SRS2_YEAST
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 03-AUG-2022, entry version 184.
DE RecName: Full=ATP-dependent DNA helicase SRS2;
DE EC=3.6.4.12;
GN Name=SRS2; Synonyms=HPR5, RADH; OrderedLocusNames=YJL092W; 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=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 -!- 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}.
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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 PDBsum; 3V62; -.
DR AlphaFoldDB; P12954; -.
DR SMR; P12954; -.
DR BioGRID; 33665; 596.
DR DIP; DIP-415N; -.
DR IntAct; P12954; 22.
DR MINT; P12954; -.
DR STRING; 4932.YJL092W; -.
DR iPTMnet; P12954; -.
DR MaxQB; P12954; -.
DR PaxDb; P12954; -.
DR PRIDE; P12954; -.
DR EnsemblFungi; YJL092W_mRNA; YJL092W; YJL092W.
DR GeneID; 853353; -.
DR KEGG; sce:YJL092W; -.
DR SGD; S000003628; SRS2.
DR VEuPathDB; FungiDB:YJL092W; -.
DR eggNOG; KOG2108; Eukaryota.
DR GeneTree; ENSGT00390000011669; -.
DR HOGENOM; CLU_004585_4_0_1; -.
DR InParanoid; P12954; -.
DR OMA; FFVAQTR; -.
DR BioCyc; YEAST:G3O-31547-MON; -.
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: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:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; 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:0006303; P:double-strand break repair via nonhomologous end joining; IDA: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:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; 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 938..961
FT /note="Polar residues"
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
