PSO2_YEAST
ID PSO2_YEAST Reviewed; 661 AA.
AC P30620; D6VZW0; Q07072;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DNA cross-link repair protein PSO2/SNM1;
DE EC=3.1.-.-;
GN Name=PSO2; Synonyms=SNM1; OrderedLocusNames=YMR137C; ORFNames=YM9375.06C;
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=1736091; DOI=10.1007/bf00279791;
RA Richter D., Niegemann E., Brendel M.;
RT "Molecular structure of the DNA cross-link repair gene SNM1 (PSO2) of the
RT yeast Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 231:194-200(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 252-467, AND MUTAGENESIS OF GLY-256.
RX PubMed=7526204; DOI=10.1016/0921-8777(94)90038-8;
RA Niegmann E., Brendel M.;
RT "A single amino acid change in SNM1-encoded protein leads to
RT thermoconditional deficiency for DNA cross-link repair in Saccharomyces
RT cerevisiae.";
RL Mutat. Res. 315:275-279(1994).
RN [5]
RP INDUCTION.
RX PubMed=8628215; DOI=10.1007/bf02174175;
RA Wolter R., Siede W., Brendel M.;
RT "Regulation of SNM1, an inducible Saccharomyces cerevisiae gene required
RT for repair of DNA cross-links.";
RL Mol. Gen. Genet. 250:162-168(1996).
RN [6]
RP FUNCTION.
RX PubMed=10980408; DOI=10.1016/s0921-8777(00)00035-5;
RA Grossmann K.F., Ward A.M., Moses R.E.;
RT "Saccharomyces cerevisiae lacking Snm1, Rev3 or Rad51 have a normal S-phase
RT but arrest permanently in G2 after cisplatin treatment.";
RL Mutat. Res. 461:1-13(2000).
RN [7]
RP FUNCTION.
RX PubMed=11738934; DOI=10.1016/s0921-8777(01)00106-9;
RA Grossmann K.F., Ward A.M., Matkovic M.E., Folias A.E., Moses R.E.;
RT "S. cerevisiae has three pathways for DNA interstrand crosslink repair.";
RL Mutat. Res. 487:73-83(2001).
RN [8]
RP DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
RX PubMed=12177301; DOI=10.1093/nar/gkf470;
RA Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.;
RT "Metallo-beta-lactamase fold within nucleic acids processing enzymes: the
RT beta-CASP family.";
RL Nucleic Acids Res. 30:3592-3601(2002).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASP-252.
RX PubMed=12509272; DOI=10.1016/s1568-7864(02)00192-1;
RA Li X., Moses R.E.;
RT "The beta-lactamase motif in Snm1 is required for repair of DNA double-
RT strand breaks caused by interstrand crosslinks in S. cerevisiae.";
RL DNA Repair 2:121-129(2003).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=14729978; DOI=10.1128/mcb.24.3.1351-1364.2004;
RA Yu J., Marshall K., Yamaguchi M., Haber J.E., Weil C.F.;
RT "Microhomology-dependent end joining and repair of transposon-induced DNA
RT hairpins by host factors in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 24:1351-1364(2004).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ASP-252.
RX PubMed=15590324; DOI=10.1016/j.dnarep.2004.08.012;
RA Li X., Hejna J., Moses R.E.;
RT "The yeast Snm1 protein is a DNA 5'-exonuclease.";
RL DNA Repair 4:163-170(2005).
RN [13]
RP FUNCTION.
RX PubMed=15743825; DOI=10.1128/mcb.25.6.2297-2309.2005;
RA Barber L.J., Ward T.A., Hartley J.A., McHugh P.J.;
RT "DNA interstrand cross-link repair in the Saccharomyces cerevisiae cell
RT cycle: overlapping roles for PSO2 (SNM1) with MutS factors and EXO1 during
RT S phase.";
RL Mol. Cell. Biol. 25:2297-2309(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for DNA interstrand cross-link repair. This requires
CC cleavage of cross-linked DNA to generate DNA double strand breaks
CC (DSBs). This protein has 5' exonuclease activity on single-stranded and
CC double-stranded DNA, which appears to be necessary for the processing
CC of DNA double strand breaks prior to ligation.
CC {ECO:0000269|PubMed:10980408, ECO:0000269|PubMed:11738934,
CC ECO:0000269|PubMed:12509272, ECO:0000269|PubMed:14729978,
CC ECO:0000269|PubMed:15590324, ECO:0000269|PubMed:15743825}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Expression is increased by ultraviolet light and agents
CC which induce DNA cross-links such as nitrogen mustard and psoralen.
CC {ECO:0000269|PubMed:8628215}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; X64004; CAA45405.1; -; Genomic_DNA.
DR EMBL; Z47071; CAA87351.1; -; Genomic_DNA.
DR EMBL; X76917; CAA54243.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10034.1; -; Genomic_DNA.
DR PIR; S19646; S19646.
DR RefSeq; NP_013857.1; NM_001182639.1.
DR AlphaFoldDB; P30620; -.
DR SMR; P30620; -.
DR BioGRID; 35314; 145.
DR DIP; DIP-6301N; -.
DR IntAct; P30620; 13.
DR MINT; P30620; -.
DR STRING; 4932.YMR137C; -.
DR iPTMnet; P30620; -.
DR MaxQB; P30620; -.
DR PaxDb; P30620; -.
DR PRIDE; P30620; -.
DR EnsemblFungi; YMR137C_mRNA; YMR137C; YMR137C.
DR GeneID; 855168; -.
DR KEGG; sce:YMR137C; -.
DR SGD; S000004745; PSO2.
DR VEuPathDB; FungiDB:YMR137C; -.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000158766; -.
DR HOGENOM; CLU_005260_7_0_1; -.
DR InParanoid; P30620; -.
DR OMA; PITANHC; -.
DR BioCyc; YEAST:G3O-32830-MON; -.
DR PRO; PR:P30620; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P30620; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:SGD.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..661
FT /note="DNA cross-link repair protein PSO2/SNM1"
FT /id="PRO_0000209130"
FT ZN_FING 144..174
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MUTAGEN 252
FT /note="D->A: Abrogates exonuclease activity."
FT /evidence="ECO:0000269|PubMed:12509272,
FT ECO:0000269|PubMed:15590324"
FT MUTAGEN 256
FT /note="G->R: In SNM1-2; increased sensitivity to DNA cross-
FT linking agents at 36 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:7526204"
SQ 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
