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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR000001 | 1 | Kringle | Kringle | Domain | 21,741 | false | false | Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [ , , ]. Kringle domains [ , , ] are characterised... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00051",
"PS50070",
"SM00130",
"cd00108"
] | [
"Kringle",
"KRINGLE_2",
"KR",
"KR"
] | [
20506,
21634,
21101,
17509
] | 4 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"PDOC00020",
"R-BTA-6798695",
"R-BTA-75205",
"R-CEL-5140745",
"R-CFA-114608",
"R-CFA-1257604",
"R-CFA-5673001",
"R-CFA-6806942",
"R-CFA-6807004",
"R-CFA-6811558",
"R-CFA-8851805",
"R-CFA-8851907",
"R-CFA-8865999",
"R-CFA-8874081",
"R-CFA-8875513",
"R-CFA-8875555",
"R-CFA-... | [
"EC:3.4.21",
"PROSITEDOC:PDOC00020",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-75205",
"REACTOME:R-CEL-5140745",
"REACTOME:R-CFA-114608",
"REACTOME:R-CFA-1257604",
"REACTOME:R-CFA-5673001",
"REACTOME:R-CFA-6806942",
"REACTOME:R-CFA-6807004",
"REACTOME:R-CFA-6811558",
"REACTOME:R-CFA-8851805",
... | 133 | [
"1a0h",
"1b2i",
"1bht",
"1cea",
"1ceb",
"1gmn",
"1gmo",
"1gp9",
"1hpj",
"1hpk",
"1i5k",
"1i71",
"1jfn",
"1kdu",
"1ki0",
"1kiv",
"1krn",
"1nk1",
"1nl1",
"1nl2",
"1pk2",
"1pk4",
"1pkr",
"1pmk",
"1pml",
"1tpk",
"1urk",
"2doh",
"2doi",
"2fd6",
"2feb",
"2hpp"... | 134 | [
"PUB00000803",
"PUB00001541",
"PUB00001620",
"PUB00002414",
"PUB00003257",
"PUB00003400"
] | [
"3891096",
"6373375",
"1879523",
"3886654",
"2157850",
"3131537"
] | [
"Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules.",
"Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases.",
"Evolutionary origin of numerous kringles in human and simian apolip... | [
1985,
1984,
1991,
1985,
1990,
1987
] | 6 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae sp. ChoanoV1",
"Pseudoalteromonas amylolytica",
"viral metagenome"
] | [
21733,
2,
1,
5
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
39,
3,
87,
43,
68
] | 6 | true | Domain | Kringle | Kringle | Kringle | 8 |
IPR000003 | 3 | Retinoid X receptor/HNF4 | Retinoid-X_rcpt/HNF4 | Family | 8,170 | false | false | Steroid or nuclear hormone receptors (NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members of the superfamily include the steroid hormone receptors and r... | [
"GO:0003677",
"GO:0003707",
"GO:0008270",
"GO:0006355",
"GO:0005634"
] | [
"DNA binding",
"nuclear steroid receptor activity",
"zinc ion binding",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00545"
] | [
"RETINOIDXR"
] | [
8170
] | 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-383280",
"R-BTA-5362517",
"R-CEL-383280",
"R-DME-159418",
"R-DME-200425",
"R-DME-381340",
"R-DME-383280",
"R-DME-400206",
"R-DME-5362517",
"R-DME-9029569",
"R-DME-9616222",
"R-DME-9623433",
"R-DME-9707564",
"R-DME-9841922",
"R-DRE-159418",
"R-DRE-381340",
"R-DRE-400206",
"R-... | [
"REACTOME:R-BTA-383280",
"REACTOME:R-BTA-5362517",
"REACTOME:R-CEL-383280",
"REACTOME:R-DME-159418",
"REACTOME:R-DME-200425",
"REACTOME:R-DME-381340",
"REACTOME:R-DME-383280",
"REACTOME:R-DME-400206",
"REACTOME:R-DME-5362517",
"REACTOME:R-DME-9029569",
"REACTOME:R-DME-9616222",
"REACTOME:R-DME... | 85 | [
"1dkf",
"1fby",
"1fm6",
"1fm9",
"1g1u",
"1g2n",
"1g5y",
"1h9u",
"1hg4",
"1k74",
"1mv9",
"1mvc",
"1mzn",
"1r1k",
"1r20",
"1rdt",
"1uhl",
"1xdk",
"1xiu",
"1xls",
"1xv9",
"1xvp",
"1z5x",
"2acl",
"2gl8",
"2nxx",
"2p1t",
"2p1u",
"2p1v",
"2q60",
"2r40",
"2zxz"... | 127 | [
"PUB00004464",
"PUB00006168",
"PUB00015853",
"PUB00057400"
] | [
"7899080",
"8165128",
"14747695",
"19440305"
] | [
"Vitamin D receptor contains multiple dimerization interfaces that are functionally different.",
"Human androgen receptor expressed in HeLa cells activates transcription in vitro.",
"Nuclear receptors: the evolution of diversity.",
"Identification of an endogenous ligand bound to a native orphan nuclear recep... | [
1995,
1994,
2004,
2009
] | 4 | [
"IPR001723"
] | [] | 1 | 0 | 1 | [
"Metazoa"
] | [
8170
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
40,
4,
22,
20,
24
] | 6 | true | Family | Retinoid X receptor/HNF4 | Retinoid X receptor/HNF4 | Retinoid-X_rcpt/HNF4 | 9 |
IPR000006 | 6 | Metallothionein, vertebrate | Metalthion_vert | Family | 2,444 | false | false | Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [ , ]. An empirical classification into three classes has been proposed by Fowler and coworkers [ ] and K... | [
"GO:0046872"
] | [
"metal ion binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS",
"PANTHER"
] | [
"PF00131",
"PR00860",
"PTHR23299"
] | [
"Metallothio",
"MTVERTEBRATE",
""
] | [
2435,
2038,
2252
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00180",
"R-BTA-5661231",
"R-CFA-5661231",
"R-DRE-5661231",
"R-GGA-5661231",
"R-HSA-5661231",
"R-HSA-877300",
"R-MMU-5661231",
"R-RNO-5661231",
"R-SSC-5661231"
] | [
"PROSITEDOC:PDOC00180",
"REACTOME:R-BTA-5661231",
"REACTOME:R-CFA-5661231",
"REACTOME:R-DRE-5661231",
"REACTOME:R-GGA-5661231",
"REACTOME:R-HSA-5661231",
"REACTOME:R-HSA-877300",
"REACTOME:R-MMU-5661231",
"REACTOME:R-RNO-5661231",
"REACTOME:R-SSC-5661231"
] | 10 | [
"1dfs",
"1dft",
"1ji9",
"1m0g",
"1mhu",
"1mrb",
"1mrt",
"2f5h",
"2fj4",
"2fj5",
"2mhu",
"2mrb",
"2mrt",
"4mt2"
] | 14 | [
"PUB00001490",
"PUB00003570",
"PUB00003571",
"PUB00005944",
"PUB00078698"
] | [
"2959513",
"1779825",
"1779826",
"2959504",
"21633816"
] | [
"Chemistry and biochemistry of metallothionein.",
"Overview of metallothionein.",
"Definitions and nomenclature of metallothioneins.",
"Nomenclature of metallothionein.",
"Metallothionein protein evolution: a miniassay."
] | [
1987,
1991,
1991,
1987,
2011
] | 5 | [] | [] | 0 | 0 | null | [
"Vertebrata"
] | [
2444
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
35,
13,
14
] | 4 | true | Family | Metallothionein, vertebrate | Metallothionein, vertebrate | Metalthion_vert | 1 |
IPR000007 | 7 | Tubby, C-terminal | Tubby_C | Domain | 15,382 | false | false | Tubby, an autosomal recessive mutation, mapping to mouse chromosome 7, was recently found to be the result of a splicing defect in a novel gene with unknown function. This mutation maps to the tub gene [ , ]. The mouse tubby mutation is the cause of maturity-onset obesity, insulin resistance and sensory deficits. By co... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS"
] | [
"PF01167",
"PR01573"
] | [
"Tub",
"SUPERTUBBY"
] | [
15378,
12899
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00923",
"R-CEL-5610787",
"R-HSA-5610787",
"R-HSA-8951664",
"R-MMU-5610787",
"R-MMU-8951664"
] | [
"PROSITEDOC:PDOC00923",
"REACTOME:R-CEL-5610787",
"REACTOME:R-HSA-5610787",
"REACTOME:R-HSA-8951664",
"REACTOME:R-MMU-5610787",
"REACTOME:R-MMU-8951664"
] | 6 | [
"1c8z",
"1i7e",
"1s31",
"2fim",
"3c5n",
"8fh3"
] | 6 | [
"PUB00000932",
"PUB00004232",
"PUB00007281",
"PUB00014197"
] | [
"8612280",
"8606774",
"10591637",
"14708010"
] | [
"Identification and characterization of the mouse obesity gene tubby: a member of a novel gene family.",
"A candidate gene for the mouse mutation tubby.",
"Implication of tubby proteins as transcription factors by structure-based functional analysis.",
"Tubby proteins: the plot thickens."
] | [
1996,
1996,
1999,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"marine metagenome"
] | [
15380,
2
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
53,
3,
34,
5,
22,
20,
34,
22,
85
] | 9 | true | Domain | Tubby, C-terminal | Tubby, C-terminal | Tubby_C | 8 |
IPR000009 | 9 | Protein phosphatase 2A regulatory subunit PR55 | PP2A_PR55 | Family | 14,179 | false | false | Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase implicated in many cellular processes, including the regulation of metabolic enzymes and proteins involved in signal transduction [ , ]. PP2A is a trimer composed of a 36kDa catalytic subunit, a 65kDa regulatory subunit (subunit A) and a variable third sub... | [
"GO:0019888",
"GO:0000159"
] | [
"protein phosphatase regulator activity",
"protein phosphatase type 2A complex"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PIRSF",
"PRINTS",
"PANTHER"
] | [
"PIRSF037309",
"PR00600",
"PTHR11871"
] | [
"PP2A_PR55",
"PP2APR55",
""
] | [
11746,
13709,
14038
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00785",
"R-CEL-2995383",
"R-CEL-69231",
"R-CEL-69273",
"R-CEL-975957",
"R-CEL-9860927",
"R-DDI-69231",
"R-DDI-69273",
"R-DME-209155",
"R-DME-209190",
"R-DME-209214",
"R-DME-209360",
"R-DME-209396",
"R-DME-209413",
"R-DME-209440",
"R-DME-209461",
"R-DME-2995383",
"R-DME-432553"... | [
"PROSITEDOC:PDOC00785",
"REACTOME:R-CEL-2995383",
"REACTOME:R-CEL-69231",
"REACTOME:R-CEL-69273",
"REACTOME:R-CEL-975957",
"REACTOME:R-CEL-9860927",
"REACTOME:R-DDI-69231",
"REACTOME:R-DDI-69273",
"REACTOME:R-DME-209155",
"REACTOME:R-DME-209190",
"REACTOME:R-DME-209214",
"REACTOME:R-DME-209360... | 42 | [
"3dw8",
"8so0",
"8ttb",
"8twe",
"8uo5",
"9c6b",
"9c7t",
"9mzw",
"9n0y",
"9n0z"
] | 10 | [
"PUB00000344",
"PUB00003499",
"PUB00075288",
"PUB00075290"
] | [
"1849734",
"1370560",
"23886942",
"21852958"
] | [
"Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform.",
"The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little ... | [
1991,
1992,
2013,
2011
] | 4 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Eukaryota"
] | [
20,
14159
] | 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... | [
18,
1,
20,
3,
21,
17,
2,
14,
30,
1,
1,
43
] | 12 | true | Family | Protein phosphatase 2A regulatory subunit PR55 | Protein phosphatase 2A regulatory subunit PR55 | PP2A_PR55 | 9 |
IPR000010 | 10 | Cystatin domain | Cystatin_dom | Domain | 22,591 | false | false | This entry represents the cystatin domain. Cystatins occur mainly as single-domain proteins. However, some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains. Cystatins are cysteine proteinase inhibitors belonging to MEROPS inhibitor family I25, clan IH [ , , ]. They m... | [
"GO:0004869"
] | [
"cysteine-type endopeptidase inhibitor activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PFAM",
"SMART",
"CDD"
] | [
"PF00031",
"PF16845",
"SM00043",
"cd00042"
] | [
"Cystatin",
"SQAPI",
"CY",
"CY"
] | [
14944,
6776,
16798,
20038
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00259",
"R-BTA-114608",
"R-BTA-381426",
"R-BTA-6798695",
"R-BTA-8957275",
"R-CEL-381426",
"R-CEL-6798695",
"R-CEL-8957275",
"R-DDI-6798695",
"R-HSA-114608",
"R-HSA-140837",
"R-HSA-375276",
"R-HSA-381426",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-6798695",
"R-HSA-6809371",
"R-HSA... | [
"PROSITEDOC:PDOC00259",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-CEL-381426",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-8957275",
"REACTOME:R-DDI-6798695",
"REACTOME:R-HSA-114608",
"REACTOME:R-HSA-140837",
"REACTOME:R-HSA... | 37 | [
"1a67",
"1a90",
"1cew",
"1cyu",
"1cyv",
"1dvc",
"1dvd",
"1eqk",
"1g96",
"1gd3",
"1gd4",
"1m9g",
"1mnl",
"1mol",
"1n9j",
"1nb3",
"1nb5",
"1r4c",
"1rn7",
"1roa",
"1stf",
"1tij",
"1yvb",
"2ch9",
"2kxg",
"2l4v",
"2mzv",
"2oct",
"2w9p",
"2w9q",
"3gax",
"3ima"... | 126 | [
"PUB00001614",
"PUB00003412",
"PUB00014312"
] | [
"1855589",
"2107324",
"14587292"
] | [
"The cystatins: protein inhibitors of cysteine proteinases.",
"Evolution of proteins of the cystatin superfamily.",
"Cystatins."
] | [
1991,
1990,
2003
] | 3 | [] | [
"IPR025760",
"IPR025764",
"IPR027358"
] | 0 | 3 | 0 | [
"Bacteria",
"Bracoviriform",
"Eukaryota",
"viral metagenome"
] | [
274,
43,
22273,
1
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
44,
4,
33,
5,
39,
71,
32,
102,
73
] | 9 | true | Domain | Cystatin domain | Cystatin domain | Cystatin_dom | 6 |
IPR000011 | 11 | Ubiquitin/SUMO-activating enzyme E1-like | UBQ/SUMO-activ_enz_E1-like | Family | 11,773 | false | false | This entry includes Ubiquitin-activating enzyme E1 (Uba1), SUMO-activating enzyme subunit 1 (Sae1) and similar proteins from eukaryotes. Sae1 is an heterodimer that acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4 and mediates ATP-dependent activation of SUMO proteins [ , , ]. The post-translational att... | [
"GO:0008641",
"GO:0036211"
] | [
"ubiquitin-like modifier activating enzyme activity",
"protein modification process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR01849"
] | [
"UBIQUITINACT"
] | [
11773
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00463",
"R-BTA-3065676",
"R-BTA-3065678",
"R-BTA-8866652",
"R-BTA-983168",
"R-DDI-1169408",
"R-DDI-3065676",
"R-DDI-3065678",
"R-DDI-8866652",
"R-DDI-936440",
"R-DDI-983168",
"R-DDI-9909505",
"R-DRE-3065676",
"R-DRE-3065678",
"R-HSA-1169408",
"R-HSA-168928",
"R-HSA-3065676",
"... | [
"PROSITEDOC:PDOC00463",
"REACTOME:R-BTA-3065676",
"REACTOME:R-BTA-3065678",
"REACTOME:R-BTA-8866652",
"REACTOME:R-BTA-983168",
"REACTOME:R-DDI-1169408",
"REACTOME:R-DDI-3065676",
"REACTOME:R-DDI-3065678",
"REACTOME:R-DDI-8866652",
"REACTOME:R-DDI-936440",
"REACTOME:R-DDI-983168",
"REACTOME:R-D... | 42 | [
"1y8q",
"1y8r",
"3cmm",
"3kyc",
"3kyd",
"4ii2",
"4ii3",
"4nnj",
"4p22",
"5knl",
"5l6h",
"5l6i",
"5l6j",
"5tr4",
"5um6",
"6cwy",
"6cwz",
"6dc6",
"6nya",
"6o82",
"6o83",
"6xog",
"6xoh",
"6xoi",
"6zhs",
"6zht",
"6zhu",
"6zqh",
"7k5j",
"7pvn",
"7pyv",
"7sol"... | 78 | [
"PUB00015619",
"PUB00015620",
"PUB00015621",
"PUB00015625",
"PUB00038452",
"PUB00058677",
"PUB00063223"
] | [
"15454246",
"14998368",
"15556404",
"15196553",
"15660128",
"20164921",
"11451954"
] | [
"The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.",
"Getting into position: the catalytic mechanisms of protein ubiquitylation.",
"Polyubiquitin chains: polymeric protein signals.",
"The novel functions of ubiquitination in signaling.",
"Structures of the SUMO E1 provi... | [
2004,
2004,
2004,
2004,
2005,
2010,
2001
] | 7 | [
"IPR045886"
] | [
"IPR018075"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Mimiviridae",
"metagenomes"
] | [
13,
12,
11729,
11,
8
] | 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... | [
12,
3,
7,
10,
14,
12,
2,
15,
24,
1,
2,
44
] | 12 | true | Family | Ubiquitin/SUMO-activating enzyme E1-like | Ubiquitin/SUMO-activating enzyme E1-like | UBQ/SUMO-activ_enz_E1-like | 9 |
IPR000012 | 12 | Retroviral VpR/VpX protein | RetroV_VpR/X | Family | 14,653 | false | false | null | [
"GO:0019058",
"GO:0042025"
] | [
"viral life cycle",
"host cell nucleus"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"PRINTS"
] | [
"MF_04080",
"PF00522",
"PR00444"
] | [
"HIV_VPR",
"VPR",
"HIVVPRVPX"
] | [
12451,
14650,
13505
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180897",
"R-HSA-180910"
] | [
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-175474",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177539",
"REACTOME:R-HSA-180... | 14 | [
"1bde",
"1ceu",
"1dsj",
"1dsk",
"1esx",
"1fi0",
"1m8l",
"1vpc",
"1x9v",
"4cc9",
"4z8l",
"5aja",
"5jk7",
"6xqi",
"6xqj",
"6zx9",
"7v7c"
] | 17 | [
"PUB00000018",
"PUB00004048"
] | [
"2611042",
"2797181"
] | [
"Genomic divergence of HIV-2 from Ghana.",
"Sequence of a novel simian immunodeficiency virus from a wild-caught African mandrill."
] | [
1989,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Actinomycetes",
"Lentivirus"
] | [
2,
14651
] | 2 | [] | [] | 0 | true | Family | Retroviral VpR/VpX protein | Retroviral VpR/VpX protein | RetroV_VpR/X | 9 |
IPR000013 | 13 | Peptidase M7, snapalysin | Peptidase_M7 | Family | 2,055 | false | false | This group of metallopeptidases belong to the MEROPS peptidase family M7 (snapalysin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA. With a molecular weight of around 16kDa, Streptomyces extracellular neutral protease ... | [
"GO:0004222",
"GO:0008270",
"GO:0006508",
"GO:0005576"
] | [
"metalloendopeptidase activity",
"zinc ion binding",
"proteolysis",
"extracellular region"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"NCBIFAM",
"PFAM",
"PIRSF",
"PRINTS"
] | [
"NF033628",
"PF02031",
"PIRSF016573",
"PR00787"
] | [
"snapalysin",
"Peptidase_M7",
"Peptidase_M7",
"NEUTRALPTASE"
] | [
758,
2055,
1003,
2007
] | 4 | [
"EC"
] | [
"3.4.24.77"
] | [
"EC:3.4.24.77"
] | 1 | [
"1c7k",
"1kuh",
"4hx3"
] | 3 | [
"PUB00003579"
] | [
"7674922"
] | [
"Evolutionary families of metallopeptidases."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillati"
] | [
2055
] | 1 | [] | [] | 0 | true | Family | Peptidase M7, snapalysin | Peptidase M7, snapalysin | Peptidase_M7 | 1 |
IPR000014 | 14 | PAS domain | PAS | Domain | 531,533 | false | false | PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [ ]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in dif... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PROFILE",
"SMART",
"NCBIFAM",
"CDD"
] | [
"PF13188",
"PF13426",
"PS50112",
"SM00091",
"TIGR00229",
"cd00130"
] | [
"PAS_8",
"PAS_9",
"PAS",
"PAS",
"sensory_box",
"PAS"
] | [
44079,
155740,
399400,
379344,
388190,
473527
] | 6 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50112",
"R-BTA-1296072",
"R-CEL-1234158",
"R-CEL-1234176",
"R-CEL-5689880",
"R-CEL-8951664",
"R-CEL-9768919",
"R-CFA-1296072",
"R-CFA-5576890",
"R-DME-1234158",
"R-DME-1234176",
"R-DME-1296072",
"R-DME-211945",
"R-DME-418555",
"R-DME-432395",
"R-DME-432408",
"R-DME-432490",
"R... | [
"PROSITEDOC:PDOC50112",
"REACTOME:R-BTA-1296072",
"REACTOME:R-CEL-1234158",
"REACTOME:R-CEL-1234176",
"REACTOME:R-CEL-5689880",
"REACTOME:R-CEL-8951664",
"REACTOME:R-CEL-9768919",
"REACTOME:R-CFA-1296072",
"REACTOME:R-CFA-5576890",
"REACTOME:R-DME-1234158",
"REACTOME:R-DME-1234176",
"REACTOME:... | 150 | [
"1byw",
"1d06",
"1d7e",
"1dp6",
"1dp8",
"1dp9",
"1drm",
"1ew0",
"1f98",
"1f9i",
"1g28",
"1gsv",
"1gsw",
"1gsx",
"1jnu",
"1kou",
"1ll8",
"1lsv",
"1lsw",
"1lsx",
"1lt0",
"1mzu",
"1n9l",
"1n9n",
"1n9o",
"1nwz",
"1odv",
"1ot6",
"1ot9",
"1ota",
"1otb",
"1otd"... | 546 | [
"PUB00005472",
"PUB00014500",
"PUB00014501",
"PUB00015791"
] | [
"9301332",
"15009198",
"12377121",
"10357859"
] | [
"PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox.",
"The PAS fold. A redefinition of the PAS domain based upon structural prediction.",
"Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation.",
"PAS domains: internal sensors of oxyg... | [
1997,
2004,
2002,
1999
] | 4 | [] | [
"IPR013655",
"IPR013656",
"IPR013767",
"IPR059127"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
16268,
413505,
96392,
84,
5284
] | 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",... | [
149,
13,
207,
64,
14,
152,
123,
14,
66,
165,
3,
7,
111
] | 13 | true | Domain | PAS domain | PAS domain | PAS | 3 |
IPR000015 | 15 | Outer membrane usher protein | Fimb_usher | Family | 29,210 | false | false | In Gram-negative bacteria the biogenesis of fimbriae (or pili) requires a two-component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher' [ , , ]. The usher protein is rather large (from 86 to 100kDa) and seems to be mainly... | [
"GO:0015473",
"GO:0009297",
"GO:0016020"
] | [
"fimbrial usher porin activity",
"pilus assembly",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER"
] | [
"PF00577",
"PTHR30451"
] | [
"Usher",
""
] | [
27974,
29124
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00886"
] | [
"PROSITEDOC:PDOC00886"
] | 1 | [
"1zdv",
"1zdx",
"1ze3",
"2kt6",
"2vqi",
"2xet",
"3bwu",
"3fcg",
"3fip",
"3l48",
"3ohn",
"3rfz",
"4b0e",
"4b0m",
"4j3o",
"6cd2",
"6e14",
"6e15",
"7b0x",
"7lhg",
"7lhh",
"7lhi",
"9bog",
"9fw9",
"9fwb",
"9fwz",
"9fx8",
"9fxb",
"9fxs",
"9fy9"
] | 30 | [
"PUB00002237",
"PUB00002841",
"PUB00005083",
"PUB00049856",
"PUB00052911"
] | [
"7906265",
"7909802",
"7906046",
"18485872",
"19380723"
] | [
"Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli.",
"Chaperone-assisted self-assembly of pili independent of cellular energy.",
"Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function coo... | [
1994,
1994,
1993,
2008,
2009
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
29088,
57,
65
] | 3 | [
"Escherichia coli (strain K12)"
] | [
11
] | 1 | true | Family | Outer membrane usher protein | Outer membrane usher protein | Fimb_usher | 3 |
IPR000018 | 18 | P2Y purinoceptor 4 | P2Y4 | Family | 710 | false | false | There are three distinct families of extracellular receptors for purine and pyrimidine nucleotides [ ], known as P1, P2X and P2Y purinoceptors [ ]. These receptors induce a wide variety of biological effects and are involved in many different cellular functions [ , , ]. P2X receptors are ligand-gated ion channels, wher... | [
"GO:0045028",
"GO:0007186",
"GO:0030321",
"GO:0016020"
] | [
"G protein-coupled purinergic nucleotide receptor activity",
"G protein-coupled receptor signaling pathway",
"transepithelial chloride transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01066"
] | [
"P2Y4PRNOCPTR"
] | [
710
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"325",
"R-HSA-417957",
"R-HSA-418594",
"R-MMU-417957",
"R-MMU-418594",
"R-RNO-417957",
"R-RNO-418594"
] | [
"IUPHAR:325",
"REACTOME:R-HSA-417957",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-417957",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-417957",
"REACTOME:R-RNO-418594"
] | 7 | [
"9k0k"
] | 1 | [
"PUB00002940",
"PUB00007054",
"PUB00028347",
"PUB00033968",
"PUB00066193",
"PUB00066194",
"PUB00066195",
"PUB00066196",
"PUB00066197",
"PUB00066198",
"PUB00066203",
"PUB00066204",
"PUB00066205",
"PUB00066206",
"PUB00066207",
"PUB00066208",
"PUB00066209",
"PUB00066210",
"PUB000662... | [
"8537336",
"12270951",
"8872457",
"11111826",
"10629443",
"20471713",
"11099464",
"19921464",
"11734617",
"16257449",
"9364468",
"7724657",
"16968944",
"8508924",
"19386608",
"8921391",
"8702478",
"12724320",
"18404483",
"9755289",
"11794691",
"16914897",
"16934527",
"1... | [
"Cloning and functional expression of a human uridine nucleotide receptor.",
"Molecular physiology of P2X receptors.",
"Modelling the P2Y purinoceptor using rhodopsin as template.",
"Molecular pharmacology of P2Y-receptors.",
"Renal vascular reactivity to P(2)-purinoceptor activation in spontaneously hypert... | [
1995,
2002,
1995,
2000,
2000,
2011,
2000,
2010,
2001,
2006,
1997,
1994,
2006,
1993,
2009,
1996,
1996,
2003,
2006,
1998,
2001,
2006,
2006,
2000,
2001,
2005,
2009,
2001,
2009,
2006,
1995,
2000,
1998,
2008,
2006,
2006,
2003
] | 37 | [
"IPR000276"
] | [] | 1 | 0 | 1 | [
"Vertebrata"
] | [
710
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
2,
2
] | 4 | true | Family | P2Y purinoceptor 4 | P2Y purinoceptor 4 | P2Y4 | 8 |
IPR000020 | 20 | Anaphylatoxin/fibulin | Anaphylatoxin/fibulin | Domain | 8,581 | false | false | This entry represents C3a, C4a and C5a anaphylatoxins, which are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins. Complement components C3, C4 and C5 are ... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF01821",
