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Database: UniProt
Entry: O13983
LinkDB: O13983
Original site: O13983 
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   16-OCT-2019, entry version 127.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, 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
CC       duplex DNA up to 120-bp and requires a long 3'-tail of at least 70
CC       nucleotides for efficient unwinding of duplex DNA (By similarity).
CC       Shows both processive helicase and DNA strand annealing activities
CC       (By similarity). Affects telomere length by a non-catalytic
CC       mechanism, probably through inhibiting telomerase by competing
CC       with it for ssDNA binding (By similarity).
CC       {ECO:0000250|UniProtKB:Q05549, 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
CC       rhp14 (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
CC       response to both chronic and acute exposures.
CC       {ECO:0000269|PubMed:22064477}.
CC   -!- SIMILARITY: Belongs to the helicase family. HRQ1 subfamily.
CC       {ECO:0000305}.
DR   EMBL; CU329670; CAA16993.2; -; Genomic_DNA.
DR   RefSeq; NP_594448.2; NM_001019877.2.
DR   BioGrid; 278518; 160.
DR   STRING; 4896.SPAC23A1.19c.1; -.
DR   iPTMnet; O13983; -.
DR   MaxQB; O13983; -.
DR   PaxDb; O13983; -.
DR   PRIDE; O13983; -.
DR   EnsemblFungi; SPAC23A1.19c.1; SPAC23A1.19c.1:pep; SPAC23A1.19c.
DR   GeneID; 2542036; -.
DR   KEGG; spo:SPAC23A1.19c; -.
DR   EuPathDB; FungiDB:SPAC23A1.19c; -.
DR   PomBase; SPAC23A1.19c; hrq1.
DR   HOGENOM; HOG000163591; -.
DR   InParanoid; O13983; -.
DR   KO; K06877; -.
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:0000405; F:bubble DNA binding; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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   InterPro; IPR014939; CDT1_Gemini-bd-like.
DR   InterPro; IPR018973; DEAD/DEAH-box_helicase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN         1   1063       ATP-dependent helicase hrq1.
FT                                /FTId=PRO_0000353818.
FT   DOMAIN      320    503       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      539    717       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     333    340       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       444    447       DEAH box.
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
//
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