{"metadata":{"accession":"PF13907","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR025260","hierarchy":null,"name":{"name":"Chromodomain-helicase-DNA-binding protein 1-like, C-terminal","short":"CHD1-like_C"},"description":[{"text":"<p>This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins, including Chromodomain-helicase-DNA-binding protein 1 from humans (CHD1), an ATP-dependent chromatin-remodeling factor which acts as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. This helical domain consists of five alpha-helices organised in a variant helical bundle topology. Its surface is positively charged and can bind dsDNA and nucleosomes, but its specific function remains unknown [[cite:PUB00100856],[cite:PUB00100857],[cite:PUB00091268]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00091268":{"PMID":27591891,"ISBN":null,"volume":"428","issue":"21","year":2016,"title":"The Chromatin Remodelling Protein CHD1 Contains a Previously Unrecognised C-Terminal Helical Domain.","URL":null,"raw_pages":"4298-4314","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Mohanty B","Helder S","Silva AP","Mackay JP","Ryan DP."],"DOI_URL":"https://doi.org/10.1016/j.jmb.2016.08.028"},"PUB00100857":{"PMID":28866611,"ISBN":null,"volume":"55","issue":"8","year":2018,"title":"Missense variants in the chromatin remodeler <i>CHD1</i> are associated with neurodevelopmental disability.","URL":null,"raw_pages":"561-566","medline_journal":"J Med Genet","ISO_journal":"J Med Genet","authors":["Pilarowski GO","Vernon HJ","Applegate CD","Boukas L","Cho MT","Gurnett CA","Benke PJ","Beaver E","Heeley JM","Medne L","Krantz ID","Azage M","Niyazov D","Henderson LB","Wentzensen IM","Baskin B","Sacoto MJG","Bowman GD","Bjornsson HT."],"DOI_URL":null},"PUB00100856":{"PMID":18042460,"ISBN":null,"volume":"28","issue":"4","year":2007,"title":"Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing.","URL":null,"raw_pages":"665-76","medline_journal":"Mol Cell","ISO_journal":"Mol Cell","authors":["Sims RJ 3rd","Millhouse S","Chen CF","Lewis BA","Erdjument-Bromage H","Tempst P","Manley JL","Reinberg D."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":106,"interactions":0,"matches":6053,"pathways":0,"proteins":6052,"proteomes":2985,"sets":0,"structural_models":{"alphafold":905},"structures":8,"taxa":7935},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":87,"alignment:full":4726},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}