",
"8u85",
"8u86",
"8u87",
"8wej",
"8x2l"
] | 22 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
61,
36930,
4
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
94,
2,
20,
6,
28,
15,
10,
38,
30,
8,
2,
98
] | 12 | true | Domain | Ferric reductase, NAD binding domain | Ferric reductase, NAD binding domain | Fe_red_NAD-bd_6 | 1 |
IPR013122 | 13,122 | Polycystin cation channel, PKD1/PKD2 | PKD1_2_channel | Domain | 17,142 | false | false | This entry contains proteins belonging to the polycystin family including Mucolipin and Polycystin-1 and -2 (PKD1 and PKD2). The domain contains the cation channel region of PKD1 and PKD2 proteins. PKD1 and PKD2 may function through a common signalling pathway that is necessary for normal tubulogenesis. The PKD2 gene p... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08016"
] | [
"PKD_channel"
] | [
17142
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-5620916",
"R-CEL-5620916",
"R-DRE-5620916",
"R-HSA-3295583",
"R-HSA-5620916",
"R-HSA-917977",
"R-MMU-3295583",
"R-MMU-5620916",
"R-MMU-917977"
] | [
"REACTOME:R-BTA-5620916",
"REACTOME:R-CEL-5620916",
"REACTOME:R-DRE-5620916",
"REACTOME:R-HSA-3295583",
"REACTOME:R-HSA-5620916",
"REACTOME:R-HSA-917977",
"REACTOME:R-MMU-3295583",
"REACTOME:R-MMU-5620916",
"REACTOME:R-MMU-917977"
] | 9 | [
"5k47",
"5mke",
"5mkf",
"5t4d",
"5w3s",
"5wj5",
"5wj9",
"5wpq",
"5wpt",
"5wpv",
"5ydz",
"5ye1",
"5ye2",
"5ye5",
"5z1w",
"6a70",
"6aye",
"6ayf",
"6ayg",
"6d1w",
"6du8",
"6e7p",
"6e7y",
"6e7z",
"6t9n",
"6t9o",
"6wb8",
"7d7e",
"7d7f",
"7dys",
"7mgl",
"7sq6"... | 69 | [
"PUB00004881",
"PUB00007622",
"PUB00007623",
"PUB00053593",
"PUB00053594",
"PUB00053595",
"PUB00099174"
] | [
"8643665",
"8650545",
"9326320",
"11013137",
"12459486",
"14749347",
"29567962"
] | [
"Polycystin, the polycystic kidney disease 1 protein, is expressed by epithelial cells in fetal, adult, and polycystic kidney.",
"PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein.",
"A spectrum of mutations in the second gene for autosomal dominant polycystic kidney disease (... | [
1996,
1996,
1997,
2000,
2002,
2004,
2018
] | 7 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine metagenome"
] | [
17141,
1
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
44,
19,
28,
21,
25
] | 6 | true | Domain | Polycystin cation channel, PKD1/PKD2 | Polycystin cation channel, PKD1/PKD2 | PKD1_2_channel | 3 |
IPR013123 | 13,123 | RNA 2-O ribose methyltransferase, substrate binding | SpoU_subst-bd | Domain | 44,066 | false | false | Most cellular RNAs undergo a number of post-transcriptional nucleoside modifications. While the biological role of many of these modifications is unknown, some have been shown to be necessary for cell growth or for resistance to antibiotics [ , ]. One of the most common modifications is 2'O-ribose methylation catalysed... | [
"GO:0008168"
] | [
"methyltransferase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF08032",
"SM00967"
] | [
"SpoU_sub_bind",
"SpoU_sub_bind"
] | [
29813,
43483
] | 2 | [
"EC",
"REACTOME"
] | [
"2.1.1",
"R-HSA-6793080"
] | [
"EC:2.1.1",
"REACTOME:R-HSA-6793080"
] | 2 | [
"1gz0",
"1ipa",
"4x3l",
"4x3m",
"5kzk",
"5l0z",
"7oi6",
"7qiu",
"9h1k",
"9hcc",
"9hcd",
"9hce",
"9muj",
"9muk"
] | 14 | [
"PUB00003946",
"PUB00006298",
"PUB00025434",
"PUB00028131",
"PUB00028132",
"PUB00101942"
] | [
"9187657",
"8266080",
"12377117",
"9917067",
"11698387",
"35710145"
] | [
"Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.",
"Functional requirement of a site-specific ribose methylation in ribosomal RNA.",
"The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a u... | [
1997,
1993,
2002,
1999,
2001,
2022
] | 6 | [] | [
"IPR053888"
] | 0 | 1 | 0 | [
"Archaeoglobaceae",
"Bacteria",
"Cotonvirus japonicus",
"Eukaryota",
"unclassified sequences"
] | [
9,
39173,
1,
4157,
726
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
1,
4,
2,
2,
3,
2,
1,
2,
5,
1,
1,
2
] | 13 | true | Domain | RNA 2-O ribose methyltransferase, substrate binding | RNA 2-O ribose methyltransferase, substrate binding | SpoU_subst-bd | 1 |
IPR013124 | 13,124 | Gap junction alpha-1 protein (Cx43), C-terminal | Connexin43_C | Domain | 1,025 | false | false | The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF03508"
] | [
"Connexin43"
] | [
1025
] | 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-190840",
"R-BTA-190861",
"R-BTA-190873",
"R-BTA-191650",
"R-BTA-196025",
"R-BTA-9013406",
"R-DRE-190840",
"R-DRE-190861",
"R-DRE-191650",
"R-DRE-9013406",
"R-HSA-190704",
"R-HSA-190827",
"R-HSA-190840",
"R-HSA-190861",
"R-HSA-190873",
"R-HSA-191650",
"R-HSA-196025",
"R-HSA-9... | [
"REACTOME:R-BTA-190840",
"REACTOME:R-BTA-190861",
"REACTOME:R-BTA-190873",
"REACTOME:R-BTA-191650",
"REACTOME:R-BTA-196025",
"REACTOME:R-BTA-9013406",
"REACTOME:R-DRE-190840",
"REACTOME:R-DRE-190861",
"REACTOME:R-DRE-191650",
"REACTOME:R-DRE-9013406",
"REACTOME:R-HSA-190704",
"REACTOME:R-HSA-1... | 33 | [
"1r5s",
"7f92",
"7f93",
"7xq9",
"7xqb",
"7z1t",
"7z22",
"7z23",
"8qko"
] | 9 | [
"PUB00000087",
"PUB00000926",
"PUB00005237",
"PUB00005511",
"PUB00005532",
"PUB00005545",
"PUB00005549"
] | [
"8811187",
"8608591",
"1320430",
"9861669",
"9769729",
"7685944",
"7570999"
] | [
"Connexins, connexons, and intercellular communication.",
"The gap junction communication channel.",
"Molecular biology and genetics of gap junction channels.",
"Diverse functions of vertebrate gap junctions.",
"Innexins: a family of invertebrate gap-junction proteins.",
"Gap junctions in the brain: where... | [
1996,
1996,
1992,
1998,
1998,
1993,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
1025
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
9,
4,
3
] | 4 | true | Domain | Gap junction alpha-1 protein (Cx43), C-terminal | Gap junction alpha-1 protein (Cx43), C-terminal | Connexin43_C | 7 |
IPR013126 | 13,126 | Heat shock protein 70 family | Hsp_70_fam | Family | 154,901 | false | false | Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding regio... | [
"GO:0005524",
"GO:0016887"
] | [
"ATP binding",
"ATP hydrolysis activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PANTHER",
"PANTHER"
] | [
"PF00012",
"PTHR19375",
"PTHR45639"
] | [
"HSP70",
"",
""
] | [
154260,
113361,
22592
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00269",
"R-BTA-3371453",
"R-BTA-3371497",
"R-BTA-3371568",
"R-BTA-3371571",
"R-BTA-450408",
"R-BTA-6798695",
"R-BTA-6799198",
"R-BTA-72163",
"R-BTA-8856828",
"R-BTA-8876725",
"R-BTA-888590",
"R-BTA-983170",
"R-BTA-9833482",
"R-BTA-9837999",
"R-BTA-9841251",
"R-BTA-9865881",
"R... | [
"PROSITEDOC:PDOC00269",
"REACTOME:R-BTA-3371453",
"REACTOME:R-BTA-3371497",
"REACTOME:R-BTA-3371568",
"REACTOME:R-BTA-3371571",
"REACTOME:R-BTA-450408",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-6799198",
"REACTOME:R-BTA-72163",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-8876725",
"REACTOME:R-B... | 165 | [
"1atr",
"1ats",
"1ba0",
"1ba1",
"1bpr",
"1bup",
"1ckr",
"1dg4",
"1dkg",
"1dkx",
"1dky",
"1dkz",
"1hjo",
"1hpm",
"1hx1",
"1kax",
"1kay",
"1kaz",
"1nga",
"1ngb",
"1ngc",
"1ngd",
"1nge",
"1ngf",
"1ngg",
"1ngh",
"1ngi",
"1ngj",
"1q5l",
"1qqm",
"1qqn",
"1qqo"... | 334 | [
"PUB00000712",
"PUB00000809",
"PUB00000958",
"PUB00001766",
"PUB00004019",
"PUB00004070",
"PUB00082583",
"PUB00090977"
] | [
"2686623",
"2944601",
"9476895",
"2841196",
"3282176",
"2143562",
"19165329",
"26655470"
] | [
"Essential roles of 70kDa heat inducible proteins.",
"Speculations on the functions of the major heat shock and glucose-regulated proteins.",
"The Hsp70 and Hsp60 chaperone machines.",
"The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization.",
"Heat-shock proteins. Coming in from... | [
1989,
1986,
1998,
1988,
1988,
1990,
2009,
2015
] | 8 | [] | [
"IPR010236",
"IPR012725",
"IPR042048",
"IPR042054"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
853,
62139,
88812,
1814,
1283
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
73,
14,
29,
37,
5,
156,
70,
10,
106,
55,
14,
9,
306
] | 13 | true | Family | Heat shock protein 70 family | Heat shock protein 70 family | Hsp_70_fam | 8 |
IPR013128 | 13,128 | Peptidase C1A | Peptidase_C1A | Family | 67,949 | false | false | This group of cysteine peptidases belong to MEROPS peptidase family C1, sub-family C1A (papain family, clan CA). It includes related cysteine proteinases such as actinidin [ ]. This entry also includes proteins classed as non-peptidase homologues such as the catalytically inactive tubulointerstitial nephritis antigen (... | [
"GO:0008234"
] | [
"cysteine-type peptidase activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR12411"
] | [
""
] | [
67949
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.22",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1592389",
"R-BTA-1679131",
"R-BTA-2022377",
"R-BTA-204005",
"R-BTA-2132295",
"R-BTA-432720",
"R-BTA-5683826",
"R-BTA-5694530",
"R-BTA-6798695",
"R-BTA-8939242",
"R-CEL-1474228",
"R-CEL-1592389",
"R-CEL-2022377",
"R-CEL-204005",
"R-... | [
"EC:3.4.22",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-1679131",
"REACTOME:R-BTA-2022377",
"REACTOME:R-BTA-204005",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-432720",
"REACTOME:R-BTA-5683826",
"REACTOME:R-BTA-5694530",
"REACTOME:R-BTA-6798695... | 101 | [
"1aec",
"1aim",
"1atk",
"1au0",
"1au2",
"1au3",
"1au4",
"1ayu",
"1ayv",
"1ayw",
"1bgo",
"1bp4",
"1bqi",
"1by8",
"1cjl",
"1cpj",
"1cqd",
"1cs8",
"1csb",
"1cte",
"1cvz",
"1deu",
"1ef7",
"1ewl",
"1ewm",
"1ewo",
"1ewp",
"1f29",
"1f2a",
"1f2b",
"1f2c",
"1fh0"... | 496 | [
"PUB00000287",
"PUB00000522",
"PUB00000685",
"PUB00003577",
"PUB00015451",
"PUB00101803"
] | [
"3117099",
"8439290",
"3148320",
"7845226",
"12188906",
"11170462"
] | [
"Purification, characterization, and amino acid composition of rabbit pulmonary bleomycin hydrolase.",
"Evolutionary families of peptidases.",
"Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin.",
"Families of cysteine peptidases.... | [
1987,
1993,
1988,
1994,
2002,
2001
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
205,
2471,
64852,
226,
195
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
143,
36,
48,
17,
142,
79,
134,
78,
194
] | 9 | true | Family | Peptidase C1A | Peptidase C1A | Peptidase_C1A | 9 |
IPR013130 | 13,130 | Ferric reductase transmembrane component-like domain | Fe3_Rdtase_TM_dom | Domain | 56,217 | false | false | This domain represents a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. These proteins may be a family of flavocytochromes capable of moving electrons across the plasma ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF01794"
] | [
"Ferric_reduct"
] | [
56217
] | 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-1222556",
"R-BTA-1236973",
"R-BTA-3299685",
"R-BTA-4420097",
"R-BTA-5668599",
"R-BTA-6798695",
"R-BTA-9013149",
"R-BTA-9013404",
"R-BTA-9013423",
"R-CEL-209968",
"R-CFA-209968",
"R-DDI-209968",
"R-DDI-3299685",
"R-DDI-6798695",
"R-DME-209968",
"R-HSA-1222556",
"R-HSA-1236973",... | [
"REACTOME:R-BTA-1222556",
"REACTOME:R-BTA-1236973",
"REACTOME:R-BTA-3299685",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5668599",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9013149",
"REACTOME:R-BTA-9013404",
"REACTOME:R-BTA-9013423",
"REACTOME:R-CEL-209968",
"REACTOME:R-CFA-209968",
"REACTOME:... | 72 | [
"5o0t",
"6hcy",
"6hd1",
"6sz5",
"6wxr",
"6wxu",
"6wxv",
"6y9b",
"7d3e",
"7d3f",
"7tai",
"7u8g",
"8gz3",
"8kei",
"8u7y",
"8u85",
"8u86",
"8u87",
"8ucd",
"8wej",
"8x2l"
] | 21 | [
"PUB00003689",
"PUB00004003",
"PUB00004004",
"PUB00005151"
] | [
"8321236",
"3600768",
"3600769",
"1318579"
] | [
"The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase.",
"The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochro... | [
1993,
1987,
1987,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
34,
14642,
41299,
242
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
94,
2,
26,
6,
1,
39,
28,
10,
38,
45,
9,
2,
90
] | 13 | true | Domain | Ferric reductase transmembrane component-like domain | Ferric reductase transmembrane component-like domain | Fe3_Rdtase_TM_dom | 4 |
IPR013132 | 13,132 | PseI/NeuA/B-like | PseI/NeuA/B-like_N | Domain | 13,172 | false | false | This entry represents the N-terminal TIM-barrel domain found in a number of proteins including NeuB, SpsE, PseI and homologues. NeuB is the prokaryotic N-acetylneuraminic acid synthase. It catalyses the direct formation of N-acetylneuraminic acid (Neu5Ac), the most common sialic acid, by condensation of phosphoenolpyru... | [
"GO:0016051"
] | [
"carbohydrate biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF03102"
] | [
"NeuB"
] | [
13172
] | 1 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"GenProp1737",
"R-DME-4085001",
"R-HSA-4085001",
"R-MMU-4085001"
] | [
"EC:2.5.1",