"PS01177",
"PS01178",
"SM00104",
"cd00017"
] | [
"ANATO",
"ANAPHYLATOXIN_1",
"ANAPHYLATOXIN_2",
"ANATO",
"ANATO"
] | [
7322,
6418,
8103,
7807,
6578
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00906",
"R-BTA-173736",
"R-BTA-174577",
"R-BTA-198933",
"R-BTA-375276",
"R-BTA-381426",
"R-BTA-418594",
"R-BTA-6798695",
"R-BTA-8957275",
"R-BTA-977606",
"R-CEL-2129379",
"R-HSA-166663",
"R-HSA-166665",
"R-HSA-173736",
"R-HSA-174577",
"R-HSA-198933",
"R-HSA-2129379",
"R-HSA-37... | [
"PROSITEDOC:PDOC00906",
"REACTOME:R-BTA-173736",
"REACTOME:R-BTA-174577",
"REACTOME:R-BTA-198933",
"REACTOME:R-BTA-375276",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-977606",
"REACTOME:R-CEL-2129379",
"REACTOME:R-HSA-1... | 47 | [
"1c5a",
"1cfa",
"1kjs",
"2a73",
"3cu7",
"3hqa",
"3hqb",
"3kls",
"3km9",
"3prx",
"3pvm",
"4e0s",
"4hw5",
"4hwj",
"4i6o",
"4p39",
"4p3a",
"4p3b",
"4uu9",
"4wb2",
"4wb3",
"5b4p",
"5hcc",
"5hcd",
"5hce",
"5i5k",
"5jpm",
"5jpn",
"6jv7",
"6jv8",
"6rqj",
"6ru5"... | 58 | [
"PUB00001343",
"PUB00002512",
"PUB00003065",
"PUB00003073",
"PUB00003181",
"PUB00011223"
] | [
"3081348",
"2777798",
"2269669",
"8245130",
"1431125",
"12778127"
] | [
"C5a fragment of bovine complement. Purification, bioassays, amino-acid sequence and other structural studies.",
"Sequence of the gene for murine complement component C4.",
"Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure.",
"Structure and expression of fibulin-2, a n... | [
1986,
1989,
1990,
1993,
1992,
2003
] | 6 | [] | [
"IPR001840"
] | 0 | 1 | 0 | [
"Eukaryota",
"Pseudomonadati"
] | [
8578,
3
] | 2 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
25,
35,
23,
29
] | 5 | true | Domain | Anaphylatoxin/fibulin | Anaphylatoxin/fibulin | Anaphylatoxin/fibulin | 4 |
IPR000023 | 23 | Phosphofructokinase domain | Phosphofructokinase_dom | Domain | 47,419 | false | false | The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes [ ]. One enzyme that utilises this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the... | [
"GO:0003872",
"GO:0006096"
] | [
"6-phosphofructokinase activity",
"glycolytic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF00365"
] | [
"PFK"
] | [
47419
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.11",
"PWY-1042",
"PWY-1861",
"PWY-5484",
"PWY-7385",
"R-BTA-6798695",
"R-BTA-70171",
"R-CEL-6798695",
"R-CEL-70171",
"R-DME-6798695",
"R-DME-70171",
"R-HSA-6798695",
"R-HSA-70171",
"R-MMU-6798695",
"R-MMU-70171",
"R-RNO-6798695",
"R-RNO-70171",
"R-SCE-6798695",
"R-SCE-7017... | [
"EC:2.7.1.11",
"METACYC:PWY-1042",
"METACYC:PWY-1861",
"METACYC:PWY-5484",
"METACYC:PWY-7385",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-70171",
"REACTOME:R-CEL-6798695",
"REACTOME:R-CEL-70171",
"REACTOME:R-DME-6798695",
"REACTOME:R-DME-70171",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-70171... | 21 | [
"1kzh",
"1mto",
"1pfk",
"1zxx",
"2f48",
"2hig",
"2pfk",
"3f5m",
"3hno",
"3k2q",
"3o8l",
"3o8n",
"3o8o",
"3opy",
"3pfk",
"3u39",
"4a3s",
"4i36",
"4i4i",
"4i7e",
"4omt",
"4pfk",
"4rh3",
"4u1r",
"4wl0",
"4xyj",
"4xyk",
"4xz2",
"5xoe",
"5xz6",
"5xz7",
"5xz8"... | 54 | [
"PUB00000020",
"PUB00003237",
"PUB00004002",
"PUB00014238"
] | [
"7825568",
"2975709",
"2953977",
"12023862"
] | [
"Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency.",
"Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.",
"Mutations in the active site of Escheric... | [
1995,
1988,
1987,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
87,
27375,
19185,
5,
767
] | 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",... | [
42,
2,
28,
6,
1,
43,
14,
1,
45,
23,
2,
1,
116
] | 13 | true | Domain | Phosphofructokinase domain | Phosphofructokinase domain | Phosphofructokinase_dom | 6 |
IPR000025 | 25 | Melatonin receptor family | Melatonin_rcpt | Family | 3,216 | false | false | Melatonin is a naturally occurring compound found in animals, plants, and microbes [ , ]. In animals melatonin is secreted by the pineal gland during darkness [ , ]. It regulates a variety of neuroendocrine functions and is thought to play an essential role in circadian rhythms [ ]. Drugs that modify the action of mela... | [
"GO:0008502",
"GO:0007186",
"GO:0016020"
] | [
"melatonin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00857"
] | [
"MELATONINR"
] | [
3216
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"288",
"R-DRE-373076",
"R-DRE-418594",
"R-GGA-373076",
"R-GGA-418594",
"R-HSA-373076",
"R-HSA-418594",
"R-MMU-373076",
"R-MMU-418594",
"R-RNO-373076",
"R-RNO-418594"
] | [
"IUPHAR:288",
"REACTOME:R-DRE-373076",
"REACTOME:R-DRE-418594",
"REACTOME:R-GGA-373076",
"REACTOME:R-GGA-418594",
"REACTOME:R-HSA-373076",
"REACTOME:R-HSA-418594",
"REACTOME:R-MMU-373076",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-373076",
"REACTOME:R-RNO-418594"
] | 11 | [
"6me2",
"6me3",
"6me4",
"6me5",
"6me6",
"6me7",
"6me8",
"6me9",
"6ps8",
"7db6",
"7vgy",
"7vgz",
"7vh0"
] | 13 | [
"PUB00066873",
"PUB00066874",
"PUB00066875",
"PUB00066876",
"PUB00066877",
"PUB00066878",
"PUB00066879",
"PUB00066880",
"PUB00066881",
"PUB00066882"
] | [
"15206778",
"19033551",
"1649044",
"17901231",
"17298593",
"16473858",
"15992934",
"8936344",
"15357831",
"9933574"
] | [
"Melatonin in plants.",
"Phytomelatonin: a review.",
"Pineal melatonin: cell biology of its synthesis and of its physiological interactions.",
"Minireview: Entrainment of the suprachiasmatic clockwork in diurnal and nocturnal mammals.",
"Melatonin: therapeutic and clinical utilization.",
"Efficacy and saf... | [
2003,
2009,
1991,
2007,
2007,
2006,
2005,
1996,
2004,
1999
] | 10 | [
"IPR000276"
] | [
"IPR002278",
"IPR002280"
] | 1 | 2 | 0 | [
"Bilateria"
] | [
3216
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
13,
7,
6,
11
] | 4 | true | Family | Melatonin receptor family | Melatonin receptor family | Melatonin_rcpt | 9 |
IPR000026 | 26 | Guanine-specific ribonuclease N1-like | N1-like | Family | 8,591 | false | false | This entry represents Guanyl-specific ribonuclease N1 from Neurospora crassa [ ], and similar sequences from fungi and bacteria, including Ribonuclease from Bacillus amyloliquefaciens (also known as Barnase) and Ribonuclease clavin from Aspergillus clavatus. Barnase hydrolyses the phosphodiester bonds in RNA and oligor... | [
"GO:0003723",
"GO:0004521"
] | [
"RNA binding",
"RNA endonuclease activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM"
] | [
"PF00545"
] | [
"Ribonuclease"
] | [
8591
] | 1 | [
"EC"
] | [
"4.6.1.24"
] | [
"EC:4.6.1.24"
] | 1 | [
"1a2p",
"1aqz",
"1ay7",
"1b20",
"1b21",
"1b27",
"1b2m",
"1b2s",
"1b2u",
"1b2x",
"1b2z",
"1b3s",
"1ban",
"1bao",
"1bgs",
"1bir",
"1bne",
"1bnf",
"1bng",
"1bni",
"1bnj",
"1bnr",
"1bns",
"1box",
"1brg",
"1brh",
"1bri",
"1brj",
"1brk",
"1brn",
"1brs",
"1bsa"... | 187 | [
"PUB00000397",
"PUB00075293",
"PUB00094167"
] | [
"8110767",
"2977130",
"8706730"
] | [
"Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.",
"The amino acid sequence of ribonuclease N1, a guanine-specific ribonuclease from the fungus Neurospora crassa.",
"Clavin, a type-1 ribosome-inactivating protein from Aspergillus clavatus IFO 8605. cDNA isolatio... | [
1994,
1988,
1996
] | 3 | [] | [
"IPR001887"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"metagenomes"
] | [
5833,
2722,
17,
19
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Guanine-specific ribonuclease N1-like | Guanine-specific ribonuclease N1-like | N1-like | 6 |
IPR000028 | 28 | Chloroperoxidase | Chloroperoxidase | Domain | 9,007 | false | false | Chloroperoxidase (CPO), also known as Heme haloperoxidase, is a ~250 residue heme-containing glycoprotein that is secreted by various fungi. Chloroperoxidase was first identified in Caldariomyces fumago where it catalyses the hydrogen peroxide-dependent chlorination of cyclopentanedione during the biosynthesis of the a... | [
"GO:0004601"
] | [
"peroxidase activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PROFILE"
] | [
"PF01328",
"PS51405"
] | [
"Peroxidase_2",
"HEME_HALOPEROXIDASE"
] | [
8999,
8880
] | 2 | [
"GP"
] | [
"GenProp0213"
] | [
"GP:GenProp0213"
] | 1 | [
"1cpo",
"2civ",
"2ciw",
"2cix",
"2ciy",
"2ciz",
"2cj0",
"2cj1",
"2cj2",
"2cpo",
"2j18",
"2j19",
"2j5m",
"2yor",
"2yp1",
"5fuj",
"5fuk",
"5oxt",
"5oxu",
"5oy1",
"5oy2",
"6ekw",
"6ekx",
"6eky",
"6ekz",
"6el0",
"6el4",
"7o1r",
"7o1x",
"7o1z",
"7o2d",
"7o2g"... | 68 | [
"PUB00005255",
"PUB00040032",
"PUB00052607",
"PUB00052608"
] | [
"8747463",
"16790441",
"16628447",
"18220360"
] | [
"The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.",
"Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate.",
"Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental... | [
1995,
2006,
2006,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"viral metagenome"
] | [
9006,
1
] | 2 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
2
] | 1 | true | Domain | Chloroperoxidase | Chloroperoxidase | Chloroperoxidase | 8 |
IPR000030 | 30 | PPE domain | PPE_dom | Domain | 12,585 | false | false | This entry represents a domain found in proteins from actinomycetes named after a conserved N-terminal region of about 180 amino acids, the PPE motif. The C-terminal end of proteins belonging to the PPE family is variable, and on the basis of this region at least three groups can be distinguished. The MPTR subgroup is ... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00823"
] | [
"PPE"
] | [
12585
] | 1 | [
"REACTOME"
] | [
"R-HSA-9636249"
] | [
"REACTOME:R-HSA-9636249"
] | 1 | [
"2g38",
"4kxr",
"4w4k",
"4w4l",
"5xfs",
"6uuj",
"6vhr",
"6vj5"
] | 8 | [
"PUB00004280",
"PUB00054031",
"PUB00054032",
"PUB00054033",
"PUB00095123",
"PUB00103913",
"PUB00103914",
"PUB00103929",
"PUB00103930"
] | [
"9634230",
"19602151",
"18981138",
"18267304",
"31375544",
"32138343",
"32139546",
"25155747",
"25275011"
] | [
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.",
"Mycobacterial PE, PPE and ESX clusters: novel insights into the secretion of these most unusual protein families.",
"The ESX-5 secretion system of Mycobacterium marinum modulates the macrophage response.",
"Mycobacter... | [
1998,
2009,
2008,
2007,
2019,
2020,
2020,
2014,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Aduncisulcus paluster",
"Bacteria",
"Chenonavirus",
"freshwater metagenome"
] | [
1,
12580,
2,
2
] | 4 | [] | [] | 0 | true | Domain | PPE domain | PPE domain | PPE_dom | 8 |
IPR000031 | 31 | PurE domain | PurE_dom | Domain | 34,722 | false | false | The novo purine biosynthesis proceeds by two divergent paths. In bacteria, yeasts, and plants, 5-aminoimidazole ribonucleotide (AIR) is converted to 4-carboxy-AIR (CAIR) by two enzymes: N5-carboxy-AIR (N5-CAIR) synthetase (PurK) and N5-CAIR mutase (class I PurE). In animals, the conversion of AIR to CAIR requires a sin... | [
"GO:0006189"
] | [
"'de novo' IMP biosynthetic process"
] | [
"biological_process"
] | 1 | [
"PFAM",
"SMART",
"NCBIFAM"
] | [
"PF00731",
"SM01001",
"TIGR01162"
] | [
"AIRC",
"AIRC",
"purE"
] | [
34633,
34572,
27260
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0110",
"GenProp1406",
"GenProp1730",
"GenProp1757",
"R-CEL-73817",
"R-DME-73817",
"R-GGA-419140",
"R-HSA-73817",
"R-MMU-73817",
"R-RNO-73817"
] | [
"GP:GenProp0110",
"GP:GenProp1406",
"GP:GenProp1730",
"GP:GenProp1757",
"REACTOME:R-CEL-73817",
"REACTOME:R-DME-73817",
"REACTOME:R-GGA-419140",
"REACTOME:R-HSA-73817",
"REACTOME:R-MMU-73817",
"REACTOME:R-RNO-73817"
] | 10 | [
"1d7a",
"1o4v",
"1qcz",
"1u11",
"1xmp",
"2ate",
"2fw1",
"2fw6",
"2fw7",
"2fw8",
"2fw9",
"2fwa",
"2fwb",
"2fwi",
"2fwj",
"2fwp",
"2h31",
"2nsh",
"2nsj",
"2nsl",
"2ywx",
"3kuu",
"3lp6",
"3oow",
"3opq",
"3ors",
"3rg8",
"3rgg",
"3trh",
"4ay3",
"4ay4",
"4b4k"... | 63 | [
"PUB00056870",
"PUB00068323",
"PUB00068324",
"PUB00080668"
] | [
"7918411",
"9500840",
"7918410",
"8111040"
] | [
"Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.",
"Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis.",
"Carboxylases in de novo purine biosynthesis. Characte... | [
1994,
1998,
1994,
1994
] | 4 | [] | [
"IPR033626",
"IPR033747"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1469,
27332,
5127,
25,
769
] | 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",... | [
11,
1,
3,
2,
1,
3,
1,
1,
4,
6,
1,
1,
16
] | 13 | true | Domain | PurE domain | PurE domain | PurE_dom | 5 |
IPR000032 | 32 | Phosphocarrier protein HPr-like | HPr-like | Domain | 37,795 | false | false | This entry represents a structural domain found in both the histidine-containing phosphocarrier protein HPr, as well as its structural homologues, which includes the catabolite repression protein Crh found in Bacillus subtilis [ , ]. This domain has a α+β structure found in two layers with an overall architecture of an... | [] | [] | [] | 0 | [
"PFAM",
"PRINTS",
"PROFILE",
"NCBIFAM",
"CDD"
] | [
"PF00381",
"PR00107",
"PS51350",
"TIGR01003",
"cd00367"
] | [
"PTS-HPr",
"PHOSPHOCPHPR",
"PTS_HPR_DOM",
"PTS_HPr_family",
"PTS-HPr_like"
] | [
37493,
32928,
36689,
32165,
31957
] | 5 | [
"GP",
"GP"
] | [
"GenProp0119",
"GenProp1324"
] | [
"GP:GenProp0119",
"GP:GenProp1324"
] | 2 | [
"1cm2",
"1cm3",
"1fu0",
"1ggr",
"1hdn",
"1j6t",
"1jem",
"1k1c",
"1ka5",
"1kkl",
"1kkm",
"1mo1",
"1mu4",
"1opd",
"1pch",
"1pfh",
"1poh",
"1ptf",
"1qfr",
"1qr5",
"1rzr",
"1sph",
"1txe",
"1vrc",
"1y4y",
"1y50",
"1y51",
"1zvv",
"2ak7",
"2fep",
"2hid",
"2hpr"... | 64 | [
"PUB00000073",
"PUB00003342",
"PUB00003612",
"PUB00004777",
"PUB00005010",
"PUB00005243",
"PUB00025027",
"PUB00032584",
"PUB00039040",
"PUB00070137"
] | [
"2197982",
"7853396",
"8246840",
"1549615",
"7686067",
"7704530",
"11054290",
"15713472",
"16316990",
"9237995"
] | [
"The bacterial phosphoenolpyruvate: glycose phosphotransferase system.",
"High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.",
"Phosphoenolpyruvate:carbohydrate phosphotr... | [
1990,
1995,
1993,
1992,
1993,
1994,
2000,
2005,
2006,
1997
] | 10 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
253,
37178,
75,
6,
283
] | 5 | [
"Escherichia coli (strain K12)"
] | [
6
] | 1 | true | Domain | Phosphocarrier protein HPr-like | Phosphocarrier protein HPr-like | HPr-like | 9 |
IPR000033 | 33 | LDLR class B repeat | LDLR_classB_rpt | Repeat | 38,754 | false | false | The low-density lipoprotein receptor (LDLR) is the major cholesterol-carrying lipoprotein of plasma, acting to regulate cholesterol homeostasis in mammalian cells. The LDL receptor binds LDL and transports it into cells by acidic endocytosis. In order to be internalized, the receptor-ligand complex must first cluster i... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00058",
"PS51120",
"SM00135"
] | [
"Ldl_recept_b",
"LDLRB",
"LY"
] | [
31367,
32652,
38584
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51120",
"R-BTA-114608",
"R-BTA-8856825",
"R-BTA-8856828",
"R-BTA-8964026",
"R-BTA-8964038",
"R-DME-114608",
"R-DME-1227986",
"R-DME-1236394",
"R-DME-1250196",
"R-DME-1257604",
"R-DME-177929",
"R-DME-179812",
"R-DME-180292",
"R-DME-180336",
"R-DME-182971",
"R-DME-1963642",
"R-D... | [
"PROSITEDOC:PDOC51120",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-8856825",
"REACTOME:R-BTA-8856828",
"REACTOME:R-BTA-8964026",
"REACTOME:R-BTA-8964038",
"REACTOME:R-DME-114608",
"REACTOME:R-DME-1227986",
"REACTOME:R-DME-1236394",
"REACTOME:R-DME-1250196",
"REACTOME:R-DME-1257604",
"REACTOME:R-... | 149 | [
"1ijq",
"1n7d",
"1npe",
"1rwi",
"1rwl",
"3m0c",
"3p5b",
"3p5c",
"3s2k",
"3s8v",
"3s8z",
"3s94",
"3sob",
"3soq",
"3sov",
"3v64",
"3v65",
"3ww8",
"3ww9",
"3wwa",
"4a0p",
"4dg6",
"5b4x",
"5fww",
"5gje",
"6f0q",
"6f0s",
"6f0t",
"6h15",
"6h16",
"6i37",
"6i38"... | 98 | [
"PUB00000798",
"PUB00003391",
"PUB00004868",
"PUB00017008",
"PUB00017009",
"PUB00017010",
"PUB00042617"
] | [
"6091915",
"9790844",
"7603991",
"3513311",
"3494949",
"11373616",
"17457719"
] | [
"The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA.",
"An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.",
"Three-dimensional structure of a cyst... | [
1984,
1998,
1995,
1986,
1987,
2001,
2007
] | 7 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
55,
1176,
37473,
50
] | 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",
"Zea mays"
] | [
6,
13,
96,
35,
90,
66,
2,
2,
69,
3
] | 10 | true | Repeat | LDLR class B repeat | LDLR class B repeat | LDLR_classB_rpt | 6 |
IPR000034 | 34 | Laminin IV | Laminin_IV | Domain | 13,238 | false | false | Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matr... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00052",
"PS51115",
"SM00281"
] | [
"Laminin_B",
"LAMININ_IVA",
"LamB"
] | [
13156,
12809,
12513
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC51115",
"R-HSA-1474228",
"R-HSA-1971475",
"R-HSA-2022090",
"R-HSA-2022928",
"R-HSA-2024096",
"R-HSA-216083",
"R-HSA-2214320",
"R-HSA-3000157",
"R-HSA-3000171",
"R-HSA-3000178",
"R-HSA-3560783",
"R-HSA-3560801",
"R-HSA-3656237",
"R-HSA-3656253",
"R-HSA-373760",
"R-HSA-381426",
... | [
"PROSITEDOC:PDOC51115",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-1971475",
"REACTOME:R-HSA-2022090",
"REACTOME:R-HSA-2022928",
"REACTOME:R-HSA-2024096",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-2214320",
"REACTOME:R-HSA-3000157",
"REACTOME:R-HSA-3000171",
"REACTOME:R-HSA-3000178",
"REACTOME:R... | 32 | [
"4yep",
"4yeq",
"9i5a",
"9i5b"
] | 4 | [
"PUB00012222",
"PUB00017000",
"PUB00017032"
] | [
"3182802",
"10842354",
"15363809"
] | [
"Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains.",
"Form and function: the laminin family of heterotrimers.",
"Assembly and tissue functions of early embryonic laminins and netrins."
] | [
1988,
2000,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Stenosarchaea group",
"hydrothermal vent metagenome"
] | [
87,
13125,
24,
2
] | 4 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
18,
67,
36,
17,
20,
28
] | 6 | true | Domain | Laminin IV | Laminin IV | Laminin_IV | 6 |
IPR000035 | 35 | Alkylbase DNA glycosidase, conserved site | Alkylbase_DNA_glycsylse_CS | Conserved_site | 2,672 | false | false | Alkylbase DNA glycosidases [ ] are DNA repair enzymes that hydrolyse the deoxyribose N-glycosidic bond to excise various alkylated bases from a damaged DNA polymer. In Escherichia coli there are two alkylbase DNA glycosidases: one (gene tag) which is constitutively expressed and which is specific for the removal of 3-m... | [
"GO:0003905",
"GO:0006281"
] | [
"alkylbase DNA N-glycosylase activity",
"DNA repair"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00516"
] | [
"ALKYLBASE_DNA_GLYCOS"
] | [
2672
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"3.2.2.21",
"PDOC00447"
] | [
"EC:3.2.2.21",
"PROSITEDOC:PDOC00447"
] | 2 | [
"1diz",
"1mpg",
"1pvs",
"3cvs",
"3cvt",
"3cw7",
"3cwa",
"3cws",
"3cwt",
"3cwu",
"3d4v",
"3ogd",
"3oh6",
"3oh9",
"3s6i",
"4b21",
"4b22",
"4b23",
"4b24",
"4hsb"
] | 20 | [
"PUB00000053",
"PUB00001200",
"PUB00001201"
] | [
"3052269",
"2265619",
"2265620"
] | [
"Regulation and expression of the adaptive response to alkylating agents.",
"Cloning and expression in Escherichia coli of a gene for an alkylbase DNA glycosylase from Saccharomyces cerevisiae; a homologue to the bacterial alkA gene.",
"Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to th... | [
1988,
1990,
1990
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Dikarya",
"unclassified sequences"
] | [
60,
2495,
106,
11
] | 4 | [
"Escherichia coli (strain K12)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
2
] | 3 | true | Conserved_site | Alkylbase DNA glycosidase, conserved site | Alkylbase DNA glycosidase, conserved site | Alkylbase_DNA_glycsylse_CS | 1 |
IPR000036 | 36 | Peptidase A26, omptin | Peptidase_A26_omptin | Family | 1,686 | false | false | This group of aspartic peptidases belongs to the MEROPS family A26 (clan AF). Members of the family are transmembrane proteins. The type example for the family is omptin (also known as protease VII) from Escherichia coli, the product of the ompT gene. Omptin preferentially cleaves polypeptides between two basically-cha... | [
"GO:0004175",
"GO:0006508",
"GO:0009279"
] | [
"endopeptidase activity",
"proteolysis",
"cell outer membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PIRSF",
"PRINTS"
] | [
"PF01278",
"PIRSF001522",
"PR00482"
] | [
"Omptin",
"Peptidase_A26",
"OMPTIN"
] | [
1686,
1234,
1423
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00657"
] | [
"PROSITEDOC:PDOC00657"
] | 1 | [
"1i78",
"2x4m",
"2x55",
"2x56",
"4dcb",
"7xw0"
] | 6 | [
"PUB00000093",
"PUB00000349",
"PUB00000522",
"PUB00001330",
"PUB00002071",
"PUB00003795",
"PUB00011023",
"PUB00011707",
"PUB00021296",
"PUB00042504",
"PUB00065205",
"PUB00066803",
"PUB00076784",
"PUB00076785",
"PUB00076786",
"PUB00076883"
] | [
"2194475",
"1851433",
"8439290",
"6795036",
"3056908",
"2526282",
"10331925",
"11566868",
"10864493",
"2682266",
"23254940",
"21765428",
"4912600",
"10497172",
"21751400",
"11401715"
] | [
"The structure and function of the aspartic proteinases.",
"Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.",
"Evolutionary families of peptidases.",
"Gastric proteinases--structure, function, evolution and mechanism of action.",
"Purification, characterizat... | [
1990,
1991,
1993,
1981,
1988,
1989,
1999,
2001,
2000,
1989,
2013,
2011,
1970,
1999,
2011,
2001
] | 16 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"Nesevirus",
"ecological metagenomes"
] | [
1681,
1,
2,
2
] | 4 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Peptidase A26, omptin | Peptidase A26, omptin | Peptidase_A26_omptin | 4 |
IPR000037 | 37 | SsrA-binding protein | SsrA-bd_prot | Family | 25,307 | false | false | This entry represents SsrA-binding protein (aka small protein B or SmpB), which is a unique RNA-binding protein that is conserved throughout the bacterial kingdom and is an essential component of the SsrA quality-control system. Tight recognition of codon-anticodon pairings by the ribosome ensures the accuracy and fide... | [
"GO:0003723"
] | [
"RNA binding"
] | [
"molecular_function"
] | 1 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00023",
"PF01668",
"PTHR30308",
"TIGR00086",
"cd09294"
] | [
"SmpB",
"SmpB",
"",
"smpB",
"SmpB"
] | [
25037,
25306,
25250,
24888,
23281
] | 5 | [
"PROSITEDOC"
] | [
"PDOC01021"
] | [
"PROSITEDOC:PDOC01021"
] | 1 | [
"1j1h",
"1k8h",
"1p6v",
"1wjx",
"1zc8",
"2czj",
"2ob7",
"3iyq",
"3iyr",
"3iz4",
"4v6t",
"4v8q",
"5zey",
"6q95",
"6q97",
"6q98",
"6q9a",
"7abz",
"7ac7",
"7acj",
"7acr",
"7ljp",
"8vs9",
"8vsa"
] | 24 | [
"PUB00006449",
"PUB00045920"
] | [
"10393194",
"19132006"
] | [
"SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA).",
"Ribosome hijacking: a role for small protein B during trans-translation."
