{"metadata":{"accession":"PF04669","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021148","hierarchy":null,"name":{"name":"PBDC1 protein","short":"PBDC1"},"description":[{"text":"<p>This entry includes PBDC1 protein from mammals and its homologues from fungi. PBDC1 homolog from S. cerevisiae also known as Ypl225w (Chp1, Chaperone 1 for eEF1A) functions as a co-translational chaperone by forming dual interactions with the eEF1A G domain nascent chain and the UBA domain of ribosome-bound nascent polypeptide-associated complex [[cite:PUB00160075]]. This protein primes the eEF1A nascent chains for binding to GTP as part of a folding mechanism which is tightly coupled to chaperone recycling [[cite:PUB00160075]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00160075":{"PMID":39900909,"ISBN":null,"volume":"16","issue":"1","year":2025,"title":"A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.","URL":null,"raw_pages":"1277","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Sabbarini IM","Reif D","Park K","McQuown AJ","Nelliat AR","Trejtnar C","Dotsch V","Shakhnovich EI","Murray AW","Denic V."],"DOI_URL":"https://doi.org/10.1038/s41467-025-56489-3"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":47,"interactions":0,"matches":3036,"pathways":0,"proteins":3007,"proteomes":2606,"sets":0,"structural_models":{"alphafold":2555},"structures":1,"taxa":6858},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":14,"alignment:full":2357},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}