"GP:GenProp1737",
"REACTOME:R-DME-4085001",
"REACTOME:R-HSA-4085001",
"REACTOME:R-MMU-4085001"
] | 5 | [
"1vli",
"1xuu",
"1xuz",
"2wqp",
"3g8r",
"4ipi",
"4ipj",
"6ncs",
"6ppw",
"6ppx",
"6ppy",
"6ppz",
"8h2c"
] | 13 | [
"PUB00007383",
"PUB00032527",
"PUB00070658",
"PUB00070659"
] | [
"10873658",
"15516336",
"10749855",
"15888312"
] | [
"Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity.",
"Structural and mechanistic analysis of sialic acid synthase NeuB from Neisseria meningitidis in complex with Mn2+, phosphoenolpyruvate, and... | [
2000,
2005,
2000,
2005
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
234,
10876,
1484,
11,
567
] | 5 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
1,
5,
2,
4
] | 5 | true | Domain | PseI/NeuA/B-like | PseI/NeuA/B-like | PseI/NeuA/B-like_N | 2 |
IPR013134 | 13,134 | RAD50, zinc hook | Zn_hook_RAD50 | Domain | 3,861 | false | false | This entry represents the zinc hook of human DNA repair protein RAD50 and similar sequences found in all cellular organisms. Dimerisation at this domain is critical for the function of the Mre11 complex [ ]. The MRN complex (Mre11-Rad50-Nbs1) plays an important role in many DNA metabolic events that involve DNA double-... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF04423",
"PS51131"
] | [
"Rad50_zn_hook",
"ZN_HOOK"
] | [
2877,
3567
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51131",
"R-CEL-5685939",
"R-CEL-5693548",
"R-CEL-5693607",
"R-DDI-2559586",
"R-DDI-5693548",
"R-DDI-5693565",
"R-DME-2559586",
"R-DME-5685939",
"R-DME-5693548",
"R-DME-5693565",
"R-DME-5693607",
"R-DME-6804756",
"R-DME-69473",
"R-HSA-2559586",
"R-HSA-5685938",
"R-HSA-5685939",
... | [
"PROSITEDOC:PDOC51131",
"REACTOME:R-CEL-5685939",
"REACTOME:R-CEL-5693548",
"REACTOME:R-CEL-5693607",
"REACTOME:R-DDI-2559586",
"REACTOME:R-DDI-5693548",
"REACTOME:R-DDI-5693565",
"REACTOME:R-DME-2559586",
"REACTOME:R-DME-5685939",
"REACTOME:R-DME-5693548",
"REACTOME:R-DME-5693565",
"REACTOME:... | 68 | [
"1l8d",
"5gox",
"6zff",
"9bi4",
"9bi5",
"9q9h",
"9q9i",
"9q9j",
"9q9k",
"9q9m"
] | 10 | [
"PUB00017209",
"PUB00017210",
"PUB00017211",
"PUB00101805",
"PUB00144938"
] | [
"12949583",
"11741547",
"12152085",
"19308707",
"28134932"
] | [
"The MRN complex: coordinating and mediating the response to broken chromosomes.",
"Human Rad50/Mre11 is a flexible complex that can tether DNA ends.",
"The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.",
"RAD50, an SMC family member with multiple roles in DNA break r... | [
2003,
2001,
2002,
2009,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
778,
377,
2684,
22
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
5,
2,
1,
3,
5,
3,
1,
4,
3,
1,
1,
10
] | 12 | true | Domain | RAD50, zinc hook | RAD50, zinc hook | Zn_hook_RAD50 | 7 |
IPR013135 | 13,135 | Vitelline membrane cysteine-rich domain | Vitelline_membr_Cys-rich-dom | Domain | 270 | false | false | In Drosophila melanogaster (Fruit fly) the vitelline membrane (VM) is the first layer of the eggshell produced by the follicular epithelium. It is composed of at least four different proteins. VM proteins are similarly organised with a central highly conserved 38-amino acid domain which is flanked by unrelated regions.... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF10542",
"PS51137"
] | [
"Vitelline_membr",
"VM"
] | [
220,
266
] | 2 | [
"PROSITEDOC"
] | [
"PDOC51137"
] | [
"PROSITEDOC:PDOC51137"
] | 1 | [] | 0 | [
"PUB00017212",
"PUB00017213"
] | [
"3143615",
"8293994"
] | [
"Drosophila vitelline membrane genes contain a 114 base pair region of highly conserved coding sequence.",
"Comparative analysis of the sequence and structure of two Drosophila melanogaster genes encoding vitelline membrane proteins."
] | [
1988,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
270
] | 1 | [
"Drosophila melanogaster"
] | [
10
] | 1 | true | Domain | Vitelline membrane cysteine-rich domain | Vitelline membrane cysteine-rich domain | Vitelline_membr_Cys-rich-dom | 5 |
IPR013136 | 13,136 | WSTF/Acf1/Cbp146 | WSTF_Acf1_Cbp146 | Domain | 5,871 | false | false | ACF (for ATP-utilising chromatin assembly and remodeling factor) is a chromatin-remodeling complex that catalyzes the ATP-dependent assembly of periodic nucleosome arrays. This reaction utilises the energy of ATP hydrolysis by ISWI, the smaller of the two subunits of ACF. Acf1, the large subunit of ACF, is essential fo... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF10537",
"PS51136"
] | [
"WAC_Acf1_DNA_bd",
"WAC"
] | [
5553,
5814
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC51136",
"R-HSA-5250924",
"R-HSA-5693565",
"R-MMU-5250924",
"R-MMU-5693565"
] | [
"PROSITEDOC:PDOC51136",
"REACTOME:R-HSA-5250924",
"REACTOME:R-HSA-5693565",
"REACTOME:R-MMU-5250924",
"REACTOME:R-MMU-5693565"
] | 5 | [
"3qkr",
"3qks"
] | 2 | [
"PUB00017214",
"PUB00017215"
] | [
"10385622",
"12192034"
] | [
"ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly.",
"Binding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly."
] | [
1999,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Wphvirus"
] | [
63,
5804,
4
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
6,
1,
4,
4,
4,
6,
1,
7,
4,
2,
6
] | 11 | true | Domain | WSTF/Acf1/Cbp146 | WSTF/Acf1/Cbp146 | WSTF_Acf1_Cbp146 | 5 |
IPR013137 | 13,137 | Zinc finger, TFIIB-type | Znf_TFIIB | Domain | 13,544 | false | false | This entry represents a zinc finger motif found in transcription factor IIB (TFIIB). In eukaryotes the initiation of transcription of protein encoding genes by the polymerase II complexe (Pol II) is modulated by general and specific transcription factors. The general transcription factors operate through common promote... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF08271",
"PS51134"
] | [
"Zn_Ribbon_TF",
"ZF_TFIIB"
] | [
12726,
11807
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51134",
"R-BTA-674695",
"R-BTA-6807505",
"R-BTA-73776",
"R-BTA-73779",
"R-BTA-75953",
"R-BTA-76042",
"R-BTA-76071",
"R-CEL-674695",
"R-CEL-6807505",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-... | [
"PROSITEDOC:PDOC51134",
"REACTOME:R-BTA-674695",
"REACTOME:R-BTA-6807505",
"REACTOME:R-BTA-73776",
"REACTOME:R-BTA-73779",
"REACTOME:R-BTA-75953",
"REACTOME:R-BTA-76042",
"REACTOME:R-BTA-76071",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6807505",
"REACTOME:R-CEL-73776",
"REACTOME:R-CEL-73779",
... | 70 | [
"1dl6",
"1pft",
"1rly",
"1ro4",
"1vd4",
"3k1f",
"3k7a",
"4bbr",
"4bbs",
"4v1n",
"4v1o",
"5fmf",
"5fyw",
"5fz5",
"5gpy",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5oqj",
"5oqm",
"5sva",
"6cnb",
"6cnc",
"6cnd",
"6cnf",
"6eu0",
"6f40"... | 123 | [
"PUB00001883",
"PUB00014077",
"PUB00017216",
"PUB00017217",
"PUB00017218",
"PUB00017220",
"PUB00035804",
"PUB00035805",
"PUB00035806",
"PUB00035807",
"PUB00035812"
] | [
"1633439",
"12665246",
"8516312",
"8504927",
"8564536",
"15024075",
"17210253",
"15963892",
"15718139",
"10529348",
"11179890"
] | [
"The basic RNA polymerase II transcriptional machinery.",
"Zinc fingers--folds for many occasions.",
"Functional domains of transcription factor TFIIB.",
"Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II.",
"The... | [
1992,
2002,
1993,
1993,
1996,
2004,
2007,
2005,
2005,
1999,
2001
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
3816,
256,
9298,
37,
137
] | 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... | [
23,
3,
8,
5,
11,
11,
1,
12,
11,
2,
2,
20
] | 12 | true | Domain | Zinc finger, TFIIB-type | Zinc finger, TFIIB-type | Znf_TFIIB | 9 |
IPR013139 | 13,139 | Omega-atracotoxin, conserved site-2 | Omega_atracotoxin_CS2 | Conserved_site | 25 | false | false | Omega-atracotoxins (ACTX) form a family of neurotoxins that block insect but not vertebrate voltage-gated calcium channels. Omega-ACTXs are environmentally benign, insect-specific toxins that represent excellent leads for the development of new pesticides. Omega-ACTXs comprise a disulphide-rich region that has a [C-C-C... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS60017"
] | [
"OMEGA_ACTX_2"
] | [
25
] | 1 | [
"PROSITEDOC"
] | [
"PDOC60016"
] | [
"PROSITEDOC:PDOC60016"
] | 1 | [
"1g9p",
"1hp3"
] | 2 | [
"PUB00017222",
"PUB00017223",
"PUB00017224"
] | [
"9228949",
"10491095",
"14625686"
] | [
"The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.",
"Structure-function studies of omega-atracotoxin, a potent antagonist of insect voltage-gated calcium channels.",
"Pharmacologically active spider peptide toxins."
] | [
1997,
1999,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
25
] | 1 | [] | [] | 0 | true | Conserved_site | Omega-atracotoxin, conserved site-2 | Omega-atracotoxin, conserved site-2 | Omega_atracotoxin_CS2 | 1 |
IPR013140 | 13,140 | Huwentoxin, conserved site-1 | Huwentoxin_CS1 | Conserved_site | 178 | false | false | The spider venoms often contain many active peptides such as neurotoxins, lectins, inhibitors to enzyme, etc. These peptides are very important for the spider's hunting and defending. During the long history of spider evolution, the peptides evolved into different structures and functions. Despite their different biolo... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS60021"
] | [
"HWTX_1"
] | [
178
] | 1 | [
"PROSITEDOC"
] | [
"PDOC60021"
] | [
"PROSITEDOC:PDOC60021"
] | 1 | [
"1mb6",
"1nix",
"1niy",
"1qk6",
"1qk7",
"1ryv",
"1s6x",
"1zjq",
"2aap",
"2jtb",
"2m4x",
"2m50",
"2mpq",
"2mqf",
"2mt7",
"2mxo",
"2n1n",
"5t3m",
"5tlr",
"5we3",
"6br0",
"6btv",
"6gft",
"6mk5",
"6w6o",
"7k48",
"9dk5"
] | 27 | [
"PUB00017225",
"PUB00017226",
"PUB00017227",
"PUB00017228",
"PUB00017229",
"PUB00028940",
"PUB00057515",
"PUB00057516",
"PUB00096648",
"PUB00097926",
"PUB00152807"
] | [
"14757201",
"8212049",
"12827284",
"12893056",
"12727268",
"12228241",
"8394998",
"20189991",
"32826759",
"30784059",
"36434808"
] | [
"cDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena.",
"Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena.",
"Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin... | [
2003,
1993,
2003,
2003,
2003,
2002,
1993,
2010,
2020,
2019,
2023
] | 11 | [] | [] | 0 | 0 | null | [
"Opisthokonta"
] | [
178
] | 1 | [] | [] | 0 | true | Conserved_site | Huwentoxin, conserved site-1 | Huwentoxin, conserved site-1 | Huwentoxin_CS1 | 8 |
IPR013141 | 13,141 | Conotoxin-I, conserved site | Conotoxin-I_CS | Conserved_site | 299 | false | false | This entry represents a conserved region characteristic of the I-superfamily of conotoxins. Cone snail toxins, conotoxins, are small peptides with disulphide connectivity, that target ion-channels or G-protein coupled receptors. Based on the number and pattern of disulphide bonds and biological activities, conotoxins c... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS60019"
] | [
"I_CONOTOXIN"
] | [
299
] | 1 | [
"PROSITEDOC"
] | [
"PDOC60004"
] | [
"PROSITEDOC:PDOC60004"
] | 1 | [
"2jry",
"2jtu",
"2p4l",
"6cei",
"9nvh"
] | 5 | [
"PUB00016427",
"PUB00016617",
"PUB00016620",
"PUB00016622",
"PUB00016662",
"PUB00017021",
"PUB00017022",
"PUB00017232"
] | [
"15450929",
"11478951",
"15225557",
"10988292",
"10903392",
"2410412",
"1390774",
"12694387"
] | [
"Novel conopeptides of the I-superfamily occur in several clades of cone snails.",
"Cone venom--from accidental stings to deliberate injection.",
"Toxins in anti-nociception and anti-inflammation.",
"lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and... | [
2004,
2001,
2004,
2000,
2000,
1985,
1992,
2003
] | 8 | [] | [] | 0 | 0 | null | [
"Protostomia"
] | [
299
] | 1 | [] | [] | 0 | true | Conserved_site | Conotoxin-I, conserved site | Conotoxin-I, conserved site | Conotoxin-I_CS | 6 |
IPR013144 | 13,144 | CRA domain | CRA_dom | Domain | 19,356 | false | false | This entry represents the CRA (or CT11-RanBPM) domain, which is a protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) and which is found in Ran-binding proteins such as Ran-binding protein 9 (RanBP9 or RanBPM) and RanBP10. RanBPM is a scaffolding protein important in regulating cellu... | [] | [] | [] | 0 | [
"SMART"
] | [
"SM00757"
] | [
"CRA"
] | [
19356
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-9861718",
"R-DDI-9861718",
"R-DME-9861718",
"R-DRE-5673001",
"R-DRE-8851805",
"R-DRE-9861718",
"R-GGA-9861718",
"R-HSA-373760",
"R-HSA-5673001",
"R-HSA-8851805",
"R-HSA-9861718",
"R-MMU-373760",
"R-MMU-5673001",
"R-MMU-8851805",
"R-MMU-9861718",
"R-RNO-9861718",
"R-SCE-9861718... | [
"REACTOME:R-BTA-9861718",
"REACTOME:R-DDI-9861718",
"REACTOME:R-DME-9861718",
"REACTOME:R-DRE-5673001",
"REACTOME:R-DRE-8851805",
"REACTOME:R-DRE-9861718",
"REACTOME:R-GGA-9861718",
"REACTOME:R-HSA-373760",
"REACTOME:R-HSA-5673001",
"REACTOME:R-HSA-8851805",
"REACTOME:R-HSA-9861718",
"REACTOME... | 22 | [
"6swy",
"7ns3",
