{"metadata":{"accession":"PF02457","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003390","hierarchy":null,"name":{"name":"DisA bacterial checkpoint controller nucleotide-binding","short":"DAC"},"description":[{"text":"<p>The DisA protein is a bacterial checkpoint protein that dimerises into an octameric complex. The protein consists of three distinct domains. This domain is the first and is a globular, nucleotide-binding region; the next 146-289 residues constitute the DisA-linker family, [pfam:PF10635], that consists of an elongated bundle of three alpha helices (alpha-6, alpha-10, and alpha-11), one side of which carries an additional three helices (alpha7-9), which thus forms a spine like-linker between domains 1 and 3. The C-terminal residues, of domain 3, are represented by family HHH, [pfam:PF00633], the specific DNA-binding domain. The octameric complex thus has structurally linked nucleotide-binding and DNA-binding HhH domains and the nucleotide-binding domains are bound to a cyclic di-adenosine phosphate such that DisA is a specific di-adenylate cyclase. This N-terminal domain has been identified as a diadenylate cyclase (DAC) responsible for producing c-di-AMP from two molecules of ATP [[cite:PUB00109173]]. The di-adenylate cyclase activity is strongly suppressed by binding to branched DNA, but not to duplex or single-stranded DNA, suggesting a role for DisA as a monitor of the presence of stalled replication forks or recombination intermediates via DNA structure-modulated c-di-AMP synthesis [[cite:PUB00044227]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00044227":{"PMID":18439896,"ISBN":null,"volume":"30","issue":"2","year":2008,"title":"Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates.","URL":null,"raw_pages":"167-78","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Witte G","Hartung S","Buttner K","Hopfner KP."],"DOI_URL":"http://dx.doi.org/10.1016/j.molcel.2008.02.020"},"PUB00109173":{"PMID":32095817,"ISBN":null,"volume":"48","issue":"6","year":2020,"title":"Cyclic di-AMP, a second messenger of primary importance: tertiary structures and binding mechanisms.","URL":null,"raw_pages":"2807-2829","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["He J","Yin W","Galperin MY","Chou SH."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":47,"interactions":0,"matches":11457,"pathways":0,"proteins":11457,"proteomes":9309,"sets":0,"structural_models":{"alphafold":7613},"structures":71,"taxa":14001},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":369,"alignment:full":6206},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7l8n","name":"Diadenylate cyclase with AMP from Streptococcus mutans"}}}