RAD51_YEAST
ID RAD51_YEAST Reviewed; 400 AA.
AC P25454; D3DM03;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=DNA repair protein RAD51;
GN Name=RAD51; OrderedLocusNames=YER095W;
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=1620128; DOI=10.1128/mcb.12.7.3235-3246.1992;
RA Basile G.M., Aker M., Mortimer R.K.;
RT "Nucleotide sequence and transcriptional regulation of the yeast
RT recombinational repair gene RAD51.";
RL Mol. Cell. Biol. 12:3235-3246(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1620127; DOI=10.1128/mcb.12.7.3224-3234.1992;
RA Aboussekhra A., Chanet R., Adjiri A., Fabre F.;
RT "Semidominant suppressors of Srs2 helicase mutations of Saccharomyces
RT cerevisiae map in the RAD51 gene, whose sequence predicts a protein with
RT similarities to procaryotic RecA proteins.";
RL Mol. Cell. Biol. 12:3224-3234(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1581961; DOI=10.1016/0092-8674(92)90447-k;
RA Shinohara A., Ogawa H., Ogawa T.;
RT "Rad51 protein involved in repair and recombination in S. cerevisiae is a
RT RecA-like protein.";
RL Cell 69:457-470(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
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 [6]
RP INTERACTION WITH RAD54.
RX PubMed=9590697; DOI=10.1038/30037;
RA Petukhova G., Stratton S., Sung P.;
RT "Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins.";
RL Nature 393:91-94(1998).
RN [7]
RP INTERACTION WITH RDH54.
RX PubMed=10970884; DOI=10.1101/gad.826100;
RA Petukhova G., Sung P., Klein H.;
RT "Promotion of Rad51-dependent D-loop formation by yeast recombination
RT factor Rdh54/Tid1.";
RL Genes Dev. 14:2206-2215(2000).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAD51.
RX PubMed=16818607; DOI=10.1101/gad.1422506;
RA Tsubouchi H., Roeder G.S.;
RT "Budding yeast Hed1 down-regulates the mitotic recombination machinery when
RT meiotic recombination is impaired.";
RL Genes Dev. 20:1766-1775(2006).
RN [10]
RP INTERACTION WITH SAW1.
RX PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
RA Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
RT "Microarray-based genetic screen defines SAW1, a gene required for
RT Rad1/Rad10-dependent processing of recombination intermediates.";
RL Mol. Cell 30:325-335(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 81-400.
RX PubMed=15235592; DOI=10.1038/nsmb795;
RA Conway A.B., Lynch T.W., Zhang Y., Fortin G.S., Fung C.W., Symington L.S.,
RA Rice P.A.;
RT "Crystal structure of a Rad51 filament.";
RL Nat. Struct. Mol. Biol. 11:791-796(2004).
CC -!- FUNCTION: Required both for recombination and for the repair of DNA
CC damage caused by X-rays. Its function may be modulated by interaction
CC with other repair proteins. RAD52 interacts directly with RAD51, via
CC its C-terminus. Forms a nucleoprotein filament with DNA as an early
CC intermediate in recombination. {ECO:0000269|PubMed:16818607}.
CC -!- SUBUNIT: Part of a repair/recombination complex that includes RAD51,
CC RAD52 and RAD54. Interacts with HED1, RDH54 and SAW1.
CC {ECO:0000269|PubMed:10970884, ECO:0000269|PubMed:16818607,
CC ECO:0000269|PubMed:18471978, ECO:0000269|PubMed:9590697}.
CC -!- INTERACTION:
CC P25454; P25454: RAD51; NbExp=3; IntAct=EBI-14709, EBI-14709;
CC P25454; P06778: RAD52; NbExp=9; IntAct=EBI-14709, EBI-14719;
CC P25454; P32863: RAD54; NbExp=2; IntAct=EBI-14709, EBI-14728;
CC P25454; P38953: RAD55; NbExp=6; IntAct=EBI-14709, EBI-14737;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16818607}. Chromosome
CC {ECO:0000269|PubMed:16818607}. Note=Localizes as foci on meiotic
CC chromosomes.
CC -!- DEVELOPMENTAL STAGE: RAD51 is cell cycle regulated, peaking around the
CC G1-to-S transition.
CC -!- INDUCTION: By X-rays.
CC -!- MISCELLANEOUS: Present with 6960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; X64270; CAA45563.1; -; Genomic_DNA.
DR EMBL; M88470; AAA34948.1; -; Genomic_DNA.
DR EMBL; D10023; BAA00913.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64650.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07757.1; -; Genomic_DNA.
DR PIR; A44348; A44348.
DR RefSeq; NP_011021.3; NM_001178986.3.
DR PDB; 1SZP; X-ray; 3.25 A; A/B/C/D/E/F=81-400.
DR PDB; 3LDA; X-ray; 2.50 A; A=1-400.
DR PDBsum; 1SZP; -.
DR PDBsum; 3LDA; -.
DR AlphaFoldDB; P25454; -.
DR SMR; P25454; -.
DR BioGRID; 36841; 533.
DR DIP; DIP-195N; -.
DR IntAct; P25454; 45.
DR MINT; P25454; -.
DR STRING; 4932.YER095W; -.
DR iPTMnet; P25454; -.
DR MaxQB; P25454; -.
DR PaxDb; P25454; -.
DR PRIDE; P25454; -.
DR EnsemblFungi; YER095W_mRNA; YER095W; YER095W.
DR GeneID; 856831; -.
DR KEGG; sce:YER095W; -.
DR SGD; S000000897; RAD51.
DR VEuPathDB; FungiDB:YER095W; -.
DR eggNOG; KOG1433; Eukaryota.
DR GeneTree; ENSGT00940000156157; -.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; P25454; -.
DR OMA; TFRIYLR; -.
DR BioCyc; YEAST:G3O-30262-MON; -.
DR Reactome; R-SCE-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR EvolutionaryTrace; P25454; -.
DR PRO; PR:P25454; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P25454; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0000150; F:DNA strand exchange activity; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IDA:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:BHF-UCL.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0000709; P:meiotic joint molecule formation; IMP:SGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0042148; P:strand invasion; IDA:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:SGD.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; DNA damage; DNA recombination;
KW DNA repair; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..400
FT /note="DNA repair protein RAD51"
FT /id="PRO_0000122925"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3LDA"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 212..222
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 296..317
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:3LDA"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:3LDA"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3LDA"
SQ SEQUENCE 400 AA; 42963 MW; 66561B60122A39A2 CRC64;
MSQVQEQHIS ESQLQYGNGS LMSTVPADLS QSVVDGNGNG SSEDIEATNG SGDGGGLQEQ
AEAQGEMEDE AYDEAALGSF VPIEKLQVNG ITMADVKKLR ESGLHTAEAV AYAPRKDLLE
IKGISEAKAD KLLNEAARLV PMGFVTAADF HMRRSELICL TTGSKNLDTL LGGGVETGSI
TELFGEFRTG KSQLCHTLAV TCQIPLDIGG GEGKCLYIDT EGTFRPVRLV SIAQRFGLDP
DDALNNVAYA RAYNADHQLR LLDAAAQMMS ESRFSLIVVD SVMALYRTDF SGRGELSARQ
MHLAKFMRAL QRLADQFGVA VVVTNQVVAQ VDGGMAFNPD PKKPIGGNIM AHSSTTRLGF
KKGKGCQRLC KVVDSPCLPE AECVFAIYED GVGDPREEDE
