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   24-JAN-2024, entry version 164.
DE   RecName: Full=DNA cross-link repair protein PSO2/SNM1;
DE            EC=3.1.-.-;
GN   Name=PSO2; Synonyms=SNM1; OrderedLocusNames=YMR137C;
GN   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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 146.
DR   DIP; DIP-6301N; -.
DR   IntAct; P30620; 13.
DR   MINT; P30620; -.
DR   STRING; 4932.YMR137C; -.
DR   iPTMnet; P30620; -.
DR   MaxQB; P30620; -.
DR   PaxDb; 4932-YMR137C; -.
DR   PeptideAtlas; P30620; -.
DR   EnsemblFungi; YMR137C_mRNA; YMR137C; YMR137C.
DR   GeneID; 855168; -.
DR   KEGG; sce:YMR137C; -.
DR   AGR; SGD:S000004745; -.
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; AQVHMHS; -.
DR   OrthoDB; 23465at2759; -.
DR   BioCyc; YEAST:G3O-32830-MONOMER; -.
DR   BioGRID-ORCS; 855168; 1 hit in 10 CRISPR screens.
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' DNA exonuclease 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   CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.12650; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR011084; DRMBL.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR23240:SF6; DNA CROSS-LINK REPAIR 1A PROTEIN; 1.
DR   PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   Pfam; PF07522; DRMBL; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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
FT                   cross-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
//