] | [
1999,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"candidate division MSBL1 archaeon SCGC-AAA382A20",
"unclassified sequences"
] | [
24543,
206,
15,
1,
542
] | 5 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | SsrA-binding protein | SsrA-binding protein | SsrA-bd_prot | 7 |
IPR000039 | 39 | Large ribosomal subunit protein eL18 | Ribosomal_eL18 | Family | 6,950 | false | false | Members of this family are large subunit ribosomal proteins which are found in eukaryotes and archaea [ , , ]. These proteins have 115 to 187 amino-acid residues. The family consists of: Vertebrate eL18 (known as L14 in Xenopus) [ , ] Plant eL18 Yeast eL18 (Rp28) Haloarcula marismortui (Halobacterium marismortui) HL29 ... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PANTHER"
] | [
"PTHR10934"
] | [
""
] | [
6950
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00850",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-CFA-156827",
"R-CFA-1799339",
"R-CFA-6791226",
"R-CFA-72689... | [
"PROSITEDOC:PDOC00850",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 79 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 671 | [
"PUB00000657",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00059102",
"PUB00101554"
] | [
"8218404",
"11297922",
"11290319",
"11114498",
"22096102",
"32669547"
] | [
"Nucleotide and deduced amino acid sequence of human ribosomal protein L18.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"The structure of the eukaryotic ribosome at 3.0 A resolution.",
"Structural sn... | [
1993,
2001,
2001,
2000,
2011,
2020
] | 6 | [] | [
"IPR022947"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
728,
6,
6198,
18
] | 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... | [
14,
1,
1,
2,
10,
10,
1,
6,
12,
2,
2,
15
] | 12 | true | Family | Large ribosomal subunit protein eL18 | Large ribosomal subunit protein eL18 | Ribosomal_eL18 | 6 |
IPR000040 | 40 | Acute myeloid leukemia 1 protein (AML1)/Runt | AML1_Runt | Family | 6,664 | false | false | null | [
"GO:0003677",
"GO:0005524",
"GO:0006355",
"GO:0005634"
] | [
"DNA binding",
"ATP binding",
"regulation of DNA-templated transcription",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PRINTS",
"PANTHER"
] | [
"PR00967",
"PTHR11950"
] | [
"ONCOGENEAML1",
""
] | [
6254,
6650
] | 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-549127",
"R-CEL-8877330",
"R-CEL-8878166",
"R-CEL-8934593",
"R-CEL-8936459",
"R-CEL-8939236",
"R-CEL-8939243",
"R-CEL-8939245",
"R-CEL-8939246",
"R-CEL-8939247",
"R-CEL-8939902",
"R-CEL-8941326",
"R-CEL-8941855",
"R-CEL-8941858",
"R-CEL-8951430",
"R-CEL-8951671",
"R-CEL-895193... | [
"REACTOME:R-CEL-549127",
"REACTOME:R-CEL-8877330",
"REACTOME:R-CEL-8878166",
"REACTOME:R-CEL-8934593",
"REACTOME:R-CEL-8936459",
"REACTOME:R-CEL-8939236",
"REACTOME:R-CEL-8939243",
"REACTOME:R-CEL-8939245",
"REACTOME:R-CEL-8939246",
"REACTOME:R-CEL-8939247",
"REACTOME:R-CEL-8939902",
"REACTOME... | 103 | [
"1cmo",
"1co1",
"1e50",
"1ean",
"1eao",
"1eaq",
"1h9d",
"1hjb",
"1hjc",
"1io4",
"1ljm",
"2j6w",
"3wts",
"3wtt",
"3wtu",
"3wtv",
"3wtw",
"3wtx",
"3wty",
"3wu1",
"4l0y",
"4l0z",
"4l18",
"6vg8",
"6vgd",
"6vge",
"6vgg"
] | 27 | [
"PUB00004459"
] | [
"7651838"
] | [
"Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia."
] | [
1995
] | 1 | [] | [
"IPR016554"
] | 0 | 1 | 0 | [
"Opisthokonta"
] | [
6664
] | 1 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
62,
23,
24,
19,
21
] | 6 | true | Family | Acute myeloid leukemia 1 protein (AML1)/Runt | Acute myeloid leukemia 1 protein (AML1)/Runt | AML1_Runt | 2 |
IPR000043 | 43 | Adenosylhomocysteinase-like | Adenosylhomocysteinase-like | Family | 32,325 | false | false | Adenosylhomocysteinase (S-adenosyl-L-homocysteine hydrolase, ) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. This enzyme is ubiquitous, highly conserved, and may play a key role in the regulation of the intr... | [] | [] | [] | 0 | [
"HAMAP",
"PFAM",
"PIRSF",
"PANTHER",
"SMART",
"NCBIFAM",
"CDD"
] | [
"MF_00563",
"PF05221",
"PIRSF001109",
"PTHR23420",
"SM00996",
"TIGR00936",
"cd00401"
] | [
"AdoHcyase",
"AdoHcyase",
"Ad_hcy_hydrolase",
"",
"AdoHcyase",
"ahcY",
"SAHH"
] | [
21082,
30992,
25259,
32094,
30320,
25484,
27797
] | 7 | [
"EC",
"GP",
"GP",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",... | [
"3.13.2.1",
"GenProp0789",
"GenProp1399",
"PWY-5041",
"PDOC00603",
"R-BTA-156581",
"R-BTA-1614635",
"R-BTA-425381",
"R-CEL-156581",
"R-CEL-1614635",
"R-DDI-156581",
"R-DDI-1614635",
"R-DME-156581",
"R-DME-1614635",
"R-DME-425381",
"R-DME-5578775",
"R-HSA-112043",
"R-HSA-1489509",
... | [
"EC:3.13.2.1",
"GP:GenProp0789",
"GP:GenProp1399",
"METACYC:PWY-5041",
"PROSITEDOC:PDOC00603",
"REACTOME:R-BTA-156581",
"REACTOME:R-BTA-1614635",
"REACTOME:R-BTA-425381",
"REACTOME:R-CEL-156581",
"REACTOME:R-CEL-1614635",
"REACTOME:R-DDI-156581",
"REACTOME:R-DDI-1614635",
"REACTOME:R-DME-156... | 42 | [
"1a7a",
"1b3r",
"1d4f",
"1k0u",
"1ky4",
"1ky5",
"1li4",
"1v8b",
"1xwf",
"2h5l",
"2ziz",
"2zj0",
"2zj1",
"3ce6",
"3d64",
"3dhy",
"3g1u",
"3glq",
"3gvp",
"3h9u",
"3mtg",
"3n58",
"3nj4",
"3ond",
"3one",
"3onf",
"3x2e",
"3x2f",
"4lvc",
"4pfj",
"4pgf",
"4yvf"... | 121 | [
"PUB00021119",
"PUB00038377",
"PUB00079516",
"PUB00079517",
"PUB00083397",
"PUB00083401",
"PUB00083402",
"PUB00083418",
"PUB00083432",
"PUB00083433",
"PUB00083434"
] | [
"9586999",
"16061414",
"11325033",
"15165742",
"12525476",
"16793548",
"16527252",
"19220705",
"24518248",
"21152975",
"27382360"
] | [
"Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength.",
"Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89.",
"Structure and function of S-adenosylhomocysteine hydrolase.",
"S-Adenosylhomocyste... | [
1998,
2005,
2000,
2004,
2003,
2006,
2006,
2009,
2014,
2011,
2016
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
975,
17748,
12842,
8,
752
] | 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... | [
15,
1,
10,
6,
14,
22,
1,
7,
20,
1,
1,
11
] | 12 | true | Family | Adenosylhomocysteinase-like | Adenosylhomocysteinase-like | Adenosylhomocysteinase-like | 3 |
IPR000044 | 44 | Uncharacterised lipoprotein MG045 | Uncharacterised_lipoprot_MG045 | Family | 79 | false | false | Mycoplasma genitalium has the smallest known genome of any free-living organism. Its complete genome sequence has been determined by whole-genome random sequencing and assembly [ ]. Only 470 putative coding regions were identified, including genes for DNA replication, transcription and translation, DNA repair, cellular... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"PRINTS"
] | [
"PR00905"
] | [
"MG045FAMILY"
] | [
79
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00002233",
"PUB00005212"
] | [
"8253680",
"7569993"
] | [
"A survey of the Mycoplasma genitalium genome by using random sequencing.",
"The minimal gene complement of Mycoplasma genitalium."
] | [
1993,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota",
"Plasmodium vivax North Korean"
] | [
78,
1
] | 2 | [] | [] | 0 | true | Family | Uncharacterised lipoprotein MG045 | Uncharacterised lipoprotein MG045 | Uncharacterised_lipoprot_MG045 | 7 |
IPR000045 | 45 | Prepilin type IV endopeptidase, peptidase domain | Prepilin_IV_endopep_pep | Domain | 31,058 | false | false | This entry represents the peptidase domain from the prepilin type IV endopeptidases [ ]. It can be found on its own such as peptidase HopD in Salmonella typhimurium , or in the case of the bifunctional enzymes such as Prepilin leader peptidase/N-methyltransferase in Vibrio cholerae , next to a methylation domain . This... | [
"GO:0004190",
"GO:0016020"
] | [
"aspartic-type endopeptidase activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF01478"
] | [
"Peptidase_A24"
] | [
31058
] | 1 | [
"EC",
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METAC... | [
"2.1.1.-",
"3.4.23.43",
"GenProp0295",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-... | [
"EC:2.1.1.-",
"EC:3.4.23.43",
"GP:GenProp0295",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
... | 148 | [
"3s0x"
] | 1 | [
"PUB00000093",
"PUB00000349",
"PUB00000522",
"PUB00001330",
"PUB00011023",
"PUB00011707",
"PUB00014343",
"PUB00014532",
"PUB00020023",
"PUB00021296",
"PUB00042504",
"PUB00065205",
"PUB00066803",
"PUB00076784",
"PUB00076785",
"PUB00076786"
] | [
"2194475",
"1851433",
"8439290",
"6795036",
"10331925",
"11566868",
"14622420",
"9224881",
"10625704",
"10864493",
"2682266",
"23254940",
"21765428",
"4912600",
"10497172",
"21751400"
] | [
"The structure and function of the aspartic proteinases.",
"Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.",
"Evolutionary families of peptidases.",
"Gastric proteinases--structure, function, evolution and mechanism of action.",
"Crystal structure of the hy... | [
1990,
1991,
1993,
1981,
1999,
2001,
2003,
1997,
2000,
2000,
1989,
2013,
2011,
1970,
1999,
2011
] | 16 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Plasmid R64",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
845,
29656,
19,
1,
536,
1
] | 6 | [
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
2,
1
] | 2 | true | Domain | Prepilin type IV endopeptidase, peptidase domain | Prepilin type IV endopeptidase, peptidase domain | Prepilin_IV_endopep_pep | 9 |
IPR000046 | 46 | Neurokinin NK1 receptor | NK1_rcpt | Family | 1,025 | false | false | This entry represents Neurokinin 1 (NK1) receptor that is involved in inflammation and pain transmission. It binds substance P, the first neuropeptide to be discovered in mammals. Neuropeptide receptors are present in very small quantities in the cell and are embedded tightly in the plasma membrane. The neuropeptides e... | [
"GO:0004995",
"GO:0007186",
"GO:0005886",
"GO:0016020"
] | [
"tachykinin receptor activity",
"G protein-coupled receptor signaling pathway",
"plasma membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR01024"
] | [
"NEUROKININ1R"
] | [
1025
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"360",
"R-CFA-380095",
"R-CFA-416476",
"R-CFA-8856825",
"R-CFA-8856828",
"R-HSA-380095",
"R-HSA-416476",
"R-HSA-8856825",
"R-HSA-8856828",
"R-MMU-380095",
"R-MMU-416476",
"R-MMU-8856825",
"R-MMU-8856828",
"R-RNO-380095",
"R-RNO-416476",
"R-RNO-8856825",
"R-RNO-8856828"
] | [
"IUPHAR:360",
"REACTOME:R-CFA-380095",
"REACTOME:R-CFA-416476",
"REACTOME:R-CFA-8856825",
"REACTOME:R-CFA-8856828",
"REACTOME:R-HSA-380095",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-8856825",
"REACTOME:R-HSA-8856828",
"REACTOME:R-MMU-380095",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-8856825",
... | 17 | [
"2ks9",
"2ksa",
"2ksb",
"6e59",
"6hll",
"6hlo",
"6hlp",
"7p00",
"7p02",
"7rmg",
"7rmh",
"7rmi",
"8u26"
] | 13 | [
"PUB00000131",
"PUB00002477",
"PUB00002518",
"PUB00004960",
"PUB00004961",
"PUB00010571",
"PUB00010572",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"2478537",
"8386361",
"8170923",
"11071315",
"9575785",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Molecular characterization of a functional cDNA for rat substance P receptor.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"Localiza... | [
1990,
1988,
1989,
1993,
1994,
2000,
1998,
2003,
1994,
2005,
2009,
2006,
2013
] | 13 | [
"IPR001681"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1025
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
4,
2,
2
] | 4 | true | Family | Neurokinin NK1 receptor | Neurokinin NK1 receptor | NK1_rcpt | 8 |
IPR000047 | 47 | Helix-turn-helix motif | HTH_motif | Conserved_site | 40,282 | false | false | null | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PRINTS"
] | [
"PR00031"
] | [
"HTHREPRESSR"
] | [
40282
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-DME-3214847",
"R-DME-8853884",
"R-GGA-9762293",
"R-HSA-210745",
"R-HSA-210747",
"R-HSA-381771",
"R-HSA-8939902",
"R-HSA-9762293",
"R-HSA-9819196",
"R-HSA-9830364",
"R-HSA-9834899",
"R-HSA-9925561",
"R-HSA-9925563",
"R-HSA-9937080",
"R-HSA-9938206",
"R-MMU-9762293"
] | [
"REACTOME:R-DME-3214847",
"REACTOME:R-DME-8853884",
"REACTOME:R-GGA-9762293",
"REACTOME:R-HSA-210745",
"REACTOME:R-HSA-210747",
"REACTOME:R-HSA-381771",
"REACTOME:R-HSA-8939902",
"REACTOME:R-HSA-9762293",
"REACTOME:R-HSA-9819196",
"REACTOME:R-HSA-9830364",
"REACTOME:R-HSA-9834899",
"REACTOME:R... | 16 | [
"1ahd",
"1b8i",
"1du0",
"1enh",
"1hdd",
"1ig7",
"1p7i",
"1p7j",
"1san",
"1ztr",
"2djn",
"2dmt",
"2hdd",
"2hoa",
"2hos",
"2hot",
"2jwt",
"2p81",
"2r5y",
"2r5z",
"3a01",
"3a02",
"3hdd",
"3lnq",
"3zob",
"4qtr",
"4rdu",
"4uus",
"4xic",
"4xid",
"4xrs",
"5jlw"... | 54 | [
"PUB00000036",
"PUB00002521",
"PUB00003978"
] | [
"6236744",
"2644244",
"6896364"
] | [
"Protein-DNA recognition.",
"The helix-turn-helix DNA binding motif.",
"Homology among DNA-binding proteins suggests use of a conserved super-secondary structure."
] | [
1984,
1989,
1982
] | 3 | [] | [] | 0 | 0 | null | [
"Eukaryota",
"Mimiviridae"
] | [
40276,
6
] | 2 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
86,
15,
98,
40,
180,
58,
40,
69,
86
] | 9 | true | Conserved_site | Helix-turn-helix motif | Helix-turn-helix motif | HTH_motif | 2 |
IPR000048 | 48 | IQ motif, EF-hand binding site | IQ_motif_EF-hand-BS | Binding_site | 129,832 | false | false | The IQ motif is an extremely basic unit of about 23 amino acids, whose conserved core usually fits the consensus A-x(3)-I-Q-x(2)-F-R-x(4)-K-K. The IQ motif, which can be present in one or more copies, serves as a binding site for different EF-hand proteins, including the essential and regulatory myosin light chains, ca... | [
"GO:0005515"
] | [
"protein binding"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"SMART"
] | [
"PF00612",
"SM00015"
] | [
"IQ",
"IQ"
] | [
105367,
118054
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50096",
"R-BTA-2029482",
"R-BTA-373760",
"R-BTA-5250924",
"R-BTA-5627123",
"R-CEL-2453902",
"R-CFA-2029482",
"R-DDI-9013418",
"R-DDI-9013419",
"R-DDI-9013420",
"R-DDI-9013422",
"R-DDI-9013425",
"R-DME-2453902",
"R-DME-350480",
"R-DME-445355",
"R-DME-5627123",
"R-DRE-8980692",
... | [
"PROSITEDOC:PDOC50096",
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-373760",
"REACTOME:R-BTA-5250924",
"REACTOME:R-BTA-5627123",
"REACTOME:R-CEL-2453902",
"REACTOME:R-CFA-2029482",
"REACTOME:R-DDI-9013418",
"REACTOME:R-DDI-9013419",
"REACTOME:R-DDI-9013420",
"REACTOME:R-DDI-9013422",
"REACTOME:R... | 143 | [
"1b7t",
"1br1",
"1br4",
"1dfk",
"1dfl",
"1i84",
"1kk7",
"1kk8",
"1kqm",
"1kwo",
"1l2o",
"1n2d",
"1oe9",
"1qvi",
"1s5g",
"1scm",
"1sr6",
"1w7i",
"1w7j",
"1wdc",
"2bl0",
"2dfs",
"2ec6",
"2ix7",
"2kxw",
"2m5e",
"2os8",
"2otg",
"2w4a",
"2w4g",
"2w4h",
"2w4t"... | 167 | [
"PUB00001532",
"PUB00004175",
"PUB00018113",
"PUB00018114",
"PUB00018115"
] | [
"9141499",
"8127365",
"1558751",
"1824695",
"8424932"
] | [
"Sequence motifs for calmodulin recognition.",
"Structure of the regulatory domain of scallop myosin at 2.8 A resolution.",
"Unconventional myosins.",
"Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identification of a consensus amino acid sequence between... | [
1997,
1994,
1992,
1991,
1993
] | 5 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
62,
129715,
10,
45
] | 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... | [
288,
17,
520,
79,
202,
174,
2,
164,
238,
3,
3,
590
] | 12 | true | Binding_site | IQ motif, EF-hand binding site | IQ motif, EF-hand binding site | IQ_motif_EF-hand-BS | 5 |
IPR000049 | 49 | Electron transfer flavoprotein, beta-subunit, conserved site | ET-Flavoprotein_bsu_CS | Conserved_site | 18,024 | false | false | The electron transfer flavoprotein (ETF) [ , ] serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is an heterodimer that consist of an alpha and a beta subunit and which bind one molecule of FAD pe... | [
"GO:0009055"
] | [
"electron transfer activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01065"
] | [
"ETF_BETA"
] | [
18024
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00816",
"R-DDI-611105",
"R-HSA-611105",
"R-HSA-8876725",
"R-MMU-611105",
"R-MMU-8876725",
"R-RNO-611105",
"R-RNO-8876725",
"R-SCE-611105",
"R-SPO-611105",
"R-SSC-611105",
"R-SSC-8876725"
] | [
"PROSITEDOC:PDOC00816",
"REACTOME:R-DDI-611105",
"REACTOME:R-HSA-611105",
"REACTOME:R-HSA-8876725",
"REACTOME:R-MMU-611105",
"REACTOME:R-MMU-8876725",
"REACTOME:R-RNO-611105",
"REACTOME:R-RNO-8876725",
"REACTOME:R-SCE-611105",
"REACTOME:R-SPO-611105",
"REACTOME:R-SSC-611105",
"REACTOME:R-SSC-8... | 12 | [
"1efp",
"1efv",
"1o94",
"1o95",
"1o96",
"1o97",
"1t9g",
"2a1t",
"2a1u",
"3clr",
"3cls",
"3clt",
"3clu",
"6fah"
] | 14 | [
"PUB00004936",
"PUB00005086"
] | [
"2326318",
"8525056"
] | [
"Biosynthesis, molecular cloning and sequencing of electron transfer flavoprotein.",
"Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta."
] | [
1990,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
75,
14664,
3129,
156
] | 4 | [
"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... | [
8,
1,
2,
2,
2,
4,
1,
1,
3,
1,
1,
4
] | 12 | true | Conserved_site | Electron transfer flavoprotein, beta-subunit, conserved site | Electron transfer flavoprotein, beta-subunit, conserved site | ET-Flavoprotein_bsu_CS | 9 |
IPR000053 | 53 | Thymidine/pyrimidine-nucleoside phosphorylase | Thymidine/pyrmidine_PPase | Family | 18,260 | false | false | Two highly similar activities are represented in this group: thymidine phosphorylase (TP, gene deoA, ) and pyrimidine-nucleoside phosphorylase (PyNP, gene pdp, ). Both are dimeric enzymes that function in the salvage pathway to catalyse the reversible phosphorolysis of pyrimidine nucleosides to the free base and sugar ... | [
"GO:0004645",
"GO:0006206"
] | [
"1,4-alpha-oligoglucan phosphorylase activity",
"pyrimidine nucleobase metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"PANTHER"
] | [
"PIRSF000478",
"PTHR10515"
] | [
"TP_PyNP",
""
] | [
14805,
18260
] | 2 | [
"EC",
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.4.2",
"2.4.2.4",
"PWY-7181",
"PDOC00557",
"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",
"PROSITEDOC:PDOC00557",
"REACTOME:R-HSA-73614",
"REACTOME:R-HSA-73621",
"REACTOME:R-MMU-73614",
"REACTOME:R-MMU-73621",
"REACTOME:R-RNO-73614",
"REACTOME:R-RNO-73621"
] | 10 | [
"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 | [
"PUB00010722",
"PUB00010723",
"PUB00010724"
] | [
"9310231",
"9698549",
"9817849"
] | [
"Platelet-derived endothelial cell growth factor thymidine phosphorylase in tumour growth and response to therapy.",
"Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.",
"The crystal structure of pyrimidine nucleoside phosphorylase in a closed... | [
1997,
1998,
1998
] | 3 | [] | [
"IPR013466",
"IPR018090"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
454,
16390,
1069,
346,
1
] | 5 | [
"Danio rerio",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
1,
11,
1,
2
] | 5 | true | Family | Thymidine/pyrimidine-nucleoside phosphorylase | Thymidine/pyrimidine-nucleoside phosphorylase | Thymidine/pyrmidine_PPase | 5 |
IPR000054 | 54 | Large ribosomal subunit protein eL31 | Ribosomal_eL31 | Family | 7,597 | false | false | A number of eukaryotic and archaebacterial large subunit ribosomal proteins can be grouped on the basis of sequence similarities. These proteins have 87 to 128 amino-acid residues. This family consists of: Yeast eL31A (also known as L34) Archaeal L31 [ ] Plants L31 Mammalian L31 [ ] Ribosomal protein eL31, which is pre... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"SMART",
"CDD"
] | [
"MF_00410",
"PF01198",
"PTHR10956",
"SM01380",
"cd00463"
] | [
"Ribosomal_eL31",
"Ribosomal_L31e",
"",
"Ribosomal_L31e",
"Ribosomal_L31e"
] | [
956,
7566,
7138,
7507,
6664
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00881",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DDI-156827",
"R-DDI-1799339",
"R-DDI-72689",
"R-DDI-72706",
"R-DDI-975956",
"R-DDI-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",
"R-DME-975956",
... | [
"PROSITEDOC:PDOC00881",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-72706",
"REACTOME:R-CEL-975956",
"REACTOME:R-CEL-975957",
"REACTOME:R-DDI-156827",
"REACTOME:R-DDI-1799339",
"REACTOME:R-DDI-72689",
"REACTOME:R-DDI-72706",
"REACTOME:R-DDI-975956... | 65 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 659 | [
"PUB00000605",
"PUB00001348",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00009424",
"PUB00028498",
"PUB00030402",
"PUB00037574",
"PUB00038013",
"PUB00079483",
"PUB00079524",
"PUB00079812",
"PUB00079813",
"PUB00079814",
"PUB00079815",
"PUB00079816",
"PUB00079817",
"PUB000798... | [
"2207169",
"3816785",
"11297922",
"11290319",
"11114498",
"11875025",
"10937989",
"14561884",
"14976550",
"15334087",
"10937990",
"11904172",
"12554856",
"12007402",
"11909526",
"7711082",
"9657144",
"11598216",
"18400176",
"2597680",
"8722009",
"15189156"
] | [
"Evidence for an additional archaebacterial gene cluster in Halobacterium marismortui encoding ribosomal proteins HL46e and HL30.",
"Nucleotide sequence of cloned cDNA specific for rat ribosomal protein L31.",
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the begi... | [
1990,
1987,
2001,
2001,
2000,
2002,
2000,
2003,
2004,
2004,
2000,
2002,
2003,
2002,
2002,
1995,
1998,
2001,
2008,
1989,
1995,
2004
] | 22 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Pseudomonadota",
"unclassified sequences"
] | [
895,
6668,
3,
31
] | 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... | [
11,
1,
1,
1,
9,
6,
1,
7,
15,
2,
1,
14
] | 12 | true | Family | Large ribosomal subunit protein eL31 | Large ribosomal subunit protein eL31 | Ribosomal_eL31 | 6 |
IPR000055 | 55 | Type I restriction modification DNA specificity domain | Restrct_endonuc_typeI_TRD | Domain | 35,744 | false | false | This domain is also known as the target recognition domain (TRD). Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides ... | [
"GO:0003677"
] | [
"DNA binding"
] | [
"molecular_function"
] | 1 | [
"PFAM"
] | [
"PF01420"
] | [
"Methylase_S"
] | [
35744
] | 1 | [
"GP"
] | [
"GenProp0455"
] | [
"GP:GenProp0455"
] | 1 | [
"1ydx",
"1yf2",
"2y7c",
"2y7h",
"3okg",
"5ybb",
"7bst",
"7bto",
"7btp",
"7btq",
"7btr",
"7eew",
"7vru",
"7vs4",
"8w0p",
"8w2p",
"8w2q"
] | 17 | [
"PUB00003392"
] | [
"9837717"
] | [
"The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutions of its polypeptide chain."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
810,
34321,
65,
42,
506
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Type I restriction modification DNA specificity domain | Type I restriction modification DNA specificity domain | Restrct_endonuc_typeI_TRD | 6 |
IPR000056 | 56 | Ribulose-phosphate 3-epimerase-like | Ribul_P_3_epim-like | Family | 36,906 | false | false | Ribulose-phosphate 3-epimerase ( ) (also known as RPE, pentose-5-phosphate 3-epimerase or PPE) is the enzyme that converts D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. In Ralstonia eutropha (Alcaligenes eutrophus) two copies of the gene coding for PPE are know... | [
"GO:0016857",
"GO:0005975"
] | [
"racemase and epimerase activity, acting on carbohydrates and derivatives",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROSITE",
"PROSITE",
"PANTHER",
"CDD"
] | [
"PF00834",
"PS01085",
"PS01086",
"PTHR11749",
"cd00429"
] | [
"Ribul_P_3_epim",
"RIBUL_P_3_EPIMER_1",
"RIBUL_P_3_EPIMER_2",
"",
"RPE"
] | [
36887,
28848,
28735,
36472,
34889
] | 5 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"5.1.3.1",
"GenProp0120",
"GenProp1294",
"GenProp1438",
"GenProp1463",
"PWY-1861",
"PWY-5723",
"PWY-8178",
"PDOC00833",
"R-HSA-71336",
"R-MMU-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:5.1.3.1",
"GP:GenProp0120",
"GP:GenProp1294",
"GP:GenProp1438",
"GP:GenProp1463",
"METACYC:PWY-1861",
"METACYC:PWY-5723",
"METACYC:PWY-8178",
"PROSITEDOC:PDOC00833",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 13 | [
"1h1y",
"1h1z",
"1rpx",
"1tqj",
"1tqx",
"2fli",
"3ct7",
"3ctl",
"3cu2",
"3inp",
"3ovp",
"3ovq",
"3ovr",
"3qc3",
"4nu7",
"5umf",
"7b1w",
"7sbj",
"7u5y"
] | 19 | [
"PUB00002204",
"PUB00051122"
] | [
"1429456",
"18700786"
] | [
"The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus.",
"Structural basis for substrate specificity in phosphate binding (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12."
