HRQ1_YEAST
ID HRQ1_YEAST Reviewed; 1077 AA.
AC Q05549; D6VSS0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent helicase HRQ1 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:23026052, ECO:0000269|PubMed:24440721};
DE AltName: Full=Homologous to recQ protein 1 {ECO:0000303|PubMed:18701350};
GN Name=HRQ1 {ECO:0000303|PubMed:18701350};
GN OrderedLocusNames=YDR291W {ECO:0000312|SGD:S000002699};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INDUCTION.
RX PubMed=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION.
RX PubMed=18701350; DOI=10.1016/j.compbiolchem.2008.07.005;
RA Barea F., Tessaro S., Bonatto D.;
RT "In silico analyses of a new group of fungal and plant RecQ4-homologous
RT proteins.";
RL Comput. Biol. Chem. 32:349-358(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP MUTAGENESIS OF LYS-318.
RX PubMed=23026052; DOI=10.1016/j.bbrc.2012.09.109;
RA Kwon S.H., Choi D.H., Lee R., Bae S.H.;
RT "Saccharomyces cerevisiae Hrq1 requires a long 3'-tailed DNA substrate for
RT helicase activity.";
RL Biochem. Biophys. Res. Commun. 427:623-628(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23456718; DOI=10.1007/s12275-013-3048-2;
RA Choi D.H., Lee R., Kwon S.H., Bae S.H.;
RT "Hrq1 functions independently of Sgs1 to preserve genome integrity in
RT Saccharomyces cerevisiae.";
RL J. Microbiol. 51:105-112(2013).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, AND
RP SUBUNIT.
RX PubMed=24440721; DOI=10.1016/j.celrep.2013.12.037;
RA Bochman M.L., Paeschke K., Chan A., Zakian V.A.;
RT "Hrq1, a homolog of the human RecQ4 helicase, acts catalytically and
RT structurally to promote genome integrity.";
RL Cell Rep. 6:346-356(2014).
RN [10]
RP FUNCTION.
RX PubMed=24700328; DOI=10.1534/g3.114.011205;
RA Leung G.P., Aristizabal M.J., Krogan N.J., Kobor M.S.;
RT "Conditional genetic interactions of RTT107, SLX4, and HRQ1 reveal dynamic
RT networks upon DNA damage in S. cerevisiae.";
RL G3 (Bethesda) 4:1059-1069(2014).
RN [11]
RP FUNCTION, INTERACTION WITH RAD4, AND MUTAGENESIS OF LYS-318.
RX PubMed=24682993; DOI=10.1007/s12275-014-4018-z;
RA Choi D.H., Min M.H., Kim M.J., Lee R., Kwon S.H., Bae S.H.;
RT "Hrq1 facilitates nucleotide excision repair of DNA damage induced by 4-
RT nitroquinoline-1-oxide and cisplatin in Saccharomyces cerevisiae.";
RL J. Microbiol. 52:292-298(2014).
CC -!- FUNCTION: Helicase with 3'-5' helicase activity involved in genome
CC stability (PubMed:23456718, PubMed:24440721, PubMed:24700328).
CC Functions in the RAD4-dependent nucleotide excision repair (NER)
CC pathway and plays a critical role in DNA interstrand cross-link repair
CC (PubMed:24440721, PubMed:24682993). Unwinds relatively long duplex DNA
CC up to 120-bp and requires a long 3'-tail of at least 70 nucleotides for
CC efficient unwinding of duplex DNA (PubMed:23026052). Activity is
CC significantly stimulated by a preexisting fork structure
CC (PubMed:24682993). Shows both processive helicase and DNA strand
CC annealing activities (PubMed:24682993). Affects telomere length by a
CC non-catalytic mechanism, probably through inhibiting telomerase by
CC competing with it for ssDNA binding (PubMed:24440721).
CC {ECO:0000269|PubMed:23026052, ECO:0000269|PubMed:23456718,
CC ECO:0000269|PubMed:24440721, ECO:0000269|PubMed:24682993,
CC ECO:0000269|PubMed:24700328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:23026052, ECO:0000269|PubMed:24440721};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23026052};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:23026052};
CC -!- SUBUNIT: Forms heptamer rings (PubMed:24440721). Interacts with RAD4
CC (PubMed:24682993). {ECO:0000269|PubMed:24440721,
CC ECO:0000269|PubMed:24682993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:10077188}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased mitotic recombination and
CC spontaneous mutation, as well as to sensitivity to 4-nitroquinoline 1-
CC oxide and cisplatin (PubMed:23456718). Causes also hypersensitivity to
CC DNA interstrand cross-links (ICLs) and telomere addition to DNA breaks
CC (PubMed:24440721). {ECO:0000269|PubMed:23456718,
CC ECO:0000269|PubMed:24440721}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the helicase family. HRQ1 subfamily.
