HUS2_SCHPO
ID HUS2_SCHPO Reviewed; 1328 AA.
AC Q09811;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ATP-dependent DNA helicase hus2/rqh1;
DE EC=3.6.4.12;
GN Name=rqh1; Synonyms=hus2, rad12, rec9; ORFNames=SPAC2G11.12;
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 [GENOMIC DNA].
RX PubMed=9184215; DOI=10.1093/emboj/16.10.2682;
RA Stewart E.C., Chapman C.R., Al-Khodairy F., Carr A.M., Enoch T.;
RT "rqh1+, a fission yeast gene related to the Bloom's and Werner's syndrome
RT genes, is required for reversible S phase arrest.";
RL EMBO J. 16:2682-2692(1997).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH TOP3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-543.
RX PubMed=12724426; DOI=10.1128/mcb.23.10.3692-3705.2003;
RA Laursen L.V., Ampatzidou E., Andersen A.H., Murray J.M.;
RT "Role for the fission yeast RecQ helicase in DNA repair in G2.";
RL Mol. Cell. Biol. 23:3692-3705(2003).
CC -!- FUNCTION: Has a role in the repair of UV-induced DNA damage in G2 via
CC recombination-mediated repair. Also has a role in the repair of
CC infrared-induced double DNA strand breaks. Exhibits an ATP-dependent
CC DNA-helicase activity that unwinds single- and double-stranded DNA in a
CC 3'-5' direction. {ECO:0000269|PubMed:12724426}.
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 -!- SUBUNIT: Interacts with top3. {ECO:0000269|PubMed:12724426}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12724426}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; Y09426; CAA70577.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91177.1; -; Genomic_DNA.
DR PIR; S62467; S62467.
DR RefSeq; NP_593092.1; NM_001018490.2.
DR AlphaFoldDB; Q09811; -.
DR SMR; Q09811; -.
DR BioGRID; 278117; 105.
DR DIP; DIP-61056N; -.
DR IntAct; Q09811; 1.
DR STRING; 4896.SPAC2G11.12.1; -.
DR iPTMnet; Q09811; -.
DR MaxQB; Q09811; -.
DR PaxDb; Q09811; -.
DR PRIDE; Q09811; -.
DR EnsemblFungi; SPAC2G11.12.1; SPAC2G11.12.1:pep; SPAC2G11.12.
DR GeneID; 2541620; -.
DR KEGG; spo:SPAC2G11.12; -.
DR PomBase; SPAC2G11.12; rqh1.
DR VEuPathDB; FungiDB:SPAC2G11.12; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_22_3_1; -.
DR InParanoid; Q09811; -.
DR OMA; GCDICCE; -.
DR PhylomeDB; Q09811; -.
DR PRO; PR:Q09811; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; 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; IC:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; TAS:PomBase.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:PomBase.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IDA:PomBase.
DR GO; GO:0006301; P:postreplication repair; IMP:PomBase.
DR GO; GO:0000725; P:recombinational repair; IGI:PomBase.
DR GO; GO:1903221; P:regulation of mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IGI:PomBase.
DR GO; GO:0071140; P:resolution of mitotic recombination intermediates; IMP:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 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..1328
FT /note="ATP-dependent DNA helicase hus2/rqh1"
FT /id="PRO_0000205058"
FT DOMAIN 528..707
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 728..876
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1115..1195
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 217..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 651..654
FT /note="DEAH box"
FT COMPBIAS 219..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1295
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 543
FT /note="T->I: Loss of helicase activity."
FT /evidence="ECO:0000269|PubMed:12724426"
SQ SEQUENCE 1328 AA; 149646 MW; 13A9A5B94E5A9BD1 CRC64;
MTVTKTNLNR HLDWFFRESP QKIENVTSPI KTLDFVKVKV SSSDIVVKDS IPHKSKNVFD
DFDDGYAIDL TEEHQSSSLN NLKWKDVEGP NILKPIKKIA VPASESEEDF DDVDEEMLRA
AEMEVFQSCQ PLAVNTADTT VSHSTSSSNV PRSLNKIHDP SRFIKDNDVE NRIHVSSASK
VASISNTSKP NPIVSENPIS ATSVSIEIPI KPKELSNNLP FPRLNNNNTN NNNDNNAIEK
RDSASPTPSS VSSQISIDFS TWPHQNLLQY LDILRDEKSE ISDRIIEVME RYPFSSRFKE
WIPKRDILSQ KISSVLEVLS NNNNSNNNNG NNGTVPNAKT FFTPPSSITQ QVPFPSTIIP
ESTVKENSTR PYVNSHLVAN DKITATPFHS EAVVSPLQSN IRNSDIAEFD EFDIDDADFT
FNTTDPINDE SGASSDVVVI DDEEDDIENR PLNQALKASK AAVSNASLLQ SSSLDRPLLG
EMKDKNHKVL MPSLDDPMLS YPWSKEVLGC LKHKFHLKGF RKNQLEAING TLSGKDVFIL
MPTGGGKSLC YQLPAVIEGG ASRGVTLVIS PLLSLMQDQL DHLRKLNIPS LPLSGEQPAD
ERRQVISFLM AKNVLVKLLY VTPEGLASNG AITRVLKSLY ERKLLARIVI DEAHCVSHWG
HDFRPDYKQL GLLRDRYQGI PFMALTATAN EIVKKDIINT LRMENCLELK SSFNRPNLFY
EIKPKKDLYT ELYRFISNGH LHESGIIYCL SRTSCEQVAA KLRNDYGLKA WHYHAGLEKV
ERQRIQNEWQ SGSYKIIVAT IAFGMGVDKG DVRFVIHHSF PKSLEGYYQE TGRAGRDGKP
AHCIMFYSYK DHVTFQKLIM SGDGDAETKE RQRQMLRQVI QFCENKTDCR RKQVLAYFGE
NFDKVHCRKG CDICCEEATY IKQDMTEFSL QAIKLLKSIS GKATLLQLMD IFRGSKSAKI
VENGWDRLEG AGVGKLLNRG DSERLFHHLV SEGVFVEKVE ANRRGFVSAY VVPGRQTIIN
SVLAGKRRII LDVKESSSKP DTSSRSLSRS KTLPALREYQ LKSTTASVDC SIGTREVDEI
YDSQMPPVKP SLIHSRNKID LEELSGQKFM SEYEIDVMTR CLKDLKLLRS NLMAIDDSRV
SSYFTDSVLL SMAKKLPRNV KELKEIHGVS NEKAVNLGPK FLQVIQKFID EKEQNLEGTE
LDPSLQSLDT DYPIDTNALS LDHEQGFSDD SDSVYEPSSP IEEGDEEVDG QRKDILNFMN
SQSLTQTGSV PKRKSTSYTR PSKSYRHKRG STSYSRKRKY STSQKDSRKT SKSANTSFIH
PMVKQNYR
