{"metadata":{"accession":"PF03656","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"Pam16","short":"Pam16"},"description":[{"text":"<p>The Pam16 protein ([swissprot:P42949]) is the fifth essential subunit of the pre-sequence translocase-associated protein import motor (PAM) [[cite:PUB00019986]].  In Saccharomyces cerevisiae, Pam16 is required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane [[cite:PUB00019986]].  Pam16 has a degenerate J domain.  J-domain proteins play important regulatory roles as co-chaperones, recruiting Hsp70 partners and accelerating the ATP-hydrolysis step of the chaperone cycle [[cite:PUB00005482]].  Pam16's J-like domain strongly interacts with Pam18's J domain, leading to a productive interaction of Pam18 with mtHsp70 at the mitochondria import channel [[cite:PUB00033671]].  Pam18 stimulates the ATPase activity of mtHsp70.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00033671":{"PMID":16105940,"ISBN":null,"volume":"102","issue":"35","year":2005,"title":"Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.","URL":null,"raw_pages":"12419-24","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["D'Silva PR","Schilke B","Walter W","Craig EA."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.0505969102"},"PUB00005482":{"PMID":9644977,"ISBN":null,"volume":"23","issue":"6","year":1998,"title":"The J-domain family and the recruitment of chaperone power.","URL":null,"raw_pages":"222-7","medline_journal":"Trends Biochem Sci","ISO_journal":"Trends Biochem. Sci.","authors":["Kelley WL."],"DOI_URL":"http://dx.doi.org/10.1016/S0968-0004(98)01215-8"},"PUB00019986":{"PMID":14981507,"ISBN":null,"volume":"11","issue":"3","year":2004,"title":"Pam16 has an essential role in the mitochondrial protein import motor.","URL":null,"raw_pages":"226-33","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat. Struct. Mol. Biol.","authors":["Frazier AE","Dudek J","Guiard B","Voos W","Li Y","Lind M","Meisinger C","Geissler A","Sickmann A","Meyer HE","Bilanchone V","Cumsky MG","Truscott KN","Pfanner N","Rehling P."],"DOI_URL":"http://dx.doi.org/10.1038/nsmb735"}},"set_info":{"accession":"CL0392","name":"Chaperone-J"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":88,"interactions":0,"matches":4516,"pathways":0,"proteins":4502,"proteomes":3157,"sets":1,"structural_models":{"alphafold":3869},"structures":1,"taxa":8470},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":3,"alignment:full":3448},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2guz","name":"Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor"}}}