ID   SRS2_YEAST              Reviewed;        1174 AA.
AC   P12954; D6VW92;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   02-SEP-2026, entry version 203.
DE   RecName: Full=ATP-dependent DNA helicase SRS2;
DE            EC=5.6.2.4;
DE   AltName: Full=DNA 3'-5' helicase SRS2 {ECO:0000305};
GN   Name=SRS2; Synonyms=HPR5, RADH; OrderedLocusNames=YJL092W;
GN   ORFNames=J0913;
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 [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=2552405; DOI=10.1093/nar/17.18.7211;
RA   Aboussekhra A., Chanet R., Zgaga Z., Cassier-Chauvat C., Heude M.,
RA   Fabre C.L.;
RT   "RADH, a gene of Saccharomyces cerevisiae encoding a putative DNA helicase
RT   involved in DNA repair. Characteristics of radH mutants and sequence of the
RT   gene.";
RL   Nucleic Acids Res. 17:7211-7219(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7985424; DOI=10.1002/yea.320100712;
RA   Miosga T., Witzel A., Zimmermann F.K.;
RT   "Sequence and function analysis of a 9.46 kb fragment of Saccharomyces
RT   cerevisiae chromosome X.";
RL   Yeast 10:965-973(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=8419328; DOI=10.1016/s0021-9258(18)54067-9;
RA   Rong L., Klein H.L.;
RT   "Purification and characterization of the SRS2 DNA helicase of the yeast
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 268:1252-1259(1993).
RN   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA repair at least
CC       for UV-induced lesions. The polarity of the helicase activity was
CC       determined to be 3' to 5'.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC   -!- INTERACTION:
CC       P12954; P39009: DUN1; NbExp=3; IntAct=EBI-18110, EBI-6194;
CC       P12954; Q06148: NEJ1; NbExp=3; IntAct=EBI-18110, EBI-34047;
CC       P12954; P15873: POL30; NbExp=10; IntAct=EBI-18110, EBI-12993;
CC       P12954; P38953: RAD55; NbExp=4; IntAct=EBI-18110, EBI-14737;
CC       P12954; Q12306: SMT3; NbExp=4; IntAct=EBI-18110, EBI-17490;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 5190 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X15665; CAA33706.1; -; Genomic_DNA.
DR   EMBL; X77087; CAA54361.1; -; Genomic_DNA.
DR   EMBL; Z49367; CAA89385.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08708.1; -; Genomic_DNA.
DR   PIR; S46586; HJBYDH.
DR   RefSeq; NP_012443.1; NM_001181525.1.
DR   PDB; 3V62; X-ray; 2.90 A; C/F=1107-1174.
DR   AlphaFoldDB; P12954; -.
DR   SMR; P12954; -.
DR   BioGRID; 33665; 607.
DR   DIP; DIP-415N; -.
DR   FunCoup; P12954; 350.
DR   IntAct; P12954; 22.
DR   MINT; P12954; -.
DR   STRING; 4932.YJL092W; -.
DR   iPTMnet; P12954; -.
DR   PaxDb; 4932-YJL092W; -.
DR   PeptideAtlas; P12954; -.
DR   EnsemblFungi; YJL092W_mRNA; YJL092W; YJL092W.
DR   GeneID; 853353; -.
DR   KEGG; sce:YJL092W; -.
DR   AGR; SGD:S000003628; -.
DR   SGD; S000003628; SRS2.
DR   VEuPathDB; FungiDB:YJL092W; -.
DR   eggNOG; KOG2108; Eukaryota.
DR   HOGENOM; CLU_004585_4_0_1; -.
DR   InParanoid; P12954; -.
DR   OMA; FFVAQTR; -.
DR   OrthoDB; 1470711at2759; -.
DR   BioCyc; YEAST:G3O-31547-MONOMER; -.
DR   BioGRID-ORCS; 853353; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P12954; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P12954; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR   GO; GO:0042262; P:DNA protection; IMP:SGD.
DR   GO; GO:1990986; P:DNA recombinase disassembly; IDA:SGD.
DR   GO; GO:0006281; P:DNA repair; IGI:SGD.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:SGD.