] | [
1992,
2008
] | 2 | [] | [
"IPR026019",
"IPR043677"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Megaviricetes",
"unclassified sequences"
] | [
188,
29663,
6322,
3,
730
] | 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",... | [
11,
1,
1,
1,
3,
11,
7,
1,
4,
6,
1,
1,
21
] | 13 | true | Family | Ribulose-phosphate 3-epimerase-like | Ribulose-phosphate 3-epimerase-like | Ribul_P_3_epim-like | 7 |
IPR000057 | 57 | CXC chemokine receptor 2 | Chemokine_CXCR2 | Family | 204 | false | false | Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang... | [
"GO:0016494",
"GO:0019959",
"GO:0006935",
"GO:0007186",
"GO:0016020"
] | [
"C-X-C chemokine receptor activity",
"interleukin-8 binding",
"chemotaxis",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 5 | [
"PRINTS"
] | [
"PR00573"
] | [
"INTRLEUKN8BR"
] | [
204
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"69",
"R-HSA-380108",
"R-HSA-418594",
"R-HSA-6798695",
"R-MMU-380108",
"R-MMU-418594",
"R-MMU-6798695",
"R-RNO-380108",
"R-RNO-418594",
"R-RNO-6798695"
] | [
"IUPHAR:69",
"REACTOME:R-HSA-380108",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6798695",
"REACTOME:R-MMU-380108",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-6798695",
"REACTOME:R-RNO-380108",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-6798695"
] | 10 | [
"6lfm",
"6lfo",
"8xvu",
"8xwa",
"8xwf",
"8xwm",
"8xwn",
"8xws",
"8xwv",
"8xx3",
"8xx6",
"8xx7",
"8xxh",
"8xxr",
"8xxx"
] | 15 | [
"PUB00009401",
"PUB00064589",
"PUB00064621",
"PUB00064622",
"PUB00064810",
"PUB00064812",
"PUB00064819",
"PUB00064820",
"PUB00064821",
"PUB00064822",
"PUB00064825",
"PUB00064834",
"PUB00067945",
"PUB00067946",
"PUB00067948",
"PUB00067949"
] | [
"11544102",
"10714678",
"10601351",
"9500790",
"8384312",
"1379593",
"10878382",
"8955112",
"12239185",
"15967374",
"12496258",
"7527448",
"9689100",
"7592998",
"16720046",
"22719179"
] | [
"Chemokine receptors.",
"Chemokines: a new classification system and their role in immunity.",
"Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.",
"Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte... | [
2001,
2000,
1999,
1998,
1993,
1992,
2000,
1996,
2002,
2005,
2003,
1994,
1998,
1995,
2006,
2012
] | 16 | [
"IPR000174"
] | [] | 1 | 0 | 1 | [
"Eutheria"
] | [
204
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
1,
2
] | 3 | true | Family | CXC chemokine receptor 2 | CXC chemokine receptor 2 | Chemokine_CXCR2 | 2 |
IPR000059 | 59 | NUDIX hydrolase, NudL, conserved site | NUDIX_hydrolase_NudL_CS | Conserved_site | 3,688 | false | false | Nudix hydrolases, which are commonly found in all kingdoms of life, are pyrophosphohydrolases predominantly acting on substrates that contain a nucleotide diphosphate linked to another moiety X [ , ]. These substrates include nucleoside triphosphates, nucleotide sugars, dinucleoside polyphosphates, dinucleotide coenzym... | [
"GO:0000287",
"GO:0016818",
"GO:0030145"
] | [
"magnesium ion binding",
"hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides",
"manganese ion binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"PROSITE"
] | [
"PS01293"
] | [
"NUDIX_COA"
] | [
3688
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.6.1.-",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289",
"PDOC00995",
"R-HSA-390918",
"R-HSA-9033241",
"R-MMU-9033241",
"R-SCE-9033241",
"R-SPO-9033241"
] | [
"EC:3.6.1.-",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289",
"PROSITEDOC:PDOC00995",
"REACTOME:R-HSA-390918",
"REACTOME:R-HSA-9033241",
... | 17 | [
"5qgg",
"5qgh",
"5qgi",
"5qgj",
"5qgk",
"5qgl",
"5qgm",
"5qgn",
"5qgo",
"5qgp",
"5qgq",
"5qgr",
"5qgs",
"5qgt",
"5qgu",
"5qgv",
"5qgw",
"5qgx",
"5qgy",
"5qgz",
"5qh0",
"5qh1",
"5qh2",
"5qh3",
"5qh4",
"5qh5",
"5qh6",
"5qh7",
"5qh8",
"5qh9",
"5qha",
"5qhb"... | 38 | [
"PUB00006662",
"PUB00034750",
"PUB00034751",
"PUB00034752"
] | [
"8810257",
"16378245",
"10922370",
"15475388"
] | [
"The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes.",
"The Nudix hydrolase superfamily.",
"The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives.",
"A novel Nudix hydrolase for oxi... | [
1996,
2006,
2000,
2004
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5,
2789,
869,
25
] | 4 | [
"Caenorhabditis elegans",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
1,
2,
1,
6,
1,
1
] | 7 | true | Conserved_site | NUDIX hydrolase, NudL, conserved site | NUDIX hydrolase, NudL, conserved site | NUDIX_hydrolase_NudL_CS | 7 |
IPR000060 | 60 | BCCT transporter family | BCCT_transptr | Family | 27,684 | false | false | These prokaryotic transport proteins belong to a family known as BCCT (for Betaine/Carnitine/Choline Transporters) [ ] and are specific for compounds containing a quaternary nitrogen atom. The BCCT proteins contain 12 transmembrane regions and are energised by proton symport. They contain a conserved region with four t... | [
"GO:0022857",
"GO:0071705",
"GO:0016020"
] | [
"transmembrane transporter activity",
"nitrogen compound transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"PF02028",
"PTHR30047",
"TIGR00842"
] | [
"BCCT",
"",
"bcct"
] | [
27665,
27513,
21650
] | 3 | [
"PROSITEDOC"
] | [
"PDOC01007"
] | [
"PROSITEDOC:PDOC01007"
] | 1 | [
"2wit",
"2wsw",
"2wsx",
"3hfx",
"3p03",
"4ain",
"4c7r",
"4doj",
"4llh",
"4m8j",
"8ybq",
"8ybr",
"8zw8",
"8zxk",
"8zxp",
"9gkk"
] | 16 | [
"PUB00002302",
"PUB00061640"
] | [
"8752321",
"20923416"
] | [
"Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD.",
"The BCCT family of carriers: from physiology to crystal structure."
] | [
1996,
2010
] | 2 | [] | [
"IPR023449"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"Phage sp. ctqZP6",
"unclassified sequences"
] | [
26577,
364,
567,
1,
175
] | 5 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Family | BCCT transporter family | BCCT transporter family | BCCT_transptr | 6 |
IPR000061 | 61 | SWAP/Surp | Surp | Domain | 20,450 | false | false | SWAP is derived from the Suppressor-of-White-APricot splicing regulator from Drosophila melanogaster. The domain is found in regulators responsible for pervasive, nonsex-specific alternative pre-mRNA splicing characteristics and has been found in splicing regulatory proteins [ ]. These ancient, conserved SWAP proteins ... | [
"GO:0003723",
"GO:0006396"
] | [
"RNA binding",
"RNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01805",
"PS50128",
"SM00648"
] | [
"Surp",
"SURP",
"SWAP"
] | [
20228,
19155,
18529
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC50128",
"R-BTA-72163",
"R-HSA-72163",
"R-MMU-72163",
"R-RNO-72163"
] | [
"PROSITEDOC:PDOC50128",
"REACTOME:R-BTA-72163",
"REACTOME:R-HSA-72163",
"REACTOME:R-MMU-72163",
"REACTOME:R-RNO-72163"
] | 5 | [
"1ug0",
"1x4o",
"1x4p",
"2dt6",
"2dt7",
"2e5z",
"2e60",
"4dgw",
"5nrl",
"5z56",
"5z57",
"5z58",
"5zwm",
"5zwo",
"6ah0",
"6ahd",
"6ff7",
"6g90",
"6qx9",
"6y53",
"6y5q",
"7abg",
"7abi",
"7dco",
"7evo",
"7oqb",
"7oqe",
"7vh9",
"7vpx",
"8ch6",
"8h6e",
"8h6j"... | 55 | [
"PUB00002852",
"PUB00006690"
] | [
"8206918",
"7971282"
] | [
"Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot.",
"SWAP pre-mRNA splicing regulators are a novel, ancient protein family sharing a highly conserved sequence motif with the prp21 famil... | [
1994,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Armadillidium vulgare iridescent virus",
"Bacteria",
"Eukaryota"
] | [
1,
19,
20430
] | 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... | [
86,
4,
25,
9,
20,
12,
2,
15,
22,
1,
1,
56
] | 12 | true | Domain | SWAP/Surp | SWAP/Surp | Surp | 5 |
IPR000064 | 64 | Endopeptidase, NLPC/P60 domain | NLP_P60_dom | Domain | 83,151 | false | false | Endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme contain two major domains: a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. This entry represents the NLPC/P60 domain, which is a primitive, papain-like peptidase in the CA ... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00877",
"PS51935"
] | [
"NLPC_P60",
"NLPC_P60"
] | [
80359,
80452
] | 2 | [] | [] | [] | 0 | [
"2evr",
"2fg0",
"2hbw",
"2k1g",
"2xiv",
"3gt2",
"3h41",
"3i86",
"3m1u",
"3ne0",
"3npf",
"3pbc",
"3pbi",
"3pvq",
"3s0q",
"4fdy",
"4hpe",
"4jxb",
"4lj1",
"4q4g",
"4q4n",
"4q4t",
"4r0k",
"4xcm",
"6b8c",
"6bim",
"6bio",
"6biq",
"6sqx",
"7cfl",
"7v6s",
"7v6t"... | 57 | [
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00047412",
"PUB00076953"
] | [
"11517925",
"9891971",
"14725770",
"19217401",
"7044372"
] | [
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.",
"The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.",
... | [
2001,
1998,
2004,
2009,
1982
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
39,
80528,
656,
1014,
914
] | 5 | [
"Escherichia coli (strain K12)",
"Mus musculus"
] | [
4,
1
] | 2 | true | Domain | Endopeptidase, NLPC/P60 domain | Endopeptidase, NLPC/P60 domain | NLP_P60_dom | 8 |
IPR000065 | 65 | Leptin | Leptin | Family | 716 | false | false | Leptin, a metabolic monitor of food intake and energy need, is expressed by the ob obesity gene. The protein may function as part of a signalling pathway from adipose tissue that acts to regulate the size of the body fat depot [ ], the hormone effectively turning the brain's appetite message off when it senses that the... | [
"GO:0005179",
"GO:0007165",
"GO:0005576"
] | [
"hormone activity",
"signal transduction",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PIRSF",
"PRINTS",
"PANTHER"
] | [
"PF02024",
"PIRSF001837",
"PR00495",
"PTHR11724"
] | [
"Leptin",
"Leptin",
"LEPTIN",
""
] | [
705,
427,
518,
690
] | 4 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-2586552",
"R-HSA-381340",
"R-HSA-381771",
"R-HSA-422085",
"R-MMU-381771",
"R-MMU-422085",
"R-RNO-381771",
"R-RNO-422085",
"R-SSC-381771",
"R-SSC-422085"
] | [
"REACTOME:R-HSA-2586552",
"REACTOME:R-HSA-381340",
"REACTOME:R-HSA-381771",
"REACTOME:R-HSA-422085",
"REACTOME:R-MMU-381771",
"REACTOME:R-MMU-422085",
"REACTOME:R-RNO-381771",
"REACTOME:R-RNO-422085",
"REACTOME:R-SSC-381771",
"REACTOME:R-SSC-422085"
] | 10 | [
"1ax8",
"7z3p",
"7z3q",
"7z3r",
"8avb",
"8avc",
"8avd",
"8ave",
"8avf",
"8avo",
"8b7q",
"8dh8",
"8dh9",
"8dha",
"8k6z",
"8x80",
"8x81",
"8x85",
"9puo"
] | 19 | [
"PUB00004193"
] | [
"7984236"
] | [
"Positional cloning of the mouse obese gene and its human homologue."
] | [
1994
] | 1 | [] | [] | 0 | 0 | null | [
"Gnathostomata"
] | [
716
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
6,
5,
3
] | 4 | true | Family | Leptin | Leptin | Leptin | 1 |
IPR000066 | 66 | Antenna complex, alpha/beta subunit | Antenna_a/b | Domain | 2,311 | false | false | The antenna complexes of photosynthetic bacteria function as light-harvesting systems that absorb light and transfer the excitation energy to the reaction centres. The antenna complexes usually comprise 2 polypeptides (alpha- and beta-chains), 2-3 bacteriochlorophyll molecules and some carotenoids [ , , , ]. The alpha-... | [
"GO:0019684",
"GO:0016020",
"GO:0030077"
] | [
"photosynthesis, light reaction",
"membrane",
"plasma membrane light-harvesting complex"
] | [
"biological_process",
"cellular_component",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00556"
] | [
"LHC"
] | [
2311
] | 1 | [] | [] | [] | 0 | [
"1dx7",
"1ijd",
"1jo5",
"1kzu",
"1lgh",
"1nkz",
"1wrg",
"1xrd",
"2fkw",
"3wmm",
"4v8k",
"4v9g",
"5b5m",
"5b5n",
"5y5s",
"5yq7",
"6et5",
"6q53",
"6z5r",
"6z5s",
"7c52",
"7c9r",
"7ddq",
"7eqd",
"7f0l",
"7o0u",
"7o0v",
"7o0w",
"7o0x",
"7oy8",
"7pbw",
"7pil"... | 90 | [
"PUB00001417",
"PUB00003468",
"PUB00153105",
"PUB00153106"
] | [
"1577009",
"1460542",
"36738736",
"36792596"
] | [
"The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila.",
"Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospiri... | [
1992,
1992,
2023,
2023
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Hemiselmis andersenii",
"freshwater sediment metagenome"
] | [
2308,
1,
2
] | 3 | [] | [] | 0 | true | Domain | Antenna complex, alpha/beta subunit | Antenna complex, alpha/beta subunit | Antenna_a/b | 5 |
IPR000067 | 67 | Flagellar M-ring protein FliF | FlgMring_FliF | Family | 13,732 | false | false | This family corresponds to the FliF protein. FliF is the major protein of the M-ring in bacterial flagellar basal body [ ]. The basal body consists of four rings (L,P,S and M) surrounding the flagellar rod, which is believed to transmit motor rotation to the filament [ ]. The M ring is integral to the inner membrane of... | [
"GO:0003774",
"GO:0071973",
"GO:0009431"
] | [
"cytoskeletal motor activity",
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum basal body, MS ring"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PIRSF",
"PRINTS",
"NCBIFAM"
] | [
"PIRSF004862",
"PR01009",
"TIGR00206"
] | [
"FliF",
"FLGMRINGFLIF",
"fliF"
] | [
12671,
13513,
13543
] | 3 | [
"GP"
] | [
"GenProp0880"
] | [
"GP:GenProp0880"
] | 1 | [
"6scn",
"6sd1",
"6sd2",
"6sd3",
"6sd4",
"6sd5",
"6tre",
"7bk0",
"7cg7",
"7cgo",
"7cik",
"7d84",
"7e81",
"7nvg",
"8fte",
"8ftf",
"8t8p",
"8umd",
"8umx",
"8uox",
"8upl",
"8vib",
"8vid",
"8vkq",
"8vkr",
"8wiw",
"8wjr",
"8wk3",
"8wk4",
"8wkk",
"8wkq",
"8wl2"... | 55 | [
"PUB00002086",
"PUB00003254"
] | [
"2544561",
"2129540"
] | [
"L-, P-, and M-ring proteins of the flagellar basal body of Salmonella typhimurium: gene sequences and deduced protein sequences.",
"FlgB, FlgC, FlgF and FlgG. A family of structurally related proteins in the flagellar basal body of Salmonella typhimurium."
] | [
1989,
1990
] | 2 | [
"IPR043427"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
13563,
24,
145
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar M-ring protein FliF | Flagellar M-ring protein FliF | FlgMring_FliF | 8 |
IPR000068 | 68 | GPCR, family 3, extracellular calcium-sensing receptor-related | GPCR_3_Ca_sens_rcpt-rel | Family | 25,048 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004930",
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS",
"PANTHER"
] | [
"PR00592",
"PTHR24061"
] | [
"CASENSINGR",
""
] | [
5689,
24957
] | 2 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"54",
"R-BTA-416476",
"R-BTA-418594",
"R-BTA-420499",
"R-DRE-416476",
"R-DRE-420499",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-420499",
"R-HSA-9717207",
"R-MMU-416476",
"R-MMU-418594",
"R-MMU-420499",
"R-MMU-9717207",
"R-RNO-416476",
"R-RNO-418594",
"R-RNO-420499",
"R-RNO-9717207",
... | [
"IUPHAR:54",
"REACTOME:R-BTA-416476",
"REACTOME:R-BTA-418594",
"REACTOME:R-BTA-420499",
"REACTOME:R-DRE-416476",
"REACTOME:R-DRE-420499",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-HSA-9717207",
"REACTOME:R-MMU-416476",
"REACTOME:R-MMU-418594",
"RE... | 21 | [
"3qek",
"3qel",
"3qem",
"5b3j",
"5ewj",
"5ewl",
"5ewm",
"5fbh",
"5fbk",
"5k5s",
"5k5t",
"5tpw",
"5tpz",
"5tq0",
"5tq2",
"5x2m",
"5x2n",
"5x2o",
"5x2p",
"5x2q",
"6e7r",
"6e7s",
"6e7t",
"6e7u",
"6e7v",
"6e7w",
"6e7x",
"7dd5",
"7dd6",
"7dd7",
"7dtt",
"7dtu"... | 83 | [
"PUB00002009",
"PUB00002720",
"PUB00003100",
"PUB00003896",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"9298824",
"1320017",
"8675635",
"7874174",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"A novel mutation (L174R) in the Ca2+-sensing receptor gene associated with familial hypocalciuric hypercalcemia.",
"Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.",
"Calcium-sensing receptor mutations in familial benign hyper... | [
1997,
1992,
1995,
1994,
1991,
1993,
1992,
1994,
1991,
2003,
1994,
2005,
2009,
2006,
2013
] | 15 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
25048
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
110,
25,
342,
191
] | 4 | true | Family | GPCR, family 3, extracellular calcium-sensing receptor-related | GPCR, family 3, extracellular calcium-sensing receptor-related | GPCR_3_Ca_sens_rcpt-rel | 3 |
IPR000069 | 69 | Envelope glycoprotein M, flavivirus | Env_glycoprot_M_flavivir | Domain | 14,821 | false | false | Flaviviruses are small enveloped viruses with virions comprised of three proteins called C, M and E [ , , ]. The envelope glycoprotein M is made as a precursor, called prM. The precursor portion of the protein is the signal peptide for the proteins entry into the membrane. prM is cleaved to form M in a late-stage cleav... | [
"GO:0019058"
] | [
"viral life cycle"
] | [
"biological_process"
] | 1 | [
"PFAM"
] | [
"PF01004"
] | [
"Flavi_M"
] | [
14821
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.1.56",
"2.1.1.57",
"2.7.7.48",
"3.4.21.91",
"3.6.1.15",
"3.6.4.13",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210",
"PWY-7375",
"PWY-7379"
] | [
"EC:2.1.1.56",
"EC:2.1.1.57",
"EC:2.7.7.48",
"EC:3.4.21.91",
"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",
"METACYC:PWY-7375",
"METACYC:PWY-7379"
] | 13 | [
"1p58",
"3c5x",
"3c6e",
"3j27",
"3j2p",
"3j6s",
"3j6t",
"3j6u",
"4b03",
"4c2i",
"4cbf",
"4cct",
"4uif",
"5a1z",
"5gzr",
"5h30",
"5h37",
"5ire",
"5iz7",
"5o6a",
"5o6v",
"5u4w",
"5wsn",
"5ywo",
"5ywp",
"6co8",
"6idi",
"6idk",
"6idl",
"6jfh",
"6jfi",
"6lnt"... | 88 | [
"PUB00000171",
"PUB00003500",
"PUB00003522"
] | [
"7913359",
"8437237",
"8676481"
] | [
"The interactions of the flavivirus envelope proteins: implications for virus entry and release.",
"Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein.",
"Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and... | [
1994,
1993,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Flaviviridae",
"Levilactobacillus bambusae"
] | [
14820,
1
] | 2 | [] | [] | 0 | true | Domain | Envelope glycoprotein M, flavivirus | Envelope glycoprotein M, flavivirus | Env_glycoprot_M_flavivir | 6 |
IPR000071 | 71 | Immunodeficiency lentiviral matrix, N-terminal | Lentvrl_matrix_N | Domain | 63,532 | false | false | Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [ ]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into... | [
"GO:0005198"
] | [
"structural molecule activity"
] | [
"molecular_function"
] | 1 | [
"PFAM",
"PRINTS"
] | [
"PF00540",
"PR00234"
] | [
"Gag_p17",
"HIV1MATRIX"
] | [
63532,
63159
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-1169408",
"R-HSA-162585",
"R-HSA-162588",
"R-HSA-162592",
"R-HSA-162594",
"R-HSA-164516",
"R-HSA-164525",
"R-HSA-164843",
"R-HSA-173107",
"R-HSA-174490",
"R-HSA-174495",
"R-HSA-175474",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910"
] | [
"REACTOME:R-HSA-1169408",
"REACTOME:R-HSA-162585",
"REACTOME:R-HSA-162588",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-162594",
"REACTOME:R-HSA-164516",
"REACTOME:R-HSA-164525",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-173107",
"REACTOME:R-HSA-174490",
"REACTOME:R-HSA-174495",
"REACTOME:R-HSA-17... | 16 | [
"1ecw",
"1ed1",
"1hiw",
"1l6n",
"1tam",
"1uph",
"2gol",
"2h3f",
"2h3i",
"2h3q",
"2h3v",
"2h3z",
"2hmx",
"2jmg",
"2k4e",
"2k4h",
"2k4i",
"2lya",
"2lyb",
"2mgu",
"2nv3",
"4jmu",
"5o2u",
"7e1i",
"7e1j",
"7e1k",
"7jxr",
"7jxs",
"7mrl",
"7ovq",
"7ovr",
"7tbp"... | 37 | [
"PUB00003338",
"PUB00014063",
"PUB00016321",
"PUB00055853"
] | [
"7966331",
"9657938",
"12465460",
"18647839"
] | [
"Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein.",
"Retroviral matrix proteins: a structural perspective.",
"HIV-1 replication.",
"D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein."
