ID   HRQ1_SCHPO              Reviewed;        1063 AA.
AC   O13983; O42856;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 4.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ATP-dependent helicase hrq1 {ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000269|PubMed:22064477};
DE   AltName: Full=Homologous to recQ protein 1 {ECO:0000303|PubMed:22064477};
GN   Name=hrq1 {ECO:0000303|PubMed:22064477};
GN   ORFNames=SPAC23A1.19c {ECO:0000312|PomBase:SPAC23A1.19c},
GN   SPAC26H5.01c {ECO:0000312|PomBase:SPAC23A1.19c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP   AND INTERACTION WITH RHP14.
RX   PubMed=22064477; DOI=10.1128/mcb.06184-11;
RA   Groocock L.M., Prudden J., Perry J.J., Boddy M.N.;
RT   "The RecQ4 orthologue Hrq1 is critical for DNA interstrand cross-link
RT   repair and genome stability in fission yeast.";
RL   Mol. Cell. Biol. 32:276-287(2012).
CC   -!- FUNCTION: Helicase with 3'-5' helicase activity involved in genome
CC       stability (PubMed:22064477). Functions in the nucleotide excision
CC       repair (NER) pathway and plays a critical role in DNA interstrand
CC       cross-link repair (PubMed:22064477). 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 (By similarity). Shows both
CC       processive helicase and DNA strand annealing activities (By
CC       similarity). Affects telomere length by a non-catalytic mechanism,
CC       probably through inhibiting telomerase by competing with it for ssDNA
CC       binding (By similarity). {ECO:0000250|UniProtKB:Q05549,
CC       ECO:0000269|PubMed:22064477}.
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:22064477};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q05549};
CC   -!- SUBUNIT: Forms heptamer rings (By similarity). Interacts with rhp14
CC       (PubMed:22064477). {ECO:0000250|UniProtKB:Q05549,
CC       ECO:0000269|PubMed:22064477}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22064477}.
CC   -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to DNA interstrand
CC       cross-linking (ICL) agents mitomycin C (MMC) and cisplatin, in response
CC       to both chronic and acute exposures. {ECO:0000269|PubMed:22064477}.
CC   -!- SIMILARITY: Belongs to the helicase family. HRQ1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAA16993.2; -; Genomic_DNA.
DR   RefSeq; NP_594448.2; NM_001019877.2.
DR   AlphaFoldDB; O13983; -.
DR   SMR; O13983; -.
DR   BioGRID; 278518; 160.
DR   STRING; 4896.SPAC23A1.19c.1; -.
DR   iPTMnet; O13983; -.
DR   MaxQB; O13983; -.
DR   PaxDb; O13983; -.
DR   EnsemblFungi; SPAC23A1.19c.1; SPAC23A1.19c.1:pep; SPAC23A1.19c.
DR   GeneID; 2542036; -.
DR   KEGG; spo:SPAC23A1.19c; -.
DR   PomBase; SPAC23A1.19c; hrq1.
DR   VEuPathDB; FungiDB:SPAC23A1.19c; -.
DR   eggNOG; KOG4150; Eukaryota.
DR   HOGENOM; CLU_000809_1_0_1; -.
DR   InParanoid; O13983; -.
DR   OMA; CIQSPKC; -.
DR   PhylomeDB; O13983; -.
DR   PRO; PR:O13983; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0000405; F:bubble DNA binding; IDA:PomBase.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:PomBase.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:PomBase.
DR   GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR014939; CDT1_Gemini-bd-like.
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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF08839; CDT1; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF09369; DUF1998; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01075; CDT1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46785; SSF46785; 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.
FT   CHAIN           1..1063
FT                   /note="ATP-dependent helicase hrq1"
FT                   /id="PRO_0000353818"
FT   DOMAIN          320..503
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          539..717
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          224..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           444..447
FT                   /note="DEAH box"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1063 AA;  120970 MW;  2E544C415AC40B03 CRC64;
     MSQTPIKKEE SNDQDDKFEF KKYINEGKLP LKADNPKKKP QLGTIQANQP IPSIFDNLFN
     LFKVINTTYT FLYLRNSLTI TFPLLNSSVK QSLKKELTIG DLSQLREICP QIIELNYKSL
     ASLALEINKN VYTDLNPELY TGSTVSQSSE YVLVIELLET QERSSKRRRR EGPTMKANIQ
     RQKLDFNNLK KAIELRNQKF LQGIKEYIKK CQLTELDPTQ QLLTQSRKNQ PVPPDSPSIP
     NDSIENCNLN TKACSIEELL NEIASESSYE GQIVQEALHT YPAVEAQYGA LSRPLSQELI
     NALYTSRNIE KTYKHQADAI NHLWNGFHVI VSTSTSSGKS LIYQIPILQS LLEDNQSTAF
     FVFPTKSLAQ DQKKSLIDIL SYMPTLKNIR VDTFDGDTPL ESRESIIRSA NIIFTNPDML
     HQTILPNANR WYYFFKNLKL FVLDEAHVYN GIFGVHVAFV LRRMRRIAEY FGNSQYRFVS
     CSATIEDPLQ HMKKIFGVDN IKLINYTSSP SGSKKFVMWN PPYVDPKHPD DGKKSAISEA
     SKLLIKFAEK RVRTIVFCRV RKTCESLMRL VRQELKTKQK GDLLSKIQSY RAGYTVQERR
     KIESEMFNGK LYGIIATNAL ELGIDIGSLD AVITIGFPYS LSNLRQQFGR AGRRNKSSLA
     VYIVETFPVD QFYLKHPILI HTQPNAELTL DLTNEVLLAS HLQCAAYELP INIRSDEKFF
     GNQIQDICEA NLEMVEESYR PHPKYLPFPA SQVRIRSVSE DMFTLVDVTN DKNVILELLE
     PFRVALTAYE GAVYVYQGKT FIIRLLNINK RIITAHQVDV EWSTLQRDFT DVDPVRSLMK
     KTMHGSTNIY FGAVKATLHV FGYFKVNKQK DILDVVDITD HPVEIDSRGF WIDVPWHIIE
     VLSLKKINGA ASIHAAQHAL LSLMPIFISN SGNDIRTECK AGEKEYKEAK SERRRPSRLI
     FYDNCGDSSG AGLCNKAYEH TDELITMAIE RIESCDCKVR EGCPGCITSS KFEGGVCSGE
     VLDKVGALIL LKMLLCQHVN LDIYADGPEI DSYHALRTLI PSC