{"metadata":{"accession":"PF04076","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR005220","hierarchy":null,"name":{"name":"Bacterial OB fold (BOF) protein","short":"BOF"},"description":[{"text":"<p>Proteins in this family form an OB-fold.  Analysis of the predicted binding site of BOF family proteins implies that they lack nucleic acid-binding properties [[cite:PUB00016305]].  They contain an predicted N-terminal signal peptide which indicates that they localise in the periplasm where they may function to bind proteins, small molecules, or other typical OB-fold ligands [[cite:PUB00016305]]. As hypothesised for the distantly related OB-fold containing bacterial enterotoxins, the loss of nucleotide-binding function and the rapid evolution of the BOF ligand-binding site may be associated with the presence of BOF proteins in mobile genetic elements and their potential role in bacterial pathogenicity [[cite:PUB00016305]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00016305":{"PMID":15178340,"ISBN":null,"volume":"567","issue":"2-3","year":2004,"title":"BOF: a novel family of bacterial OB-fold proteins.","URL":null,"raw_pages":"297-301","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["Ginalski K","Kinch L","Rychlewski L","Grishin NV."],"DOI_URL":"http://dx.doi.org/10.1016/j.febslet.2004.04.086"}},"set_info":{"accession":"CL0021","name":"OB"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":5,"interactions":0,"matches":2146,"pathways":0,"proteins":2142,"proteomes":1544,"sets":1,"structural_models":{"alphafold":1372},"structures":1,"taxa":2390},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":5,"alignment:full":677},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1nnx","name":"Structure of the hypothetical protein ygiW from E. coli."}}}