] | [
1994,
1998,
2001,
2008
] | 4 | [] | [] | 0 | 0 | null | [
"Lentivirus",
"Opisthokonta",
"Thalassovita mangrovi"
] | [
63528,
3,
1
] | 3 | [] | [] | 0 | true | Domain | Immunodeficiency lentiviral matrix, N-terminal | Immunodeficiency lentiviral matrix, N-terminal | Lentvrl_matrix_N | 7 |
IPR000072 | 72 | PDGF/VEGF domain | PDGF/VEGF_dom | Domain | 12,421 | false | false | Platelet-derived growth factor (PDGF) [ , , ] is a potent mitogen for cells of mesenchymal origin, including smooth muscle cells and glial cells. In both mouse and human, the PDGF signalling network consists of four ligands, PDGFA-D, and two receptors, PDGFRalpha and PDGFRbeta. All PDGFs function as secreted, disulphid... | [
"GO:0008083",
"GO:0016020"
] | [
"growth factor activity",
"membrane"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00341",
"PS50278",
"SM00141",
"cd00135"
] | [
"PDGF",
"PDGF_2",
"PDGF",
"PDGF"
] | [
12120,
12325,
10428,
9856
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00222",
"R-BTA-114608",
"R-BTA-1257604",
"R-BTA-186763",
"R-BTA-186797",
"R-BTA-194313",
"R-BTA-195399",
"R-BTA-4420097",
"R-BTA-5218921",
"R-BTA-5673001",
"R-BTA-6811558",
"R-CFA-114608",
"R-CFA-1257604",
"R-CFA-186763",
"R-CFA-186797",
"R-CFA-5673001",
"R-CFA-6811558",
"R-DR... | [
"PROSITEDOC:PDOC00222",
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-1257604",
"REACTOME:R-BTA-186763",
"REACTOME:R-BTA-186797",
"REACTOME:R-BTA-194313",
"REACTOME:R-BTA-195399",
"REACTOME:R-BTA-4420097",
"REACTOME:R-BTA-5218921",
"REACTOME:R-BTA-5673001",
"REACTOME:R-BTA-6811558",
"REACTOME:R-CFA... | 61 | [
"1bj1",
"1cz8",
"1flt",
"1fzv",
"1kat",
"1mjv",
"1mkg",
"1mkk",
"1pdg",
"1qty",
"1rv6",
"1tzh",
"1tzi",
"1vpf",
"1vpp",
"1wq8",
"1wq9",
"2c7w",
"2fjg",
"2fjh",
"2gnn",
"2qr0",
"2vpf",
"2vwe",
"2x1w",
"2x1x",
"2xac",
"2xv7",
"3bdy",
"3mjg",
"3mjk",
"3p9w"... | 72 | [
"PUB00000590",
"PUB00001228",
"PUB00001288",
"PUB00004494",
"PUB00004886",
"PUB00014075",
"PUB00032112",
"PUB00081653",
"PUB00081654",
"PUB00081655"
] | [
"2546599",
"1425569",
"8617204",
"7681160",
"8637916",
"12952899",
"9207067",
"7640655",
"8323751",
"11345501"
] | [
"Structure and function of platelet-derived growth factor (PDGF) and related proteins.",
"Structural and functional studies on platelet-derived growth factor.",
"A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases.",
"Two alternati... | [
1989,
1992,
1996,
1993,
1996,
2003,
1997,
1995,
1993,
2001
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses"
] | [
24,
12297,
100
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
44,
11,
41,
26,
58
] | 6 | true | Domain | PDGF/VEGF domain | PDGF/VEGF domain | PDGF/VEGF_dom | 9 |
IPR000073 | 73 | Alpha/beta hydrolase fold-1 | AB_hydrolase_1 | Domain | 640,336 | false | false | This entry represents fold-1 of α/β hydrolases. 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 enzymes are believed t... | [] | [] | [] | 0 | [
"PFAM",
"PFAM",
"PRINTS"
] | [
"PF00561",
"PF12697",
"PR00111"
] | [
"Abhydrolase_1",
"Abhydrolase_6",
"ABHYDROLASE"
] | [
427948,
194820,
239612
] | 3 | [
"GP",
"GP",
"GP",
"GP",
"GP",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"... | [
"GenProp1287",
"GenProp1364",
"GenProp1458",
"GenProp1473",
"GenProp1558",
"R-BTA-1483191",
"R-BTA-156584",
"R-BTA-156588",
"R-BTA-426048",
"R-BTA-69273",
"R-CEL-1482839",
"R-CEL-1483191",
"R-CEL-69273",
"R-DDI-1483191",
"R-DDI-69273",
"R-DRE-426048",
"R-GGA-426048",
"R-HSA-1482839... | [
"GP:GenProp1287",
"GP:GenProp1364",
"GP:GenProp1458",
"GP:GenProp1473",
"GP:GenProp1558",
"REACTOME:R-BTA-1483191",
"REACTOME:R-BTA-156584",
"REACTOME:R-BTA-156588",
"REACTOME:R-BTA-426048",
"REACTOME:R-BTA-69273",
"REACTOME:R-CEL-1482839",
"REACTOME:R-CEL-1483191",
"REACTOME:R-CEL-69273",
... | 71 | [
"1a7u",
"1a88",
"1a8q",
"1a8s",
"1a8u",
"1azw",
"1b6g",
"1be0",
"1bee",
"1bez",
"1bn6",
"1bn7",
"1bro",
"1brt",
"1c4x",
"1cij",
"1cqw",
"1cqz",
"1cr6",
"1cv2",
"1cvl",
"1d07",
"1dwo",
"1dwp",
"1dwq",
"1e89",
"1e8d",
"1eb8",
"1eb9",
"1edb",
"1edd",
"1ede"... | 997 | [
"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"
] | [
5537,
445711,
183388,
1,
314,
5385
] | 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",... | [
487,
18,
66,
59,
7,
109,
74,
30,
278,
109,
15,
10,
466
] | 13 | true | Domain | Alpha/beta hydrolase fold-1 | Alpha/beta hydrolase fold-1 | AB_hydrolase_1 | 8 |
IPR000074 | 74 | Apolipoprotein A/E | ApoA_E | Family | 5,659 | false | false | Exchangeable apolipoproteins (apoA, apoC and apoE) have the same genomic structure and are members of a multi-gene family that probably evolved from a common ancestral gene. This entry includes the ApoA1, ApoA4, Apo5 and ApoE proteins. ApoA1, ApoA4 and Apo5 are part of the APOA1/C3/A4/A5 gene cluster on chromosome 11 [... | [
"GO:0008289",
"GO:0006869",
"GO:0042157",
"GO:0005576"
] | [
"lipid binding",
"lipid transport",
"lipoprotein metabolic process",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PFAM"
] | [
"PF01442"
] | [
"Apolipoprotein"
] | [
5659
] | 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-3000471",
"R-BTA-381426",
"R-BTA-8957275",
"R-BTA-8963888",
"R-BTA-8963896",
"R-BTA-8963901",
"R-BTA-8964011",
"R-BTA-8964058",
"R-BTA-9707616",
"R-BTA-975634",
"R-CFA-3000480",
"R-CFA-381426",
"R-CFA-8957275",
"R-CFA-8963888",
"R-CFA-8963901",
"R-CFA-8964026",... | [
"REACTOME:R-BTA-114608",
"REACTOME:R-BTA-3000471",
"REACTOME:R-BTA-381426",
"REACTOME:R-BTA-8957275",
"REACTOME:R-BTA-8963888",
"REACTOME:R-BTA-8963896",
"REACTOME:R-BTA-8963901",
"REACTOME:R-BTA-8964011",
"REACTOME:R-BTA-8964058",
"REACTOME:R-BTA-9707616",
"REACTOME:R-BTA-975634",
"REACTOME:R... | 86 | [
"1av1",
"1b68",
"1bz4",
"1ea8",
"1gs9",
"1h7i",
"1le2",
"1le4",
"1lpe",
"1nfn",
"1nfo",
"1or2",
"1or3",
"1ya9",
"2kc3",
"2l7b",
"2lem",
"2msc",
"2msd",
"2mse",
"2n5e",
"3k2s",
"3r2p",
"3s84",
"4v6m",
"6cc9",
"6cch",
"6ccx",
"6cfe",
"6clz",
"6cm1",
"6iwb"... | 55 | [
"PUB00005140",
"PUB00015448",
"PUB00015449"
] | [
"2063194",
"15108119",
"15234552"
] | [
"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E.",
"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.",
"Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins."
] | [
1991,
2004,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Caudoviricetes code 15 clade",
"Eukaryota",
"metagenomes"
] | [
3,
1178,
4,
4467,
7
] | 5 | [
"Caenorhabditis elegans",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
12,
11,
19,
17,
20
] | 5 | true | Family | Apolipoprotein A/E | Apolipoprotein A/E | ApoA_E | 6 |
IPR000076 | 76 | K/Cl co-transporter | KCL_cotranspt | Family | 8,227 | false | false | K+Cl- cotransporters (KCCs) belong to the SLC12 family and act as electroneutral symporters of K+ and Cl- ions across the plasma membrane [ , ]. They are major determinants of osmotic homeostasis. They are involved in the regulatory volume decrease in response to cell swelling in red blood cells, and have been proposed... | [
"GO:0015379",
"GO:0006811",
"GO:0016020"
] | [
"potassium:chloride symporter activity",
"monoatomic ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01081"
] | [
"KCLTRNSPORT"
] | [
8227
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-426117",
"R-HSA-5619039",
"R-MMU-426117",
"R-RNO-426117"
] | [
"REACTOME:R-HSA-426117",
"REACTOME:R-HSA-5619039",
"REACTOME:R-MMU-426117",
"REACTOME:R-RNO-426117"
] | 4 | [
"6kkr",
"6kkt",
"6kku",
"6m1y",
"6m22",
"6m23",
"6ukn",
"6y5r",
"6y5v",
"7ain",
"7aio",
"7aip",
"7aiq",
"7air",
"7d14",
"7d8z",
"7d90",
"7d99",
"7ngb",
"7tth",
"7tti"
] | 21 | [
"PUB00002955",
"PUB00002956",
"PUB00004291",
"PUB00072348",
"PUB00072350",
"PUB00072352"
] | [
"8663127",
"8663311",
"9930699",
"11125215",
"6929518",
"10347194"
] | [
"Molecular cloning and functional expression of the K-Cl cotransporter from rabbit, rat, and human. A new member of the cation-chloride cotransporter family.",
"Molecular characterization of a putative K-Cl cotransporter in rat brain. A neuronal-specific isoform.",
"The K+/Cl- co-transporter KCC2 renders GABA h... | [
1996,
1996,
1999,
2000,
1980,
1999
] | 6 | [
"IPR004842"
] | [
"IPR000622"
] | 1 | 1 | 0 | [
"Opisthokonta"
] | [
8227
] | 1 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
33,
6,
20,
25,
20
] | 5 | true | Family | K/Cl co-transporter | K/Cl co-transporter | KCL_cotranspt | 3 |
IPR000077 | 77 | Large ribosomal subunit protein eL39 | Ribosomal_eL39 | Family | 4,884 | false | false | A number of eukaryotic and archaebacterial large subunit ribosomal proteins can be grouped on the basis of sequence similarities. This entry represents the large ribosomal subunit protein eL39, of about 50 residues long, being the smallest protein of eukaryotic-type ribosomes. In mammals, eL39 has been described as the... | [
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM"
] | [
"MF_00629",
"PF00832"
] | [
"Ribosomal_eL39",
"Ribosomal_L39"
] | [
3098,
4882
] | 2 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00050",
"R-BTA-156827",
"R-BTA-1799339",
"R-BTA-6791226",
"R-BTA-72689",
"R-BTA-72706",
"R-BTA-975956",
"R-BTA-975957",
"R-CEL-156827",
"R-CEL-1799339",
"R-CEL-72689",
"R-CEL-72706",
"R-CEL-975956",
"R-CEL-975957",
"R-DME-156827",
"R-DME-1799339",
"R-DME-72689",
"R-DME-72706",... | [
"PROSITEDOC:PDOC00050",
"REACTOME:R-BTA-156827",
"REACTOME:R-BTA-1799339",
"REACTOME:R-BTA-6791226",
"REACTOME:R-BTA-72689",
"REACTOME:R-BTA-72706",
"REACTOME:R-BTA-975956",
"REACTOME:R-BTA-975957",
"REACTOME:R-CEL-156827",
"REACTOME:R-CEL-1799339",
"REACTOME:R-CEL-72689",
"REACTOME:R-CEL-7270... | 64 | [
"1ffk",
"1jj2",
"1k73",
"1k8a",
"1k9m",
"1kc8",
"1kd1",
"1kqs",
"1m1k",
"1m90",
"1n8r",
"1nji",
"1q7y",
"1q81",
"1q82",
"1q86",
"1qvf",
"1qvg",
"1s72",
"1vq4",
"1vq5",
"1vq6",
"1vq7",
"1vq8",
"1vq9",
"1vqk",
"1vql",
"1vqm",
"1vqn",
"1vqo",
"1vqp",
"1w2b"... | 633 | [
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00151098",
"PUB00151099"
] | [
"11297922",
"11290319",
"11114498",
"34428590",
"36517592"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins.",
"Deletion of ribosomal paralogs Rpl39 and Rpl39l compromises cell proliferation via protein synthesis and mitochondrial activity.",
"A male germ-cell-specific ... | [
2001,
2001,
2000,
2021,
2022
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Pseudomonadati",
"unclassified sequences"
] | [
809,
4059,
3,
13
] | 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,
1,
2,
3,
3,
1,
3,
9,
1,
1,
13
] | 12 | true | Family | Large ribosomal subunit protein eL39 | Large ribosomal subunit protein eL39 | Ribosomal_eL39 | 2 |
IPR000079 | 79 | High mobility group protein HMGN | HMGN_fam | Family | 5,052 | false | false | This entry represents the HMGN family, whose members promote chromatin unfolding, enhance access to nucleosomes, and modulate transcription from chromatin templates. HMGNs are expressed only in vertebrates [ ]. The high mobility group (HMG) proteins are the most abundant and ubiquitous nonhistone chromosomal proteins. ... | [
"GO:0031492",
"GO:0000785",
"GO:0005634"
] | [
"nucleosomal DNA binding",
"chromatin",
"nucleus"
] | [
"molecular_function",
"cellular_component",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PROSITE",
"SMART"
] | [
"PF01101",
"PR00925",
"PS00355",
"SM00527"
] | [
"HMG14_17",
"NONHISHMG17",
"HMG14_17",
"HMG17"
] | [
4966,
4724,
2672,
4702
] | 4 | [
"PROSITEDOC"
] | [
"PDOC00307"
] | [
"PROSITEDOC:PDOC00307"
] | 1 | [] | 0 | [
"PUB00074432"
] | [
"25281808"
] | [
"Evolution of high mobility group nucleosome-binding proteins and its implications for vertebrate chromatin specialization."
] | [
2015
] | 1 | [] | [
"IPR040164"
] | 0 | 1 | 0 | [
"Eukaryota"
] | [
5052
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
10,
24,
14,
32
] | 4 | true | Family | High mobility group protein HMGN | High mobility group protein HMGN | HMGN_fam | 6 |
IPR000081 | 81 | Peptidase C3, picornavirus core protein 2A | Peptidase_C3 | Domain | 8,780 | false | false | This domain defines cysteine peptidases belong to MEROPS peptidase family C3 (picornain, clan PA(C)), subfamilies 3CA and 3CB. The protein fold of this peptidase domain for members of this family resembles that of the serine peptidase, chymotrypsin [ ], the type example for clan PA. Picornaviral proteins are expressed ... | [
"GO:0008233",
"GO:0006508",
"GO:0016032"
] | [
"peptidase activity",
"proteolysis",
"viral process"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"PFAM"
] | [
"PF00947"
] | [
"Pico_P2A"
] | [
8780
] | 1 | [
"EC",
"EC",
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.48",
"3.4.22.28",
"3.4.22.29",
"3.6.1.15",
"PWY-6545",
"PWY-7184",
"PWY-7185",
"PWY-7198",
"PWY-7210"
] | [
"EC:2.7.7.48",
"EC:3.4.22.28",
"EC:3.4.22.29",
"EC:3.6.1.15",
"METACYC:PWY-6545",
"METACYC:PWY-7184",
"METACYC:PWY-7185",
"METACYC:PWY-7198",
"METACYC:PWY-7210"
] | 9 | [
"1z8r",
"2hrv",
"2m5t",
"3w95",
"4fvb",
"4fvd",
"4mg3",
"5x45",
"7ara",
"7da6",
"7h2t",
"7h2u",
"7h2v",
"7h2w",
"7h2x",
"7h2y",
"7h2z",
"7h30",
"7h31",
"7h32",
"7h33",
"7h34",
"7h35",
"7h36",
"7h37",
"7h38",
"7h39",
"7h3a",
"7h3b",
"7h3c",
"7h3d",
"7h3e"... | 485 | [
"PUB00003174",
"PUB00004181",
"PUB00011704",
"PUB00020025",
"PUB00030423",
"PUB00076953"
] | [
"9460917",
"8164744",
"11517925",
"9891971",
"14725770",
"7044372"
] | [
"Genetic analysis of mengovirus protein 2A: its function in polyprotein processing and virus reproduction.",
"Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.",
"Evolutionary lines of cysteine peptidases.",
"Identification of the active site of legumain links i... | [
1998,
1994,
2001,
1998,
2004,
1982
] | 6 | [] | [] | 0 | 0 | null | [
"Picornaviridae",
"Trichinella"
] | [
8775,
5
] | 2 | [] | [] | 0 | true | Domain | Peptidase C3, picornavirus core protein 2A | Peptidase C3, picornavirus core protein 2A | Peptidase_C3 | 5 |
IPR000082 | 82 | SEA domain | SEA_dom | Domain | 24,299 | false | false | The SEA domain has been named after the first three proteins in which it was identified (Sperm protein, Enterokinase and Agrin). The SEA domain has around 120 residues, it is an extracellular domain found in a number of cell surface and secreted proteins in which it could be present in one or two copies [ ]. Many SEA d... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF01390",
"PS50024",
"SM00200"
] | [
"SEA",
"SEA",
"SEA"
] | [
19367,
23611,
8083
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50024",
"R-HSA-1442490",
"R-HSA-1474228",
"R-HSA-1971475",
"R-HSA-2022928",
"R-HSA-2024096",
"R-HSA-216083",
"R-HSA-3000157",
"R-HSA-3000171",
"R-HSA-3000178",
"R-HSA-3560783",
"R-HSA-3560801",
"R-HSA-3656237",
"R-HSA-3656253",
"R-HSA-419037",
"R-HSA-4420332",
"R-HSA-5083625",
... | [
"PROSITEDOC:PDOC50024",
"REACTOME:R-HSA-1442490",
"REACTOME:R-HSA-1474228",
"REACTOME:R-HSA-1971475",
"REACTOME:R-HSA-2022928",
"REACTOME:R-HSA-2024096",
"REACTOME:R-HSA-216083",
"REACTOME:R-HSA-3000157",
"REACTOME:R-HSA-3000171",
"REACTOME:R-HSA-3000178",
"REACTOME:R-HSA-3560783",
"REACTOME:R... | 61 | [
"1ivz",
"2acm",
"2e7v",
"6bsb",
"6bsc",
"7sa9",
"7wxu",
"7wxw",
"7wy0",
"7wz7",
"7x2v",
"8gkl",
"8hc0",
"8s9p",
"8vis",
"8vm1",
"9nrc",
"9p1c"
] | 18 | [
"PUB00005026",
"PUB00018083",
"PUB00018084",
"PUB00097339"
] | [
"7670383",
"9762901",
"9030729",
"27977898"
] | [
"The SEA module: a new extracellular domain associated with O-glycosylation.",
"Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding activity.",
"Characterization of recombinant perlecan domain I and its substitution by... | [
1995,
1998,
1997,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Methanodesulfokora washburnensis",
"Eukaryota"
] | [
123,
1,
24175
] | 3 | [
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
166,
9,
112,
51,
92
] | 6 | true | Domain | SEA domain | SEA domain | SEA_dom | 1 |
IPR000083 | 83 | Fibronectin, type I | Fibronectin_type1 | Domain | 4,943 | false | false | Fibronectin type I repeats are one of the three repeats found in the fibronectin protein. Fibronectin is a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Type I domain (FN1) is approximately 40 residues in length. Four conserved cysteines are involved ... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PROSITE",
"PROFILE",
"SMART",
"CDD"
] | [
"PF00039",
"PS01253",
"PS51091",
"SM00058",
"cd00061"
] | [
"fn1",
"FN1_1",
"FN1_2",
"FN1",
"FN1"
] | [
4347,
4805,
4380,
4759,
4339
] | 5 | [
"EC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.4.21",
"PDOC00965",
"R-GGA-114608",
"R-GGA-1474228",
"R-GGA-1566977",
"R-GGA-2129379",
"R-GGA-216083",
"R-GGA-3000170",
"R-GGA-3000178",
"R-GGA-354192",
"R-GGA-354194",
"R-GGA-372708",
"R-GGA-381426",
"R-GGA-5674135",
"R-GGA-8874081",
"R-GGA-8957275",
"R-GGA-9860927",
"R-HSA-114... | [
"EC:3.4.21",
"PROSITEDOC:PDOC00965",
"REACTOME:R-GGA-114608",
"REACTOME:R-GGA-1474228",
"REACTOME:R-GGA-1566977",
"REACTOME:R-GGA-2129379",
"REACTOME:R-GGA-216083",
"REACTOME:R-GGA-3000170",
"REACTOME:R-GGA-3000178",
"REACTOME:R-GGA-354192",
"REACTOME:R-GGA-354194",
"REACTOME:R-GGA-372708",
... | 95 | [
"1e88",
"1e8b",
"1fbr",
"1o9a",
"1qgb",
"1qo6",
"1tpg",
"1tpm",
"1tpn",
"2cg6",
"2cg7",
"2cku",
"2ec3",
"2rky",
"2rkz",
"2rl0",
"3cal",
"3ejh",
"3gxe",
"3m7p",
"3mql",
"3zrz",
"4bdw",
"4bdx",
"4pz5",
"8os5"
] | 26 | [
"PUB00002685",
"PUB00003289",
"PUB00004065",
"PUB00005265"
] | [
"1900516",
"1602484",
"2112232",
"7582899"
] | [
"High resolution analysis of functional determinants on human tissue-type plasminogen activator.",
"Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance.",
"Structure of the fibronectin type 1 module.",
"The solution structure ... | [
1991,
1992,
1990,
1995
] | 4 | [] | [] | 0 | 0 | null | [
"Dehalococcoides mccartyi",
"Eukaryota"
] | [
1,
4942
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
7,
37,
24,
18
] | 4 | true | Domain | Fibronectin, type I | Fibronectin, type I | Fibronectin_type1 | 1 |
IPR000084 | 84 | PE-PGRS family, N-terminal | PE-PGRS_N | Domain | 12,089 | false | false | This family is named after a PE motif near to the amino terminus. The carboxyl terminus of this family are variable and fall into several classes. The largest class of PE proteins is the highly repetitive PGRS class which have a high glycine content. The function of these proteins is uncertain but it has been suggested... | [] | [] | [] | 0 | [
"PFAM"
] | [
"PF00934"
] | [
"PE"
] | [
12089
] | 1 | [] | [] | [] | 0 | [
"2g38",
"4kxr",
"4w4k",
"4w4l",
"5xfs",
"6uuj",
"6vhr",
"6vj5"
] | 8 | [
"PUB00004280",
"PUB00054031",
"PUB00054032",
"PUB00054033",
"PUB00095124",
"PUB00103913",
"PUB00103914",
"PUB00103929",
"PUB00103930"
] | [
"9634230",
"19602151",
"18981138",
"18267304",
"31662454",
"32138343",
"32139546",
"25155747",
"25275011"
] | [
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.",
"Mycobacterial PE, PPE and ESX clusters: novel insights into the secretion of these most unusual protein families.",
"The ESX-5 secretion system of Mycobacterium marinum modulates the macrophage response.",
"Mycobacter... | [
1998,
2009,
2008,
2007,
2019,
2020,
2020,
2014,
2014
] | 9 | [] | [] | 0 | 0 | null | [
"Bacillati",
"Tulasnella calospora MUT 4182",
"freshwater metagenome"
] | [
12087,
1,
1
] | 3 | [] | [] | 0 | true | Domain | PE-PGRS family, N-terminal | PE-PGRS family, N-terminal | PE-PGRS_N | 3 |
IPR000085 | 85 | Holliday junction branch migration complex subunit RuvA | RuvA | Family | 25,336 | false | false | In prokaryotes, RuvA, RuvB, and RuvC process the universal DNA intermediate of homologous recombination, termed Holliday junction. The tetrameric DNA helicase RuvA, known as Holliday junction branch migration complex subunit RuvA, specifically binds to the Holliday junction and facilitates the isomerization of the junc... | [
"GO:0003678",
"GO:0006281",
"GO:0006310"
] | [
"DNA helicase activity",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00031",
"TIGR00084"
] | [
"DNA_HJ_migration_RuvA",
"ruvA"
] | [
25147,
25327
] | 2 | [
"GP"
] | [
"GenProp0198"
] | [
"GP:GenProp0198"
] | 1 | [
"1bdx",
"1c7y",
"1cuk",
"1d8l",
"1hjp",
"1ixr",
"2h5x",
"2ztc",
"2ztd",
"2zte",
"7oa5",
"7pbu",
"7x5a",
"7x7q",
"8gh8"
] | 15 | [
"PUB00013198"
] | [
"12408833"
] | [
"Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"unclassified Caudoviricetes",
"unclassified sequences"
] | [
24687,
41,
41,
2,
565
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Holliday junction branch migration complex subunit RuvA | Holliday junction branch migration complex subunit RuvA | RuvA | 9 |
IPR000086 | 86 | NUDIX hydrolase domain | NUDIX_hydrolase_dom | Domain | 361,445 | false | false | The Nudix superfamily is widespread among eukaryotes, bacteria, archaea and viruses and consists mainly of pyrophosphohydrolases that act upon substrates of general structure NUcleoside DIphosphate linked to another moiety, X (NDP-X) to yield NMP plus P-X. Such substrates include (d)NTPs (both canonical and oxidised de... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00293",
"PS51462"
] | [
"NUDIX",
"NUDIX"
] | [
334568,
355320
] | 2 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REA... | [
"3.6.1",
"3.6.1.-",
"GenProp1017",
"GenProp1296",
"GenProp1621",
"PWY-5757",
"PWY-6147",
"PWY-6383",
"PWY-6797",
"PWY-7206",
"PWY-7419",
"PWY-7539",
"PWY-7719",
"PWY-7821",
"PWY-8289",
"PDOC00695",
"R-BTA-1855167",
"R-BTA-196807",
"R-BTA-2393930",
"R-BTA-3299685",
"R-BTA-4809... | [
"EC:3.6.1",
"EC:3.6.1.-",
"GP:GenProp1017",
"GP:GenProp1296",
"GP:GenProp1621",
"METACYC:PWY-5757",
"METACYC:PWY-6147",
"METACYC:PWY-6383",
"METACYC:PWY-6797",
"METACYC:PWY-7206",
"METACYC:PWY-7419",
"METACYC:PWY-7539",
"METACYC:PWY-7719",
"METACYC:PWY-7821",
"METACYC:PWY-8289",
"PROSI... | 117 | [
"1f3y",
"1g0s",
"1g9q",
"1ga7",
"1hx3",
"1hzt",
"1i9a",
"1iry",
"1jkn",
"1jrk",
"1k26",
"1k2e",
"1khz",
"1kt9",
"1ktg",
"1mk1",
"1mp2",
"1mqe",
"1mqw",
"1mr2",
"1mut",
"1nfs",
"1nfz",
"1nqy",
"1nqz",
"1ow2",
"1ppv",
"1ppw",
"1ppx",
"1pun",
"1puq",
"1pus"... | 740 | [
"PUB00006662",
"PUB00034750",
"PUB00048421",
"PUB00068733"
] | [
"8810257",
"16378245",
"17698004",
"19340986"
] | [
"The MutT proteins or \"Nudix\" hydrolases, a family of versatile, widely distributed, \"housecleaning\" enzymes.",
"The Nudix hydrolase superfamily.",
"Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.",
"Biochemical and physi... | [
1996,
2006,
2007,
2009
] | 4 | [] | [
"IPR020476",
"IPR033716",
"IPR042970",
"IPR044099",
"IPR047198",
"IPR049734"
] | 0 | 6 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
5469,
273859,
77026,
1141,
3950
] | 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",... | [
154,
15,
58,
31,
14,
78,
63,
16,
63,
101,
7,
8,
148
] | 13 | true | Domain | NUDIX hydrolase domain | NUDIX hydrolase domain | NUDIX_hydrolase_dom | 3 |
IPR000089 | 89 | Biotin/lipoyl attachment | Biotin_lipoyl | Domain | 221,430 | false | false | The biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. The 80 residues surrounding the biotinyl-binding lysine residue display some sequence similarity to that around the lipoyl-binding lysine residue. Biotin plays a catalytic role in some carboxyl transfer reactions and is... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE"
] | [
"PF00364",
"PS50968"
] | [
"Biotin_lipoyl",
"BIOTINYL_LIPOYL"
] | [
191881,
213601
] | 2 | [
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"R... | [
"GenProp1408",
