{"metadata":{"accession":"PF25559","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR057691","hierarchy":null,"name":{"name":"Domain of unknown function (DUF7931)","short":"DUF7931"},"description":[{"text":"<p>This entry represents a domain of unknown function mostly found in bacteria. According to structure predictions it might adopt a phospholipase D/nuclease fold. Whilst the typical phospholipase D motif HxK(x)4D(x)6GSxN is not strictly conserved the overall fold suggests a potential distant evolutionary relationship to the PLD superfamily. The PLD nucleases can have endonuclease or exonuclease activity. These enzymes use the imidazole group of histidine as a nucleophile in their catalytic mechanism [[cite:PUB00152066],[cite:PUB00160607],[cite:PUB00024729]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Domain_of_unknown_function","extract":"<p>A <b>domain of unknown function</b> (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. As of 2019, there are almost 4,000 DUF families within the Pfam database representing over 22% of known families. Some DUFs are not named using the nomenclature due to popular usage but are nevertheless DUFs.</p>","thumbnail":null}],"literature":{"PUB00160607":{"PMID":20854710,"ISBN":null,"volume":"44","issue":"1","year":2011,"title":"Nucleases: diversity of structure, function and mechanism.","URL":null,"raw_pages":"1-93","medline_journal":"Q Rev Biophys","ISO_journal":"Q Rev Biophys","authors":["Yang W."],"DOI_URL":"https://doi.org/10.1017/S0033583510000181"},"PUB00024729":{"PMID":10873862,"ISBN":null,"volume":"8","issue":"6","year":2000,"title":"The first crystal structure of a phospholipase D.","URL":null,"raw_pages":"655-67","medline_journal":"Structure","ISO_journal":"Structure","authors":["Leiros I","Secundo F","Zambonelli C","Servi S","Hough E."],"DOI_URL":"http://dx.doi.org/10.1016/S0969-2126(00)00150-7"},"PUB00152066":{"PMID":25429979,"ISBN":null,"volume":"42","issue":"22","year":2014,"title":"Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.","URL":null,"raw_pages":"14022-30","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["Tamulaitiene G","Silanskas A","Grazulis S","Zaremba M","Siksnys V."],"DOI_URL":"https://doi.org/10.1093/nar/gku1237"}},"set_info":{"accession":"CL0479","name":"PLD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":6,"interactions":0,"matches":941,"pathways":0,"proteins":941,"proteomes":938,"sets":1,"structural_models":{"alphafold":593},"structures":0,"taxa":1387},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":67,"alignment:full":477},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}