DR   GO; GO:0007127; P:meiosis I; IMP:SGD.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:SGD.
DR   GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   CDD; cd22877; Srs2_C; 1.
DR   FunFam; 3.40.50.300:FF:001201; ATP-dependent DNA helicase UvrD2; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 1.10.486.10; PCRA, domain 4; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000212; UvrD-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR014017; UvrD-like_C.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
DR   PDBsum; 3V62; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Isomerase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1174
FT                   /note="ATP-dependent DNA helicase SRS2"
FT                   /id="PRO_0000102071"
FT   DOMAIN          14..316
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          317..654
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   REGION          222..243
FT                   /note="Leucine-zipper"
FT   REGION          676..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        909..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1023
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         833
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        173..182
FT                   /note="IKKQISKLKS -> TQETDIKAKI (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        534..548
FT                   /note="YEYLYKDGKKKNDQL -> VRILGTRMVRKKMSQF (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1152..1160
FT                   /evidence="ECO:0007829|PDB:3V62"
FT   STRAND          1170..1172
FT                   /evidence="ECO:0007829|PDB:3V62"
SQ   SEQUENCE   1174 AA;  134306 MW;  AE8061B114C32120 CRC64;
     MSSNNDLWLH LVSQLNTQQR AAALFDYTRG LQVIAGPGTG KTKVLTSRVA YLILHHHIHP
     RDIIVTTFTN KAANEMKERL QEMLRGAGVN ISELLIGTFH SICLKILYRF GHLVDLQKDW
     RIIDEKEIDV ILDDMIEKVP DQIRDYASSI TRKVNLCMPS KNGDEWTIHP KLIKKQISKL
     KSNAILPEEY ILDSNHDAAL GYFYQIYQSE LSKKNTLDFD DLLMYTFRLL TRVRVLSNIK
     HVLVDEFQDT NGIQLDLMFL FAKGNHHLSR GMTIVGDPDQ SIYAFRNALA HNFLEMGRKC
     PIEYSTIILV ENYRSSQKIL NTSEILITQQ NKGRQNRAPL RAQFDLDFPP VYMNFPAYFL
     EAPSLVRELL YLKALPNLFT FNDFAILVRQ RRQIKRIESA LIEHRIPYKI IRGHSFWDSK
     ETRAMLNLLK LIFSPNDKHA ILASLLYPAR GLGPATGEKI KNALDTLATD VSCFQILKDI
     SSKKIMLDIP TKGRSVIADF ISMIENCQLL LQSTLLGGLS DLFDKLYELS GLKYEYLYKD
     GKKKNDQLEK SEPNLLNARH KNIELLKNYF LALLSKSESS DKEKNEAIKA ATDEAEPIEN
     KVITPKEYLR NFFNSLSLHS DAAEEEESES NKDAKIKREK NGFVTISTIH GAKGLEWPVV
     FIPGCEEGII PCVFNDDKKD ESEEDEEEDQ ENSKKDASPK KTRVLSVEDS IDEERRMFFV
     AQTRAKYLLY LSNTVTVEDV DRPRIASRFL TTDLIKAMSD SQKLFESTNS IKKLYRILNK
     KPPAEDDKLF SLDQLRKDYN QFIENRRERM IWQGIQMNDV YGIQLSRNKL LGSVSDFTSA
     ADQLRLETQN SIFPQKKLIE KSRPSKINGN YAPKSRVKSP EKRYAPETTS FHSPTKKKVY
     APQYVSTTNV PSRQEFHSST GKNIPFLRRE DRSITDISPR SSTRSLKGAS PNKTSHMSDD
     LMRPSPTRKD KVTRNIHFAT AGTFRIETQS NVDELHPPEY SNKSGQSLTS SEFSGFSSAC
     SNSDQPTNLI EDINNELDLS DEELLNDISI ERRRELLGSK KTKKIKPKTR NRKSKRGDKV
     KVEEVIDLKS EFEEDDSRNT TAAELLHNPD DTTVDNRPII SNAKFLADAA MKKTQKFSKK
     VKNEPASSQM DIFSQLSRAK KKSKLNNGEI IVID
//