{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q96YR7","uniProtkbId":"HERA_SULTO","entryAudit":{"firstPublicDate":"2015-10-14","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-12-01","entryVersion":95,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)","commonName":"Sulfolobus tokodaii","taxonId":273063,"lineage":["Archaea","Thermoproteota","Thermoprotei","Sulfolobales","Sulfolobaceae","Sulfurisphaera"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA double-strand break repair helicase HerA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"5.6.2.3"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Bidirectional DNA 3'-5' and 5'-3' helicase HerA"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18243819"}],"value":"StoHerA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18243819"}],"value":"herA"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"BAB67210.1"}],"value":"STK_21060"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8U1P0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"Involved in DNA double-strand break (DSB) repair (PubMed:18243819). Probably acts with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Has DNA-dependent ATPase activity and bidirectional DNA helicase activity (PubMed:18243819). Loads on either a 3' or a 5' DNA tail for subsequent DNA unwinding (PubMed:18243819). Can also unwind blunt-ended dsDNA, Holliday junction and splayed-arm DNA (PubMed:18243819)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"ATPase activity is slightly stimulated by either circular single- or double-stranded (ds)DNA with a weak preference for dsDNA (PubMed:18243819). Helicase activity is stimulated by Mre11 (PubMed:18243819)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"Forms a hexamer or a heptamer (PubMed:18243819). Interacts with Mre11 (PubMed:18243819)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"value":"Part of the nurA-rad50-mre11-herA operon, these genes are cotranscribed"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the HerA family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"DNA double-strand break repair helicase HerA","featureId":"PRO_0000434026"},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q97WG8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q97WG8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q97WG8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Mutagenesis","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"Lack of ATPase and helicase activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Strong decrease in ATPase and helicase activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Lack of ATPase and helicase activities. Decreases ssDNA-binding ability. Does not bind to blunt-ended dsDNA and Holliday junction substrate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Strong decrease in ATPase and helicase activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18243819"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"11572479","citationType":"journal article","authors":["Kawarabayasi Y.","Hino Y.","Horikawa H.","Jin-no K.","Takahashi M.","Sekine M.","Baba S.","Ankai A.","Kosugi H.","Hosoyama A.","Fukui S.","Nagai Y.","Nishijima K.","Otsuka R.","Nakazawa H.","Takamiya M.","Kato Y.","Yoshizawa T.","Tanaka T.","Kudoh Y.","Yamazaki J.","Kushida N.","Oguchi A.","Aoki K.","Masuda S.","Yanagii M.","Nishimura M.","Yamagishi A.","Oshima T.","Kikuchi H."],"citationCrossReferences":[{"database":"PubMed","id":"11572479"},{"database":"DOI","id":"10.1093/dnares/8.4.123"}],"title":"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7.","publicationDate":"2001","journal":"DNA Res.","firstPage":"123","lastPage":"140","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"DSM 16993 / JCM 10545 / NBRC 100140 / 7","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"18243819","citationType":"journal article","authors":["Zhang S.","Wei T.","Hou G.","Zhang C.","Liang P.","Ni J.","Sheng D.","Shen Y."],"citationCrossReferences":[{"database":"PubMed","id":"18243819"},{"database":"DOI","id":"10.1016/j.dnarep.2007.10.010"}],"title":"Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates.","publicationDate":"2008","journal":"DNA Repair","firstPage":"380","lastPage":"391","volume":"7"},"referencePositions":["FUNCTION AS A BIDIRECTIONAL HELICASE","CATALYTIC ACTIVITY","ACTIVITY REGULATION","SUBUNIT","INTERACTION WITH MRE11","INDUCTION","DNA-BINDING","MUTAGENESIS OF LYS-153; 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