SAW1_YEAST
ID SAW1_YEAST Reviewed; 261 AA.
AC P39735; D6VPJ1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Single-strand annealing weakened protein 1;
GN Name=SAW1; OrderedLocusNames=YAL027W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP INTERACTION WITH RAD1 AND RAD10.
RX PubMed=17989249; DOI=10.1101/gr.6667007;
RA Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I.,
RA Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J.,
RA Greenblatt J.F., Giaever G., Nislow C., Stagljar I.;
RT "Examining protein protein interactions using endogenously tagged yeast
RT arrays: the cross-and-capture system.";
RL Genome Res. 17:1774-1782(2007).
RN [7]
RP FUNCTION, INTERACTION WITH RAD1; MSH2; MSH3; RAD51 AND RAD52, AND
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Catalyzes 3'-non-homologous tail removal of RAD1/RAD10-
CC dependent single-strand annealing recombination intermediates. Plays a
CC key role in targeting RAD1/RAD10 complex to 3'-flap cleavage substrate
CC in recombination. Also contributes to the integrity of ribosomal DNA
CC arrays. {ECO:0000269|PubMed:18471978}.
CC -!- SUBUNIT: Interacts with MSH2, MSH3, RAD1, RAD10, RAD51 and RAD52.
CC {ECO:0000269|PubMed:17989249, ECO:0000269|PubMed:18471978}.
CC -!- INTERACTION:
CC P39735; P06777: RAD1; NbExp=4; IntAct=EBI-20627, EBI-14752;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Accumulates recombination intermediates blocked
CC at the RAD1/RAD10-dependent 3' flap cleavage step. Abolishes
CC association of RAD1 at single-strand annealing (SSA) intermediates.
CC Insensitive to MMS, HU, or phleomycin treatment. Doesn't sensitize
CC cells to UV lesions. Substantially increases the rDNA recombination
CC rate. {ECO:0000269|PubMed:18471978}.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U12980; AAC05005.1; -; Genomic_DNA.
DR EMBL; AY692559; AAT92578.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06961.1; -; Genomic_DNA.
DR PIR; S51994; S51994.
DR RefSeq; NP_009375.1; NM_001178172.1.
DR AlphaFoldDB; P39735; -.
DR BioGRID; 31739; 79.
DR ComplexPortal; CPX-1363; SAW1-RAD1-RAD10 endonuclease complex.
DR DIP; DIP-6595N; -.
DR IntAct; P39735; 22.
DR MINT; P39735; -.
DR STRING; 4932.YAL027W; -.
DR MaxQB; P39735; -.
DR PaxDb; P39735; -.
DR PRIDE; P39735; -.
DR TopDownProteomics; P39735; -.
DR EnsemblFungi; YAL027W_mRNA; YAL027W; YAL027W.
DR GeneID; 851206; -.
DR KEGG; sce:YAL027W; -.
DR SGD; S000000025; SAW1.
DR VEuPathDB; FungiDB:YAL027W; -.
DR eggNOG; ENOG502S0N2; Eukaryota.
DR HOGENOM; CLU_091781_0_0_1; -.
DR InParanoid; P39735; -.
DR OMA; KFKYKLH; -.
DR BioCyc; YEAST:G3O-28838-MON; -.
DR PRO; PR:P39735; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39735; protein.
DR GO; GO:1905348; C:endonuclease complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070337; F:3'-flap-structured DNA binding; IDA:SGD.
DR GO; GO:0070338; F:5'-flap-structured DNA binding; IDA:SGD.
DR GO; GO:0000736; P:double-strand break repair via single-strand annealing, removal of nonhomologous ends; IMP:SGD.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IDA:SGD.
DR InterPro; IPR021624; Saw1.
DR Pfam; PF11561; Saw1; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..261
FT /note="Single-strand annealing weakened protein 1"
FT /id="PRO_0000202414"
SQ SEQUENCE 261 AA; 29770 MW; F525EF2E5347E500 CRC64;
MAPSIATVKI ARDMVLPLRI FVNRKQILQT NDKTSNKSNA TIFEAPLLSN NSIICLKSPN
TRIYLSQQDK KNLCDEIKED LLLIVYELAS PEIISSVLSK IRVGHSTDFQ INVLPKLFAG
ADTDNAVTSH IQSVTRLAKF KYKLHYKHKW ELDIFINSIK KIANLRHYLM FQTLTLNGFS
LNAGPKTLLA RKIEKQPQVP NLLIENGDAD ALDTPVEEDI KPVIEFMYKP VINLGEIIDV
HVLHRPRRHK VRTQSKQPQE E