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DNA cross-link repair protein PSO2/SNM1 (EC 3.1.-.-)

 PSO2_YEAST              Reviewed;         661 AA.
P30620; D6VZW0; Q07072;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
18-JUL-2018, entry version 134.
RecName: Full=DNA cross-link repair protein PSO2/SNM1;
EC=3.1.-.-;
Name=PSO2; Synonyms=SNM1; OrderedLocusNames=YMR137C;
ORFNames=YM9375.06C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1736091;
Richter D., Niegemann E., Brendel M.;
"Molecular structure of the DNA cross-link repair gene SNM1 (PSO2) of
the yeast Saccharomyces cerevisiae.";
Mol. Gen. Genet. 231:194-200(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 252-467, AND MUTAGENESIS OF
GLY-256.
PubMed=7526204; DOI=10.1016/0921-8777(94)90038-8;
Niegmann E., Brendel M.;
"A single amino acid change in SNM1-encoded protein leads to
thermoconditional deficiency for DNA cross-link repair in
Saccharomyces cerevisiae.";
Mutat. Res. 315:275-279(1994).
[5]
INDUCTION.
PubMed=8628215; DOI=10.1007/BF02174175;
Wolter R., Siede W., Brendel M.;
"Regulation of SNM1, an inducible Saccharomyces cerevisiae gene
required for repair of DNA cross-links.";
Mol. Gen. Genet. 250:162-168(1996).
[6]
FUNCTION.
PubMed=10980408; DOI=10.1016/S0921-8777(00)00035-5;
Grossmann K.F., Ward A.M., Moses R.E.;
"Saccharomyces cerevisiae lacking Snm1, Rev3 or Rad51 have a normal S-
phase but arrest permanently in G2 after cisplatin treatment.";
Mutat. Res. 461:1-13(2000).
[7]
FUNCTION.
PubMed=11738934; DOI=10.1016/S0921-8777(01)00106-9;
Grossmann K.F., Ward A.M., Matkovic M.E., Folias A.E., Moses R.E.;
"S. cerevisiae has three pathways for DNA interstrand crosslink
repair.";
Mutat. Res. 487:73-83(2001).
[8]
DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
PubMed=12177301; DOI=10.1093/nar/gkf470;
Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.;
"Metallo-beta-lactamase fold within nucleic acids processing enzymes:
the beta-CASP family.";
Nucleic Acids Res. 30:3592-3601(2002).
[9]
FUNCTION, AND MUTAGENESIS OF ASP-252.
PubMed=12509272; DOI=10.1016/S1568-7864(02)00192-1;
Li X., Moses R.E.;
"The beta-lactamase motif in Snm1 is required for repair of DNA
double-strand breaks caused by interstrand crosslinks in S.
cerevisiae.";
DNA Repair 2:121-129(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION.
PubMed=14729978; DOI=10.1128/MCB.24.3.1351-1364.2004;
Yu J., Marshall K., Yamaguchi M., Haber J.E., Weil C.F.;
"Microhomology-dependent end joining and repair of transposon-induced
DNA hairpins by host factors in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 24:1351-1364(2004).
[12]
FUNCTION, AND MUTAGENESIS OF ASP-252.
PubMed=15590324; DOI=10.1016/j.dnarep.2004.08.012;
Li X., Hejna J., Moses R.E.;
"The yeast Snm1 protein is a DNA 5'-exonuclease.";
DNA Repair 4:163-170(2005).
[13]
FUNCTION.
PubMed=15743825; DOI=10.1128/MCB.25.6.2297-2309.2005;
Barber L.J., Ward T.A., Hartley J.A., McHugh P.J.;
"DNA interstrand cross-link repair in the Saccharomyces cerevisiae
cell cycle: overlapping roles for PSO2 (SNM1) with MutS factors and
EXO1 during S phase.";
Mol. Cell. Biol. 25:2297-2309(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Required for DNA interstrand cross-link repair. This
requires cleavage of cross-linked DNA to generate DNA double
strand breaks (DSBs). This protein has 5' exonuclease activity on
single-stranded and double-stranded DNA, which appears to be
necessary for the processing of DNA double strand breaks prior to
ligation. {ECO:0000269|PubMed:10980408,
ECO:0000269|PubMed:11738934, ECO:0000269|PubMed:12509272,
ECO:0000269|PubMed:14729978, ECO:0000269|PubMed:15590324,
ECO:0000269|PubMed:15743825}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- INDUCTION: Expression is increased by ultraviolet light and agents
which induce DNA cross-links such as nitrogen mustard and
psoralen. {ECO:0000269|PubMed:8628215}.