"7nsb",
"7nsc",
"7wug",
"8pjn"
] | 6 | [
"PUB00044453"
] | [
"15381419"
] | [
"The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
19356
] | 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... | [
50,
3,
14,
10,
18,
11,
4,
13,
16,
2,
4,
47
] | 12 | true | Domain | CRA domain | CRA domain | CRA_dom | 1 |
IPR013146 | 13,146 | LEM-like domain | LEM-like_dom | Domain | 2,084 | false | false | The LEM (LAP2, emerin, MAN1) domain is a globular module of approximately 40 amino acids, which is mostly found in the nucleoplasmic portions of metazoan inner nuclear membrane proteins. The LEM domain has been shown to mediate binding to BAF (barrier-to-autointegration factor) and BAF-DNA complexes. | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF08198",
"PS50955",
"SM01261"
] | [
"Thymopoietin",
"LEM_LIKE",
"Thymopoietin"
] | [
2009,
1990,
2070
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50954",
"R-HSA-2980766",
"R-HSA-2995383",
"R-HSA-4419969",
"R-HSA-8980692",
"R-HSA-9013106",
"R-HSA-9013148",
"R-HSA-9013149",
"R-HSA-9013404",
"R-HSA-9013405",
"R-HSA-9013408",
"R-HSA-9013409",
"R-HSA-9013423",
"R-HSA-9035034"
] | [
"PROSITEDOC:PDOC50954",
"REACTOME:R-HSA-2980766",
"REACTOME:R-HSA-2995383",
"REACTOME:R-HSA-4419969",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013106",
"REACTOME:R-HSA-9013148",
"REACTOME:R-HSA-9013149",
"REACTOME:R-HSA-9013404",
"REACTOME:R-HSA-9013405",
"REACTOME:R-HSA-9013408",
"REACTOME:... | 14 | [
"1gjj",
"1h9e"
] | 2 | [
"PUB00017332",
"PUB00017333",
"PUB00018424"
] | [
"10671519",
"11435115",
"11500367"
] | [
"MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin.",
"Structural characterization of the LEM motif common to three human inner nuclear membrane proteins.",
"Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LE... | [
2000,
2001,
2001
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
9,
2075
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
27,
4,
6,
7
] | 4 | true | Domain | LEM-like domain | LEM-like domain | LEM-like_dom | 2 |
IPR013147 | 13,147 | CD47-like, transmembrane | CD47-like_TM | Domain | 1,292 | false | false | This entry represents the transmembrane region found at the C-terminal end of Leukocyte surface antigen CD47 proteins from chordates [ ] and CD47-like proteins A38, also known as Protein OPG166, from Poxvirus. Human CD47 is an adhesive protein that mediates cell-to-cell interactions [ , ]. It is involved in signal tran... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF04549"
] | [
"CD47"
] | [
1292
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-202733",
"R-HSA-216083",
"R-HSA-391160",
"R-HSA-6798695",
"R-MMU-202733",
"R-MMU-216083",
"R-MMU-391160",
"R-MMU-6798695",
"R-RNO-202733",
"R-RNO-216083",
"R-RNO-391160",
"R-RNO-6798695",
"R-SSC-202733",
"R-SSC-216083",
"R-SSC-391160",
"R-SSC-6798695"
] | [
"REACTOME:R-HSA-202733",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-391160",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-202733",
"REACTOME:R-MMU-216083",
"REACTOME:R-MMU-391160",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-202733",
"REACTOME:R-RNO-216083",
"REACTOME:R-RNO-391160",
"REACTOME:R-RNO-6... | 16 | [
"7myz",
"7wn8"
] | 2 | [
"PUB00017115",
"PUB00017128",
"PUB00088077",
"PUB00095391",
"PUB00103704",
"PUB00103705",
"PUB00103706",
"PUB00103707",
"PUB00103712"
] | [
"8794870",
"12124426",
"15383453",
"8551630",
"19004835",
"11509594",
"32679764",
"27742621",
"34471125"
] | [
"Integrin-associated protein immunoglobulin domain is necessary for efficient vitronectin bead binding.",
"Expression of CD47/integrin-associated protein induces death of cultured cerebral cortical neurons.",
"Adhesion of human T cells to antigen-presenting cells through SIRPbeta2-CD47 interaction costimulates ... | [
1996,
2002,
2005,
1996,
2009,
2001,
2020,
2017,
2021
] | 9 | [] | [] | 0 | 0 | null | [
"Amniota",
"Chordopoxvirinae"
] | [
1183,
109
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
10,
12
] | 3 | true | Domain | CD47-like, transmembrane | CD47-like, transmembrane | CD47-like_TM | 3 |
IPR013148 | 13,148 | Glycosyl hydrolase family 32, N-terminal | Glyco_hydro_32_N | Domain | 30,008 | false | false | This domain corresponds to the N-terminal domain of glycosyl transferase family 32 which forms a five bladed β propeller structure [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00251"
] | [
"Glyco_hydro_32N"
] | [
30008
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"3.2.1",
"3.2.1.26",
"PWY-8314"
] | [
"EC:3.2.1",
"EC:3.2.1.26",
"METACYC:PWY-8314"
] | 3 | [
"1st8",
"1uyp",
"1w2t",
"1y4w",
"1y9g",
"1y9m",
"2ac1",
"2add",
"2ade",
"2aey",
"2aez",
"2oxb",
"2qqu",
"2qqv",
"2qqw",
"2xqr",
"3kf3",
"3kf5",
"3lf7",
"3lfi",
"3pig",
"3pij",
"3rwk",
"3sc7",
"3u14",
"3u75",
"3ugf",
"3ugg",
"3ugh",
"4eqv",
"4fff",
"4ffg"... | 79 | [
"PUB00017131"
] | [
"14973124"
] | [
"The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Viruses",
"metagenomes"
] | [
17404,
12298,
151,
5,
150
] | 5 | [
"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"
] | [
52,
2,
53,
1,
2,
65
] | 6 | true | Domain | Glycosyl hydrolase family 32, N-terminal | Glycosyl hydrolase family 32, N-terminal | Glyco_hydro_32_N | 5 |
IPR013149 | 13,149 | Alcohol dehydrogenase-like, C-terminal | ADH-like_C | Domain | 383,749 | false | false | This entry represents the cofactor-binding domain in alcohol dehydrogenases, which is normally found towards the C-terminal. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) [ , , ]. This entry also includes NADP-dependent quinone oxidoreductase ( ), an enzyme found in bac... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00107"
] | [
"ADH_zinc_N"
] | [
383749
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"1.1.1",
"GenProp1220",
"GenProp1226",
"GenProp1228",
"GenProp1245",
"GenProp1267",
"GenProp1342",
"GenProp1425",
"GenProp1497",
"GenProp1527",
"GenProp1696",
"GenProp1715",
"GenProp1722",
"GenProp1762",
"R-BTA-5652227",
"R-BTA-5661270",
"R-BTA-71384",
"R-CEL-2161541",
"R-CEL-536... | [
"EC:1.1.1",
"GP:GenProp1220",
"GP:GenProp1226",
"GP:GenProp1228",
"GP:GenProp1245",
"GP:GenProp1267",
"GP:GenProp1342",
"GP:GenProp1425",
"GP:GenProp1497",
"GP:GenProp1527",
"GP:GenProp1696",
"GP:GenProp1715",
"GP:GenProp1722",
"GP:GenProp1762",
"REACTOME:R-BTA-5652227",
"REACTOME:R-BT... | 72 | [
"1a71",
"1a72",
"1adb",
"1adc",
"1adf",
"1adg",
"1agn",
"1axe",
"1axg",
"1bto",
"1bxz",
"1cdo",
"1d1s",
"1d1t",
"1deh",
"1e3e",
"1e3i",
"1e3j",
"1e3l",
"1ee2",
"1f8f",
"1gu7",
"1guf",
"1gyr",
"1h0k",
"1h2b",
"1hdx",
"1hdy",
"1hdz",
"1het",
"1heu",
"1hf3"... | 440 | [
"PUB00001354",
"PUB00001655",
"PUB00001658",
"PUB00003420",
"PUB00022446",
"PUB00027598",
"PUB00028130"
] | [
"3622514",
"8486156",
"8504864",
"1593644",
"12962626",
"12627956",
"7602590"
] | [
"Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases.",
"Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.",
"Dual relationships of xylitol and alcohol dehydrogenases in families of two ... | [
1987,
1993,
1993,
1992,
2003,
2003,
1995
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4516,
245647,
130136,
30,
3420
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
173,
13,
30,
6,
18,
53,
33,
27,
106,
62,
17,
11,
202
] | 13 | true | Domain | Alcohol dehydrogenase-like, C-terminal | Alcohol dehydrogenase-like, C-terminal | ADH-like_C | 6 |
IPR013150 | 13,150 | Transcription factor TFIIB, cyclin-like domain | TFIIB_cyclin | Domain | 18,258 | false | false | In eukaryotes, transcription initiation of all protein encoding genes involves the polymerase II system. This sytem is modulated by both general and specific transcription factors. The general factors (which include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIG and TFIIH) operate through common promoter elements, such as th... | [
"GO:0017025"
] | [
"TBP-class protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF00382"
] | [
"TFIIB"
] | [
18258
] | 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-674695",
"R-CEL-6807505",
"R-CEL-73776",
"R-CEL-73779",
"R-CEL-75953",
"R-CEL-76042",
"R-DDI-674695",
"R-DDI-6807505",
"R-DDI-73776",
"R-DDI-73779",
"R-DDI-75953",
"R-DDI-76042",
"R-DME-674695",
"R-DME-6807505",
"R-DME-73776",
"R-DME-73779",
"R-DME-75953",
"R-DME-76042",
"... | [
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6807505",
"REACTOME:R-CEL-73776",
"REACTOME:R-CEL-73779",
"REACTOME:R-CEL-75953",
"REACTOME:R-CEL-76042",
"REACTOME:R-DDI-674695",
"REACTOME:R-DDI-6807505",
"REACTOME:R-DDI-73776",
"REACTOME:R-DDI-73779",
"REACTOME:R-DDI-75953",
"REACTOME:R-DDI-76042",
... | 59 | [
"1ais",
"1c9b",
"1d3u",
"1tfb",
"1vol",
"2phg",
"3k7a",
"4bbr",
"4bbs",
"4roc",
"4rod",
"4roe",
"4v1n",
"4v1o",
"5fmf",
"5fyw",
"5fz5",
"5iy6",
"5iy7",
"5iy8",
"5iy9",
"5iya",
"5iyb",
"5iyc",
"5iyd",
"5oqj",
"5oqm",
"5sva",
"5wh1",
"6cnb",
"6cnc",
"6cnd"... | 103 | [
"PUB00004101",
"PUB00004866",
"PUB00005378",
"PUB00021313",
"PUB00023347"
] | [
"1876184",
"7597027",
"1949150",
"10619841",
"9177165"
] | [
"Cloning of a human gene encoding the general transcription initiation factor IIB.",
"Transcription in archaea: similarity to that in eucarya.",
"Transcriptional activation: enter TFIIB.",
"Structural basis of preinitiation complex assembly on human pol II promoters.",
"The 2.1-A crystal structure of an arc... | [
1991,
1995,
1991,
2000,
1997
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
4677,
10,
13051,
76,
444
] | 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... | [
52,
3,
8,
5,
14,
6,
2,
21,
8,
2,
2,
48
] | 12 | true | Domain | Transcription factor TFIIB, cyclin-like domain | Transcription factor TFIIB, cyclin-like domain | TFIIB_cyclin | 4 |
IPR013151 | 13,151 | Immunoglobulin-like beta-sandwich domain | Immunoglobulin_dom | Domain | 51,746 | false | false | This entry represents the immunoglobulin-like domain that is found in a number of proteins with diverse functions. Examples include T-cell surface glycoprotein CD4, Neurotrimin, Interleukin-1 receptor accessory protein-like 1, Receptor tyrosine kinases among others. Immunoglobulin-like domains may be involved in protei... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00047"
] | [
"ig"
] | [
51746
] | 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-114608",
"R-BTA-163125",
"R-BTA-6798695",
"R-CEL-114608",
"R-CFA-1257604",
"R-CFA-1433557",
"R-CFA-1433559",
"R-CFA-202424",
"R-CFA-202427",
"R-CFA-202430",
"R-CFA-202433",
"R-CFA-389948",
"R-CFA-449836",
"R-CFA-5673001",
"R-CFA-5690714",
"R-CFA-6811558",
"R-CFA-8856825",
"R... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-163125",
"REACTOME:R-BTA-6798695",
"REACTOME:R-CEL-114608",
"REACTOME:R-CFA-1257604",
"REACTOME:R-CFA-1433557",
"REACTOME:R-CFA-1433559",
"REACTOME:R-CFA-202424",
"REACTOME:R-CFA-202427",
"REACTOME:R-CFA-202430",
"REACTOME:R-CFA-202433",
"REACTOME:R-CFA... | 344 | [
"1b6u",
"1cdh",
"1cdi",
"1cdj",
"1cdu",
"1cdy",
"1efx",
"1g9m",
"1g9n",
"1gc1",
"1im9",
"1jl4",
"1m4k",
"1n26",
"1nkr",
"1olz",
"1ovz",
"1ow0",
"1r70",
"1rzj",
"1rzk",
"1uct",
"1wio",
"1wip",
"1wiq",
"1zvo",
"2b4c",
"2c9a",
"2ckn",
"2cr3",
"2dl2",
"2dli"... | 221 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"marine sediment metagenome"
] | [
25,
51409,
311,
1
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
191,
50,
1083,
201,
223
] | 6 | true | Domain | Immunoglobulin-like beta-sandwich domain | Immunoglobulin-like beta-sandwich domain | Immunoglobulin_dom | 2 |
IPR013152 | 13,152 | Gastrin/cholecystokinin, conserved site | Gastrin/cholecystokinin_CS | Conserved_site | 1,810 | false | false | Gastrin and cholecystokinin (CCK) are structurally and functionally related peptide hormones that function as hormonal regulators of various digestive processes and feeding behaviours. They are known to induce gastric secretion, stimulate pancreatic secretion, increase blood circulation and water secretion in the stoma... | [] | [] | [] | 0 | [
"PROSITE"
] | [
"PS00259"
] | [
"GASTRIN"
] | [
1810
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00232",
"R-BTA-375276",
"R-BTA-416476",
"R-BTA-881907",
"R-CFA-416476",
"R-CFA-881907",
"R-HSA-375276",
"R-HSA-416476",
"R-HSA-881907",
"R-MMU-375276",
"R-MMU-416476",
"R-MMU-881907",
"R-RNO-375276",
"R-RNO-416476",
"R-RNO-881907",
"R-SSC-375276",
"R-SSC-416476"
] | [
"PROSITEDOC:PDOC00232",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-881907",
"REACTOME:R-CFA-416476",
"REACTOME:R-CFA-881907",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-881907",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-8819... | 17 | [
"1d6g",
"5wrj",
"7ezh",
"7ezk",
"7ezm",
"7f8v",
"7f8w",
"7mbx",
"7mby",
"7xou",
"7xow",
"8ia7",
"9bkj",
"9bkk"
] | 14 | [
"PUB00000180",
"PUB00001548",
"PUB00002432",
"PUB00002458",
