ID   EXO1_YEAST              Reviewed;         702 AA.
AC   P39875; D6W299;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   04-NOV-2026, entry version 210.
DE   RecName: Full=Exodeoxyribonuclease 1;
DE            EC=3.1.-.-;
DE   AltName: Full=Exodeoxyribonuclease I;
DE            Short=EXO I;
DE            Short=Exonuclease I;
DE   AltName: Full=Protein DHS1;
GN   Name=EXO1; Synonyms=DHS1; OrderedLocusNames=YOR033C; ORFNames=OR26.23;
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], FUNCTION, AND INTERACTION WITH MSH2.
RX   PubMed=9207118; DOI=10.1073/pnas.94.14.7487;
RA   Tishkoff D.X., Boerger A.L., Bertrand P., Filosi N., Gaida G.M., Kane M.F.,
RA   Kolodner R.D.;
RT   "Identification and characterization of Saccharomyces cerevisiae EXO1, a
RT   gene encoding an exonuclease that interacts with MSH2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7487-7492(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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 220-702.
RX   PubMed=7764548; DOI=10.1271/bbb.58.391;
RA   Lee Y.S., Shimizu J., Yoda K., Yamasaki M.;
RT   "Molecular cloning of a gene, DHS1, which complements a drug-hypersensitive
RT   mutation of the yeast Saccharomyces cerevisiae.";
RL   Biosci. Biotechnol. Biochem. 58:391-395(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9111347; DOI=10.1128/mcb.17.5.2764;
RA   Fiorentini P., Huang K.N., Tishkoff D.X., Kolodner R.D., Symington L.S.;
RT   "Exonuclease I of Saccharomyces cerevisiae functions in mitotic
RT   recombination in vivo and in vitro.";
RL   Mol. Cell. Biol. 17:2764-2773(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=11102356; DOI=10.1093/genetics/156.4.1549;
RA   Kirkpatrick D.T., Ferguson J.R., Petes T.D., Symington L.S.;
RT   "Decreased meiotic intergenic recombination and increased meiosis I
RT   nondisjunction in exo1 mutants of Saccharomyces cerevisiae.";
RL   Genetics 156:1549-1557(2000).
RN   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=15629726; DOI=10.1016/j.molcel.2004.11.032;
RA   Cotta-Ramusino C., Fachinetti D., Lucca C., Doksani Y., Lopes M., Sogo J.,
RA   Foiani M.;
RT   "Exo1 processes stalled replication forks and counteracts fork reversal in
RT   checkpoint-defective cells.";
RL   Mol. Cell 17:153-159(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP   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: 5'->3' double-stranded DNA exonuclease involved in mismatch
CC       repair and eventually also in mitotic recombination between direct
CC       repeats. Also has a minor role in the correction of large DNA
CC       mismatches that occur in the heteroduplex DNA during meiotic
CC       recombination at the HIS4 locus. {ECO:0000269|PubMed:11102356,
CC       ECO:0000269|PubMed:15629726, ECO:0000269|PubMed:9111347,
CC       ECO:0000269|PubMed:9207118}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inactivated by calcium and zinc ions.
CC   -!- SUBUNIT: Interacts with mismatch repair protein MSH2.
CC       {ECO:0000269|PubMed:9207118}.
CC   -!- INTERACTION:
CC       P39875; P38920: MLH1; NbExp=3; IntAct=EBI-6738, EBI-11003;
CC       P39875; P25847: MSH2; NbExp=3; IntAct=EBI-6738, EBI-11352;
CC       P39875; P43246: MSH2; Xeno; NbExp=2; IntAct=EBI-6738, EBI-355888;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U86134; AAB47428.1; -; Genomic_DNA.
DR   EMBL; X87331; CAA60749.1; -; Genomic_DNA.
DR   EMBL; Z74941; CAA99223.1; -; Genomic_DNA.
DR   EMBL; S69545; AAC60570.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10815.1; -; Genomic_DNA.
DR   PIR; S62169; S62169.
DR   RefSeq; NP_014676.1; NM_001183452.1.
DR   PDB; 4FMO; X-ray; 3.04 A; C=443-450.
DR   AlphaFoldDB; P39875; -.
DR   MDRepo; P39875; -.
DR   SMR; P39875; -.
