{"metadata":{"accession":"PF16319","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR032529","hierarchy":null,"name":{"name":"Surface glycan binding protein BT4661-like, N-terminal","short":"Ig_BT4661_1st"},"description":[{"text":"<p>This entry, mainly found in Bacteroides, includes the putative surface glycan binding protein (SGBP) BT4661 from Bacteroides thetaiotaomicron ([swissprot:Q89YS0]). BT4661 appears to play a role in the bacterial degrading apparatus of the host glycosaminoglycans heparin (Hep) and heparan sulfate (HS). It shows six discrete domains that adopt an Ig-like fold arranged in an extended, curved conformation [[cite:PUB00100963]]. This is the first Ig-like domain.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100963":{"PMID":28630303,"ISBN":null,"volume":"114","issue":"27","year":2017,"title":"How members of the human gut microbiota overcome the sulfation problem posed by glycosaminoglycans.","URL":null,"raw_pages":"7037-7042","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Cartmell A","Lowe EC","Basle A","Firbank SJ","Ndeh DA","Murray H","Terrapon N","Lombard V","Henrissat B","Turnbull JE","Czjzek M","Gilbert HJ","Bolam DN."],"DOI_URL":null}},"set_info":{"accession":"CL0159","name":"E-set"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":6,"interactions":0,"matches":46,"pathways":0,"proteins":46,"proteomes":46,"sets":1,"structural_models":{"alphafold":30},"structures":1,"taxa":92},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":13,"alignment:full":23},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}