"PUB00002602",
"PUB00005098"
] | [
"3778455",
"3743781",
"3753978",
"2842322",
"2303439",
"3749893"
] | [
"Leucosulfakinin-II, a blocked sulfated insect neuropeptide with homology to cholecystokinin and gastrin.",
"Isolation from chicken antrum, and primary amino acid sequence of a novel 36-residue peptide of the gastrin/CCK family.",
"Sequence of preprocaerulein cDNAs cloned from skin of Xenopus laevis. A small fa... | [
1986,
1986,
1986,
1988,
1990,
1986
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Bilateria",
"Halorubrum ezzemoulense"
] | [
16,
1793,
1
] | 3 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
2,
4,
3,
5
] | 5 | true | Conserved_site | Gastrin/cholecystokinin, conserved site | Gastrin/cholecystokinin, conserved site | Gastrin/cholecystokinin_CS | 7 |
IPR013153 | 13,153 | PrkA, AAA domain | Prk_AAA | Domain | 8,239 | false | false | This entry represents the N-terminal AAA domain [ ] in PrkA proteins. ATP-dependent protease PrkA proteins are bacterial and archaeal serine kinases, approximately 630 residues in length. They possesses the A-motif of nucleotide-binding proteins and exhibit distant homology to eukaryotic protein kinases [ ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08298",
"SM00763"
] | [
"AAA_PrkA",
"AAA_PrkA"
] | [
8128,
8061
] | 2 | [
"EC"
] | [
"2.7.11.1"
] | [
"EC:2.7.11.1"
] | 1 | [] | 0 | [
"PUB00012839"
] | [
"8626065"
] | [
"Cloning and characterization of the Bacillus subtilis prkA gene encoding a novel serine protein kinase."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine phage"
] | [
602,
7547,
19,
70,
1
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | PrkA, AAA domain | PrkA, AAA domain | Prk_AAA | 8 |
IPR013154 | 13,154 | Alcohol dehydrogenase-like, N-terminal | ADH-like_N | Domain | 439,160 | false | false | This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc-binding domain. This domain has a GroES-like structure, a name derived from the superfamily of proteins with a GroES fold. Proteins with a GroES fold structure have a highly conserved hydrophobic core and a glycyl-aspartate di... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08240"
] | [
"ADH_N"
] | [
439160
] | 1 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"GenProp1226",
"GenProp1228",
"GenProp1245",
"GenProp1267",
"GenProp1342",
"GenProp1425",
"GenProp1497",
"GenProp1527",
"GenProp1715",
"GenProp1722",
"GenProp1762",
"R-BTA-5652227",
"R-BTA-5661270",
"R-BTA-71384",
"R-CEL-2161541",
"R-CEL-5365859",
"R-CEL-71384",
"R-CEL-77346",
"R... | [
"GP:GenProp1226",
"GP:GenProp1228",
"GP:GenProp1245",
"GP:GenProp1267",
"GP:GenProp1342",
"GP:GenProp1425",
"GP:GenProp1497",
"GP:GenProp1527",
"GP:GenProp1715",
"GP:GenProp1722",
"GP:GenProp1762",
"REACTOME:R-BTA-5652227",
"REACTOME:R-BTA-5661270",
"REACTOME:R-BTA-71384",
"REACTOME:R-CE... | 66 | [
"1a71",
"1a72",
"1adb",
"1adc",
"1adf",
"1adg",
"1agn",
"1axe",
"1axg",
"1bto",
"1bxz",
"1cdo",
"1d1s",
"1d1t",
"1deh",
"1e3e",
"1e3i",
"1e3j",
"1e3l",
"1ee2",
"1f8f",
"1gu7",
"1guf",
"1gyr",
"1h0k",
"1h2b",
"1hdx",
"1hdy",
"1hdz",
"1het",
"1heu",
"1hf3"... | 421 | [
"PUB00001354",
"PUB00001655",
"PUB00001658",
"PUB00003420",
"PUB00015341",
"PUB00017153"
] | [
"3622514",
"8486156",
"8504864",
"1593644",
"8804825",
"10556240"
] | [
"Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases.",
"Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic.",
"Dual relationships of xylitol and alcohol dehydrogenases in families of two ... | [
1987,
1993,
1993,
1992,
1996,
1999
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5068,
286264,
144264,
33,
3531
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
122,
11,
31,
10,
16,
58,
45,
34,
117,
65,
19,
9,
182
] | 13 | true | Domain | Alcohol dehydrogenase-like, N-terminal | Alcohol dehydrogenase-like, N-terminal | ADH-like_N | 4 |
IPR013155 | 13,155 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | M/V/L/I-tRNA-synth_anticd-bd | Domain | 118,238 | false | false | This domain is found methionyl, valyl, leucyl and isoleucyl tRNA synthetases. It binds to the anticodon of the tRNA. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These e... | [
"GO:0004812",
"GO:0006418"
] | [
"aminoacyl-tRNA ligase activity",
"tRNA aminoacylation for protein translation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF08264"
] | [
"Anticodon_1"
] | [
118238
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.1.1",
"R-DDI-9837999",
"R-DDI-9856649",
"R-HSA-2408522",
"R-HSA-379716",
"R-HSA-379726",
"R-HSA-9837999",
"R-HSA-9856649",
"R-MMU-9837999",
"R-MMU-9856649",
"R-SCE-9837999",
"R-SPO-9837999"
] | [
"EC:6.1.1",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DDI-9856649",
"REACTOME:R-HSA-2408522",
"REACTOME:R-HSA-379716",
"REACTOME:R-HSA-379726",
"REACTOME:R-HSA-9837999",
"REACTOME:R-HSA-9856649",
"REACTOME:R-MMU-9837999",
"REACTOME:R-MMU-9856649",
"REACTOME:R-SCE-9837999",
"REACTOME:R-SPO-9837999"... | 12 | [
"1ffy",
"1gax",
"1h3n",
"1ile",
"1ivs",
"1iyw",
"1jzq",
"1jzs",
"1obc",
"1obh",
"1qu2",
"1qu3",
"1wkb",
"1wz2",
"2bte",
"2byt",
"2csx",
"2ct8",
"2v0c",
"2v0g",
"3zgz",
"3ziu",
"3zjt",
"3zju",
"3zjv",
"4aq7",
"4arc",
"4ari",
"4as1",
"4cqn",
"4qrd",
"4qre"... | 106 | [
"PUB00000386",
"PUB00000723",
"PUB00004391",
"PUB00005365",
"PUB00006477",
"PUB00007191",
"PUB00007363",
"PUB00079872",
"PUB00079873"
] | [
"8364025",
"8274143",
"1852601",
"2053131",
"10673435",
"2203971",
"10447505",
"10704480",
"12458790"
] | [
"Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.",
"The aminoacyl-tRNA synthetase family: modules at work.",
"Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.",
"Classes of aminoacyl-tRNA synthetases and the establ... | [
1993,
1993,
1991,
1991,
2000,
1990,
1999,
2000,
2002
] | 9 | [] | [
"IPR033705",
"IPR033708",
"IPR033709"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
3132,
84832,
28098,
63,
2113
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
40,
9,
7,
12,
3,
61,
20,
5,
33,
19,
4,
6,
88
] | 13 | true | Domain | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding | M/V/L/I-tRNA-synth_anticd-bd | 9 |
IPR013156 | 13,156 | Pseudin antimicrobial peptide | Antimicrobial_19 | Family | 6 | false | false | Pseudins are a subfamily of the FSAP family (Frog Secreted Active Peptides) extracted from the skin of the paradoxical frog Pseudis paradoxa. The pseudins belong to the class of cationic, amphipathic-helical antimicrobial peptides [ ]. | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08225"
] | [
"Antimicrobial19"
] | [
6
] | 1 | [] | [] | [] | 0 | [
"2ncx",
"2ncy"
] | 2 | [
"PUB00017169"
] | [
"11689009"
] | [
"Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Aquirufa beregesia",
"Pseudis"
] | [
1,
5
] | 2 | [] | [] | 0 | true | Family | Pseudin antimicrobial peptide | Pseudin antimicrobial peptide | Antimicrobial_19 | 6 |
IPR013157 | 13,157 | Aurein antibiotic peptide family | Aurein_antimicrobial_peptide | Family | 26 | false | false | This family of antibacterial peptides are secreted from the granular dorsal glands of Litoria aurea (Green and golden bell frog), Litoria raniformis (Southern bell frog), Litoria citropa (Australian blue mountains tree frog) and frogs from genus Uperoleia. They are a part of the FSAP peptide family. Amongst the more ac... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08256"
] | [
"Antimicrobial20"
] | [
26
] | 1 | [] | [] | [] | 0 | [
"1vm4",
"1vm5",
"5mxl",
"6gs9",
"7qv6",
"9hgb",
"9hgl",
"9hgt",
"9hi8",
"9hid",
"9hpp"
] | 11 | [
"PUB00017125",
"PUB00017157"
] | [
"10951191",
"10504394"
] | [
"The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.",
"Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide ... | [
2000,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Neobatrachia"
] | [
26
] | 1 | [] | [] | 0 | true | Family | Aurein antibiotic peptide family | Aurein antibiotic peptide family | Aurein_antimicrobial_peptide | 6 |
IPR013158 | 13,158 | Activation-induced cytidine deaminase AID | AID | Domain | 916 | false | false | This entry represents Activation-induced cytidine deaminase (AID), which is a single-stranded DNA-specific cytidine deaminase. It is involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes by deaminating C to U during transcription of Ig-variable and Ig-switch region DNA. It ... | [
"GO:0008270",
"GO:0016814"
] | [
"zinc ion binding",
"hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF08210"
] | [
"AID"
] | [
916
] | 1 | [
"EC",
"REACTOME"
] | [
"3.5.4.38",
"R-HSA-9821002"
] | [
"EC:3.5.4.38",
"REACTOME:R-HSA-9821002"
] | 2 | [
"5jj4",
"5w0r",
"5w0u",
"5w0z",
"5w1c"
] | 5 | [
"PUB00017103",
"PUB00088593",
"PUB00091285",
"PUB00161717",
"PUB00161722"
] | [
"12683974",
"26608778",
"29555751",
"27283515",
"12692563"
] | [
"Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.",
"DNA Editing by APOBECs: A Genomic Preserver and Transformer.",
"Diversification of AID/APOBEC-like deaminases in metazoa: multiplicity of clades and widespread roles in immunity.",
"The APOBEC Protein ... | [
2003,
2016,
2018,
2016,
2003
] | 5 | [
"IPR002125"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
916
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
18,
13,
4
] | 4 | true | Domain | Activation-induced cytidine deaminase AID | Activation-induced cytidine deaminase AID | AID | 1 |
IPR013162 | 13,162 | CD80-like, immunoglobulin C2-set | CD80_C2-set | Domain | 43,753 | false | false | This entry represents the C2-set type domains found in the T-cell antigen CD80, as well as in related proteins. CD80 (B7-1) is a glycoprotein expressed on antigen-presenting cells [ ]. The shared ligands on CD80 and CD86 (B7-2) deliver the co-stimulatory signal through CD28 and CTLA-4 on T-cells, where CD28 augments th... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08205"
] | [
"C2-set_2"
] | [
43753
] | 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-198933",
"R-CEL-373753",
"R-DME-373753",
"R-DME-418990",
"R-DME-420597",
"R-DRE-198933",
"R-DRE-418990",
"R-DRE-420597",
"R-GGA-2132263",
"R-GGA-2132286",
"R-HSA-1257604",
"R-HSA-193634",
"R-HSA-198933",
"R-HSA-210991",
"R-HSA-2172127",
"R-HSA-2219530",
"R-HSA-373753",
"R-HS... | [
"REACTOME:R-BTA-198933",
"REACTOME:R-CEL-373753",
"REACTOME:R-DME-373753",
"REACTOME:R-DME-418990",
"REACTOME:R-DME-420597",
"REACTOME:R-DRE-198933",
"REACTOME:R-DRE-418990",
"REACTOME:R-DRE-420597",
"REACTOME:R-GGA-2132263",
"REACTOME:R-GGA-2132286",
"REACTOME:R-HSA-1257604",
"REACTOME:R-HSA-... | 89 | [
"1dgi",
"1dr9",
"1i8l",
"1nn8",
"2pet",
"2pf6",
"3alp",
"3bik",
"3bis",
"3cjj",
"3epc",
"3epd",
"3epf",
"3fn3",
"3j8f",
"3j9f",
"3o3u",
"3sbw",
"3sku",
"3u82",
"3u83",
"3uro",
"4bfe",
"4bfg",
"4bfi",
"4fmf",
"4fmk",
"4fn0",
"4fom",
"4fqp",
"4frw",
"4fs0"... | 87 | [
"PUB00010610",
"PUB00014840",
"PUB00015110",
"PUB00021423",
"PUB00025943",
"PUB00027656"
] | [
"11377196",
"9417933",
"15327963",
"10661405",
"11279502",
"10698639"
] | [
"Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state.",
"Sequence profiles of immunoglobulin and immunoglobulin-like domains.",
"Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and ot... | [
2001,
1997,
2004,
2000,
2001,
2000
] | 6 | [
"IPR007110"
] | [
"IPR033320",
"IPR037676",
"IPR041850"
] | 1 | 3 | 0 | [
"Metazoa",
"Orthoherpesviridae"
] | [
43654,
99
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
9,
228,
82,
134,
98,
126
] | 6 | true | Domain | CD80-like, immunoglobulin C2-set | CD80-like, immunoglobulin C2-set | CD80_C2-set | 6 |
IPR013164 | 13,164 | Cadherin, N-terminal | Cadherin_N | Domain | 36,928 | false | false | Cadherins are a family of adhesion molecules that mediate Ca2+-dependent cell-cell adhesion in all solid tissues of the organism which modulate a wide variety of processes including cell polarisation and migration [ , ]. Cadherin-mediated cell-cell junctions are formed as a result of interaction between extracellular d... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08266"
] | [
"Cadherin_2"
] | [
36928
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-114608",
"R-HSA-8980692",
"R-HSA-9013026",
"R-HSA-9830364"
] | [
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-8980692",
"REACTOME:R-HSA-9013026",
"REACTOME:R-HSA-9830364"
] | 4 | [
"1wuz",
"1wyj",
"4zi8",
"4zi9",
"4zpl",
"4zpm",
"4zpn",
"4zpo",
"4zpp",
"4zpq",
"4zps",
"5dzv",
"5dzw",
"5dzx",
"5dzy",
"5iu9",
"5k8r",
"5szl",
"5szm",
"5szn",
"5szo",
"5szp",
"5t9t",
"6bx7",
"6e6b",
"6meq",
"6mer",
"6mga",
"6vfp",
"6vfq",
"6vfr",
"6vft"... | 43 | [
"PUB00000071",
"PUB00007174",
"PUB00014193"
] | [
"2197976",
"11736639",
"14570569"
] | [
"Cadherins: a molecular family important in selective cell-cell adhesion.",
"Structure and functions of classical cadherins.",
"Cadherins as modulators of cellular phenotype."