"GenProp1439",
"GenProp1629",
"GenProp1673",
"PDOC50968",
"R-BTA-196780",
"R-BTA-204174",
"R-BTA-5362517",
"R-BTA-6783984",
"R-BTA-70263",
"R-BTA-70268",
"R-BTA-70895",
"R-BTA-9013407",
"R-BTA-9837999",
"R-BTA-9857492",
"R-BTA-9859138",
"R-BTA-9861559",
"R-CEL-196780... | [
"GP:GenProp1408",
"GP:GenProp1439",
"GP:GenProp1629",
"GP:GenProp1673",
"PROSITEDOC:PDOC50968",
"REACTOME:R-BTA-196780",
"REACTOME:R-BTA-204174",
"REACTOME:R-BTA-5362517",
"REACTOME:R-BTA-6783984",
"REACTOME:R-BTA-70263",
"REACTOME:R-BTA-70268",
"REACTOME:R-BTA-70895",
"REACTOME:R-BTA-901340... | 121 | [
"1a6x",
"1bdo",
"1dcz",
"1dd2",
"1dxm",
"1fyc",
"1ghj",
"1ghk",
"1gjx",
"1hpc",
"1htp",
"1iyu",
"1iyv",
"1k8m",
"1k8o",
"1lab",
"1lac",
"1o78",
"1onl",
"1pmr",
"1qjo",
"1y8n",
"1y8o",
"1y8p",
"1z6h",
"1z7t",
"1zko",
"1zy8",
"2b8f",
"2b8g",
"2bdo",
"2d5d"... | 200 | [
"PUB00000614",
"PUB00002740",
"PUB00005256",
"PUB00014190"
] | [
"1825611",
"1526981",
"8747466",
"8950276"
] | [
"Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme.",
"The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.",
"Structure of the biotinyl domain of... | [
1991,
1992,
1995,
1996
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
2431,
164766,
51448,
4,
2781
] | 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",... | [
80,
14,
65,
17,
4,
59,
23,
8,
41,
61,
9,
6,
189
] | 13 | true | Domain | Biotin/lipoyl attachment | Biotin/lipoyl attachment | Biotin_lipoyl | 3 |
IPR000090 | 90 | Flagellar motor switch protein FliG | Flg_Motor_Flig | Family | 13,486 | false | false | The flagellar motor switch in Escherichia coli and Salmonella typhimurium regulates the direction of flagellar rotation and hence controls swimming behaviour [ ]. The switch is a complex apparatus that responds to signals transduced by the chemotaxis sensory signalling system during chemotactic behaviour [ ]. CheY, the... | [
"GO:0003774",
"GO:0006935",
"GO:0071973",
"GO:0009288"
] | [
"cytoskeletal motor activity",
"chemotaxis",
"bacterial-type flagellum-dependent cell motility",
"bacterial-type flagellum"
] | [
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"PIRSF003161",
"PR00954",
"PTHR30534",
"TIGR00207"
] | [
"FliG",
"FLGMOTORFLIG",
"",
"fliG"
] | [
9416,
13227,
13433,
10105
] | 4 | [
"GP",
"GP",
"GP"
] | [
"GenProp0883",
"GenProp1183",
"GenProp1194"
] | [
"GP:GenProp0883",
"GP:GenProp1183",
"GP:GenProp1194"
] | 3 | [
"1lkv",
"1qc7",
"3ajc",
"3hjl",
"3soh",
"3usw",
"3usy",
"4fhr",
"4fq0",
"4qrm",
"5tdy",
"5wuj",
"8ucs",
"8umd",
"8umx",
"8uox",
"8upl",
"8vib",
"8vid",
"8vkq",
"8vkr",
"8wiw",
"8wo5",
"8woe",
"8xp0",
"8xp1",
"8yjt",
"8z4d",
"8z4g",
"9n49",
"9n4z"
] | 31 | [
"PUB00001834",
"PUB00002083",
"PUB00002290",
"PUB00004790"
] | [
"8224881",
"2656645",
"8631704",
"1631122"
] | [
"Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG.",
"Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.",
"A mutational analysis of the interaction between FliG and FliM, two compone... | [
1993,
1989,
1996,
1992
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
13229,
32,
225
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Flagellar motor switch protein FliG | Flagellar motor switch protein FliG | Flg_Motor_Flig | 8 |
IPR000091 | 91 | Huntingtin | Huntingtin | Family | 2,138 | false | false | null | [
"GO:0005634",
"GO:0005737"
] | [
"nucleus",
"cytoplasm"
] | [
"cellular_component",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00375"
] | [
"HUNTINGTIN"
] | [
2138
] | 1 | [
"REACTOME"
] | [
"R-HSA-9022692"
] | [
"REACTOME:R-HSA-9022692"
] | 1 | [
"6ez8",
"6rmh",
"6x9o",
"6yej",
"7dxj",
"7dxk",
"8vlx",
"8w15",
"8yae",
"8yao",
"9pmw",
"9pn0"
] | 12 | [
"PUB00003898",
"PUB00004844",
"PUB00061735",
"PUB00061736"
] | [
"7647794",
"8202492",
"16181417",
"9660943"
] | [
"Comparative sequence analysis of the human and pufferfish Huntington's disease genes.",
"Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases.",
"Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of... | [
1995,
1994,
2005,
1998
] | 4 | [
"IPR028426"
] | [] | 1 | 0 | 1 | [
"Opisthokonta"
] | [
2138
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
8,
5,
2,
6
] | 4 | true | Family | Huntingtin | Huntingtin | Huntingtin | 3 |
IPR000092 | 92 | Polyprenyl synthetase-like | Polyprenyl_synt | Family | 87,241 | false | false | This entry includes a group of polyprenyl synthetase enzymes from all cellular organisms. It has been shown [ , , , , ] that these enzymes share some regions of sequence similarity. From 3D structure analysis, it was revealed that they also share structure and reaction mechanisms, using similar strategies for substrate... | [
"GO:0004659",
"GO:0008299"
] | [
"prenyltransferase activity",
"isoprenoid biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM",
"CDD"
] | [
"PF00348",
"cd00685"
] | [
"polyprenyl_synt",
"Trans_IPPS_HT"
] | [
87240,
74902
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.5.1",
"GenProp0758",
"GenProp1322",
"GenProp1411",
"GenProp1479",
"GenProp1498",
"GenProp1530",
"GenProp1541",
"GenProp1585",
"GenProp1594",
"GenProp1694",
"GenProp1704",
"PDOC00407",
"R-BTA-191273",
"R-DDI-191273",
"R-DDI-2142789",
"R-HSA-191273",
"R-HSA-2142789",
"R-HSA-2426... | [
"EC:2.5.1",
"GP:GenProp0758",
"GP:GenProp1322",
"GP:GenProp1411",
"GP:GenProp1479",
"GP:GenProp1498",
"GP:GenProp1530",
"GP:GenProp1541",
"GP:GenProp1585",
"GP:GenProp1594",
"GP:GenProp1694",
"GP:GenProp1704",
"PROSITEDOC:PDOC00407",
"REACTOME:R-BTA-191273",
"REACTOME:R-DDI-191273",
"R... | 27 | [
"1fps",
"1rqi",
"1rqj",
"1rtr",
"1ubv",
"1ubw",
"1ubx",
"1uby",
"1v4e",
"1v4h",
"1v4i",
"1v4j",
"1v4k",
"1vg2",
"1vg3",
"1vg4",
"1vg6",
"1vg7",
"1wkz",
"1wl0",
"1wl1",
"1wl2",
"1wl3",
"1wmw",
"1wy0",
"1yhk",
"1yhl",
"1yhm",
"1yq7",
"1yv5",
"1zw5",
"2azj"... | 424 | [
"PUB00002344",
"PUB00002569",
"PUB00002687",
"PUB00004527",
"PUB00004795",
"PUB00010618",
"PUB00154479",
"PUB00154480"
] | [
"2089044",
"2198286",
"1826006",
"1303794",
"1495965",
"12135472",
"34357940",
"38261827"
] | [
"Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli.",
"Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase.",
"The Neurospora crassa carotenoi... | [
1990,
1990,
1991,
1992,
1992,
2002,
2021,
2024
] | 8 | [] | [
"IPR014119",
"IPR033965",
"IPR039702",
"IPR053378"
] | 0 | 4 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1797,
57986,
26019,
28,
1411
] | 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",... | [
71,
2,
10,
9,
2,
18,
21,
3,
33,
19,
3,
3,
59
] | 13 | true | Family | Polyprenyl synthetase-like | Polyprenyl synthetase-like | Polyprenyl_synt | 2 |
IPR000093 | 93 | DNA recombination protein RecR | DNA_Rcmb_RecR | Family | 24,774 | false | false | The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair [ , , , ]. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA [ , ]. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a... | [
"GO:0003677",
"GO:0046872",
"GO:0006281",
"GO:0006310"
] | [
"DNA binding",
"metal ion binding",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00017",
"PTHR30446",
"TIGR00615"
] | [
"RecR",
"",
"recR"
] | [
24573,
24769,
23897
] | 3 | [
"GP"
] | [
"GenProp0491"
] | [
"GP:GenProp0491"
] | 1 | [
"1vdd",
"2v1c",
"3vdp",
"3vdu",
"3ve5",
"4jcv",
"4o6o",
"4o6p",
"5z2v",
"5zvq",
"8a93",
"8ab0",
"8bpr",
"8k3f"
] | 14 | [
"PUB00004365",
"PUB00032061",
"PUB00064122",
"PUB00101156"
] | [
"2674903",
"15116069",
"23019218",
"29633970"
] | [
"The recR locus of Escherichia coli K-12: molecular cloning, DNA sequencing and identification of the gene product.",
"Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair.",
"RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssD... | [
1989,
2004,
2012,
2018
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences",
"uncultured marine thaumarchaeote KM3_70_D04"
] | [
24119,
58,
1,
595,
1
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)"
] | [
1,
1
] | 2 | true | Family | DNA recombination protein RecR | DNA recombination protein RecR | DNA_Rcmb_RecR | 3 |
IPR000095 | 95 | CRIB domain | CRIB_dom | Domain | 39,583 | false | false | This entry represents the CRIB domain. Many putative downstream effectors of the small GTPases Cdc42 and Rac contain a GTPase binding domain (GBD), also called p21 binding domain (PBD), which has been shown to specifically bind the GTP bound form of Cdc42 or Rac, with a preference for Cdc42 [ , ]. The most conserved re... | [] | [] | [] | 0 | [
"PFAM",
"PROFILE",
"SMART"
] | [
"PF00786",
"PS50108",
"SM00285"
] | [
"PBD",
"CRIB",
"PBD"
] | [
28956,
37570,
31054
] | 3 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC50108",
"R-BTA-202433",
"R-BTA-2029482",
"R-BTA-203641",
"R-BTA-2871796",
"R-BTA-373753",
"R-BTA-389359",
"R-BTA-3928662",
"R-BTA-3928664",
"R-BTA-399954",
"R-BTA-418885",
"R-BTA-445144",
"R-BTA-445355",
"R-BTA-5218920",
"R-BTA-5627123",
"R-BTA-5663213",
"R-BTA-5687128",
"R-BT... | [
"PROSITEDOC:PDOC50108",
"REACTOME:R-BTA-202433",
"REACTOME:R-BTA-2029482",
"REACTOME:R-BTA-203641",
"REACTOME:R-BTA-2871796",
"REACTOME:R-BTA-373753",
"REACTOME:R-BTA-389359",
"REACTOME:R-BTA-3928662",
"REACTOME:R-BTA-3928664",
"REACTOME:R-BTA-399954",
"REACTOME:R-BTA-418885",
"REACTOME:R-BTA-... | 190 | [
"1cee",
"1e0a",
"1ees",
"1ej5",
"1f3m",
"1t84",
"2k42",
"2lnh",
"2odb",
"2ov2",
"2qme",
"4fie",
"4mit",
"5upk",
"5upl",
"6uhc",
"8s5t",
"9lbf",
"9lbg",
"9m41",
"9r3y",
"9r4v"
] | 22 | [
"PUB00000927",
"PUB00002937",
"PUB00014097",
"PUB00018127",
"PUB00018128",
"PUB00018129",
"PUB00018130",
"PUB00018131",
"PUB00018132"
] | [
"8625410",
"7493928",
"10724160",
"8107774",
"9660763",
"9601050",
"10975528",
"10966102",
"10360579"
] | [
"Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization.",
"A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases.",
"Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.",
"A b... | [
1996,
1995,
2000,
1994,
1998,
1998,
2000,
2000,
1999
] | 9 | [] | [
"IPR033923"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Geoglobus acetivorans",
"Ralstonia phage phiRSL1",
"metagenomes"
] | [
234,
39340,
1,
1,
7
] | 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... | [
69,
16,
114,
16,
66,
54,
4,
43,
70,
5,
2,
105
] | 12 | true | Domain | CRIB domain | CRIB domain | CRIB_dom | 7 |
IPR000096 | 96 | Serum amyloid A protein | Serum_amyloid_A | Family | 1,672 | false | false | The serum amyloid A (SAA) proteins comprise a family of vertebrate amphipathic α-helical apolipoproteins that associate predominantly with high density lipoproteins (HDL) [ , ]. They play a role in the mobilisation of cholesterol for tissue repair and regeneration [ ]. The synthesis of these proteins is greatly increas... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF",
"PRINTS",
"PROSITE",
"SMART"
] | [
"PF00277",
"PIRSF002472",
"PR00306",
"PS00992",
"SM00197"
] | [
"SAA",
"Serum_amyloid_A",
"SERUMAMYLOID",
"SAA",
"SAA"
] | [
1672,
915,
1537,
1190,
1637
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00762",
"R-HSA-3000471",
"R-HSA-416476",
"R-HSA-418594",
"R-HSA-444473",
"R-HSA-445989",
"R-HSA-6785807",
"R-HSA-879415",
"R-HSA-933542",
"R-HSA-977225"
] | [
"PROSITEDOC:PDOC00762",
"REACTOME:R-HSA-3000471",
"REACTOME:R-HSA-416476",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-444473",
"REACTOME:R-HSA-445989",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-879415",
"REACTOME:R-HSA-933542",
"REACTOME:R-HSA-977225"
] | 10 | [
"4ip8",
"4ip9",
"4q5g",
"6dso",
"6mst",
"6pxz",
"6py0",
"6zcf",
"6zcg",
"6zch",
"7ovt",
"7zh7",
"7zky",
"9r4z"
] | 14 | [
"PUB00000177",
"PUB00001955",
"PUB00095063",
"PUB00095064"
] | [
"7504491",
"8188253",
"30165816",
"30852808"
] | [
"Serum amyloid A (SAA): an acute phase protein and apolipoprotein.",
"Evolution of the serum amyloid A (SAA) protein superfamily.",
"Serum amyloid A - a review.",
"Serum amyloid A levels are associated with polymorphic variants in the serum amyloid A 1 and 2 genes."
] | [
1993,
1994,
2018,
2019
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eumetazoa"
] | [
28,
1644
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
12,
12,
7
] | 4 | true | Family | Serum amyloid A protein | Serum amyloid A protein | Serum_amyloid_A | 7 |
IPR000098 | 98 | Interleukin-10 | IL-10 | Family | 1,085 | false | false | Interleukin 10 (IL-10) is a secreted 17-21kDa protein that is non- glycosylated in humans but exists as a non-covalent homodimer. IL-10 is secreted by some types of T-lymphocyte, B-lymphocytes and macrophages late after antigen activation. Generally, IL-10 inhibits T-cell and natural killer cell synthesis of other cyto... | [
"GO:0005125",
"GO:0006955",
"GO:0005576"
] | [
"cytokine activity",
"immune response",
"extracellular region"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR01294"
] | [
"INTRLEUKIN10"
] | [
1085
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00450",
"R-GGA-6783783",
"R-HSA-6783783",
"R-HSA-6785807",
"R-HSA-8950505",
"R-HSA-9662834",
"R-HSA-9664323",
"R-HSA-9725370",
"R-MMU-6783783",
"R-RNO-6783783",
"R-SSC-6783783"
] | [
"PROSITEDOC:PDOC00450",
"REACTOME:R-GGA-6783783",
"REACTOME:R-HSA-6783783",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-8950505",
"REACTOME:R-HSA-9662834",
"REACTOME:R-HSA-9664323",
"REACTOME:R-HSA-9725370",
"REACTOME:R-MMU-6783783",
"REACTOME:R-RNO-6783783",
"REACTOME:R-SSC-6783783"
] | 11 | [
"1ilk",
"1inr",
"1j7v",
"1lk3",
"1vlk",
"1y6k",
"1y6m",
"1y6n",
"2h24",
"2ilk",
"4x51",
"6x93",
"8sve"
] | 13 | [] | [] | [] | [] | 0 | [
"IPR020443"
] | [] | 1 | 0 | 1 | [
"Gnathostomata",
"Viruses"
] | [
932,
153
] | 2 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
2,
6,
3,
2
] | 4 | true | Family | Interleukin-10 | Interleukin-10 | IL-10 | 4 |
IPR000100 | 100 | Ribonuclease P | RNase_P | Family | 24,192 | false | false | Ribonuclease P ( ) (RNase P) [ , , ] is a site specific endonuclease that generates mature tRNAs by catalysing the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. In bacteria RNase P is known to be composed of two components: a... | [
"GO:0000049",
"GO:0004526",
"GO:0008033"
] | [
"tRNA binding",
"ribonuclease P activity",
"tRNA processing"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00227",
"PF00825",
"PTHR33992",
"TIGR00188"
] | [
"RNase_P",
"Ribonuclease_P",
"",
"rnpA"
] | [
21221,
24191,
22352,
22040
] | 4 | [
"EC",
"GP",
"PROSITEDOC"
] | [
"3.1.26.5",
"GenProp1360",
"PDOC00558"
] | [
"EC:3.1.26.5",
"GP:GenProp1360",
"PROSITEDOC:PDOC00558"
] | 3 | [
"1a6f",
"1d6t",
"1nz0",
"2ljp",
"3q1q",
"3q1r",
"4jg4",
"6cqc",
"6d1r",
"6max",
"6ov1",
"7uo0",
"7uo1",
"7uo2",
"7uo5"
] | 15 | [
"PUB00002589",
"PUB00002604",
"PUB00004402"
] | [
"1700778",
"1689306",
"1374553"
] | [
"Ribonuclease P. Postscript.",
"Ribonuclease P: function and variation.",
"Ribonuclease P RNA and protein subunits from bacteria."
] | [
1990,
1990,
1992
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"candidate division MSBL1 archaeon SCGC-AAA382N08",
"unclassified sequences"
] | [
23598,
153,
2,
1,
438
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ribonuclease P | Ribonuclease P | RNase_P | 7 |
IPR000101 | 101 | Gamma-glutamyltranspeptidase | GGT_peptidase | Family | 33,003 | false | false | Gamma-glutamyltranspeptidase ( ) (GGT) [ ] catalyses the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobi... | [
"GO:0036374",
"GO:0006751"
] | [
"glutathione hydrolase activity",
"glutathione catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PANTHER",
"PANTHER",
"NCBIFAM"
] | [
"PTHR11686",
"PTHR45027",
"TIGR00066"
] | [
"",
"",
"g_glut_trans"
] | [
13115,
656,
24844
] | 3 | [
"EC",
"EC",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"RE... | [
"2.3.2.2",
"3.4.19.13",
"GenProp1346",
"GenProp1653",
"GenProp1664",
"PWY-4041",
"PWY-4061",
"PWY-5826",
"PWY-6842",
"PWY-7112",
"PWY-7559",
"PWY-8001",
"PWY-8301",
"PWY-8355",
"PDOC00404",
"R-BTA-174403",
"R-BTA-5423646",
"R-BTA-9753281",
"R-HSA-174403",
"R-HSA-2142691",
"R-... | [
"EC:2.3.2.2",
"EC:3.4.19.13",
"GP:GenProp1346",
"GP:GenProp1653",
"GP:GenProp1664",
"METACYC:PWY-4041",
"METACYC:PWY-4061",
"METACYC:PWY-5826",
"METACYC:PWY-6842",
"METACYC:PWY-7112",
"METACYC:PWY-7559",
"METACYC:PWY-8001",
"METACYC:PWY-8301",
"METACYC:PWY-8355",
"PROSITEDOC:PDOC00404",
... | 41 | [
"2dbu",
"2dbw",
"2dbx",
"2dg5",
"2e0w",
"2e0x",
"2e0y",
"2nqo",
"2qm6",
"2qmc",
"2v36",
"2z8i",
"2z8j",
"2z8k",
"3a75",
"3fnm",
"3whq",
"3whr",
"3whs",
"4gdx",
"4gg2",
"4ott",
"4otu",
"4y23",
"4z9o",
"4zbk",
"4zc6",
"4zcg",
"5b5t",
"5bpk",
"5v4q",
"5xlu"... | 39 | [
"PUB00000636",
"PUB00002088",
"PUB00003561",
"PUB00006169",
"PUB00092777"
] | [
"1358202",
"2570061",
"2868390",
"1378736",
"23148443"
] | [
"Nucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain.",
"DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt.",
"gamma-Glutamyl transpeptidase from kidney.",
"Gamma-glutamyltransferase: nucleotide sequence of the human p... | [
1992,
1989,
1985,
1992,
2012
] | 5 | [] | [
"IPR051792"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Diachasmimorpha longicaudata entomopoxvirus",
"Eukaryota",
"unclassified sequences"
] | [
184,
18764,
2,
13836,
217
] | 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",... | [
20,
13,
25,
13,
1,
44,
22,
1,
11,
15,
1,
2,
8
] | 13 | true | Family | Gamma-glutamyltranspeptidase | Gamma-glutamyltranspeptidase | GGT_peptidase | 8 |
IPR000102 | 102 | Neuraxin/MAP1B repeat | MAP1B_neuraxin | Repeat | 320 | false | false | In microtubule-associated protein 1B (MAP1B) the basic region containing the KKEE and KKEVI motifs is responsible for the interaction between MAP1B and microtubules in vivo . This region bears no sequence relationship to the microtubule binding domains of kinesin, MAP2, or tau [ ]. Neuraxin is a putative structural pro... | [] | [] | [] | 0 | [
"PFAM",
"PROSITE"
] | [
"PF00414",
"PS00230"
] | [
"MAP1B_neuraxin",
"MAP1B_NEURAXIN"
] | [
286,
314
] | 2 | [
"PROSITEDOC",
"REACTOME"
] | [
"PDOC00202",
"R-HSA-9833110"
] | [
"PROSITEDOC:PDOC00202",
"REACTOME:R-HSA-9833110"
] | 2 | [] | 0 | [
"PUB00001173",
"PUB00003063"
] | [
"2555150",
"2480963"
] | [
"Neuraxin, a novel putative structural protein of the rat central nervous system that is immunologically related to microtubule-associated protein 5.",
"The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau."
] | [
1989,
1989
] | 2 | [] | [] | 0 | 0 | null | [
"Opisthokonta",
"Pseudomonadati"
] | [
317,
3
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
2,
2
] | 3 | true | Repeat | Neuraxin/MAP1B repeat | Neuraxin/MAP1B repeat | MAP1B_neuraxin | 5 |
IPR000104 | 104 | Antifreeze protein, type I | Antifreeze_1 | Family | 1,580 | false | false | Marine teleosts from polar oceans can be protected from freezing in icy sea-water by serum antifreeze proteins (AFPs) or glycoproteins (AFGPs) [ ]: these function by binding to, and preventing the growth of, ice crystals within the fish and depressing the non-equilibrium freezing point to below that of the melting poin... | [
"GO:0016172",
"GO:0050825"
] | [
"antifreeze activity",
"ice binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PRINTS"
] | [
"PR00308"
] | [
"ANTIFREEZEI"
] | [
1580
] | 1 | [] | [] | [] | 0 | [
"1j5b",
"1wfa",
"1wfb",
"4ke2",
"4v7h",
"4v9h",
"4v9i",
"4x8w",
"5gao",
"5lij",
"5nrl",
"5zwn",
"6fti",
"6g4s",
"6gaw",
"6gb2",
"6ha8",
"6hiv",
"6hix",
"6q3g",
"6skg",
"6t9i",
"6t9k",
"6tf9",
"6tnu",
"6x62",
"6xyw",
"6zce",
"6zm5",
"6zp4",
"6zvj",
"7a09"... | 38 | [
"PUB00002793",
"PUB00003280",
"PUB00005033",
"PUB00007091"
] | [
"8344924",
"1738160",
"7540906",
"12171656"
] | [
"Structure-function relationships in an antifreeze polypeptide. The role of charged amino acids.",
"Energy-optimized structure of antifreeze protein and its binding mechanism.",
"Comparative modeling of the three-dimensional structure of type II antifreeze protein.",
"Structure and function of antifreeze prot... | [
1993,
1992,
1995,
2002
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
74,
1499,
4,
3
] | 4 | [
"Rattus norvegicus"
] | [
2
] | 1 | true | Family | Antifreeze protein, type I | Antifreeze protein, type I | Antifreeze_1 | 9 |
IPR000105 | 105 | Mu opioid receptor | Mu_opioid_rcpt | Family | 1,214 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004979",
"GO:0007186",
"GO:0016020"
] | [
"beta-endorphin receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00537"
] | [
"MUOPIOIDR"
] | [
1214
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"319",
"R-HSA-111885",
"R-HSA-202040",
"R-HSA-375276",
"R-HSA-418594",
"R-HSA-6785807",
"R-HSA-9022699",
"R-MMU-111885",
"R-MMU-202040",
"R-MMU-375276",
"R-MMU-418594",
"R-RNO-111885",
"R-RNO-202040",
"R-RNO-375276",
"R-RNO-418594"
] | [
"IUPHAR:319",
"REACTOME:R-HSA-111885",
"REACTOME:R-HSA-202040",
"REACTOME:R-HSA-375276",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-6785807",
"REACTOME:R-HSA-9022699",
"REACTOME:R-MMU-111885",
"REACTOME:R-MMU-202040",
"REACTOME:R-MMU-375276",
"REACTOME:R-MMU-418594",
"REACTOME:R-RNO-111885",
"... | 15 | [
"5c1m",
"6dde",
"6ddf",
"7sbf",
"7scg",
"7t2g",
"7t2h",
"7u2k",
"7u2l",
"7ul4",
"8e0g",
"8ef5",
"8ef6",
"8efb",
"8efl",
"8efo",
"8efq",
"8f7q",
"8f7r",
"8k9k",
"8k9l",
"8qot",
"8y72",
"8y73",
"9bjk",
"9bqj",
"9mqh",
"9mqi",
"9mqj",
"9pxu",
"9pxv",
"9pxw"... | 37 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR001418"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
1214
] | 1 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
19,
16,
17
] | 4 | true | Family | Mu opioid receptor | Mu opioid receptor | Mu_opioid_rcpt | 6 |
IPR000109 | 109 | Proton-dependent oligopeptide transporter family | POT_fam | Family | 77,393 | false | false | The proton-dependent oligopeptide transporter (POT) family (also known as the peptide transport (PTR) family) is made up of a group of energy-dependent transporters found in organisms as diverse as bacteria and humans. The POT family of proteins is distinct from the ABC-type peptide transporters and was uncovered by se... | [
"GO:0022857",
"GO:0055085",
"GO:0016020"
] | [
"transmembrane transporter activity",
"transmembrane transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM"
] | [
"PF00854"
] | [
"PTR2"
] | [
77393
] | 1 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00784",
"R-BTA-427975",
"R-BTA-6798695",
"R-BTA-9860276",
"R-CEL-427975",
"R-DME-427975",
"R-HSA-427975",
"R-HSA-6798695",
"R-HSA-9860276",
"R-MMU-427975",
"R-MMU-6798695",
"R-MMU-9860276",
"R-RNO-427975",
"R-RNO-6798695",
"R-RNO-9860276",
"R-SCE-427975",
"R-SCE-6798695",
"R-S... | [
"PROSITEDOC:PDOC00784",
"REACTOME:R-BTA-427975",
"REACTOME:R-BTA-6798695",
"REACTOME:R-BTA-9860276",
"REACTOME:R-CEL-427975",
"REACTOME:R-DME-427975",
"REACTOME:R-HSA-427975",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9860276",
"REACTOME:R-MMU-427975",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU... | 19 | [
"2xut",
"4aps",
"4d2b",
"4d2c",
"4d2d",
"4ikv",
"4ikw",
"4ikx",
"4iky",
"4ikz",
"4lep",
"4oh3",
"4q65",
"4tpg",
"4tph",
"4tpj",
"4uvm",
"4w6v",
"4xni",
"4xnj",
"5a2n",
"5a2o",
"5d58",
"5d59",
"5d6k",
"5mmt",
"5oxk",
"5oxl",
"5oxm",
"5oxn",
"5oxo",
"5oxp"... | 96 | [
"PUB00003872",
"PUB00005425",
"PUB00060979"
] | [
"7476181",
"7817396",
"17481610"
] | [
"The PTR family: a new group of peptide transporters.",
"The POT family of transport proteins.",
"Nitrate transporters and peptide transporters."
