RAD52_CANGA
ID RAD52_CANGA Reviewed; 505 AA.
AC Q6FSW2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=DNA repair and recombination protein RAD52;
GN Name=RAD52; OrderedLocusNames=CAGL0G07381g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair and
CC recombination. Promotes the annealing of complementary single-stranded
CC DNA and by stimulation of the RAD51 recombinase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of a complex that includes RAD51, RAD52 and RAD59.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR EMBL; CR380953; CAG59609.1; -; Genomic_DNA.
DR RefSeq; XP_446682.1; XM_446682.1.
DR AlphaFoldDB; Q6FSW2; -.
DR SMR; Q6FSW2; -.
DR STRING; 5478.XP_446682.1; -.
DR EnsemblFungi; CAG59609; CAG59609; CAGL0G07381g.
DR GeneID; 2888225; -.
DR KEGG; cgr:CAGL0G07381g; -.
DR CGD; CAL0130821; CAGL0G07381g.
DR VEuPathDB; FungiDB:CAGL0G07381g; -.
DR eggNOG; KOG4141; Eukaryota.
DR HOGENOM; CLU_011431_3_2_1; -.
DR InParanoid; Q6FSW2; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0000228; C:nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:EnsemblFungi.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IEA:EnsemblFungi.
DR GO; GO:0006277; P:DNA amplification; IEA:EnsemblFungi.
DR GO; GO:0000730; P:DNA recombinase assembly; IEA:EnsemblFungi.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IEA:EnsemblFungi.
DR GO; GO:0000709; P:meiotic joint molecule formation; IEA:EnsemblFungi.
DR GO; GO:0043504; P:mitochondrial DNA repair; IEA:EnsemblFungi.
DR GO; GO:1904877; P:positive regulation of DNA ligase activity; IEA:EnsemblFungi.
DR GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR Gene3D; 3.30.390.80; -; 1.
DR InterPro; IPR004585; DNA_recomb/repair_Rad52.
DR InterPro; IPR041247; Rad52_fam.
DR InterPro; IPR007232; Rad52_Rad59_Rad22.
DR InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR PANTHER; PTHR12132; PTHR12132; 1.
DR Pfam; PF04098; Rad52_Rad22; 1.
DR TIGRFAMs; TIGR00607; rad52; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..505
FT /note="DNA repair and recombination protein RAD52"
FT /id="PRO_0000173885"
FT DNA_BIND 130..134
FT /evidence="ECO:0000250"
FT REGION 178..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 56143 MW; BC9EC893C789B82F CRC64;
MVKEEEKDKV HFNHDDIQQK LDKKLGPEYI SKRIGFGSSR VAYIEGWRAI NLANQIFGYN
GWSTEVKNII VDFLDERQGK FSIGCTAIVR VSLADGTYRE DIGYGAVENE RRKPAAFERA
KKSAVTDALK RCLRGFGNAL GNCLYDKEFL SRIDKVKFDP PDFDEGNLFR PSDEISEYSR
SNTIDNDNPA VKRQKLNNQN SIPDTNKVKY NGSAPAPAIT YNNAPKKPVQ SEERYAPNGS
RGKENAQNKS ENEDLLDDSF MFSDDLQDDE LISLMNKNSS DPDRRFNNAP KENTGDITFV
TARAADSYQS TENVPENLKF DPKYVPHSMK LTIDQNTSKH IPLSVLKEKG VTATSREAIY
SRFAAKGKQI PNPIDDSTDS RLAENDKSNE NDDTETSHST EIEKSAISSV NNGTNISGST
ESSVTTVPSH NSTSQTTNIE AKVDKADSQV SEKQSQKGIK YAPQVPVVHP NTSAAIPLNQ
NKPLRREVGR PKINNVGPKK PSPTP