{"metadata":{"accession":"PF01935","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002789","hierarchy":null,"name":{"name":"Helicase HerA, central domain","short":"DUF87"},"description":[{"text":"<p>This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA ([ec:3.6.4.12]). HerA is a helicase which is able to utilise either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding [[cite:PUB00076694]]. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus [[cite:PUB00076695]]. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle [[cite:PUB00078094]]. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.</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":{"PUB00076695":{"PMID":25880130,"ISBN":null,"volume":"16","issue":null,"year":2015,"title":"Efficient 5'-3' DNA end resection by HerA and NurA is essential for cell viability in the crenarchaeon Sulfolobus islandicus.","URL":null,"raw_pages":"2","medline_journal":"BMC Mol Biol","ISO_journal":"BMC Mol. Biol.","authors":["Huang Q","Liu L","Liu J","Ni J","She Q","Shen Y."],"DOI_URL":"http://dx.doi.org/10.1186/s12867-015-0030-z"},"PUB00078094":{"PMID":25420454,"ISBN":null,"volume":"5","issue":null,"year":2014,"title":"Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.","URL":null,"raw_pages":"5506","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Rzechorzek NJ","Blackwood JK","Bray SM","Maman JD","Pellegrini L","Robinson NP."],"DOI_URL":"http://dx.doi.org/10.1038/ncomms6506"},"PUB00076694":{"PMID":14990749,"ISBN":null,"volume":"32","issue":"4","year":2004,"title":"A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea.","URL":null,"raw_pages":"1439-47","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res.","authors":["Constantinesco F","Forterre P","Koonin EV","Aravind L","Elie C."],"DOI_URL":"http://dx.doi.org/10.1093/nar/gkh283"}},"set_info":{"accession":"CL0023","name":"P-loop_NTPase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":87,"interactions":0,"matches":11481,"pathways":0,"proteins":11479,"proteomes":6966,"sets":1,"structural_models":{"alphafold":7658},"structures":38,"taxa":11524},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":45,"alignment:full":5906},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}