] | [
1995,
1994,
2007
] | 3 | [] | [
"IPR004768",
"IPR005279",
"IPR044739"
] | 0 | 3 | 0 | [
"Bacteria",
"Eukaryota",
"Methanobacteriaceae",
"metagenomes"
] | [
21392,
55813,
6,
182
] | 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",... | [
221,
3,
22,
9,
4,
27,
26,
2,
315,
27,
1,
1,
287
] | 13 | true | Family | Proton-dependent oligopeptide transporter family | Proton-dependent oligopeptide transporter family | POT_fam | 4 |
IPR000110 | 110 | Small ribosomal subunit protein bS1 | Ribosomal_bS1 | Family | 10,325 | false | false | The small ribosomal subunit protein bS1 (also known as 30S ribosomal protein S1) [ ] contains the S1 domain that has been found in a large number of RNA-associated proteins. bS1 is a prominent component of the Escherichia coli ribosome and is most probably required for translation of most, if not all, natural mRNAs in ... | [
"GO:0003723",
"GO:0003735",
"GO:0006412",
"GO:0005840"
] | [
"RNA binding",
"structural constituent of ribosome",
"translation",
"ribosome"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF002111",
"TIGR00717"
] | [
"RpsA",
"rpsA"
] | [
9066,
9595
] | 2 | [] | [] | [] | 0 | [
"6bu8",
"6h4n",
"6h58",
"6vu3",
"6vyq",
"6vyr",
"6vys",
"6vyt",
"6vyu",
"6vyw",
"6vyx",
"6vyy",
"6vyz",
"6vz2",
"6vz5",
"6vz7",
"6vzj",
"6x6t",
"6x7f",
"6x7k",
"6x9q",
"6xdq",
"6xdr",
"6xgf",
"6xii",
"6xij",
"6ztj",
"7qgh",
"7qgr",
"8a3l",
"8peg",
"8r3v"... | 62 | [
"PUB00006376",
"PUB00006418",
"PUB00006481",
"PUB00007068",
"PUB00007069",
"PUB00007070",
"PUB00150654",
"PUB00151100",
"PUB00151101"
] | [
"9179491",
"9677288",
"6348874",
"11297922",
"11290319",
"11114498",
"25122749",
"24339747",
"22908248"
] | [
"Comparison between the Escherichia coli and Bacillus subtilis genomes suggests that a major function of polynucleotide phosphorylase is to synthesize CDP.",
"Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo.",
"Structure and functions of ribosomal ... | [
1997,
1998,
1983,
2001,
2001,
2000,
2014,
2013,
2012
] | 9 | [
"IPR035104"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
10182,
19,
1,
123
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Small ribosomal subunit protein bS1 | Small ribosomal subunit protein bS1 | Ribosomal_bS1 | 2 |
IPR000111 | 111 | Glycoside hydrolase family 27/36, conserved site | Glyco_hydro_27/36_CS | Conserved_site | 17,878 | false | false | O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,... | [
"GO:0004553",
"GO:0005975"
] | [
"hydrolase activity, hydrolyzing O-glycosyl compounds",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00512"
] | [
"ALPHA_GALACTOSIDASE"
] | [
17878
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.2.1.22",
"PWY-6527",
"PDOC00443",
"R-HSA-6798695",
"R-HSA-9840310",
"R-MMU-6798695",
"R-MMU-9840310",
"R-SPO-6798695"
] | [
"EC:3.2.1.22",
"METACYC:PWY-6527",
"PROSITEDOC:PDOC00443",
"REACTOME:R-HSA-6798695",
"REACTOME:R-HSA-9840310",
"REACTOME:R-MMU-6798695",
"REACTOME:R-MMU-9840310",
"REACTOME:R-SPO-6798695"
] | 8 | [
"1ktb",
"1ktc",
"1r46",
"1r47",
"1szn",
"1t0o",
"1uas",
"2xn0",
"2xn1",
"2xn2",
"2yfn",
"2yfo",
"3gxn",
"3gxp",
"3gxt",
"3h53",
"3h54",
"3h55",
"3hg2",
"3hg3",
"3hg4",
"3hg5",
"3igu",
"3lrk",
"3lrl",
"3lrm",
"3lx9",
"3lxa",
"3lxb",
"3lxc",
"3mi6",
"3s5y"... | 71 | [
"PUB00000002",
"PUB00002094",
"PUB00002595",
"PUB00004870",
"PUB00005266"
] | [
"4561015",
"2556373",
"2174888",
"7624375",
"8535779"
] | [
"Biochemistry of -galactosidases.",
"Nucleotide sequences and operon structure of plasmid-borne genes mediating uptake and utilization of raffinose in Escherichia coli.",
"Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alph... | [
1972,
1989,
1990,
1995,
1995
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ct3z32",
"unclassified sequences"
] | [
12,
9574,
8212,
1,
79
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
13,
1,
2,
3,
15,
11,
8,
8,
1,
14
] | 10 | true | Conserved_site | Glycoside hydrolase family 27/36, conserved site | Glycoside hydrolase family 27/36, conserved site | Glyco_hydro_27/36_CS | 3 |
IPR000112 | 112 | GPCR, family 3, metabotropic glutamate receptor 6 | GPCR_3__mGluR6 | Family | 202 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01056"
] | [
"MTABOTROPC6R"
] | [
202
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"294",
"R-HSA-418594",
"R-HSA-420499",
"R-MMU-418594",
"R-MMU-420499",
"R-RNO-418594",
"R-RNO-420499"
] | [
"IUPHAR:294",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-420499",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-420499"
] | 7 | [] | 0 | [
"PUB00001481",
"PUB00002720",
"PUB00002780",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"9215706",
"1320017",
"8389366",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"The whole nucleotide sequence and chromosomal localization of the gene for human metabotropic glutamate receptor subtype 6.",
"Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.",
"Molecular characterization of a novel retinal me... | [
1997,
1992,
1993,
1991,
1993,
1992,
1994,
1991,
1997,
2007,
2000,
2003,
1994,
2005,
2009,
2006,
2013
] | 17 | [
"IPR000162"
] | [] | 1 | 0 | 1 | [
"Theria"
] | [
202
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
3,
3
] | 3 | true | Family | GPCR, family 3, metabotropic glutamate receptor 6 | GPCR, family 3, metabotropic glutamate receptor 6 | GPCR_3__mGluR6 | 1 |
IPR000114 | 114 | Large ribosomal subunit protein uL16, bacteria | Ribosomal_uL16_bact | Family | 46,097 | false | false | Ribosomal protein uL16 is one of the proteins from the large ribosomal subunit from bacteria and its homologues from chloroplast and mitochondria. In Escherichia coli, uL16 is known to bind directly the 23S rRNA and to be located at the A site of the peptidyltransferase centre. uL16 is a protein of 133 to 185 amino-aci... | [
"GO:0003735",
"GO:0019843",
"GO:0006412"
] | [
"structural constituent of ribosome",
"rRNA binding",
"translation"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"PRINTS",
"PANTHER",
"NCBIFAM"
] | [
"MF_01342",
"PR00060",
"PTHR12220",
"TIGR01164"
] | [
"Ribosomal_uL16",
"RIBOSOMALL16",
"",
"rplP_bact"
] | [
36840,
44114,
45855,
41858
] | 4 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"PDOC00506",
"R-BTA-5389840",
"R-BTA-5419276",
"R-BTA-9937383",
"R-HSA-5368286",
"R-HSA-5389840",
"R-HSA-5419276",
"R-HSA-9937383",
"R-MMU-5389840",
"R-MMU-5419276",
"R-MMU-9937383",
"R-RNO-5389840",
"R-RNO-5419276",
"R-RNO-9937383"
] | [
"PROSITEDOC:PDOC00506",
"REACTOME:R-BTA-5389840",
"REACTOME:R-BTA-5419276",
"REACTOME:R-BTA-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",
"REACTOME:... | 14 | [
"1njm",
"1njp",
"1nkw",
"1nwx",
"1nwy",
"1sm1",
"1vvj",
"1vy4",
"1vy5",
"1vy6",
"1vy7",
"1wki",
"1xbp",
"1y69",
"2ftc",
"2j28",
"2rdo",
"2zjp",
"2zjq",
"2zjr",
"3bbx",
"3cf5",
"3dll",
"3iy9",
"3j5l",
"3j6b",
"3j7y",
"3j7z",
"3j8g",
"3j9m",
"3j9w",
"3j9y"... | 1,200 | [
"PUB00007068",
"PUB00007069",
"PUB00007070"
] | [
"11297922",
"11290319",
"11114498"
] | [
"Atomic structures at last: the ribosome in 2000.",
"The ribosome in focus.",
"The end of the beginning: structural studies of ribosomal proteins."
] | [
2001,
2001,
2000
] | 3 | [
"IPR047873"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
23395,
22275,
427
] | 3 | [
"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",... | [
13,
1,
4,
2,
1,
2,
2,
1,
7,
5,
1,
1,
5
] | 13 | true | Family | Large ribosomal subunit protein uL16, bacteria | Large ribosomal subunit protein uL16, bacteria | Ribosomal_uL16_bact | 5 |
IPR000115 | 115 | Phosphoribosylglycinamide synthetase | PRibGlycinamide_synth | Family | 32,537 | false | false | Phosphoribosylglycinamide synthetase ( ) (GARS) (phosphoribosylamine glycine ligase) [ ] catalyses the second step in the de novo biosynthesis of purine. The reaction catalysed by phosphoribosylglycinamide synthetase is the ATP-dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide: ... | [
"GO:0004637",
"GO:0009113"
] | [
"phosphoribosylamine-glycine ligase activity",
"purine nucleobase biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00138",
"PTHR43472",
"TIGR00877"
] | [
"GARS",
"",
"purD"
] | [
29788,
29050,
30804
] | 3 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.3.4.13",
"GenProp0110",
"GenProp1216",
"GenProp1284",
"GenProp1406",
"GenProp1628",
"GenProp1689",
"PWY-6121",
"PWY-6122",
"PWY-6277",
"PDOC00164",
"R-BTA-73817",
"R-DDI-73817",
"R-DME-73817",
"R-GGA-419140",
"R-HSA-73817",
"R-MMU-73817",
"R-SCE-73817",
"R-SPO-73817"
] | [
"EC:6.3.4.13",
"GP:GenProp0110",
"GP:GenProp1216",
"GP:GenProp1284",
"GP:GenProp1406",
"GP:GenProp1628",
"GP:GenProp1689",
"METACYC:PWY-6121",
"METACYC:PWY-6122",
"METACYC:PWY-6277",
"PROSITEDOC:PDOC00164",
"REACTOME:R-BTA-73817",
"REACTOME:R-DDI-73817",
"REACTOME:R-DME-73817",
"REACTOME... | 19 | [
"1gso",
"1vkz",
"2ip4",
"2qk4",
"2xcl",
"2xd4",
"2yrw",
"2yrx",
"2ys6",
"2ys7",
"2yw2",
"2yya",
"3lp8",
"3mjf",
"5vev",
"7lvo"
] | 16 | [
"PUB00002527",
"PUB00075622",
"PUB00075625"
] | [
"2687276",
"2147474",
"3097325"
] | [
"Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli.",
"De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-gly... | [
1989,
1990,
1986
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1056,
25372,
5387,
15,
707
] | 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",... | [
3,
1,
4,
5,
1,
9,
6,
1,
5,
5,
1,
1,
15
] | 13 | true | Family | Phosphoribosylglycinamide synthetase | Phosphoribosylglycinamide synthetase | PRibGlycinamide_synth | 8 |
IPR000116 | 116 | High mobility group protein HMGA | HMGA | Family | 4,531 | false | false | This entry represents the HMGA family, whose members contain DNA-binding domains, also known as AT hooks due to their ability to interact with the narrow minor groove of AT-rich DNA sequences. They play an important role in chromatin organisation [ ]. The high mobility group (HMG) proteins are the most abundant and ubi... | [
"GO:0003677",
"GO:0006355",
"GO:0000785",
"GO:0005634"
] | [
"DNA binding",
"regulation of DNA-templated transcription",
"chromatin",
"nucleus"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"PRINTS"
] | [
"PR00930"
] | [
"HIGHMOBLTYIY"
] | [
4531
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-2559584",
"R-HSA-162592",
"R-HSA-164843",
"R-HSA-175567",
"R-HSA-177539",
"R-HSA-180689",
"R-HSA-180910",
"R-HSA-2559584",
"R-MMU-2559584"
] | [
"REACTOME:R-CFA-2559584",
"REACTOME:R-HSA-162592",
"REACTOME:R-HSA-164843",
"REACTOME:R-HSA-175567",
"REACTOME:R-HSA-177539",
"REACTOME:R-HSA-180689",
"REACTOME:R-HSA-180910",
"REACTOME:R-HSA-2559584",
"REACTOME:R-MMU-2559584"
] | 9 | [
"2ezd",
"2eze"
] | 2 | [
"PUB00074432",
"PUB00074434"
] | [
"25281808",
"14645522"
] | [
"Evolution of high mobility group nucleosome-binding proteins and its implications for vertebrate chromatin specialization.",
"Transcriptional activation of the cyclin A gene by the architectural transcription factor HMGA2."
] | [
2015,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"viral metagenome"
] | [
18,
4512,
1
] | 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",
"Zea mays"
] | [
3,
5,
17,
11,
2,
9,
5,
15
] | 8 | true | Family | High mobility group protein HMGA | High mobility group protein HMGA | HMGA | 7 |
IPR000117 | 117 | Kappa casein | Casein_kappa | Family | 517 | false | false | Kappa-casein is a mammalian milk protein involved in a number of important physiological processes [ ]. In the gut, the ingested protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of dig... | [
"GO:0005576"
] | [
"extracellular region"
] | [
"cellular_component"
] | 1 | [
"PFAM",
"PIRSF",
"PANTHER"
] | [
"PF00997",
"PIRSF002374",
"PTHR11470"
] | [
"Casein_kappa",
"Casein_kappa",
""
] | [
513,
130,
510
] | 3 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-5223345",
"R-MMU-5223345",
"R-RNO-5223345",
"R-SSC-5223345"
] | [
"REACTOME:R-HSA-5223345",
"REACTOME:R-MMU-5223345",
"REACTOME:R-RNO-5223345",
"REACTOME:R-SSC-5223345"
] | 4 | [] | 0 | [
"PUB00001943"
] | [
"9409842"
] | [
"Nucleotide sequence evolution at the kappa-casein locus: evidence for positive selection within the family Bovidae."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Eumetazoa"
] | [
517
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
2
] | 3 | true | Family | Kappa casein | Kappa casein | Casein_kappa | 4 |
IPR000119 | 119 | Histone-like DNA-binding protein | Hist_DNA-bd | Family | 62,749 | false | false | Bacteria synthesise a set of small, usually basic proteins of about 90 residues that bind DNA and are known as histone-like proteins [ , ]. Examples include the HU protein in Escherichia coli which is a dimer of closely related alpha and beta chains and in other bacteria can be a dimer of identical chains. HU-type prot... | [
"GO:0003677",
"GO:0030527"
] | [
"DNA binding",
"structural constituent of chromatin"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"PFAM",
"PRINTS",
"PANTHER",
"SMART"
] | [
"PF00216",
"PR01727",
"PTHR33175",
"SM00411"
] | [
"Bac_DNA_binding",
"DNABINDINGHU",
"",
"BHL"
] | [
61738,
54191,
59800,
59957
] | 4 | [
"GP",
"PROSITEDOC"
] | [
"GenProp1207",
"PDOC00044"
] | [
"GP:GenProp1207",
"PROSITEDOC:PDOC00044"
] | 2 | [
"1b8z",
"1exe",
"1hue",
"1huu",
"1ihf",
"1mul",
"1ouz",
"1owf",
"1owg",
"1p51",
"1p71",
"1p78",
"1riy",
"1wtu",
"2ht0",
"2iie",
"2iif",
"2ndp",
"2np2",
"2o97",
"3rhi",
"4dky",
"4p3v",
"4pt4",
"4qjn",
"4qju",
"4yew",
"4yex",
"4yey",
"4yf0",
"4yfh",
"4yft"... | 54 | [
"PUB00000820",
"PUB00002462",
"PUB00003604",
"PUB00003987",
"PUB00004416",
"PUB00004725"
] | [
"2972385",
"3047111",
"3118156",
"6540370",
"8464748",
"1961745"
] | [
"Integration host factor: a protein for all reasons.",
"Histone-like proteins and bacterial chromosome structure.",
"Histonelike proteins of bacteria.",
"3-A resolution structure of a protein with histone-like properties in prokaryotes.",
"An African swine fever virus gene with similarity to bacterial DNA b... | [
1988,
1988,
1987,
1984,
1993,
1991
] | 6 | [] | [
"IPR005684",
"IPR005685",
"IPR005902"
] | 0 | 3 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
45,
60475,
602,
423,
1204
] | 5 | [
"Escherichia coli (strain K12)"
] | [
4
] | 1 | true | Family | Histone-like DNA-binding protein | Histone-like DNA-binding protein | Hist_DNA-bd | 5 |
IPR000120 | 120 | Amidase | Amidase | Family | 85,306 | false | false | Amidase signature (AS) enzymes are a large group of hydrolytic enzymes that contain a conserved stretch of approximately 130 amino acids known as the AS sequence. They are widespread, being found in both prokaryotes and eukaryotes. AS enzymes catalyse the hydrolysis of amide bonds (CO-NH2), although the family has dive... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER"
] | [
"PTHR11895"
] | [
""
] | [
85306
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"6.3.5.7",
"PDOC00494"
] | [
"EC:6.3.5.7",
"PROSITEDOC:PDOC00494"
] | 2 | [
"1o9n",
"1o9o",
"1o9p",
"1o9q",
"1obi",
"1obj",
"1obk",
"1obl",
"1och",
"1ock",
"1ocl",
"1ocm",
"2dc0",
"2df4",
"2dqn",
"2f2a",
"2g5h",
"2g5i",
"2gi3",
"3a1i",
"3a1k",
"3a2p",
"3a2q",
"3al0",
"3h0l",
"3h0m",
"3h0r",
"3ip4",
"3kfu",
"4cp8",
"4gyr",
"4gys"... | 47 | [
"PUB00035563",
"PUB00035564",
"PUB00035565",
"PUB00035566"
] | [
"15595822",
"17015445",
"12032064",
"12521300"
] | [
"Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate.",
"A second fatty acid amide hydrolase with variable distribution among placental mammals.",
"Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalyti... | [
2004,
2006,
2002,
2002
] | 4 | [] | [
"IPR004412",
"IPR014087"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
1359,
68509,
13809,
2,
1627
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
17,
6,
2,
3,
3,
1,
4,
16,
3,
1,
1,
61
] | 12 | true | Family | Amidase | Amidase | Amidase | 4 |
IPR000121 | 121 | PEP-utilising enzyme, C-terminal | PEP_util_C | Domain | 55,350 | false | false | A number of enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [ , , , ]. All these enzymes share the same catalytic mechanism: they bind PEP and transfer the phosphoryl group from it to a histidine resi... | [
"GO:0016772",
"GO:0016310"
] | [
"transferase activity, transferring phosphorus-containing groups",
"phosphorylation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PFAM"
] | [
"PF02896"
] | [
"PEP-utilizers_C"
] | [
55350
] | 1 | [
"PROSITEDOC"
] | [
"PDOC00527"
] | [
"PROSITEDOC:PDOC00527"
] | 1 | [
"1dik",
"1ggo",
"1jde",
"1kbl",
"1kc7",
"1vbg",
"1vbh",
"2bg5",
"2dik",
"2hro",
"2hwg",
"2kx9",
"2l5h",
"2n5t",
"2ols",
"2r82",
"2wqd",
"2x0s",
"2xdf",
"2xz7",
"2xz9",
"5jvj",
"5jvl",
"5jvn",
"5lu4",
"6v9k",
"6vbj",
"6vu0",
"8a8e",
"9dae",
"9pzl"
] | 31 | [
"PUB00000317",
"PUB00001868",
"PUB00003750",
"PUB00005010",
"PUB00049284"
] | [
"2176881",
"8973315",
"1557039",
"7686067",
"18052212"
] | [
"Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.",
"Novel phosphotransferase-encoding genes revealed by a... | [
1990,
1996,
1992,
1993,
2007
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Imitervirales",
"unclassified sequences"
] | [
1338,
50984,
2094,
7,
927
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
5,
6,
66
] | 4 | true | Domain | PEP-utilising enzyme, C-terminal | PEP-utilising enzyme, C-terminal | PEP_util_C | 9 |
IPR000123 | 123 | RNA-directed DNA polymerase (reverse transcriptase), msDNA | Reverse_transcriptase_msDNA | Family | 8,428 | false | false | The use of an RNA template to produce DNA, for integration into the host genome and exploitation of a host cell, is a strategy employed in the replication of retroid elements, such as the retroviruses and bacterial retrons. The enzyme catalysing polymerisation is an RNA-directed DNA-polymerase, or reverse trancriptase ... | [
"GO:0003723",
"GO:0003964",
"GO:0006278"
] | [
"RNA binding",
"RNA-directed DNA polymerase activity",
"RNA-templated DNA biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"PRINTS",
"CDD"
] | [
"PR00866",
"cd03487"
] | [
"RNADNAPOLMS",
"RT_Bac_retron_II"
] | [
8320,
4341
] | 2 | [
"EC"
] | [
"2.7.7.49"
] | [
"EC:2.7.7.49"
] | 1 | [
"5hhj",
"5hhk",
"5hhl",
"5irf",
"5irg",
"6ar1",
"6ar3",
"7k9y",
"7kft",
"7kfu",
"7v9u",
"7v9x",
"7xjg",
"8bgj",
"8qbk",
"8qbl",
"8qbm",
"9e8z",
"9jm0",
"9kjx",
"9kjy",
"9kjz",
"9kk1",
"9kk2",
"9lm3",
"9n69",
"9n6b",
"9n6c",
"9nnb",
"9nnh",
"9p4j",
"9p4k"... | 32 | [
"PUB00006269",
"PUB00006358"
] | [
"1720608",
"8828137"
] | [
"msDNA and bacterial reverse transcriptase.",
"Structure, function, and evolution of bacterial reverse transcriptase."
] | [
1991,
1995
] | 2 | [] | [
"IPR049976"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
23,
8260,
12,
13,
120
] | 5 | [] | [] | 0 | true | Family | RNA-directed DNA polymerase (reverse transcriptase), msDNA | RNA-directed DNA polymerase (reverse transcriptase), msDNA | Reverse_transcriptase_msDNA | 3 |
IPR000124 | 124 | Spermadhesin | Spermadhesin | Family | 189 | false | false | A family of mammalian sperm proteins has been characterised [ , ]. As shown in the following schematic representation these proteins, which have from 110 to 130 amino acid residues, contain four conserved cysteines involved in two disulphide bonds. Structurally, the spermadhesins consist of a CUB domain [ ]. +---------... | [
"GO:0007338"
] | [
"single fertilization"
] | [
"biological_process"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00985",
"PS00986"
] | [
"SPERMADHESIN_1",
"SPERMADHESIN_2"
] | [
167,
155
] | 2 | [
"PROSITEDOC"
] | [
"PDOC00758"
] | [
"PROSITEDOC:PDOC00758"
] | 1 | [
"1sfp",
"1spp"
] | 2 | [
"PUB00001117",
"PUB00001447",
"PUB00003306"
] | [
"8397818",
"8269963",
"8510165"
] | [
"Molecular cloning and sequence analysis of two porcine seminal proteins, PSP-I and PSP-II: new members of the spermadhesin family.",
"Characterization of two glycosylated boar spermadhesins.",
"The CUB domain. A widespread module in developmentally regulated proteins."
