"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"
"IPR024639"	"{'subfamilies': 0, 'domain_architectures': 26, 'interactions': 0, 'matches': 1841, 'pathways': 44, 'proteins': 1841, 'proteomes': 1126, 'sets': 0, 'structural_models': {'alphafold': 1696, 'bfvd': 0}, 'structures': 4, 'taxa': 4013}"	"{}"	"[{'text': '<p>This domain is found in the N-terminal of DNA polymerase epsilon subunit B proteins. It contains a single completely conserved phenylalanine residue that may be functionally important. It forms a primarily α helical structure in which four helices are arranged in two hairpins with connecting loops containing β strands which form a short parallel sheet.</p>\r\n\r\n<p>DNA polymerase epsilon is required in DNA replication for synthesis of the leading strand. The N-terminal domain has close structural relation to AAA+ protein C-terminal domains [[cite:PUB00049604]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	"{'accession': 'IPR024639', 'name': 'DNA polymerase epsilon subunit B, N-terminal', 'type': 'Domain', 'children': []}"	""	False	False	False	"{'PUB00049604': {'PMID': 18676977, 'ISBN': None, 'volume': '36', 'issue': '15', 'year': 2008, 'title': 'The solution structure of the amino-terminal domain of human DNA polymerase epsilon subunit B is homologous to C-domains of AAA+ proteins.', 'URL': None, 'raw_pages': '5102-10', 'medline_journal': 'Nucleic Acids Res', 'ISO_journal': 'Nucleic Acids Res.', 'authors': ['Nuutinen T', 'Tossavainen H', 'Fredriksson K', 'Pirila P', 'Permi P', 'Pospiech H', 'Syvaoja JE.'], 'DOI_URL': 'http://dx.doi.org/10.1093/nar/gkn497'}}"	"{'pfam': {'PF12213': 'DNA polymerases epsilon N terminal'}}"	"{'name': 'DNA polymerase epsilon subunit B, N-terminal', 'short': 'DNA_pol_e_bsu_N'}"	""	""	""	"interpro"	"domain"	""