{"metadata":{"accession":"PF18281","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR040747","hierarchy":null,"name":{"name":"BILBO1 N-terminal domain","short":"BILBO1_N"},"description":[{"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}],"wikipedia":null,"literature":{"PUB00091242":{"PMID":24362019,"ISBN":null,"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":null,"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"}},"set_info":{"accession":"CL0072","name":"Ubiquitin"},"overlaps_with":null,"counters":{"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},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":2,"alignment:full":30},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7a1i","name":"Crystal structure of the BILBO2/FPC4 complex"}}}