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{
"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"
}
}
}