-!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
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EMBL; X64004; CAA45405.1; -; Genomic_DNA.
EMBL; Z47071; CAA87351.1; -; Genomic_DNA.
EMBL; X76917; CAA54243.1; -; Genomic_DNA.
EMBL; BK006946; DAA10034.1; -; Genomic_DNA.
PIR; S19646; S19646.
RefSeq; NP_013857.1; NM_001182639.1.
ProteinModelPortal; P30620; -.
SMR; P30620; -.
BioGrid; 35314; 138.
DIP; DIP-6301N; -.
IntAct; P30620; 17.
MINT; P30620; -.
STRING; 4932.YMR137C; -.
iPTMnet; P30620; -.
MaxQB; P30620; -.
PaxDb; P30620; -.
PRIDE; P30620; -.
EnsemblFungi; YMR137C; YMR137C; YMR137C.
GeneID; 855168; -.
KEGG; sce:YMR137C; -.
EuPathDB; FungiDB:YMR137C; -.
SGD; S000004745; PSO2.
GeneTree; ENSGT00530000063183; -.
HOGENOM; HOG000115743; -.
InParanoid; P30620; -.
KO; K15340; -.
OMA; LYERETH; -.
OrthoDB; EOG092C1ILX; -.
BioCyc; YEAST:G3O-32830-MONOMER; -.
PRO; PR:P30620; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IC:SGD.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:SGD.
GO; GO:0003684; F:damaged DNA binding; IMP:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IMP:SGD.
GO; GO:0006302; P:double-strand break repair; TAS:SGD.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; IMP:SGD.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR011084; DRMBL.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF07522; DRMBL; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase;
Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Zinc;
Zinc-finger.
CHAIN 1 661 DNA cross-link repair protein PSO2/SNM1.
/FTId=PRO_0000209130.
ZN_FING 145 169 {ECO:0000255}.
MUTAGEN 252 252 D->A: Abrogates exonuclease activity.
{ECO:0000269|PubMed:12509272,
ECO:0000269|PubMed:15590324}.
MUTAGEN 256 256 G->R: In SNM1-2; increased sensitivity to
DNA cross-linking agents at 36 degrees
Celsius. {ECO:0000269|PubMed:7526204}.
SEQUENCE 661 AA; 76399 MW; 56F14DEBAC86EAE2 CRC64;
MSRKSIVQIR RSEVKRKRSS TASSTSEGKT LHKNTHTSSK RQRTLTEFNI PTSSNLPVRS
SSYSFSRFSC STSNKNTEPV IINDDDHNSI CLEDTAKVEI TIDTDEEELV SLHDNEVSAI
ENRTEDRIVT ELEEQVNVKV STEVIQCPIC LENLSHLELY ERETHCDTCI GSDPSNMGTP
KKNIRSFISN PSSPAKTKRD IATSKKPTRV KLVLPSFKII KFNNGHEIVV DGFNYKASET
ISQYFLSHFH SDHYIGLKKS WNNPDENPIK KTLYCSKITA ILVNLKFKIP MDEIQILPMN
KRFWITDTIS VVTLDANHCP GAIIMLFQEF LANSYDKPIR QILHTGDFRS NAKMIETIQK
WLAETANETI DQVYLDTTYM TMGYNFPSQH SVCETVADFT LRLIKHGKNK TFGDSQRNLF
HFQRKKTLTT HRYRVLFLVG TYTIGKEKLA IKICEFLKTK LFVMPNSVKF SMMLTVLQNN
ENQNDMWDES LLTSNLHESS VHLVPIRVLK SQETIEAYLK SLKELETDYV KDIEDVVGFI
PTGWSHNFGL KYQKKNDDDE NEMSGNTEYC LELMKNDRDN DDENGFEISS ILRQYKKYNK
FQVFNVPYSE HSSFNDLVKF GCKLKCSEVI PTVNLNNLWK VRYMTNWFQC WENVRKTRAA
K


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