XRS2_YEAST
ID XRS2_YEAST Reviewed; 854 AA.
AC P33301; D6VT00;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=DNA repair protein XRS2;
GN Name=XRS2; OrderedLocusNames=YDR369C; ORFNames=D9481.13;
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=EI303;
RX PubMed=8164689; DOI=10.1128/mcb.14.5.3414-3425.1994;
RA Ivanov E.L., Sugawara N., White C.I., Fabre F., Haber J.E.;
RT "Mutations in XRS2 and RAD50 delay but do not prevent mating-type switching
RT in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 14:3414-3425(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 509-854.
RC STRAIN=M5;
RA Miosga T., Juhnke H., Sterkel C., Zimmermann F.K.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION.
RX PubMed=1468624; DOI=10.1093/genetics/132.3.651;
RA Ivanov E.L., Korolev V.G., Fabre F.;
RT "XRS2, a DNA repair gene of Saccharomyces cerevisiae, is needed for meiotic
RT recombination.";
RL Genetics 132:651-664(1992).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-533 AND SER-534, AND
RP IDENTIFICATION BY 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-553 AND THR-555, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: During meiosis is involved in homologous recombination and
CC during vegetative growth it is necessary for DNA repair. It probably
CC regulates the 5'-3' exonuclease degradation of double strand breaks
CC either at the initiation stage or a later stage.
CC -!- INTERACTION:
CC P33301; P32829: MRE11; NbExp=19; IntAct=EBI-20599, EBI-11255;
CC P33301; P46946: SAE2; NbExp=3; IntAct=EBI-20599, EBI-16440;
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L22856; AAA35220.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64805.1; -; Genomic_DNA.
DR EMBL; X80642; CAA56687.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12210.1; -; Genomic_DNA.
DR PIR; S61164; S61164.
DR RefSeq; NP_010657.3; NM_001180677.3.
DR AlphaFoldDB; P33301; -.
DR BioGRID; 32428; 373.
DR ComplexPortal; CPX-1872; MRE11-RAD50-XRS2 meiotic recombination initiation complex.
DR DIP; DIP-2420N; -.
DR IntAct; P33301; 17.
DR MINT; P33301; -.
DR STRING; 4932.YDR369C; -.
DR iPTMnet; P33301; -.
DR MaxQB; P33301; -.
DR PaxDb; P33301; -.
DR PRIDE; P33301; -.
DR EnsemblFungi; YDR369C_mRNA; YDR369C; YDR369C.
DR GeneID; 851975; -.
DR KEGG; sce:YDR369C; -.
DR SGD; S000002777; XRS2.
DR VEuPathDB; FungiDB:YDR369C; -.
DR eggNOG; ENOG502QU0B; Eukaryota.
DR HOGENOM; CLU_017587_0_0_1; -.
DR InParanoid; P33301; -.
DR OMA; MWILRYQ; -.
DR BioCyc; YEAST:G3O-29919-MON; -.
DR PRO; PR:P33301; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33301; protein.
DR GO; GO:0030870; C:Mre11 complex; IPI:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IC:ComplexPortal.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Meiosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..854
FT /note="DNA repair protein XRS2"
FT /id="PRO_0000066050"
FT REGION 429..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 854 AA; 96365 MW; 833DAD6D20F6693E CRC64;
MWVVRYQNTL EDGSISFISC CLQAFKTYSI GRSSKNPLII KNDKSISRQH ITFKWEINNS
SDLKHSSLCL VNKGKLTSLN KKFMKVGETF TINASDVLKS TIIELGTTPI RIEFEWINEV
WNIPPHLTQF RTMLSEYGIS TEISINDIPA NLMISDYPKS EDNSIRELYA LVSTIPMKKS
RFLMELCNTL LPTSKTNLKF DEMWNDMISN PEYNVFDFDP NILLSKFMRL NNIRVLTTIK
SEPRLSSLLR TFNINLFAFD NIDSLYKYVD SLEASTEYLI LTTTDKKENG KILCTIKTML
TSIIDGTLSA VINMKGASSR TLDNGKFDQI SEGMSTILKT SRAPEVEASP VVSKKRKLNR
RRVLPLDSLD FFAGGLSTKT LSENRSLTDA KRLNCGAESK TVISSPNIAE ADEKHAPFLQ
NALKPTEDIG KKSGHSSPGA IIVSSPNLGT VNTSEDSLDK SLQSHKLPQP SLPEVAGIGS
QTISSNSADY ETAAVNSMDD AEVTKNFRVN HHQNIEQPSK NIRKLSNYSR EISSPLQENC
KSPVKELSIK EKSGTPHAFV EAIQETKNRE VKRVKSTIVE LKDEELSEEA INQLKNLAIV
EPSNNLLRKS FDSEGNKTSR TTEKWENSLM EPEWHKRKNF KTFVKVRPKS KAHKEEGKNN
TQSSDFIRNA AFLITRNYVP LKKYSKKDTT TKWGTEENED MFALTEMERF GSNTFMSDNI
NSNTIQKRSQ ALNRFTNEDS SNEGEEDSFS FSRCSGTAAS VQPLKNKIFI TDEDDLGDID
DKSDRLNHRE NNRNLFVVKE MNLRPNLSEE CSKQSRHSRS ATSRSRGSFG ASNNGDGDDD
DDDGPKFTFK RRKG
