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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR000352",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0003747",
"name": "translation release factor activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006415",
"name": "translational termination",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"prosite": {
"PS00745": "Prokaryotic-type class I peptide chain release factors signature"
},
"pfam": {
"PF00472": "RF-1 domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR000352",
"name": "Peptide chain release factor class I",
"type": "Domain",
"children": []
},
"name": {
"name": "Peptide chain release factor class I",
"short": "Pep_chain_release_fac_I"
},
"description": [
{
"text": "<p>Peptide chain release factors (RFs) are required for the termination of protein biosynthesis [[cite:PUB00004944]]. At present two classes of RFs can be distinguished. Class I RFs bind to ribosomes that have encountered a stop codon at their decoding site and induce release of the nascent polypeptide. Class II RFs are GTP-binding proteins that interact with class I RFs and enhance class I RF activity. In prokaryotes there are two class I RFs that act in a codon specific manner [[cite:PUB00003804]]: RF-1(gene prfA) mediates UAA and UAG-dependent termination while RF-2 (gene prfB) mediates UAA and UGA-dependent termination. RF-1 and RF-2 are structurally and evolutionary related proteins which have been shown to be part of a larger family [[cite:PUB00004407]].</p>",
"llm": false,
"checked": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00004944": {
"PMID": 8821264,
"ISBN": null,
"volume": "52",
"issue": null,
"year": 1996,
"title": "Hidden infidelities of the translational stop signal.",
"URL": null,
"raw_pages": "293-335",
"medline_journal": "Prog Nucleic Acid Res Mol Biol",
"ISO_journal": "Prog. Nucleic Acid Res. Mol. Biol.",
"authors": [
"Tate WP",
"Poole ES",
"Mannering SA."
],
"DOI_URL": null
},
"PUB00003804": {
"PMID": 2215213,
"ISBN": null,
"volume": "4",
"issue": "6",
"year": 1990,
"title": "Recent advances in peptide chain termination.",
"URL": null,
"raw_pages": "861-5",
"medline_journal": "Mol Microbiol",
"ISO_journal": "Mol. Microbiol.",
"authors": [
"Craigen WJ",
"Lee CC",
"Caskey CT."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1365-2958.1990.tb00658.x"
},
"PUB00004407": {
"PMID": 1408743,
"ISBN": null,
"volume": "20",
"issue": "17",
"year": 1992,
"title": "Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure.",
"URL": null,
"raw_pages": "4423-8",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Pel HJ",
"Rep M",
"Grivell LA."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/20.17.4423"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR045853",
"name": "Peptide chain release factor class I superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 328,
"interactions": 0,
"matches": 84036,
"pathways": 12,
"proteins": 83999,
"proteomes": 20747,
"sets": 0,
"structural_models": {
"alphafold": 66305,
"bfvd": 4
},
"structures": 184,
"taxa": 40699
},
"entry_annotations": {
"alignment:seed": 648,
"alignment:full": 34462
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00607",
"url": "http://prosite.expasy.org/PDOC00607"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
