CSM2_YEAST
ID CSM2_YEAST Reviewed; 213 AA.
AC P40465; D6VVF5; Q45U15;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chromosome segregation in meiosis protein 2;
GN Name=CSM2; OrderedLocusNames=YIL132C;
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=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 FUNCTION.
RX PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3;
RA Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E.,
RA Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E.,
RA Klein F., Knop M., Nasmyth K.;
RT "A screen for genes required for meiosis and spore formation based on
RT whole-genome expression.";
RL Curr. Biol. 11:1001-1009(2001).
RN [5]
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 [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 FUNCTION.
RX PubMed=12972632; DOI=10.1073/pnas.2035018100;
RA Huang M.-E., Rio A.-G., Nicolas A., Kolodner R.D.;
RT "A genomewide screen in Saccharomyces cerevisiae for genes that suppress
RT the accumulation of mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11529-11534(2003).
RN [8]
RP FUNCTION.
RX PubMed=15184655; DOI=10.1073/pnas.0403093101;
RA Smith S., Hwang J.-Y., Banerjee S., Majeed A., Gupta A., Myung K.;
RT "Mutator genes for suppression of gross chromosomal rearrangements
RT identified by a genome-wide screening in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9039-9044(2004).
RN [9]
RP IDENTIFICATION IN THE SHU COMPLEX, AND FUNCTION.
RX PubMed=15654096; DOI=10.1534/genetics.104.036764;
RA Shor E., Weinstein J., Rothstein R.;
RT "A genetic screen for top3 suppressors in Saccharomyces cerevisiae
RT identifies SHU1, SHU2, PSY3 and CSM2: four genes involved in error-free DNA
RT repair.";
RL Genetics 169:1275-1289(2005).
RN [10]
RP IDENTIFICATION IN THE SHU COMPLEX, AND FUNCTION.
RX PubMed=19496932; DOI=10.1111/j.1365-2958.2009.06748.x;
RA Ball L.G., Zhang K., Cobb J.A., Boone C., Xiao W.;
RT "The yeast Shu complex couples error-free post-replication repair to
RT homologous recombination.";
RL Mol. Microbiol. 73:89-102(2009).
CC -!- FUNCTION: Involved in chromosome segregation during meiosis. Promotes
CC efficient recombinational repair and functions in the protection of the
CC genome from spontaneous and induced DNA damage like mutations and gross
CC chromosomal rearrangements (GCRs). {ECO:0000269|PubMed:11470404,
CC ECO:0000269|PubMed:12972632, ECO:0000269|PubMed:15184655,
CC ECO:0000269|PubMed:15654096, ECO:0000269|PubMed:19496932}.
CC -!- SUBUNIT: Component of the SHU complex composed of at least CSM2, PSY3,
CC SHU1 and SHU2. {ECO:0000269|PubMed:15654096,
CC ECO:0000269|PubMed:19496932}.
CC -!- INTERACTION:
CC P40465; Q12318: PSY3; NbExp=4; IntAct=EBI-25229, EBI-37340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CSM2 family. {ECO:0000305}.
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DR EMBL; DQ115392; AAZ22495.1; -; Genomic_DNA.
DR EMBL; Z38059; CAA86146.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08421.1; -; Genomic_DNA.
DR PIR; S48402; S48402.
DR RefSeq; NP_012134.1; NM_001179480.1.
DR PDB; 3VU9; X-ray; 1.75 A; B=1-213.
DR PDB; 4DT1; X-ray; 1.90 A; A=1-213.
DR PDB; 4EQ6; X-ray; 1.80 A; A=1-213.
DR PDB; 5XYN; X-ray; 3.30 A; B=1-213.
DR PDBsum; 3VU9; -.
DR PDBsum; 4DT1; -.
DR PDBsum; 4EQ6; -.
DR PDBsum; 5XYN; -.
DR AlphaFoldDB; P40465; -.
DR SMR; P40465; -.
DR BioGRID; 34859; 116.
DR ComplexPortal; CPX-3087; Shu complex.
DR DIP; DIP-1901N; -.
DR IntAct; P40465; 6.
DR MINT; P40465; -.
DR STRING; 4932.YIL132C; -.
DR PaxDb; P40465; -.
DR PRIDE; P40465; -.
DR EnsemblFungi; YIL132C_mRNA; YIL132C; YIL132C.
DR GeneID; 854674; -.
DR KEGG; sce:YIL132C; -.
DR SGD; S000001394; CSM2.
DR VEuPathDB; FungiDB:YIL132C; -.
DR eggNOG; ENOG502S2QF; Eukaryota.
DR HOGENOM; CLU_108124_0_0_1; -.
DR InParanoid; P40465; -.
DR OMA; YIDCKNS; -.
DR BioCyc; YEAST:G3O-31383-MON; -.
DR PRO; PR:P40465; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40465; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0097196; C:Shu complex; IDA:SGD.
DR GO; GO:0035861; C:site of double-strand break; IMP:SGD.
DR GO; GO:0000730; P:DNA recombinase assembly; IMP:SGD.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IC:ComplexPortal.
DR GO; GO:0070987; P:error-free translesion synthesis; IC:SGD.
DR GO; GO:0043007; P:maintenance of rDNA; IGI:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR GO; GO:1903112; P:positive regulation of single-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031783; Csm2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16834; CSM2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Meiosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..213
FT /note="Chromosome segregation in meiosis protein 2"
FT /id="PRO_0000202960"
FT CONFLICT 18
FT /note="N -> D (in Ref. 1; AAZ22495)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4EQ6"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 132..150
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3VU9"
SQ SEQUENCE 213 AA; 24953 MW; 55E26899275087AB CRC64;
MEYEDLELIT IWPSPTKNKL CQFIKQNLSK EHVVTQLFFI DATSSFPLSQ FQKLVPPTLP
ENVRIYENIR INTCLDLEEL SAITVKLLQI LSMNKINAQR GTEDAVTEPL KIILYINGLE
VMFRNSQFKS SPQRSHELLR DTLLKLRVMG NDENENASIR TLLEFPKEQL LDYYLKKNNN
TRTSSVRSKR RRIKNGDSLA EYIWKYYADS LFE
