EXO1_YEAST
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 03-AUG-2022, entry version 192.
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;
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 PDBsum; 4FMO; -.
DR AlphaFoldDB; P39875; -.
DR SMR; P39875; -.
DR BioGRID; 34435; 232.
DR DIP; DIP-2421N; -.
DR IntAct; P39875; 6.
DR STRING; 4932.YOR033C; -.
DR iPTMnet; P39875; -.
DR MaxQB; P39875; -.
DR PaxDb; P39875; -.
DR PRIDE; P39875; -.
DR EnsemblFungi; YOR033C_mRNA; YOR033C; YOR033C.
DR GeneID; 854198; -.
DR KEGG; sce:YOR033C; -.
DR SGD; S000005559; EXO1.
DR VEuPathDB; FungiDB:YOR033C; -.
DR eggNOG; KOG2518; Eukaryota.
DR GeneTree; ENSGT00510000047676; -.
DR HOGENOM; CLU_008978_5_0_1; -.
DR InParanoid; P39875; -.
DR OMA; WLHRAAC; -.
DR BioCyc; YEAST:G3O-33579-MON; -.
DR BRENDA; 3.1.11.1; 984.
DR Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
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' exodeoxyribonuclease activity; IBA:GO_Central.
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:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0007534; P:gene conversion at mating-type locus; 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 InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR032641; Exo1.
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; PTHR11081; 1.
DR PANTHER; PTHR11081:SF8; PTHR11081:SF8; 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; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 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 478..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..680
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
