"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"IPR000352"	"{'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}"	"{'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'}]}}"	"[{'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, 'updated': False}]"	""	"[{'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'}}]"	"{'accession': 'IPR000352', 'name': 'Peptide chain release factor class I', 'type': 'Domain', 'children': []}"	""	False	False	False	"{'PUB00004944': {'PMID': 8821264, 'ISBN': None, 'volume': '52', 'issue': None, 'year': 1996, 'title': 'Hidden infidelities of the translational stop signal.', 'URL': None, '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': None}, 'PUB00003804': {'PMID': 2215213, 'ISBN': None, 'volume': '4', 'issue': '6', 'year': 1990, 'title': 'Recent advances in peptide chain termination.', 'URL': None, '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': None, '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': None, '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'}}"	"{'prosite': {'PS00745': 'Prokaryotic-type class I peptide chain release factors signature'}, 'pfam': {'PF00472': 'RF-1 domain'}}"	"{'name': 'Peptide chain release factor class I', 'short': 'Pep_chain_release_fac_I'}"	"[{'accession': 'IPR045853', 'name': 'Peptide chain release factor class I superfamily', 'type': 'homologous_superfamily'}]"	""	""	"interpro"	"domain"	""