CC {ECO:0000305}.
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DR EMBL; U51031; AAB64466.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12130.1; -; Genomic_DNA.
DR PIR; S70120; S70120.
DR RefSeq; NP_010577.3; NM_001180599.3.
DR AlphaFoldDB; Q05549; -.
DR SMR; Q05549; -.
DR BioGRID; 32343; 2119.
DR IntAct; Q05549; 1.
DR MINT; Q05549; -.
DR STRING; 4932.YDR291W; -.
DR iPTMnet; Q05549; -.
DR MaxQB; Q05549; -.
DR PaxDb; Q05549; -.
DR PRIDE; Q05549; -.
DR EnsemblFungi; YDR291W_mRNA; YDR291W; YDR291W.
DR GeneID; 851885; -.
DR KEGG; sce:YDR291W; -.
DR SGD; S000002699; HRQ1.
DR VEuPathDB; FungiDB:YDR291W; -.
DR eggNOG; KOG4150; Eukaryota.
DR HOGENOM; CLU_000809_1_0_1; -.
DR InParanoid; Q05549; -.
DR OMA; CIQSPKC; -.
DR BioCyc; YEAST:G3O-29854-MON; -.
DR BRENDA; 3.6.4.12; 984.
DR PRO; PR:Q05549; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05549; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IGI:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR018973; MZB.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF09369; DUF1998; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..1077
FT /note="ATP-dependent helicase HRQ1"
FT /id="PRO_0000253813"
FT DOMAIN 299..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 521..678
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 423..426
FT /note="DEAH box"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 318
FT /note="K->A: Impairs helicase and ATPase activities."
FT /evidence="ECO:0000269|PubMed:23026052,
FT ECO:0000269|PubMed:24682993"
SQ SEQUENCE 1077 AA; 123550 MW; 948F024154FBE9A6 CRC64;
MEEGPIKKKL KSAGQGSGKT DAFRNFEQFF FRLNTLYTFL ICRKHVVPTF KTLCGPIETA
LKRTVTKEDL AMVMALMPRE CVFKYIDENQ IYTETKIFDF NNGGFQQKEN DIFELKDVDD
QNQTQKSTQL LIFEFIDGTM QRSWSASDRF SQIKIPTYTT EEMKKMISKR EALFKSRLRE
FILEKEKANL DPFSELTNLA QKYIPRERDY EDPIEAMMKA KQESNEMSIP NYSNNSVITT
IPQMIEKLKS TEFYASQIKH CFTIPSRTAK YKGLCFELAP EVYQGMEHEN FYSHQADAIN
SLHQGENVII TTSTSSGKSL IYQLAAIDLL LKDPESTFMY IFPTKALAQD QKRAFKVILS
KIPELKNAVV DTYDGDTEPE ERAYIRKNAR VIFTNPDMIH TSILPNHANW RHFLYHLKLV
VVDELHIYKG LFGSHVALVM RRLLRLCHCF YENSGLQFIS CSATLKSPVQ HMKDMFGINE
VTLIHEDGSP TGAKHLVVWN PPILPQHERK RENFIRESAK ILVQLILNNV RTIAFCYVRR
VCELLMKEVR NIFIETGRED LVTEVMSYRG GYSASDRRKI EREMFHGNLK AVISTNALEL
GIDIGGLDAV LMCGFPLSMA NFHQQSGRAG RRNNDSLTLV VASDSPVDQH YVAHPESLLE
VNNFESYQDL VLDFNNILIL EGHIQCAAFE LPINFERDKQ YFTESHLRKI CVERLHHNQD
GYHASNRFLP WPSKCVSLRG GEEDQFAVVD ITNGRNIIIE EIEASRTSFT LYDGGIFIHQ
GYPYLVKEFN PDERYAKVQR VDVDWVTNQR DFTDVDPQEI ELIRSLRNSD VPVYFGKIKT
TIIVFGFFKV DKYKRIIDAI ETHNPPVIIN SKGLWIDMPK YALEICQKKQ LNVAGAIHGA
QHAIMGMLPR FIVAGVDEIQ TECKAPEKEF AERQTKRKRP ARLIFYDSKG GKYGSGLCVK
AFEHIDDIIE SSLRRIEECP CSDGCPDCVA ASFCKENSLV LSKPGAQVVL HCILGHSEDS
FIDLIKDGPE PNMPEIKVET VIPVSEHVNF SDDFKIIDVR RATKDDTHTN EIIKKEI
