ID RAD57_YEAST Reviewed; 460 AA.
AC P25301; D6VRZ2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=DNA repair protein RAD57;
GN Name=RAD57; OrderedLocusNames=YDR004W; ORFNames=YD8119.10;
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].
RX PubMed=1937004; DOI=10.1016/0378-1119(91)90527-i;
RA Kans J.A., Mortimer R.K.;
RT "Nucleotide sequence of the RAD57 gene of Saccharomyces cerevisiae.";
RL Gene 105:139-140(1991).
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 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).
CC -!- FUNCTION: Participates in the repair of X-ray-induced damage to DNA and
CC in meiosis. It may act in part by stabilizing a repair complex of other
CC RAD genes.
CC -!- INTERACTION:
CC P25301; Q06032: CST9; NbExp=2; IntAct=EBI-14744, EBI-30044;
CC P25301; P38953: RAD55; NbExp=9; IntAct=EBI-14744, EBI-14737;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
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DR EMBL; M65061; AAA34950.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88064.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11852.1; -; Genomic_DNA.
DR PIR; JQ1275; JQ1275.
DR RefSeq; NP_010287.1; NM_001180312.1.
DR AlphaFoldDB; P25301; -.
DR SMR; P25301; -.
DR BioGRID; 32057; 272.
DR ComplexPortal; CPX-3139; RAD55-RAD57 complex.
DR DIP; DIP-4774N; -.
DR IntAct; P25301; 17.
DR STRING; 4932.YDR004W; -.
DR iPTMnet; P25301; -.
DR PaxDb; 4932-YDR004W; -.
DR PeptideAtlas; P25301; -.
DR EnsemblFungi; YDR004W_mRNA; YDR004W; YDR004W.
DR GeneID; 851567; -.
DR KEGG; sce:YDR004W; -.
DR AGR; SGD:S000002411; -.
DR SGD; S000002411; RAD57.
DR VEuPathDB; FungiDB:YDR004W; -.
DR eggNOG; KOG1564; Eukaryota.
DR GeneTree; ENSGT00930000151053; -.
DR HOGENOM; CLU_045144_0_0_1; -.
DR InParanoid; P25301; -.
DR OMA; ISHHMRV; -.
DR OrthoDB; 1382780at2759; -.
DR BioCyc; YEAST:G3O-29626-MONOMER; -.
DR BioGRID-ORCS; 851567; 0 hits in 10 CRISPR screens.
DR PRO; PR:P25301; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P25301; Protein.
DR GO; GO:0033065; C:Rad51C-XRCC3 complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:SGD.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IPI:SGD.
DR GO; GO:0042148; P:DNA strand invasion; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:ComplexPortal.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IDA:ComplexPortal.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0000707; P:meiotic DNA recombinase assembly; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1903112; P:positive regulation of single-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR CDD; cd19491; XRCC3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR047348; XRCC3-like_C.
DR PANTHER; PTHR22942:SF66; DNA REPAIR PROTEIN RAD57; 1.
DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1.
DR Pfam; PF08423; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..460
FT /note="DNA repair protein RAD57"
FT /id="PRO_0000122956"
FT BINDING 125..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 52247 MW; FCB80C31721AD344 CRC64;
MPRALSIKFD NTYMDLYDEL PESKLLYDEE FSYLLDAVRQ NGVCVVDFLT LTPKELARLI
QRSINEVFRF QQLLVHEYNE KYLEICEKNS ISPDNGPECF TTADVAMDEL LGGGIFTHGI
TEIFGESSTG KSQLLMQLAL SVQLSEPAGG LGGKCVYITT EGDLPTQRLE SMLSSRPAYE
KLGITQSNIF TVSCNDLINQ EHIINVQLPI LLERSKGSIK LVIIDSISHH LRVELQNKSF
RESQENKNYL DRMAEKLQIL AHDYSLSVVV ANQVGDKPLA NSPVAHRTYV TDYDYQLGWL
VGWKNSTILY RQMNSLLGAS SNNDEILSDD EDYMLIERVM STVNDRNYDF FSKKKPPIIE
NKTVERNSSS PISRQSKKRK FDYRVPNLGL TWSNHVSTRI LLQKSFKAST IIQRGEAHLY
KGGDSASFWQ VKRTMKVVYS TFAKPGQIAY QITKRGIETA
//