] | [
1990,
2001,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Desulfobacca acetoxidans",
"Eumetazoa"
] | [
1,
36927
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
157,
134,
179,
162
] | 4 | true | Domain | Cadherin, N-terminal | Cadherin, N-terminal | Cadherin_N | 1 |
IPR013166 | 13,166 | Citrate lyase ligase, C-terminal | Citrate_lyase_ligase_C | Domain | 3,384 | false | false | [Citrate (pro-3S)-lyase] ligase ( ), also known as citrate lyase ligase, is responsible for acetylation of the prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase. It converts the inactive thiol form of the enzyme to the active form. In Clostridium sphenoides, citrate ... | [
"GO:0008771"
] | [
"[citrate (pro-3S)-lyase] ligase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF08218",
"SM00764"
] | [
"Citrate_ly_lig",
"Citrate_ly_lig"
] | [
3279,
3346
] | 2 | [] | [] | [] | 0 | [
"3x1j",
"3x1k",
"3x1m",
"4ruk",
"5ts2",
"5x6f"
] | 6 | [
"PUB00044603"
] | [
"3935436"
] | [
"Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation."
] | [
1985
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3365,
3,
16
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Citrate lyase ligase, C-terminal | Citrate lyase ligase, C-terminal | Citrate_lyase_ligase_C | 2 |
IPR013167 | 13,167 | COG4 transport protein, middle alpha-helical bundle | COG4_M | Domain | 5,135 | false | false | COG4 is a component of the conserved oligomeric Golgi (COG) complex which mediates the proper glycosylation of proteins trafficking through the Golgi apparatus. It is included in the CATCHR (complexes associated with tethering containing helical rods) family, which includes components of the exocyst, GARP, and DSL1 com... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08318",
"SM00762"
] | [
"COG4_m",
"Cog4"
] | [
5130,
4807
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-6807878",
"R-BTA-6811438",
"R-BTA-6811440",
"R-CEL-6807878",
"R-CEL-6811438",
"R-DDI-6807878",
"R-DDI-6811438",
"R-DME-6807878",
"R-DME-6811438",
"R-DME-6811440",
"R-HSA-6807878",
"R-HSA-6811438",
"R-HSA-6811440",
"R-MMU-6807878",
"R-MMU-6811438",
"R-MMU-6811440"
] | [
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811438",
"REACTOME:R-BTA-6811440",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811438",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-6811438",
"REACTOME:R-DME-6807878",
"REACTOME:R-DME-6811438",
"REACTOME:R-DME-6811440",
"REACTOME:R-HSA-6807878",
"REACTOM... | 16 | [] | 0 | [
"PUB00017118",
"PUB00053070",
"PUB00100040",
"PUB00100047",
"PUB00100076"
] | [
"12006647",
"19651599",
"28098232",
"34061181",
"30290151"
] | [
"Identification of Sec36p, Sec37p, and Sec38p: components of yeast complex that contains Sec34p and Sec35p.",
"Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.",
"Crystal structure of Sec10, a subunit of the exocyst complex.",
"Homology and Modular Evolution of CATCHR a... | [
2002,
2009,
2017,
2021,
2018
] | 5 | [] | [] | 0 | 0 | null | [
"Bathymodiolus azoricus thioautotrophic gill symbiont",
"Eukaryota"
] | [
1,
5134
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
1,
1,
1,
13,
4,
1,
3,
4,
1,
1,
12
] | 12 | true | Domain | COG4 transport protein, middle alpha-helical bundle | COG4 transport protein, middle alpha-helical bundle | COG4_M | 4 |
IPR013168 | 13,168 | Cpl-7 lysozyme, C-terminal | Cpl_7_lyso_C | Domain | 928 | false | false | This domain was originally found in the C-terminal moiety of the Cp-7 lysin (lysozyme, ) encoded by Bacteriophage Cp-7 [ ]. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif [ ]. | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08230",
"SM01095"
] | [
"CW_7",
"Cpl-7"
] | [
914,
880
] | 2 | [] | [] | [] | 0 | [
"4cvd",
"5i8l"
] | 2 | [
"PUB00085046",
"PUB00085047"
] | [
"23056389",
"20720016"
] | [
"Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.",
"Cpl-7, a lysozyme encoded by a pneumococcal bacteriophage with a novel cell wall-binding motif."
] | [
2012,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"organismal metagenomes"
] | [
816,
5,
105,
2
] | 4 | [] | [] | 0 | true | Domain | Cpl-7 lysozyme, C-terminal | Cpl-7 lysozyme, C-terminal | Cpl_7_lyso_C | 3 |
IPR013169 | 13,169 | mRNA splicing factor Cwf18-like | mRNA_splic_Cwf18-like | Family | 3,948 | false | false | The cwf18 family is involved in mRNA splicing. It has been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe (Fission yeast) [ ]. This entry also includes Ccdc12 from animals and RXLR100 from Plasmopara viticola [ ]. | [] | [] | [] | 0 | [
"PFAM",
"PANTHER"
] | [
"PF08315",
"PTHR31551"
] | [
"cwf18",
""
] | [
3945,
3791
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-72163",
"R-MMU-72163",
"R-SPO-72163"
] | [
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-SPO-72163"
] | 3 | [
"8ro0",
"8ro1",
"8ro2",
"9fmd",
"9l5r",
"9l5s",
"9l5t"
] | 7 | [
"PUB00008533",
"PUB00094750"
] | [
"11884590",
"29706971"
] | [
"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.",
"In Planta Functional Analysis and Subcellular Localization of the Oomycete Pathogen Plasmopara viticola Candidate RXLR Effector Repertoi... | [
2002,
2018
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
3948
] | 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... | [
3,
1,
1,
2,
7,
3,
1,
2,
4,
1,
2
] | 11 | true | Family | mRNA splicing factor Cwf18-like | mRNA splicing factor Cwf18-like | mRNA_splic_Cwf18-like | 5 |
IPR013170 | 13,170 | mRNA splicing factor Cwf21 domain | mRNA_splic_Cwf21_dom | Domain | 9,300 | false | false | The cwf21 domain is found in proteins involved in mRNA splicing. Proteins containing this domain have been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe (Fission yeast) [ ]. In yeast, this domain binds the protein Prp8p [ ], a large and highly conserved U5 snRNP protein which has been proposed... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08312",
"SM01115"
] | [
"cwf21",
"cwf21"
] | [
8682,
8185
] | 2 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-72163",
"R-MMU-72163"
] | [
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163"
] | 2 | [
"2e62",
"5gm6",
"5gmk",
"5lj3",
"5lj5",
"5mps",
"5mq0",
"5mqf",
"5wsg",
"5xjc",
"5ylz",
"5yzg",
"5z56",
"5z57",
"6bk8",
"6exn",
"6ff4",
"6ff7",
"6icz",
"6j6g",
"6j6h",
"6j6n",
"6j6q",
"6zym",
"7a5p",
"7b9v",
"7dco",
"7dvq",
"7qtt",
"7w59",
"7w5a",
"7w5b"... | 46 | [
"PUB00008533",
"PUB00053973",
"PUB00053974"
] | [
"11884590",
"11017191",
"19854871"
] | [
"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.",
"The question remains: is the spliceosome a ribozyme?",
"Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300... | [
2002,
2000,
2009
] | 3 | [] | [
"IPR047488",
"IPR047489",
"IPR047490",
"IPR047491"
] | 0 | 4 | 0 | [
"Eukaryota",
"Nesterenkonia flava",
"bird metagenome"
] | [
9298,
1,
1
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
13,
1,
26,
10,
11,
9,
1,
9,
15,
1,
1,
52
] | 12 | true | Domain | mRNA splicing factor Cwf21 domain | mRNA splicing factor Cwf21 domain | mRNA_splic_Cwf21_dom | 9 |
IPR013172 | 13,172 | Bomanin | Bomanin | Family | 231 | false | false | Drosophila immune-induced molecules (DIMs), also know as bomanins, are short proteins induced during the immune response of Drosophila [ , ]. The Bomanins (Boms) are a family of a dozen secreted peptides, this entry includes Bomanin Short 1-3/5/6, Bomanin Bicipital 1, and Bomanin Tailed2 which play a role in resistance... | [
"GO:0006952"
] | [
"defense response"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08194"
] | [
"DIM"
] | [
231
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00017165",
"PUB00093706",
"PUB00093707"
] | [
"9736738",
"25915418",
"29920489"
] | [
"Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study.",
"An effector Peptide family required for Drosophila toll-mediated immunity.",
"Short-Form Bomanins Mediate Humoral Immunity in Drosophila."
... | [
1998,
2015,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
3,
228
] | 2 | [
"Drosophila melanogaster"
] | [
16
] | 1 | true | Family | Bomanin | Bomanin | Bomanin | 3 |
IPR013173 | 13,173 | DNA primase DnaG, DnaB-binding domain | DNA_primase_DnaG_DnaB-bd_dom | Domain | 9,951 | false | false | Eubacterial DnaG primases interact with several factors to form the replisome. One of these factors is DnaB, a helicase. This domain has been demonstrated to be responsible for the interaction between DnaG and DnaB [ ]. This domain has a multi-helical structure that forms an orthogonal bundle [ ]. | [
"GO:0006269"
] | [
"DNA replication, synthesis of primer"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF08278",
"SM00766"
] | [
"DnaG_DnaB_bind",
"DnaG_DnaB_bind"
] | [
9464,
8875
] | 2 | [
"EC"
] | [
"2.7.7.101"
] | [
"EC:2.7.7.101"
] | 1 | [
"1t3w",
"2haj",
"4im9",
"5z51",
"6cbr",
"6cbs",
"6cbt",
"7t22",
"9eco"
] | 9 | [
"PUB00017119",
"PUB00031319"
] | [
"8308039",
"15649896"
] | [
"Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork.",
"Crystal and solution structures of the helicase-binding domain of Escherichia coli primase."
] | [
1994,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Peduoviridae",
"unclassified sequences"
] | [
9739,
7,
2,
203
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | DNA primase DnaG, DnaB-binding domain | DNA primase DnaG, DnaB-binding domain | DNA_primase_DnaG_DnaB-bd_dom | 6 |
IPR013174 | 13,174 | Dolichol-phosphate mannosyltransferase subunit 3 | DPM3 | Family | 3,440 | false | false | This family corresponds to subunit 3 of dolichol-phosphate mannosyltransferase, an enzyme which generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation. DPM3 is an integral membrane protein and plays a role in stabilising the dolichol-phosphate mannosyl transferase compl... | [
"GO:0009101"
] | [
"glycoprotein biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"PANTHER"
] | [
"PF08285",
"PTHR16433"
] | [
"DPM3",
""
] | [
3434,
3194
] | 2 | [
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp1455",
"R-BTA-162699",
"R-HSA-162699",
"R-HSA-4717374",
"R-HSA-4719360",
"R-HSA-4719377",
"R-MMU-162699"
] | [
"GP:GenProp1455",
"REACTOME:R-BTA-162699",
"REACTOME:R-HSA-162699",
"REACTOME:R-HSA-4717374",
"REACTOME:R-HSA-4719360",
"REACTOME:R-HSA-4719377",
"REACTOME:R-MMU-162699"
] | 7 | [] | 0 | [
"PUB00017132"
] | [
"10835346"
] | [
"Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Paludibacter jiangxiensis"
] | [
3439,
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... | [
3,
1,
1,
2,
6,
1,
1,
3,
2,
1,
6
] | 11 | true | Family | Dolichol-phosphate mannosyltransferase subunit 3 | Dolichol-phosphate mannosyltransferase subunit 3 | DPM3 | 2 |
IPR013175 | 13,175 | INO80 complex, subunit Ies4 | INO80_su_Ies4 | Family | 1,115 | false | false | The INO80 ATPase is a member of the SNF2 family of ATPases and functions as an integral component of a multisubunit ATP-dependent chromatin remodelling complex. This family of proteins corresponds to the fungal Ies4 subunit of INO80. | [
"GO:0006338",
"GO:0031011"
] | [
"chromatin remodeling",
"Ino80 complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PFAM",
"PANTHER"
] | [
"PF08193",
"PTHR28061"
] | [
"INO80_Ies4",
""
] | [
1115,
1064
] | 2 | [] | [] | [] | 0 | [
"8a5d",
"8a5p",
"8a5q"
] | 3 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
1115
] | 1 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1
] | 2 | true | Family | INO80 complex, subunit Ies4 | INO80 complex, subunit Ies4 | INO80_su_Ies4 | 7 |
IPR013176 | 13,176 | Vacuolar fusion protein Ccz1 | Ccz1 | Family | 4,872 | false | false | This entry includes the fungal vacuolar fusion protein Ccz1 which forms a complex with Mon1. The CCZ1-MON1 complex acts where vesicles fuse with the vacuole and is required in several vacuolar delivery pathways including autophagy, pexophagy and endocytosis as well cytoplasm to vacuole transport [ , , ]. Ccz1 interacts... | [
"GO:0016192",
"GO:0035658"
] | [
"vesicle-mediated transport",
"Mon1-Ccz1 complex"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF011668",
"PTHR13056"
] | [
"DUF1712_fun",
""
] | [
15,
4872
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-8876198",
"R-DDI-8876198",
"R-DME-8876198",
"R-HSA-8876198",
"R-MMU-8876198",
"R-SCE-8876198"
] | [
"REACTOME:R-BTA-8876198",
"REACTOME:R-DDI-8876198",
"REACTOME:R-DME-8876198",
"REACTOME:R-HSA-8876198",
"REACTOME:R-MMU-8876198",
"REACTOME:R-SCE-8876198"
] | 6 | [
"5ldd",
"7qla",
"8c7g",
"8jbe",
"9l0d",
"9rs6",
"9rs7"
] | 7 | [
"PUB00044731",
"PUB00045031",
"PUB00083136",
"PUB00083138"
] | [
"12364329",
"14662743",
"15721293",
"11590240"
] | [
"The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways.",
"Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage.",
"Multiple functions of the vacuolar sorting protein Ccz1p in Saccharomyces cerevisiae.",
"The Ccz1 protein ... | [
2002,
2003,
2005,
2001
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4872
] | 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... | [
10,
1,
2,
1,
5,
1,
1,
3,
8,
1,
11
] | 11 | true | Family | Vacuolar fusion protein Ccz1 | Vacuolar fusion protein Ccz1 | Ccz1 | 4 |
