{"metadata":{"accession":"PF23859","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR055645","hierarchy":null,"name":{"name":"DeoxyPurine in DNA protein A","short":"DpdA"},"description":[{"text":"<p>This entry represents the DpdA family of proteins, which are involved in the insertion of deazapurine modifications in bacterial and phage DNA. DpdA proteins are paralogues of tRNA-guanine transglycosylases (TGT), but have evolved to act on DNA rather than RNA. They catalyze the incorporation of 7-deazaguanine derivatives such as dADG (7-amido-7- deazaguanine) and dpreQ0 (7-cyano-7-deazaguanine) into DNA, which is thought to function as a protection mechanism against endonucleases. The dpdA gene is typically part of a genomic island, along with dpdB, dpdC and dpdD genes, and is proposed to be part of a restriction/ modification system that protects bacteria from foreign DNA.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00160605":{"PMID":27937735,"ISBN":null,"volume":"14","issue":"9","year":2017,"title":"Deazaguanine derivatives, examples of crosstalk between RNA and DNA modification pathways.","URL":null,"raw_pages":"1175-1184","medline_journal":"RNA Biol","ISO_journal":"RNA Biol","authors":["Hutinet G","Swarjo MA","de Crecy-Lagard V."],"DOI_URL":"https://doi.org/10.1080/15476286.2016.1265200"}},"set_info":{"accession":"CL0036","name":"TIM_barrel"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":6,"interactions":0,"matches":479,"pathways":0,"proteins":468,"proteomes":394,"sets":1,"structural_models":{"alphafold":270},"structures":0,"taxa":733},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":2,"alignment:full":307},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}