] | [
1993,
1993,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Chordata"
] | [
189
] | 1 | [] | [] | 0 | true | Family | Spermadhesin | Spermadhesin | Spermadhesin | 9 |
IPR000125 | 125 | Glycoside hydrolase, family 14A, bacterial | Glyco_hydro_14A_bac | Family | 177 | false | false | This entry represents bacterial beta-amylases, which belong to the glycoside hydrolase family 14 ( , ). Beta-amylases hydrolyse 1,4-alpha-glycosidic linkages in starch-type polysaccharide substrates, removing successive maltose units from the non-reducing ends of the chains [ ]. These enzymes consists of two domains: t... | [
"GO:0016161",
"GO:0005976"
] | [
"beta-amylase activity",
"polysaccharide metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PRINTS"
] | [
"PR00841"
] | [
"GLHYDLASE14A"
] | [
177
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"3.2.1.2",
"PWY-6724",
"PWY-842"
] | [
"EC:3.2.1.2",
"METACYC:PWY-6724",
"METACYC:PWY-842"
] | 3 | [
"1b90",
"1b9z",
"1itc",
"1j0y",
"1j0z",
"1j10",
"1j11",
"1j12",
"1j18",
"1vem",
"1ven",
"1veo",
"1vep",
"3voc",
"5bca",
"8zrz"
] | 16 | [
"PUB00002354",
"PUB00004870",
"PUB00005266",
"PUB00023561",
"PUB00163179"
] | [
"1491009",
"7624375",
"8535779",
"10353816",
"39288698"
] | [
"Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin.",
"Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.",
"Structures and mechanisms of glycosyl hydrol... | [
1992,
1995,
1995,
1999,
2024
] | 5 | [
"IPR001554"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
177
] | 1 | [] | [] | 0 | true | Family | Glycoside hydrolase, family 14A, bacterial | Glycoside hydrolase, family 14A, bacterial | Glyco_hydro_14A_bac | 8 |
IPR000126 | 126 | Serine proteases, V8 family, serine active site | V8_ser_AS | Active_site | 1,022 | false | false | A number of prokaryotic proteases have been shown [ , ] to be evolutionary related; their catalytic activity is provided by a charge relay system similar to that of the trypsin family of serine proteases but which probably evolved by independent convergent evolution. The sequence around the residues involved in the cat... | [
"GO:0008236",
"GO:0006508"
] | [
"serine-type peptidase activity",
"proteolysis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PROSITE"
] | [
"PS00673"
] | [
"V8_SER"
] | [
1022
] | 1 | [
"EC",
"PROSITEDOC"
] | [
"3.4.21.19",
"PDOC00571"
] | [
"EC:3.4.21.19",
"PROSITEDOC:PDOC00571"
] | 2 | [
"1agj",
"1dt2",
"1dua",
"1exf",
"1qtf",
"1qy6",
"1wcz",
"2o8l",
"4jcn",
"5c2z",
"6e0u",
"6q12",
"6tya",
"6u1b",
"8dax",
"8t3i",
"8t3j",
"9bsh",
"9bsm",
"9j9a"
] | 20 | [
"PUB00001410",
"PUB00001590",
"PUB00002096",
"PUB00017979"
] | [
"1346764",
"2384148",
"2105291",
"9065774"
] | [
"Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis.",
"The epidermolytic toxins are serine proteases.",
"Gene encoding a novel extracellular metalloprotease in Bacillus subtilis.",
"Chemistry of collagen cross-linking: biochemical changes in collagen durin... | [
1992,
1990,
1990,
1997
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
8,
909,
93,
8,
4
] | 5 | [] | [] | 0 | true | Active_site | Serine proteases, V8 family, serine active site | Serine proteases, V8 family, serine active site | V8_ser_AS | 2 |
IPR000128 | 128 | Progesterone receptor | Progest_rcpt | Family | 677 | false | false | Steroid or nuclear hormone receptors (NRs) constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members of the superfamily include the steroid hormone receptors and r... | [
"GO:0003677",
"GO:0003707",
"GO:0005496",
"GO:0006355",
"GO:0043401",
"GO:0005634"
] | [
"DNA binding",
"nuclear steroid receptor activity",
"steroid binding",
"regulation of DNA-templated transcription",
"steroid hormone receptor signaling pathway",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process",
"cellular_component"
] | 6 | [
"PFAM",
"PRINTS"
] | [
"PF02161",
"PR00544"
] | [
"Prog_receptor",
"PROGESTRONER"
] | [
674,
638
] | 2 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-CFA-3371497",
"R-CFA-383280",
"R-HSA-1251985",
"R-HSA-3371497",
"R-HSA-383280",
"R-HSA-4090294",
"R-HSA-9018519",
"R-MMU-3371497",
"R-MMU-383280",
"R-MMU-4090294",
"R-MMU-9018519",
"R-RNO-3371497",
"R-RNO-383280",
"R-RNO-4090294",
"R-RNO-9018519"
] | [
"REACTOME:R-CFA-3371497",
"REACTOME:R-CFA-383280",
"REACTOME:R-HSA-1251985",
"REACTOME:R-HSA-3371497",
"REACTOME:R-HSA-383280",
"REACTOME:R-HSA-4090294",
"REACTOME:R-HSA-9018519",
"REACTOME:R-MMU-3371497",
"REACTOME:R-MMU-383280",
"REACTOME:R-MMU-4090294",
"REACTOME:R-MMU-9018519",
"REACTOME:R... | 15 | [] | 0 | [
"PUB00004464",
"PUB00006168"
] | [
"7899080",
"8165128"
] | [
"Vitamin D receptor contains multiple dimerization interfaces that are functionally different.",
"Human androgen receptor expressed in HeLa cells activates transcription in vitro."
] | [
1995,
1994
] | 2 | [
"IPR001723"
] | [] | 1 | 0 | 1 | [
"Bilateria",
"Nocardioides zhouii"
] | [
676,
1
] | 2 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
6,
4,
6
] | 3 | true | Family | Progesterone receptor | Progesterone receptor | Progest_rcpt | 7 |
IPR000131 | 131 | ATP synthase, F1 complex, gamma subunit | ATP_synth_F1_gsu | Family | 33,199 | false | false | The ATPase F1 complex gamma subunit forms the central shaft that connects the F0 rotary motor to the F1 catalytic core. The gamma subunit functions as a rotary motor inside the cylinder formed by the α(3)β(3) subunits in the F1 complex [ ]. The most conserved region of the gamma subunit is its C terminus, which seems t... | [
"GO:0046933",
"GO:0015986",
"GO:0045259"
] | [
"proton-transporting ATP synthase activity, rotational mechanism",
"proton motive force-driven ATP synthesis",
"proton-transporting ATP synthase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PFAM",
"PRINTS",
"PANTHER",
"NCBIFAM",
"CDD"
] | [
"MF_00815",
"PF00231",
"PR00126",
"PTHR11693",
"TIGR01146",
"cd12151"
] | [
"ATP_synth_gamma_bact",
"ATP-synt",
"ATPASEGAMMA",
"",
"ATPsyn_F1gamma",
"F1-ATPase_gamma"
] | [
25690,
33134,
31906,
32245,
29739,
31111
] | 6 | [
"GP",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"GenProp0128",
"PDOC00138",
"R-BTA-163210",
"R-BTA-8949613",
"R-BTA-9837999",
"R-DDI-9837999",
"R-DME-163210",
"R-DME-8949613",
"R-DME-9837999",
"R-HSA-163210",
"R-HSA-8949613",
"R-HSA-9837999",
"R-MMU-163210",
"R-MMU-8949613",
"R-MMU-9837999",
"R-RNO-163210",
"R-RNO-8949613",
"R-R... | [
"GP:GenProp0128",
"PROSITEDOC:PDOC00138",
"REACTOME:R-BTA-163210",
"REACTOME:R-BTA-8949613",
"REACTOME:R-BTA-9837999",
"REACTOME:R-DDI-9837999",
"REACTOME:R-DME-163210",
"REACTOME:R-DME-8949613",
"REACTOME:R-DME-9837999",
"REACTOME:R-HSA-163210",
"REACTOME:R-HSA-8949613",
"REACTOME:R-HSA-98379... | 20 | [
"1bmf",
"1cow",
"1e1q",
"1e1r",
"1e79",
"1efr",
"1fs0",
"1h8e",
"1h8h",
"1mab",
"1nbm",
"1ohh",
"1qo1",
"1w0j",
"1w0k",
"2ck3",
"2f43",
"2hld",
"2jdi",
"2jiz",
"2jj1",
"2jj2",
"2qe7",
"2v7q",
"2w6e",
"2w6f",
"2w6g",
"2w6h",
"2w6i",
"2w6j",
"2wpd",
"2wss"... | 347 | [
"PUB00009752",
"PUB00020603",
"PUB00020604",
"PUB00020605",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"11309608",
"15473999",
"15078220",
"16154570",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation of the F0F1-ATP ... | [
2001,
2004,
2004,
2005,
2010,
2008,
1992,
1998
] | 8 | [] | [
"IPR017709"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
29,
25614,
6994,
562
] | 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",... | [
12,
1,
2,
1,
1,
4,
10,
1,
7,
8,
1,
1,
36
] | 13 | true | Family | ATP synthase, F1 complex, gamma subunit | ATP synthase, F1 complex, gamma subunit | ATP_synth_F1_gsu | 8 |
IPR000132 | 132 | Nitrilase/cyanide hydratase, conserved site | Nitrilase/CN_hydratase_CS | Conserved_site | 12,081 | false | false | This family includes both nitrilases and cyanide hydratase. Nitrilases ( ) are enzymes that convert nitriles into their corresponding acids and ammonia. They are widespread in microbes as well as in plants where they convert indole-3-acetonitrile to the hormone indole-3- acetic acid. A conserved cysteine has been shown... | [
"GO:0003824"
] | [
"catalytic activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE",
"PROSITE"
] | [
"PS00920",
"PS00921"
] | [
"NITRIL_CHT_1",
"NITRIL_CHT_2"
] | [
9301,
5650
] | 2 | [
"EC",
"PROSITEDOC"
] | [
"3.5.5",
"PDOC00712"
] | [
"EC:3.5.5",
"PROSITEDOC:PDOC00712"
] | 2 | [
"3n05",
"3wuy",
"6i00",
"6i5t",
"6i5u",
"6zby",
"8c5i",
"8p4i",
"8uxu",
"9er3"
] | 10 | [
"PUB00000214",
"PUB00002743",
"PUB00004812"
] | [
"1382413",
"1400390",
"8419930"
] | [
"Cloning and properties of a cyanide hydratase gene from the phytopathogenic fungus Gloeocercospora sorghi.",
"Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue.",
"Nitrilase in biosynthesis of the plant hormone indole-3-acet... | [
1992,
1992,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
9,
7397,
4351,
324
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"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)",
"Zea mays"
] | [
23,
1,
2,
4,
1,
14
] | 6 | true | Conserved_site | Nitrilase/cyanide hydratase, conserved site | Nitrilase/cyanide hydratase, conserved site | Nitrilase/CN_hydratase_CS | 5 |
IPR000133 | 133 | ER lumen protein retaining receptor | ER_ret_rcpt | Family | 11,448 | false | false | Proteins resident in the lumen of the endoplasmic reticulum (ER) contain a C-terminal tetrapeptide, commonly known as Lys-Asp-Glu-Leu (KDEL) in mammals and His-Asp-Glu-Leu (HDEL) in yeast (Saccharomyces cerevisiae) that acts as a signal for their retrieval from subsequent compartments of the secretory pathway. The rece... | [
"GO:0046923",
"GO:0006621",
"GO:0016020"
] | [
"ER retention sequence binding",
"protein retention in ER lumen",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PFAM",
"PRINTS",
"PROSITE",
"PROSITE",
"PANTHER"
] | [
"PF00810",
"PR00660",
"PS00951",
"PS00952",
"PTHR10585"
] | [
"ER_lumen_recept",
"ERLUMENR",
"ER_LUMEN_RECEPTOR_1",
"ER_LUMEN_RECEPTOR_2",
""
] | [
11380,
10553,
5483,
5892,
11174
] | 5 | [
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACT... | [
"PDOC00732",
"R-BTA-6807878",
"R-BTA-6811434",
"R-CEL-6807878",
"R-CEL-6811434",
"R-DDI-6807878",
"R-DDI-6811434",
"R-DME-6807878",
"R-DME-6811434",
"R-DRE-6811434",
"R-GGA-6807878",
"R-GGA-6811434",
"R-HSA-381038",
"R-HSA-6807878",
"R-HSA-6811434",
"R-MMU-6807878",
"R-MMU-6811434",
... | [
"PROSITEDOC:PDOC00732",
"REACTOME:R-BTA-6807878",
"REACTOME:R-BTA-6811434",
"REACTOME:R-CEL-6807878",
"REACTOME:R-CEL-6811434",
"REACTOME:R-DDI-6807878",
"REACTOME:R-DDI-6811434",
"REACTOME:R-DME-6807878",
"REACTOME:R-DME-6811434",
"REACTOME:R-DRE-6811434",
"REACTOME:R-GGA-6807878",
"REACTOME:... | 26 | [
"6i6b",
"6i6h",
"6i6j",
"6y7v",
"6zxr",
"7oxe",
"7oye",
"7rxc",
"8apy"
] | 9 | [
"PUB00001233"
] | [
"8392934"
] | [
"Mutational analysis of the human KDEL receptor: distinct structural requirements for Golgi retention, ligand binding and retrograde transport."
] | [
1993
] | 1 | [] | [] | 0 | 0 | null | [
"Eukaryota"
] | [
11448
] | 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... | [
34,
2,
6,
1,
5,
5,
2,
16,
11,
1,
1,
38
] | 12 | true | Family | ER lumen protein retaining receptor | ER lumen protein retaining receptor | ER_ret_rcpt | 8 |
IPR000136 | 136 | Oleosin | Oleosin | Family | 3,899 | false | false | Oleosins [ ] are the proteinaceous components of plants' lipid storage bodies called oil bodies. Oil bodies are small droplets (0.2 to 1.5 mu-m in diameter) containing mostly triacylglycerol that are surrounded by a phospholipid/ oleosin annulus. Oleosins may have a structural role in stabilising the lipid body during ... | [
"GO:0012511",
"GO:0016020"
] | [
"monolayer-surrounded lipid storage body",
"membrane"
] | [
"cellular_component",
"cellular_component"
] | 2 | [
"PFAM",
"PROSITE",
"PANTHER"
] | [
"PF01277",
"PS00811",
"PTHR33203"
] | [
"Oleosin",
"OLEOSINS",
""
] | [
3877,
1532,
3719
] | 3 | [
"PROSITEDOC"
] | [
"PDOC00639"
] | [
"PROSITEDOC:PDOC00639"
] | 1 | [] | 0 | [
"PUB00000622",
"PUB00002731"
] | [
"1989697",
"1639802"
] | [
"A class of amphipathic proteins associated with lipid storage bodies in plants. Possible similarities with animal serum apolipoproteins.",
"Characterization of the charged components and their topology on the surface of plant seed oil bodies."
] | [
1991,
1992
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota"
] | [
2,
3897
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
89,
12,
33
] | 3 | true | Family | Oleosin | Oleosin | Oleosin | 2 |
IPR000138 | 138 | Hydroxymethylglutaryl-CoA lyase, active site | HMG_CoA_lyase_AS | Active_site | 5,089 | false | false | Synonym(s): 3-hydroxy-3-methylglutaryl-coenzyme A synthase, HMG-CoA lyase. HMG-CoA lyase catalyses the transformation of HMG-CoA into acetyl-CoA and acetoacetate. In vertebrates it is a mitochondrial enzyme that is involved in ketogenesis and in leucine catabolism [ ]. In some bacteria, such as Pseudomonas mevalonii, i... | [
"GO:0004419"
] | [
"hydroxymethylglutaryl-CoA lyase activity"
] | [
"molecular_function"
] | 1 | [
"PROSITE"
] | [
"PS01062"
] | [
"HMG_COA_LYASE"
] | [
5089
] | 1 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.1.3.4",
"PWY-5074",
"PDOC00813",
"R-BTA-77111",
"R-BTA-9033241",
"R-HSA-77111",
"R-HSA-9033241",
"R-MMU-77111",
"R-MMU-9033241",
"R-RNO-77111",
"R-RNO-9033241"
] | [
"EC:4.1.3.4",
"METACYC:PWY-5074",
"PROSITEDOC:PDOC00813",
"REACTOME:R-BTA-77111",
"REACTOME:R-BTA-9033241",
"REACTOME:R-HSA-77111",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-77111",
"REACTOME:R-MMU-9033241",
"REACTOME:R-RNO-77111",
"REACTOME:R-RNO-9033241"
] | 11 | [
"2cw6",
"2ftp",
"3mp3",
"3mp4",
"3mp5"
] | 5 | [
"PUB00000366",
"PUB00002821"
] | [
"1637819",
"8440722"
] | [
"3-Hydroxy-3-methylglutaryl coenzyme A lyase: affinity labeling of the Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active site.",
"3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency."
] | [
1992,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
2362,
2698,
29
] | 3 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
2,
3,
2,
3,
4,
5
] | 6 | true | Active_site | Hydroxymethylglutaryl-CoA lyase, active site | Hydroxymethylglutaryl-CoA lyase, active site | HMG_CoA_lyase_AS | 6 |
IPR000141 | 141 | Prostaglandin F receptor | PglndnF_rcpt | Family | 748 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0004958",
"GO:0007186",
"GO:0016020"
] | [
"prostaglandin F receptor activity",
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"PRINTS"
] | [
"PR00855"
] | [
"PRSTNOIDFPR"
] | [
748
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"344",
"R-HSA-391908",
"R-HSA-416476",
"R-MMU-391908",
"R-MMU-416476",
"R-RNO-391908",
"R-RNO-416476"
] | [
"IUPHAR:344",
"REACTOME:R-HSA-391908",
"REACTOME:R-HSA-416476",
"REACTOME:R-MMU-391908",
"REACTOME:R-MMU-416476",
"REACTOME:R-RNO-391908",
"REACTOME:R-RNO-416476"
] | 7 | [
"8iq4",
"8iq6",
"8iuk",
"8iul",
"8ium",
"8xjk",
"8xjl",
"8xjm"
] | 8 | [
"PUB00000131",
"PUB00002477",
"PUB00004960",
"PUB00004961",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"2111655",
"2830256",
"8386361",
"8170923",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"G proteins in signal transduction.",
"G protein involvement in receptor-effector coupling.",
"Design of a discriminating fingerprint for G-protein-coupled receptors.",
"Fingerprinting G-protein-coupled receptors.",
"The G protein-coupled receptor repertoires of human and mouse.",
"GCRDb: a G-protein-coup... | [
1990,
1988,
1993,
1994,
2003,
1994,
2005,
2009,
2006,
2013
] | 10 | [
"IPR008365"
] | [] | 1 | 0 | 1 | [
"Gnathostomata"
] | [
748
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
3,
4,
2
] | 3 | true | Family | Prostaglandin F receptor | Prostaglandin F receptor | PglndnF_rcpt | 1 |
IPR000143 | 143 | Geminivirus MSV 27Kd coat protein | Gemcoat_MSV | Family | 845 | false | false | Geminiviruses are characterised by a genome of circular single-stranded DNA encapsidated in twinned (geminate) quasi-isometric particles, from which the group derives its name [ ]. Most geminiviruses can be divided into two subgroups on the basis of host range and/or insect vector: i.e. those that infect dicotyledenous... | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR00226"
] | [
"GEMCOATMSV"
] | [
845
] | 1 | [] | [] | [] | 0 | [
"8ugq",
"8uh4"
] | 2 | [
"PUB00001133",
"PUB00001145",
"PUB00003142",
"PUB00003143",
"PUB00004348",
"PUB00004397",
"PUB00005574",
"PUB00005578"
] | [
"6526009",
"16453696",
"1919519",
"1588314",
"2829117",
"1840676",
"1984668",
"1926771"
] | [
"The nucleotide sequence of maize streak virus DNA.",
"The nucleotide sequence of an infectious clone of the geminivirus beet curly top virus.",
"The nucleotide sequence and genome structure of the geminivirus miscanthus streak virus.",
"The nucleotide sequence of an infectious insect-transmissible clone of t... | [
1984,
1986,
1991,
1992,
1988,
1991,
1991,
1991
] | 8 | [
"IPR000263"
] | [] | 1 | 0 | 1 | [
"Pentapetalae",
"Viruses"
] | [
6,
839
] | 2 | [] | [] | 0 | true | Family | Geminivirus MSV 27Kd coat protein | Geminivirus MSV 27Kd coat protein | Gemcoat_MSV | 6 |
IPR000144 | 144 | GPCR, family 3, metabotropic glutamate receptor 8 | GPCR_3_mGluR8 | Family | 572 | false | false | G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can... | [
"GO:0007186",
"GO:0016020"
] | [
"G protein-coupled receptor signaling pathway",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"PRINTS"
] | [
"PR01058"
] | [
"MTABOTROPC8R"
] | [
572
] | 1 | [
"IUPHAR",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"296",
"R-HSA-418594",
"R-HSA-420499",
"R-MMU-418594",
"R-MMU-420499",
"R-RNO-418594",
"R-RNO-420499"
] | [
"IUPHAR:296",
"REACTOME:R-HSA-418594",
"REACTOME:R-HSA-420499",
"REACTOME:R-MMU-418594",
"REACTOME:R-MMU-420499",
"REACTOME:R-RNO-418594",
"REACTOME:R-RNO-420499"
] | 7 | [
"6bsz",
"6bt5",
"6e5v",
"9mb9",
"9mba",
"9mbb",
"9mbc",
"9mbd"
] | 8 | [
"PUB00002720",
"PUB00003464",
"PUB00003888",
"PUB00004090",
"PUB00004161",
"PUB00004309",
"PUB00004961",
"PUB00005138",
"PUB00007343",
"PUB00036049",
"PUB00036050",
"PUB00053635",
"PUB00063577",
"PUB00063578",
"PUB00063579",
"PUB00063580",
"PUB00063816"
] | [
"1320017",
"7722646",
"9016353",
"1847995",
"8255296",
"1309649",
"8170923",
"1656524",
"9292726",
"17266540",
"10773016",
"12679517",
"8081729",
"15914470",
"18948278",
"16753280",
"23020293"
] | [
"Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction.",
"A novel metabotropic glutamate receptor expressed in the retina and olfactory bulb.",
"Cloning and expression of rat metabotropic glutamate receptor 8 reveals a distinct pharm... | [
1992,
1995,
1997,
1991,
1993,
1992,
1994,
1991,
1997,
2007,
2000,
2003,
1994,
2005,
2009,
2006,
2013
] | 17 | [
"IPR000162"
] | [] | 1 | 0 | 1 | [
"Euteleostomi"
] | [
572
] | 1 | [
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
5,
4,
3
] | 3 | true | Family | GPCR, family 3, metabotropic glutamate receptor 8 | GPCR, family 3, metabotropic glutamate receptor 8 | GPCR_3_mGluR8 | 5 |
IPR000145 | 145 | Outer capsid protein VP5, Orbivirus | Capsid_VP5_Orbivir | Family | 844 | false | false | The orbivirus VP5 protein is one of the two proteins (with VP2) which make up the virus particle outer capsid. Cryoelectron microscopy indicates that VP5 is a trimer suggesting that there are 360 copies of VP5 per virion [ ]. | [
"GO:0005198",
"GO:0019028"
] | [
"structural molecule activity",
"viral capsid"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"PFAM"
] | [
"PF00901"
] | [
"Orbi_VP5"
] | [
844
] | 1 | [
"GP"
] | [
"GenProp1006"
] | [
"GP:GenProp1006"
] | 1 | [
"3iyk",
"3j9e",
"7rtn",
"7rto",
"8rt0",
"8rt1"
] | 6 | [
"PUB00005622"
] | [
"9281498"
] | [
"Structure of Broadhaven virus by cryoelectron microscopy: correlation of structural and antigenic properties of Broadhaven virus and bluetongue virus outer capsid proteins."
] | [
1997
] | 1 | [] | [] | 0 | 0 | null | [
"Haptolina brevifila",
"Riboviria"
] | [
1,
843
] | 2 | [] | [] | 0 | true | Family | Outer capsid protein VP5, Orbivirus | Outer capsid protein VP5, Orbivirus | Capsid_VP5_Orbivir | 8 |
IPR000146 | 146 | Fructose-1,6-bisphosphatase class 1 | FBPase_class-1 | Family | 21,480 | false | false | This entry represents the fructose-1,6-bisphosphatase (FBPase) class 1 family. FBPase is a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [ , ]. It is involved in many different metabolic pathways and found in most org... | [
"GO:0016791",
"GO:0005975"
] | [
"phosphatase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PIRSF",
"PANTHER",
"CDD"
] | [
"MF_01855",
"PIRSF000904",
"PTHR11556",
"cd00354"
] | [
"FBPase_class1",
"FBPtase_SBPase",
"",
"FBPase"
] | [
18914,
19181,
21402,
18813
] | 4 | [
"EC",
"METACYC",
"PROSITEDOC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.11",
"PWY-5484",
"PDOC00114",
"R-BTA-70263",
"R-DDI-70263",
"R-HSA-70263",
"R-MMU-70263",
"R-RNO-70263",
"R-SCE-70263",
"R-SPO-70263",
"R-SSC-70263"
] | [
"EC:3.1.3.11",
"METACYC:PWY-5484",
"PROSITEDOC:PDOC00114",
"REACTOME:R-BTA-70263",
"REACTOME:R-DDI-70263",
"REACTOME:R-HSA-70263",
"REACTOME:R-MMU-70263",
"REACTOME:R-RNO-70263",
"REACTOME:R-SCE-70263",
"REACTOME:R-SPO-70263",
"REACTOME:R-SSC-70263"
] | 11 | [
"1bk4",
"1cnq",
"1d9q",
"1dbz",
"1dcu",
"1eyi",
"1eyj",
"1eyk",
"1fbc",
"1fbd",
"1fbe",
"1fbf",
"1fbg",
"1fbh",
"1fbp",
"1fj6",
"1fj9",
"1fpb",
"1fpd",
"1fpe",
"1fpf",
"1fpg",
"1fpi",
"1fpj",
"1fpk",
"1fpl",
"1frp",
"1fsa",
"1fta",
"1kz8",
"1lev",
"1nuw"... | 153 | [
"PUB00000153",
"PUB00000179",
"PUB00000219",
"PUB00004864"
] | [
"2159755",
"3008716",
"8382485",
"7761465"
] | [
"Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase.",
"Amino acid sequence homology among fructose-1,6-bisphosphatases.",
"Structural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase.",
"Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase prote... | [
1990,
1986,
1993,
1995
] | 4 | [] | [
"IPR023079",
"IPR028343"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Imitervirales",
"metagenomes"
] | [
472,
10708,
10129,
5,
166
] | 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",... | [
11,
1,
4,
3,
1,
8,
17,
2,
15,
5,
1,
1,
26
] | 13 | true | Family | Fructose-1,6-bisphosphatase class 1 | Fructose-1,6-bisphosphatase class 1 | FBPase_class-1 | 2 |
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