IPR013177 | 13,177 | Ribosomal protein bS22, C-terminal | Ribosomal_bS22_C | Domain | 6,670 | false | false | This domain is found at the C-terminal of small ribosomal subunit protein bS22m (formerly known as mS38; also called COX24 in yeast). The mitochondrial protein bS22m shares sequence homology with bacterial bS22, particularly in the N-terminal region, leading to its renaming to reflect their common evolutionary origin. ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08213",
"SM01155"
] | [
"COX24_C",
"DUF1713"
] | [
6559,
6534
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383"
] | [
"REACTOME:R-HSA-5368286",
"REACTOME:R-HSA-5389840",
"REACTOME:R-HSA-5419276",
"REACTOME:R-HSA-9937383",
"REACTOME:R-MMU-5389840",
"REACTOME:R-MMU-5419276",
"REACTOME:R-MMU-9937383"
] | 7 | [
"3j9m",
"3jd5",
"5aj3",
"5aj4",
"5mrc",
"5mre",
"5mrf",
"5o5j",
"5o61",
"5v93",
"5xyu",
"5zeb",
"5zep",
"5zeu",
"6dzi",
"6dzk",
"6gaw",
"6gaz",
"6neq",
"6nf8",
"6nu2",
"6nu3",
"6rw4",
"6rw5",
"6vlz",
"6vmi",
"6xyw",
"6ydp",
"6ydw",
"6yw5",
"6ywe",
"6ywx"... | 118 | [
"PUB00076420",
"PUB00078824",
"PUB00089004",
"PUB00098057",
"PUB00163225",
"PUB00163226"
] | [
"16339141",
"17125467",
"25609543",
"28154081",
"37034768",
"30968120"
] | [
"COX24 codes for a mitochondrial protein required for processing of the COX1 transcript.",
"Aurora-A kinase interacting protein 1 (AURKAIP1) promotes Aurora-A degradation through an alternative ubiquitin-independent pathway.",
"Organization of the mitochondrial translation machinery studied in situ by cryoelect... | [
2006,
2007,
2015,
2017,
2023,
2019
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3137,
3502,
31
] | 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... | [
3,
1,
2,
4,
1,
3,
1,
1,
1,
3
] | 10 | true | Domain | Ribosomal protein bS22, C-terminal | Ribosomal protein bS22, C-terminal | Ribosomal_bS22_C | 5 |
IPR013178 | 13,178 | Histone acetyltransferase Rtt109/CBP | Histone_AcTrfase_Rtt109/CBP | Family | 12,859 | false | false | Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal RTT109 protein, which is required for H3K56 acetylation [ ]. In Schizosaccharomyces pombe (Fission yeast) loss of RTT109 results in the loss of H3K56 acetylation, both ... | [
"GO:0004402",
"GO:0006355"
] | [
"histone acetyltransferase activity",
"regulation of DNA-templated transcription"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PANTHER",
"SMART"
] | [
"PF08214",
"PTHR13808",
"SM01250"
] | [
"HAT_KAT11",
"",
"KAT11"
] | [
10524,
11127,
10425
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.3.1.48",
"R-CEL-1234158",
"R-CEL-201722",
"R-CEL-3899300",
"R-CEL-5250924",
"R-CEL-5689901",
"R-CEL-8936459",
"R-CEL-8939243",
"R-CEL-8939246",
"R-CEL-8951936",
"R-CEL-9617629",
"R-CEL-9701898",
"R-CEL-9759194",
"R-CEL-9856649",
"R-HSA-1234158",
"R-HSA-1368108",
"R-HSA-156711",
... | [
"EC:2.3.1.48",
"REACTOME:R-CEL-1234158",
"REACTOME:R-CEL-201722",
"REACTOME:R-CEL-3899300",
"REACTOME:R-CEL-5250924",
"REACTOME:R-CEL-5689901",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-8939243",
"REACTOME:R-CEL-8939246",
"REACTOME:R-CEL-8951936",
"REACTOME:R-CEL-9617629",
"REACTOME:R-CEL-9701... | 131 | [
"1f81",
"1kdx",
"1l3e",
"1l8c",
"1p4q",
"1r8u",
"1sb0",
"1tot",
"1u2n",
"2agh",
"2k8f",
"2ka4",
"2ka6",
"2kje",
"2kwf",
"2lqh",
"2lqi",
"2lww",
"2lxs",
"2lxt",
"2mh0",
"2mzd",
"2n1a",
"2rim",
"2zfn",
"3biy",
"3cz7",
"3io2",
"3p57",
"3q33",
"3q35",
"3q66"... | 114 | [
"PUB00042670",
"PUB00045009",
"PUB00051225",
"PUB00053723",
"PUB00053724",
"PUB00074833",
"PUB00074834",
"PUB00074835"
] | [
"17272723",
"17046836",
"18568037",
"11701890",
"16287980",
"11359896",
"15313412",
"15313417"
] | [
"Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication.",
"Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II.",
"Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.",
"A transcripti... | [
2007,
2006,
2008,
2001,
2005,
2001,
2004,
2004
] | 8 | [] | [
"IPR016849"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Nidovirales"
] | [
4,
12853,
2
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
32,
8,
62,
4,
29,
12,
1,
7,
11,
1,
1,
48
] | 12 | true | Family | Histone acetyltransferase Rtt109/CBP | Histone acetyltransferase Rtt109/CBP | Histone_AcTrfase_Rtt109/CBP | 6 |
IPR013180 | 13,180 | Beta-catenin-like protein 1, N-terminal | CTNNBL1_N | Domain | 4,932 | false | false | This entry represents the N-terminal domain of the beta-catenin-like protein 1 (CTNNBL1). CTNNBL1 is a component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. In humans, it participates in AID/AICDA-mediated Ig class switching recombination (... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08216",
"SM01156"
] | [
"CTNNBL",
"DUF1716"
] | [
4931,
4426
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-72163",
"R-MMU-72163",
"R-RNO-72163",
"R-SPO-72163"
] | [
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-72163",
"REACTOME:R-SPO-72163"
] | 4 | [
"4cb8",
"4cb9",
"4cba",
"4hm9",
"4hnm",
"4mfu",
"4mfv",
"7abi"
] | 8 | [
"PUB00017164",
"PUB00066736"
] | [
"12659813",
"18722174"
] | [
"Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class intron-containing gene--evidence for a role in apoptosis.",
"Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1."
] | [
2003,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
4932
] | 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... | [
5,
1,
2,
1,
2,
3,
1,
3,
6,
1,
5
] | 11 | true | Domain | Beta-catenin-like protein 1, N-terminal | Beta-catenin-like protein 1, N-terminal | CTNNBL1_N | 3 |
IPR013181 | 13,181 | Protein of unknown function DUF1719 | DUF1719 | Family | 1,217 | false | false | This is a group of proteins of unknown function from Gramineae (grasses). | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08224",
"SM01157"
] | [
"DUF1719",
"DUF1719"
] | [
1217,
1171
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Poaceae"
] | [
1217
] | 1 | [
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
38,
26
] | 2 | true | Family | Protein of unknown function DUF1719 | Protein of unknown function DUF1719 | DUF1719 | 6 |
IPR013182 | 13,182 | Domain of unknown function DUF1720 | DUF1720 | Domain | 2,016 | false | false | This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. It is found in proteins of the actin cytoskeleton-regulatory complex. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08226"
] | [
"DUF1720"
] | [
2016
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-SCE-416482",
"R-SCE-8856828",
"R-SCE-9013148",
"R-SCE-9013406",
"R-SCE-9013420",
"R-SPO-416482",
"R-SPO-8856825",
"R-SPO-8856828",
"R-SPO-9013148",
"R-SPO-9013406",
"R-SPO-9013420",
"R-SPO-9696270"
] | [
"REACTOME:R-SCE-416482",
"REACTOME:R-SCE-8856828",
"REACTOME:R-SCE-9013148",
"REACTOME:R-SCE-9013406",
"REACTOME:R-SCE-9013420",
"REACTOME:R-SPO-416482",
"REACTOME:R-SPO-8856825",
"REACTOME:R-SPO-8856828",
"REACTOME:R-SPO-9013148",
"REACTOME:R-SPO-9013406",
"REACTOME:R-SPO-9013420",
"REACTOME:... | 12 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
9,
2007
] | 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)"
] | [
2,
1,
3
] | 3 | true | Domain | Domain of unknown function DUF1720 | Domain of unknown function DUF1720 | DUF1720 | 3 |
IPR013183 | 13,183 | DASH complex subunit Hsk3-like | Hsk3-like | Family | 2,069 | false | false | Hsk3 is a subunit of the DASH complex, a microtubule-binding complex that is transferred to the kinetochore prior to mitosis [ ]. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro [ , ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08227"
] | [
"DASH_Hsk3"
] | [
2069
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162658",
"R-MMU-162658",
"R-RNO-162658"
] | [
"REACTOME:R-HSA-162658",
"REACTOME:R-MMU-162658",
"REACTOME:R-RNO-162658"
] | 3 | [
"6cfz",
"8q84",
"8q85"
] | 3 | [
"PUB00017174",
"PUB00033281",
"PUB00033282",
"PUB00062892",
"PUB00062893"
] | [
"11799062",
"15640796",
"15664196",
"11739401",
"10879493"
] | [
"The mitotic spindle is required for loading of the DASH complex onto the kinetochore.",
"The yeast DASH complex forms closed rings on microtubules.",
"Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex.",
"A GRASP55-rab2 effector complex linking Golgi structur... | [
2002,
2005,
2005,
2001,
2000
] | 5 | [] | [
"IPR042332"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
2069
] | 1 | [
"Danio rerio",
"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)"
] | [
3,
4,
3,
1,
3,
1,
1
] | 7 | true | Family | DASH complex subunit Hsk3-like | DASH complex subunit Hsk3-like | Hsk3-like | 9 |
IPR013184 | 13,184 | Lactococcus phage c2, E2 | Lactococcus_phage_c2_E2 | Family | 10 | false | false | This is a family of short conserved proteins of 37 amino acids, described in Lactococcus phage c2 and in related phage. The function of these proteins is unknown. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08199"
] | [
"E2"
] | [
10
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Ceduovirus",
"Marine Group I thaumarchaeote"
] | [
9,
1
] | 2 | [] | [] | 0 | true | Family | Lactococcus phage c2, E2 | Lactococcus phage c2, E2 | Lactococcus_phage_c2_E2 | 9 |
IPR013185 | 13,185 | Translation elongation factor, KOW-like | Transl_elong_KOW-like | Domain | 29,589 | false | false | This entry represents the N-terminal domain of homologues of elongation factor P, which probably are translation initiation factors. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08207"
] | [
"EFP_N"
] | [
29589
] | 1 | [] | [] | [] | 0 | [
"1ueb",
"1yby",
"3a5z",
"3oyy",
"3tre",
"4v6a",
"5j3b",
"5wxk",
"6enj",
"6enu",
"6j7m",
"6rji",
"6rk3",
"6s8z",
"8s8u",
"8vwq",
"8w2n"
] | 17 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2,
27312,
1692,
2,
581
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
11,
2,
7,
10
] | 4 | true | Domain | Translation elongation factor, KOW-like | Translation elongation factor, KOW-like | Transl_elong_KOW-like | 2 |
IPR013186 | 13,186 | Early nodulin 40 | ENOD40 | Family | 13 | false | false | This entry represents the family of nodulin 40 proteins. The soybean early nodulin 40 (ENOD40) mRNA contains two short overlapping ORFs; in vitro translation yields two peptides of 12 and 24 amino acids [ ]. The putative role of the ENOD40 genes has been in favour of organogenesis, such as induction of the cortical cel... | [
"GO:0009877"
] | [
"nodulation"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF08247"
] | [
"ENOD40"
] | [
13
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00017133",
"PUB00017176"
] | [
"11842184",
"12114565"
] | [
"Soybean ENOD40 encodes two peptides that bind to sucrose synthase.",
"The white clover enod40 gene family. Expression patterns of two types of genes indicate a role in vascular function."
] | [
2002,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"50 kb inversion clade"
] | [
13
] | 1 | [] | [] | 0 | true | Family | Early nodulin 40 | Early nodulin 40 | ENOD40 | 6 |
IPR013187 | 13,187 | F-box associated beta-propeller, type 3 | F-box-assoc_dom_typ3 | Domain | 25,711 | false | false | This β-propeller domain occurs in a diverse superfamily of genes in plants. Most examples are found C-terminal to an F-box ( ), a 60 amino acid motif involved in ubiquitination of target proteins to mark them for degradation. Two-hybid experiments support the idea that most members are interchangeable F-box subunits of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08268"
] | [
"FBA_3"
] | [
25711
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009649"
] | [
"12169662"
] | [
"The F-box subunit of the SCF E3 complex is encoded by a diverse superfamily of genes in Arabidopsis."
] | [
2002
] | 1 | [
"IPR017451"
] | [] | 1 | 0 | 1 | [
"Embryophyta"
] | [
25711
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
597,
193,
27
] | 3 | true | Domain | F-box associated beta-propeller, type 3 | F-box associated beta-propeller, type 3 | F-box-assoc_dom_typ3 | 9 |
IPR013188 | 13,188 | Influenza matrix M1, C-terminal | Flu_matrix_M1_C | Domain | 70,365 | false | false | Matrix protein (M1) of Influenza virus is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously. M1 is comprised of two domains connected by a linker sequence. The C-t... | [
"GO:0003723",
"GO:0005198"
] | [
"RNA binding",
"structural molecule activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"SMART"
] | [
"PF08289",
"SM00759"
] | [
"Flu_M1_C",
"Flu_M1_C"
] | [
70365,
70285
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-168255",
"R-HSA-168275",
"R-HSA-168288",
"R-HSA-168298",
"R-HSA-168302",
"R-HSA-168303",
"R-HSA-168316",
"R-HSA-168330",
"R-HSA-168333",
"R-HSA-168336",
"R-HSA-192823"
] | [
"REACTOME:R-HSA-168255",
"REACTOME:R-HSA-168275",
"REACTOME:R-HSA-168288",
"REACTOME:R-HSA-168298",
"REACTOME:R-HSA-168302",
"REACTOME:R-HSA-168303",
"REACTOME:R-HSA-168316",
"REACTOME:R-HSA-168330",
"REACTOME:R-HSA-168333",
"REACTOME:R-HSA-168336",
"REACTOME:R-HSA-192823"
] | 11 | [
"6z5j",
"6z5l",
"7jm3"
] | 3 | [
"PUB00019569",
"PUB00035992"
] | [
"12590584",
"15892972"
] | [
"Zinc- and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1.",
"A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence."