DR   BioGRID; 34435; 263.
DR   DIP; DIP-2421N; -.
DR   FunCoup; P39875; 265.
DR   IntAct; P39875; 6.
DR   STRING; 4932.YOR033C; -.
DR   iPTMnet; P39875; -.
DR   PaxDb; 4932-YOR033C; -.
DR   PeptideAtlas; P39875; -.
DR   EnsemblFungi; YOR033C_mRNA; YOR033C; YOR033C.
DR   GeneID; 854198; -.
DR   KEGG; sce:YOR033C; -.
DR   AGR; SGD:S000005559; -.
DR   SGD; S000005559; EXO1.
DR   VEuPathDB; FungiDB:YOR033C; -.
DR   eggNOG; KOG2518; Eukaryota.
DR   HOGENOM; CLU_008978_5_0_1; -.
DR   InParanoid; P39875; -.
DR   OMA; AAHSCAM; -.
DR   OrthoDB; 26491at2759; -.
DR   BioCyc; YEAST:G3O-33579-MONOMER; -.
DR   BRENDA; 3.1.11.1; 984.
DR   BioGRID-ORCS; 854198; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P39875; -.
DR   PRO; PR:P39875; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P39875; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IDA:SGD.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0000729; P:DNA double-strand break processing; IMP:SGD.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0007534; P:gene conversion at mating-type locus; IMP:SGD.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
DR   GO; GO:0000706; P:meiotic DNA double-strand break processing; IGI:SGD.
DR   GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR   GO; GO:0044818; P:mitotic G2/M transition checkpoint; IGI:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR   GO; GO:0031860; P:telomeric 3' overhang formation; IGI:SGD.
DR   CDD; cd09908; H3TH_EXO1; 1.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   FunFam; 1.10.150.20:FF:000011; exonuclease 1; 1.
DR   FunFam; 3.40.50.1010:FF:000002; Exonuclease 1, putative; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR037315; EXO1_H3TH.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR044752; PIN-like_EXO1.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081:SF65; DNA DAMAGE-INDUCIBLE PROTEIN DIN7-RELATED; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA excision; DNA repair; DNA-binding;
KW   Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..702
FT                   /note="Exodeoxyribonuclease 1"
FT                   /id="PRO_0000154045"
FT   REGION          1..96
FT                   /note="N-domain"
FT   REGION          114..247
FT                   /note="I-domain"
FT   REGION          465..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..550
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..571
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   702 AA;  80162 MW;  78E22F6B265DB3AA CRC64;
     MGIQGLLPQL KPIQNPVSLR RYEGEVLAID GYAWLHRAAC SCAYELAMGK PTDKYLQFFI
     KRFSLLKTFK VEPYLVFDGD AIPVKKSTES KRRDKRKENK AIAERLWACG EKKNAMDYFQ
     KCVDITPEMA KCIICYCKLN GIRYIVAPFE ADSQMVYLEQ KNIVQGIISE DSDLLVFGCR
     RLITKLNDYG ECLEICRDNF IKLPKKFPLG SLTNEEIITM VCLSGCDYTN GIPKVGLITA
     MKLVRRFNTI ERIILSIQRE GKLMIPDTYI NEYEAAVLAF QFQRVFCPIR KKIVSLNEIP
     LYLKDTESKR KRLYACIGFV IHRETQKKQI VHFDDDIDHH LHLKIAQGDL NPYDFHQPLA
     NREHKLQLAS KSNIEFGKTN TTNSEAKVKP IESFFQKMTK LDHNPKVANN IHSLRQAEDK
     LTMAIKRRKL SNANVVQETL KDTRSKFFNK PSMTVVENFK EKGDSIQDFK EDTNSQSLEE
     PVSESQLSTQ IPSSFITTNL EDDDNLSEEV SEVVSDIEED RKNSEGKTIG NEIYNTDDDG
     DGDTSEDYSE TAESRVPTSS TTSFPGSSQR SISGCTKVLQ KFRYSSSFSG VNANRQPLFP
     RHVNQKSRGM VYVNQNRDDD CDDNDGKNQI TQRPSLRKSL IGARSQRIVI DMKSVDERKS
     FNSSPILHEE SKKRDIETTK SSQARPAVRS ISLLSQFVYK GK
//