"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"
"PF18281"	"{'subfamilies': 0, 'domain_architectures': 3, 'interactions': 0, 'matches': 97, 'pathways': 0, 'proteins': 97, 'proteomes': 29, 'sets': 1, 'structural_models': {'alphafold': 91, 'bfvd': 0}, 'structures': 3, 'taxa': 81}"	"{}"	"[{'text': '<p>This is the N-terminal domain of BIBLO1 present in Trypanosoma brucei. BILBO1 is a flagella pocket collar component. Depletion of BIBLO1 prevents flagella pocket and flagella pocket collar biogenesis and leads to cell death. This domain has a ubiquitin-like fold and has a conserved patch of four aromatic residues (Phe-12, Trp-71, Tyr-87, and Phe-89) and three basic residues (Lys-15, Lys-60, and Lys-62) [[cite:PUB00091242]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR040747"	False	False	False	"{'PUB00091242': {'PMID': 24362019, 'ISBN': None, 'volume': '289', 'issue': '6', 'year': 2014, 'title': 'Structure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch.', 'URL': None, 'raw_pages': '3724-35', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Vidilaseris K', 'Morriswood B', 'Kontaxis G', 'Dong G.'], 'DOI_URL': 'https://doi.org/10.1074/jbc.M113.529032'}}"	""	"{'name': 'BILBO1 N-terminal domain', 'short': 'BILBO1_N'}"	""	"{'accession': '7a1i', 'name': 'Crystal structure of the BILBO2/FPC4 complex'}"	"{'accession': 'CL0072', 'name': 'Ubiquitin'}"	"pfam"	"domain"	""