] | [
2003,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Orthomyxoviridae"
] | [
12,
70353
] | 2 | [] | [] | 0 | true | Domain | Influenza matrix M1, C-terminal | Influenza matrix M1, C-terminal | Flu_matrix_M1_C | 9 |
IPR013189 | 13,189 | Glycosyl hydrolase family 32, C-terminal | Glyco_hydro_32_C | Domain | 25,076 | false | false | This domain corresponds to the C-terminal domain of glycosyl hydrolase family 32. It forms a β sandwich module [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08244"
] | [
"Glyco_hydro_32C"
] | [
25076
] | 1 | [
"EC",
"EC",
"METACYC"
] | [
"3.2.1",
"3.2.1.26",
"PWY-8314"
] | [
"EC:3.2.1",
"EC:3.2.1.26",
"METACYC:PWY-8314"
] | 3 | [
"1st8",
"1uyp",
"1w2t",
"1y4w",
"1y9g",
"1y9m",
"2ac1",
"2add",
"2ade",
"2aey",
"2aez",
"2oxb",
"2qqu",
"2qqv",
"2qqw",
"2xqr",
"3kf3",
"3kf5",
"3ldk",
"3ldr",
"3lem",
"3lf7",
"3lfi",
"3lig",
"3lih",
"3pig",
"3pij",
"3rwk",
"3sc7",
"3u14",
"3u75",
"3ugf"... | 76 | [
"PUB00017131"
] | [
"14973124"
] | [
"The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Herelleviridae",
"Methanobacteriota",
"metagenomes"
] | [
13692,
11142,
2,
147,
93
] | 5 | [
"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"
] | [
57,
1,
52,
1,
2,
68
] | 6 | true | Domain | Glycosyl hydrolase family 32, C-terminal | Glycosyl hydrolase family 32, C-terminal | Glyco_hydro_32_C | 6 |
IPR013191 | 13,191 | Glycosyl hydrolase family 98, central domain | GH98_central | Domain | 288 | false | false | This domain can be found in the central of the blood-group-substance endo-1,4-beta-galactosidase EabC from Clostridium perfringens, which is a member of the glycosyl hydrolase family 98. EabC is an endo-beta-galactosidase capable of releasing both the blood group A trisaccharide (A-Tri; GalNAcalpha1-->3(Fucalpha1-->2)G... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08306"
] | [
"Glyco_hydro_98M"
] | [
288
] | 1 | [] | [] | [] | 0 | [
"2wmf",
"2wmg",
"2wmh",
"2wmi",
"2wmj",
"2wmk",
"4d6c",
"4d6d",
"4d6e",
"4d6f",
"4d6g",
"4d6h",
"4d6i",
"4d6j",
"4d71",
"4d72",
"7pmo",
"7q1w",
"7q20",
"9h6f",
"9h6g",
"9h6h"
] | 22 | [
"PUB00072703"
] | [
"15618227"
] | [
"A clostridial endo-beta-galactosidase that cleaves both blood group A and B glycotopes: the first member of a new glycoside hydrolase family, GH98."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Porphyridium purpureum",
"metagenomes"
] | [
284,
1,
3
] | 3 | [] | [] | 0 | true | Domain | Glycosyl hydrolase family 98, central domain | Glycosyl hydrolase family 98, central domain | GH98_central | 7 |
IPR013192 | 13,192 | Hepatitis C virus, Non-structural 5a protein, domain 1a | HCV_NS5A_1a | Domain | 19,132 | false | false | The exact function of the Hepatitis C non-structural 5A (NS5A) protein is not known, but it is an active component of the replicase, regulates replication and modulates a range of cellular processes including innate immunity and dysregulated cell growth. NS5A is organised into three domains, labelled I, II and III. Dom... | [
"GO:0008270"
] | [
"zinc ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08300"
] | [
"HCV_NS5a_1a"
] | [
19132
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME"
] | [
"2.7.7.48",
"3.4.21.98",
"3.4.22.-",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"R-HSA-5621480",
"R-HSA-8854214"
] | [
"EC:2.7.7.48",
"EC:3.4.21.98",
"EC:3.4.22.-",
"EC:3.6.1.15",
"EC:3.6.4.13",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210",
"REACTOME:R-HSA-5621480",
"REACTOME:R-HSA-8854214"
] | 12 | [
"1zh1",
"3fqm",
"3fqq",
"4cl1"
] | 4 | [
"PUB00017175",
"PUB00052025",
"PUB00097472"
] | [
"15902263",
"19244328",
"24639329"
] | [
"Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase.",
"Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus.",
"The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HC... | [
2005,
2009,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Riboviria"
] | [
19132
] | 1 | [] | [] | 0 | true | Domain | Hepatitis C virus, Non-structural 5a protein, domain 1a | Hepatitis C virus, Non-structural 5a protein, domain 1a | HCV_NS5A_1a | 5 |
IPR013194 | 13,194 | Histone deacetylase interacting domain | HDAC_interact_dom | Domain | 9,684 | false | false | This domain is found in the transcriptional repressor Sin3. It forms interactions with histone deacetylases [ ]. Budding yeast Sin3 is a component of both the Rpd3S and Rpd3L histone deacetylase complexes [ ]. In mammals there are two Sin3 paraologues, Sin3A and Sin3B. They forms the larger Sin3L/Rpd3L and the smaller ... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08295",
"SM00761"
] | [
"Sin3_corepress",
"HDAC_interact"
] | [
9647,
9600
] | 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-CEL-8936459",
"R-CEL-9824594",
"R-CEL-9825892",
"R-HSA-3899300",
"R-HSA-400206",
"R-HSA-427413",
"R-HSA-8936459",
"R-HSA-9022538",
"R-HSA-9022692",
"R-HSA-9022699",
"R-HSA-9022702",
"R-HSA-9615017",
"R-HSA-9701898",
"R-HSA-9707564",
"R-HSA-9824594",
"R-HSA-9825892",
"R-HSA-983231"... | [
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-9824594",
"REACTOME:R-CEL-9825892",
"REACTOME:R-HSA-3899300",
"REACTOME:R-HSA-400206",
"REACTOME:R-HSA-427413",
"REACTOME:R-HSA-8936459",
"REACTOME:R-HSA-9022538",
"REACTOME:R-HSA-9022692",
"REACTOME:R-HSA-9022699",
"REACTOME:R-HSA-9022702",
"REACTOME:... | 24 | [
"2n2h",
"7yi0",
"7yi2",
"7yi3",
"7yi4",
"7yi5",
"8bpa",
"8bpb",
"8bpc",
"8c60",
"8ga8",
"8hpo",
"8hxx",
"8hxy",
"8hy0",
"8i02",
"8i03",
"8ifg",
"8ihn",
"8iht",
"8jho",
"8kc7",
"8kd2",
"8kd3",
"8kd4",
"8kd5",
"8kd6",
"8kd7",
"8tof",
"8w9c",
"8w9d",
"8w9e"... | 33 | [
"PUB00017120",
"PUB00033324",
"PUB00075991"
] | [
"12773392",
"16314178",
"26124119"
] | [
"Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity.",
"Stable incorporation of sequence specific repressors Ash1 and Ume6 into the Rpd3L complex.",
"Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepre... | [
2003,
2005,
2015
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
9684
] | 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... | [
49,
1,
8,
10,
10,
3,
1,
10,
10,
1,
3,
62
] | 12 | true | Domain | Histone deacetylase interacting domain | Histone deacetylase interacting domain | HDAC_interact_dom | 7 |
IPR013195 | 13,195 | Hepatitis B virus, capsid N-terminal | Hepatitis_B_virus_capsid_N | Domain | 14,488 | false | false | This entry represent a short region found at the N terminus of some viral capsid (HBcAg) proteins from various Hepatitis B virus (HBV), which is a major human pathogen. The conservation of four Cys residues suggests that this region acts as a zinc binding domain. Hepatitis virus is composed of an outer envelope of host... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF08290"
] | [
"Hep_core_N"
] | [
14488
] | 1 | [] | [] | [] | 0 | [
"6t36"
] | 1 | [
"PUB00030260"
] | [
"10394365"
] | [
"The crystal structure of the human hepatitis B virus capsid."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Hepadnaviridae",
"Trichinella spiralis"
] | [
14487,
1
] | 2 | [] | [] | 0 | true | Domain | Hepatitis B virus, capsid N-terminal | Hepatitis B virus, capsid N-terminal | Hepatitis_B_virus_capsid_N | 3 |
IPR013196 | 13,196 | Helix-turn-helix, type 11 | HTH_11 | Domain | 66,258 | false | false | Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif, where the "wings", or loops, are small β-sheets. The winged helix motif consists of two wings (W1, W2), three α helices (H1, H2, H3) and three β-sheets (S1, S2, S3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 [ ]. The DNA-rec... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08279"
] | [
"HTH_11"
] | [
66258
] | 1 | [] | [] | [] | 0 | [
"1bia",
"1bib",
"1hxd",
"1j5y",
"2ewn",
"3rir",
"3rkw",
"3rkx",
"3rky",
"3v7c",
"3v7r",
"3v7s",
"3v8j",
"3v8k",
"3v8l",
"4dq2",
"4ha8",
"4wf2",
"6apw",
"6aqq",
"6ndl",
"6oru",
"7cv0",
"7cv2",
"7ueb",
"8eni",
"8f8u",
"8fi3",
"9ebr"
] | 29 | [
"PUB00004803",
"PUB00005019",
"PUB00013195",
"PUB00028128",
"PUB00028129"
] | [
"1409631",
"8019415",
"10679470",
"12042311",
"10438772"
] | [
"Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.",
"Novel phosphotransferase system genes revealed by bacterial genome analysis: unique, putative fructose- and glucoside-specific systems.",
"Winged helix proteins.",
"The Sulfolobus ... | [
1992,
1994,
2000,
2002,
1999
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
939,
64900,
80,
27,
312
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
3,
2
] | 2 | true | Domain | Helix-turn-helix, type 11 | Helix-turn-helix, type 11 | HTH_11 | 9 |
IPR013197 | 13,197 | RNA polymerase III subunit RPC82-related, helix-turn-helix | RNA_pol_III_RPC82-rel_HTH | Domain | 4,024 | false | false | DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08221"
] | [
"HTH_9"
] | [
4024
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-BTA-76061",
"R-BTA-76066",
"R-BTA-76071",
"R-DDI-76061",
"R-DDI-76066",
"R-HSA-1834949",
"R-HSA-73780",
"R-HSA-73980",
"R-HSA-749476",
"R-HSA-76061",
"R-HSA-76066",
"R-HSA-76071",
"R-MMU-76061",
"R-MMU-76066",
"R-MMU-76071",
"R-RNO-76061",
"R-RNO-76066",
"R-RNO-76071",
"R-SCE-... | [
"REACTOME:R-BTA-76061",
"REACTOME:R-BTA-76066",
"REACTOME:R-BTA-76071",
"REACTOME:R-DDI-76061",
"REACTOME:R-DDI-76066",
"REACTOME:R-HSA-1834949",
"REACTOME:R-HSA-73780",
"REACTOME:R-HSA-73980",
"REACTOME:R-HSA-749476",
"REACTOME:R-HSA-76061",
"REACTOME:R-HSA-76066",
"REACTOME:R-HSA-76071",
"... | 21 | [
"2xub",
"2xv4",
"5afq",
"5fj8",
"5fj9",
"5fja",
"6cnb",
"6cnc",
"6cnd",
"6cnf",
"6eu0",
"6eu1",
"6eu2",
"6eu3",
"6f40",
"6f41",
"6f42",
"6f44",
"6tut",
"7a6h",
"7ae1",
"7ae3",
"7aea",
"7ast",
"7d58",
"7d59",
"7dn3",
"7du2",
"7fji",
"7fjj",
"7n6g",
"7z0h"... | 58 | [
"PUB00000061",
"PUB00011444",
"PUB00033173"
] | [
"3052291",
"1406632",
"10499798"
] | [
"Structure and function of bacterial sigma factors.",
"RPC82 encodes the highly conserved, third-largest subunit of RNA polymerase C (III) from Saccharomyces cerevisiae.",
"Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution."
] | [
1988,
1992,
1999
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Thermoproteati",
"freshwater metagenome"
] | [
6,
4002,
10,
6
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
7,
1,
6,
1,
7,
3,
1,
3,
3,
1,
1,
2
] | 12 | true | Domain | RNA polymerase III subunit RPC82-related, helix-turn-helix | RNA polymerase III subunit RPC82-related, helix-turn-helix | RNA_pol_III_RPC82-rel_HTH | 2 |
IPR013198 | 13,198 | Global transcriptional regulator CodY, C-terminal | GTP_trans_reg_CodY_C | Domain | 3,280 | false | false | This entry represents the C-terminal helix-turn-helix domain found in several bacterial GTP-sensing transcriptional pleiotropic repressor CodY proteins. CodY has been found to repress the dipeptide transport operon (dpp) of Bacillus subtilis in nutrient-rich conditions [ ]. The CodY protein also has a repressor effect ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08222"
] | [
"HTH_CodY"
] | [
3280
] | 1 | [] | [] | [] | 0 | [
"2b0l",
"5ey0",
"5ey1",
"5ey2",
"5lnh",
"5loe",
"5loj",
"5loo",
"8c7o",
"8c7s",
"8c7t",
"8c7u"
] | 12 | [
"PUB00012225",
"PUB00012226"
] | [
"7783641",
"11401725"
] | [
"A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon.",
"Pleiotropic transcriptional repressor CodY senses the intracellular pool of branched-chain amino acids in Lactococcus lactis."
] | [
1995,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3260,
2,
18
] | 3 | [] | [] | 0 | true | Domain | Global transcriptional regulator CodY, C-terminal | Global transcriptional regulator CodY, C-terminal | GTP_trans_reg_CodY_C | 3 |
IPR013199 | 13,199 | M protein trans-acting positive regulator (MGA) HTH domain | HTH_Mga_DNA-bd_dom | Domain | 1,556 | false | false | Mga is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions. It appears to contain two DNA-binding domains that are required for direct activation of the Mga virulence regulon in vivo [ ]. This entry represents... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08280"
] | [
"HTH_Mga"
] | [
1556
] | 1 | [] | [] | [] | 0 | [
"3sqn",
"5way",
"9atx"
] | 3 | [
"PUB00010185"
] | [
"11952907"
] | [
"Two DNA-binding domains of Mga are required for virulence gene activation in the group A streptococcus."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
7,
1542,
5,
2
] | 4 | [] | [] | 0 | true | Domain | M protein trans-acting positive regulator (MGA) HTH domain | M protein trans-acting positive regulator (MGA) HTH domain | HTH_Mga_DNA-bd_dom | 9 |
IPR013201 | 13,201 | Cathepsin propeptide inhibitor domain (I29) | Prot_inhib_I29 | Domain | 41,185 | false | false | This entry represents a peptidase inhibitor domain, which belongs to MEROPS peptidase inhibitor family I29. The domain is also found at the N terminus of a variety of peptidase precursors that belong to MEROPS peptidase subfamily C1A; these include cathepsin L, papain, and procaricain ( ) [ ]. It forms an α-helical dom... | [] | [] | [] | 0 | [
"PFAM",
"SMART"
] | [
"PF08246",
"SM00848"
] | [
"Inhibitor_I29",
"Inhibitor_I29"
] | [
40804,
40086
] | 2 | [
"EC",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.4.22",
"GenProp1728",
"R-BTA-1442490",
"R-BTA-1474228",
"R-BTA-1592389",
"R-BTA-1679131",
"R-BTA-2132295",
"R-BTA-5683826",
"R-BTA-6798695",
"R-BTA-8939242",
"R-CEL-1474228",
"R-CEL-1592389",
"R-CEL-2132295",
"R-CEL-6798695",
"R-CEL-8939242",
"R-CFA-1474228",
"R-CFA-1592389",
"R... | [
"EC:3.4.22",
"GP:GenProp1728",
"REACTOME:R-BTA-1442490",
"REACTOME:R-BTA-1474228",
"REACTOME:R-BTA-1592389",
"REACTOME:R-BTA-1679131",
"REACTOME:R-BTA-2132295",
"REACTOME:R-BTA-5683826",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8939242",
"REACTOME:R-CEL-1474228",
"REACTOME:R-CEL-1592389",
"... | 78 | [
"1by8",
"1cjl",
"1cs8",
"1pci",
"1xkg",
"2c0y",
"2l95",
"2o6x",
"3f75",
"3qj3",
"3qt4",
"3tnx",
"3usv",
"4qrg",
"4qrv",
"4qrx",
"5ef4",
"5egw",
"5jt8",
"5z5o",
"6czk",
"6czs",
"6jd0",
"6jd8",
"6u7d",
"7avm",
"7pck",
"7qbm",
"7qbo",
"7w33",
"7w34",
"8gx2"... | 36 | [
"PUB00022428",
"PUB00028125"
] | [
"8939744",
"14505823"
] | [
"The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft.",
"A new type of cysteine proteinase inhibitor--the salarin gene from Atlantic salmon (Salmo salar L.) and Arctic charr (Salvelinus alpinus)."
