"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"
"PF18553"	"{'subfamilies': 0, 'domain_architectures': 98, 'interactions': 0, 'matches': 4271, 'pathways': 0, 'proteins': 4267, 'proteomes': 2797, 'sets': 1, 'structural_models': {'alphafold': 3810, 'bfvd': 0}, 'structures': 2, 'taxa': 8006}"	"{}"	"[{'text': ""<p>This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNAPhe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains [[cite:PUB00091172]].</p>"", 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR040725"	False	False	False	"{'PUB00091172': {'PMID': 20223217, 'ISBN': None, 'volume': '18', 'issue': '3', 'year': 2010, 'title': 'Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns.', 'URL': None, 'raw_pages': '343-53', 'medline_journal': 'Structure', 'ISO_journal': 'Structure', 'authors': ['Finarov I', 'Moor N', 'Kessler N', 'Klipcan L', 'Safro MG.'], 'DOI_URL': 'https://doi.org/10.1016/j.str.2010.01.002'}}"	""	"{'name': 'PheRS DNA binding domain 3', 'short': 'PheRS_DBD3'}"	""	""	"{'accession': 'CL0123', 'name': 'HTH'}"	"pfam"	"domain"	""