] | [
1996,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
8,
40958,
131,
88
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
120,
11,
70,
17,
79,
60,
133,
63,
149
] | 9 | true | Domain | Cathepsin propeptide inhibitor domain (I29) | Cathepsin propeptide inhibitor domain (I29) | Prot_inhib_I29 | 7 |
IPR013202 | 13,202 | Kinin peptide | Kinin_peptide | Family | 5 | false | false | This entry represents neuropeptides that are the first members of the insect kinin-family isolated from the American cockroach. Their occurrence in the retrocerebral complex suggests a physiological role as a neurohormone. The C-terminal sequence Phe-X-Ser-Trp-Gly-NH2 characterised the peptides as members of the insect... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08260"
] | [
"Kinin"
] | [
5
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00017097"
] | [
"9350979"
] | [
"Isolation and structural elucidation of eight kinins from the retrocerebral complex of the American cockroach, Periplaneta americana."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Blattodea"
] | [
5
] | 1 | [] | [] | 0 | true | Family | Kinin peptide | Kinin peptide | Kinin_peptide | 3 |
IPR013203 | 13,203 | Leader peptide, Arg-2/CPA1 | Leader_Arg2_CPA1 | Family | 57 | false | false | In this family there are leader peptides involved in the regulation of the glutaminase subunit (small subunit) of arginine-specific carbamoyl phosphate synthetase. In Neurospora crassa it is a small upstream ORF of 24 codons above the arg-2 locus [ ]. In yeast it is the leader peptide of the CPA1 gene. The 5' region of... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08252"
] | [
"Leader_CPA1"
] | [
57
] | 1 | [] | [] | [] | 0 | [
"2xl1"
] | 1 | [
"PUB00002557",
"PUB00017104"
] | [
"2141606",
"3555844"
] | [
"The Neurospora crassa arg-2 locus. Structure and expression of the gene encoding the small subunit of arginine-specific carbamoyl phosphate synthetase.",
"The leader peptide of yeast gene CPA1 is essential for the translational repression of its expression."
] | [
1990,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Pseudomonadati"
] | [
54,
3
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)"
] | [
1,
1
] | 2 | true | Family | Leader peptide, Arg-2/CPA1 | Leader peptide, Arg-2/CPA1 | Leader_Arg2_CPA1 | 7 |
IPR013204 | 13,204 | Leader peptide, Erm | Leader_Erm | Family | 61 | false | false | These short proteins are leader peptides (15-19 amino acids) of erm genes that code for resistance determinants in Staphylococcus aureus [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08253"
] | [
"Leader_Erm"
] | [
61
] | 1 | [] | [] | [] | 0 | [
"3j7z"
] | 1 | [
"PUB00017126"
] | [
"2985541"
] | [
"Nucleotide sequence of ermA, a macrolide-lincosamide-streptogramin B determinant in Staphylococcus aureus."
] | [
1985
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"plasmids"
] | [
59,
2
] | 2 | [] | [] | 0 | true | Family | Leader peptide, Erm | Leader peptide, Erm | Leader_Erm | 2 |
IPR013205 | 13,205 | Leader peptide, tryptophan-operon | Leader_Trp_op | Family | 362 | false | false | The tryptophan operon regulatory region of Citrobacter freundii (leader transcript) encodes a 14-residue peptide containing characteristic tandem tryptophan residues. It is about 10 nucleotides shorter than those of Escherichia coli and Salmonella typhimurium [ ]. | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08255"
] | [
"Leader_Trp"
] | [
362
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00017129"
] | [
"6749821"
] | [
"Evolutionary divergence of the Citrobacter freundii tryptophan operon regulatory region: comparison with other enteric bacteria."
] | [
1982
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
362
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Leader peptide, tryptophan-operon | Leader peptide, tryptophan-operon | Leader_Trp_op | 8 |
IPR013206 | 13,206 | Leucophaea maderae tachykinin-related peptide | Lem_TRP | Family | 4 | false | false | These peptides are designated Leucophaea maderae (Madeira cockroach) tachykinin-related peptides (Lem TRPs). Some were isolated from the midgut of L. maderae, whereas others appear to be brain specific. The Lem TRPs of the brain are myotropic and induce increases in the amplitude and frequency of spontaneous contractio... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08262"
] | [
"Lem_TRP"
] | [
4
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00017110",
"PUB00017137"
] | [
"9114447",
"2132575"
] | [
"Seven tachykinin-related peptides isolated from the brain of the Madeira cockroach: evidence for tissue-specific expression of isoforms.",
"Locustatachykinin III and IV: two additional insect neuropeptides with homology to peptides of the vertebrate tachykinin family."
] | [
1997,
1990
] | 2 | [] | [] | 0 | 0 | null | [
"Polyneoptera"
] | [
4
] | 1 | [] | [] | 0 | true | Family | Leucophaea maderae tachykinin-related peptide | Leucophaea maderae tachykinin-related peptide | Lem_TRP | 8 |
IPR013207 | 13,207 | LGFP | LGFP | Repeat | 5,587 | false | false | This 54 amino acid repeat is found in many hypothetical proteins. Several hypothetical proteins from Corynebacterium glutamicum (Brevibacterium flavum) and Corynebacterium efficiens along with PS1 protein contain this repeat region. The N-terminal region of PS1 contains an esterase domain which transfers corynomycolic ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08310"
] | [
"LGFP"
] | [
5587
] | 1 | [] | [] | [] | 0 | [
"6swz",
"6sx4"
] | 2 | [
"PUB00017162"
] | [
"12740729"
] | [
"Identification and functional analysis of six mycolyltransferase genes of Corynebacterium glutamicum ATCC 13032: the genes cop1, cmt1, and cmt2 can replace each other in the synthesis of trehalose dicorynomycolate, a component of the mycolic acid layer of the cell envelope."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"Stenosarchaea group",
"ecological metagenomes"
] | [
5343,
150,
73,
6,
15
] | 5 | [] | [] | 0 | true | Repeat | LGFP | LGFP | LGFP | 2 |
IPR013209 | 13,209 | Lipin/Ned1/Smp2 (LNS2) | LNS2 | Domain | 11,160 | false | false | This domain is found in lipins and lipin homologues from Saccharomyces cerevisiae (Smp2) and from Schizosaccharomyces pombe (Ned1) [ ]. Smp2 (also known as PAH1) is involved in plasmid maintenance and respiration [ ] and has been identified as a Mg2+-dependent phosphatidate phosphatase ( ) that contains a haloacid deha... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08235"
] | [
"LNS2"
] | [
11160
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"3.1.3.4",
"PWY-6453",
"PWY-7782",
"PWY-8051",
"PWY-8052",
"PWY-8053",
"PWY-8055",
"R-HSA-1483191",
"R-HSA-1483213",
"R-HSA-4419969",
"R-HSA-75109",
"R-HSA-9841922",
"R-MMU-1483191",
"R-MMU-1483213",
"R-MMU-4419969",
"R-MMU-75109",
"R-SCE-1483191",
"R-SCE-1483213",
"R-SCE-4419969... | [
"EC:3.1.3.4",
"METACYC:PWY-6453",
"METACYC:PWY-7782",
"METACYC:PWY-8051",
"METACYC:PWY-8052",
"METACYC:PWY-8053",
"METACYC:PWY-8055",
"REACTOME:R-HSA-1483191",
"REACTOME:R-HSA-1483213",
"REACTOME:R-HSA-4419969",
"REACTOME:R-HSA-75109",
"REACTOME:R-HSA-9841922",
"REACTOME:R-MMU-1483191",
"R... | 24 | [
"6tzy",
"6tzz",
"7lhk",
"9d13",
"9d14",
"9d15",
"9d16"
] | 7 | [
"PUB00010121",
"PUB00017108",
"PUB00045014",
"PUB00075503"
] | [
"11792863",
"12376568",
"16467296",
"23603613"
] | [
"Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin.",
"An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin.",
"The Saccharomyces cerevisiae L... | [
2002,
2002,
2006,
2013
] | 4 | [
"IPR031315"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
11160
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
11,
1,
13,
11,
8,
18,
1,
9,
14,
1,
1,
29
] | 12 | true | Domain | Lipin/Ned1/Smp2 (LNS2) | Lipin/Ned1/Smp2 (LNS2) | LNS2 | 7 |
IPR013212 | 13,212 | Mad3/Bub1 homology region 1 | Mad3/Bub1_I | Domain | 6,861 | false | false | Proteins containing this domain are checkpoint proteins involved in cell division. This region has been shown to be essential for the binding of Bub1 and Mad3 to Cdc20 [ ]. | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF08311",
"PS51489",
"SM00777"
] | [
"Mad3_BUB1_I",
"BUB1_N",
"Mad3_BUB1_I"
] | [
6634,
6637,
6621
] | 3 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"2.7.11.1",
"R-DDI-141430",
"R-DDI-174184",
"R-DDI-176409",
"R-DDI-179409",
"R-HSA-141430",
"R-HSA-141444",
"R-HSA-174184",
"R-HSA-176409",
"R-HSA-179409",
"R-HSA-2467813",
"R-HSA-2500257",
"R-HSA-5663220",
"R-HSA-68877",
"R-HSA-9648025",
"R-MMU-141430",
"R-MMU-141444",
"R-MMU-1741... | [
"EC:2.7.11.1",
"REACTOME:R-DDI-141430",
"REACTOME:R-DDI-174184",
"REACTOME:R-DDI-176409",
"REACTOME:R-DDI-179409",
"REACTOME:R-HSA-141430",
"REACTOME:R-HSA-141444",
"REACTOME:R-HSA-174184",
"REACTOME:R-HSA-176409",
"REACTOME:R-HSA-179409",
"REACTOME:R-HSA-2467813",
"REACTOME:R-HSA-2500257",
... | 27 | [
"2lah",
"2wvi",
"3esl",
"3si5",
"4a1g",
"4aez",
"5khu",
"5lcw",
"6tlj"
] | 9 | [
"PUB00017177"
] | [
"10704439"
] | [
"MAD3 encodes a novel component of the spindle checkpoint which interacts with Bub3p, Cdc20p, and Mad2p."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
3,
6858
] | 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... | [
12,
1,
5,
4,
9,
9,
1,
11,
6,
2,
2,
16
] | 12 | true | Domain | Mad3/Bub1 homology region 1 | Mad3/Bub1 homology region 1 | Mad3/Bub1_I | 3 |
IPR013213 | 13,213 | Mastoparan | Mastoparan | Family | 12 | false | false | Mastoparans are a family of tetradecapeptides from wasp venom that have been shown to directly activate GTP-binding regulatory proteins. These peptides show selectivity among G proteins: they strongly activate Go and Gi but not Gs or Gt. The peptides of this family are composed by 14 amino acids but they can assume dif... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08249"
] | [
"Mastoparan"
] | [
12
] | 1 | [] | [] | [] | 0 | [
"1a13",
"1d7n",
"1smz",
"2czp",
"6dul",
"6duu"
] | 6 | [
"PUB00017142"
] | [
"9537994"
] | [
"G protein-bound conformation of mastoparan-X: heteronuclear multidimensional transferred nuclear overhauser effect analysis of peptide uniformly enriched with 13C and 15N."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Vespidae"
] | [
12
] | 1 | [] | [] | 0 | true | Family | Mastoparan | Mastoparan | Mastoparan | 2 |
IPR013214 | 13,214 | Mastoparan peptide | Mastoparan_peptide | Family | 8 | false | false | Mastoparan (MP) peptides I, II and III are extracted from the venom gland of Protopolybia exigua (Neotropical social wasp) [ ]. They are tetradecapeptides presenting from seven to ten hydrophobic amino acid residues and from two to four lysine residues in their primary sequences. These peptides cause the degranulation ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF08251"
] | [
"Mastoparan_2"
] | [
8
] | 1 | [] | [] | [] | 0 | [
"6q08"
] | 1 | [
"PUB00019837",
"PUB00100333",
"PUB00100334",
"PUB00100335",
"PUB00100788"
] | [
"15581688",
"30974767",
"15052574",
"19463874",
"28108242"
] | [
"Structural and biological characterization of three novel mastoparan peptides from the venom of the neotropical social wasp Protopolybia exigua (Saussure).",
"Antimicrobial and Antibiofilm Effects of Peptides from Venom of Social Wasp and Scorpion on Multidrug-Resistant <i>Acinetobacter baumannii</i>.",
"Struc... | [
2005,
2019,
2004,
2009,
2017
] | 5 | [] | [] | 0 | 0 | null | [
"Polistinae"
] | [
8
] | 1 | [] | [] | 0 | true | Family | Mastoparan peptide | Mastoparan peptide | Mastoparan_peptide | 4 |
IPR013215 | 13,215 | Cobalamin-independent methionine synthase MetE, N-terminal | Cbl-indep_Met_Synth_N | Domain | 17,464 | false | false | Cobalamin-independent methionine synthase, MetE, catalyses the synthesis of the amino acid methionine by the transfer of a methyl group from methyltetrahydrofolate to homocysteine [ ]. The N-terminal and C-terminal domains of MetE together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind... | [
"GO:0003871",
"GO:0008270",
"GO:0008652"
] | [
"5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity",
"zinc ion binding",
"amino acid biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF08267"
] | [
"Meth_synt_1"
] | [
17464
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.14",
"PWY-5041",
"PWY-6151",
"PWY-6936",
"PWY-702"
] | [
"EC:2.1.1.14",
"METACYC:PWY-5041",
"METACYC:PWY-6151",
"METACYC:PWY-6936",
"METACYC:PWY-702"
] | 5 | [
"1t7l",
"1u1h",
"1u1j",
"1u1u",
"1u22",
"1xdj",
"1xpg",
"1xr2",
"2nq5",
"3bq5",
"3bq6",
"3l7r",
"3ppc",
"3ppf",
"3ppg",
"3pph",
"3t0c",
"4l5z",
"4l61",
"4l64",
"4l65",
"4l6h",
"4l6o",
"4qqu",
"4ztx",
"4zty"
] | 26 | [
"PUB00017130"
] | [
"15326182"
] | [
"Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
393,
12769,
4234,
68
] | 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"
] | [
16,
1,
1,
8,
1,
1,
18
] | 7 | true | Domain | Cobalamin-independent methionine synthase MetE, N-terminal | Cobalamin-independent methionine synthase MetE, N-terminal | Cbl-indep_Met_Synth_N | 7 |
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