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Protein

Exodeoxyribonuclease 1

Gene

EXO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.4 Publications

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.By similarity

Enzyme regulationi

Inactivated by calcium and zinc ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301Magnesium 1By similarity
Metal bindingi78 – 781Magnesium 1By similarity
Metal bindingi150 – 1501Magnesium 1By similarity
Metal bindingi152 – 1521Magnesium 1By similarity
Metal bindingi171 – 1711Magnesium 2By similarity
Metal bindingi173 – 1731Magnesium 2By similarity
Metal bindingi227 – 2271Magnesium 2By similarity

GO - Molecular functioni

  • 5'-3' exodeoxyribonuclease activity Source: InterPro
  • 5'-3' exonuclease activity Source: SGD
  • 5'-flap endonuclease activity Source: SGD
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • DNA double-strand break processing Source: SGD
  • gene conversion at mating-type locus, DNA double-strand break processing Source: SGD
  • meiotic DNA double-strand break processing Source: SGD
  • mismatch repair Source: SGD
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • telomere maintenance Source: SGD
  • telomeric 3' overhang formation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Excision nuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA excision, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33579-MONOMER.
BRENDAi3.1.11.1. 984.
ReactomeiR-SCE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

Names & Taxonomyi

Protein namesi
Recommended name:
Exodeoxyribonuclease 1 (EC:3.1.-.-)
Alternative name(s):
Exodeoxyribonuclease I
Short name:
EXO I
Short name:
Exonuclease I
Protein DHS1
Gene namesi
Name:EXO1
Synonyms:DHS1
Ordered Locus Names:YOR033C
ORF Names:OR26.23
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR033C.
SGDiS000005559. EXO1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 702702Exodeoxyribonuclease 1PRO_0000154045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei372 – 3721PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39875.

PTM databases

iPTMnetiP39875.

Interactioni

Subunit structurei

Interacts with mismatch repair protein MSH2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P258473EBI-6738,EBI-11352
MSH2P432462EBI-6738,EBI-355888From a different organism.

Protein-protein interaction databases

BioGridi34435. 112 interactions.
DIPiDIP-2421N.
IntActiP39875. 3 interactions.
MINTiMINT-553509.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FMOX-ray3.04C443-450[»]
ProteinModelPortaliP39875.
SMRiP39875. Positions 2-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9696N-domainAdd
BLAST
Regioni114 – 247134I-domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi501 – 52020Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi537 – 55317Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi618 – 6258Asp-rich (acidic)

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00510000047676.
HOGENOMiHOG000112416.
InParanoidiP39875.
KOiK10746.
OrthoDBiEOG77HDQN.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR020045. 5-3_exonuclease_C.
IPR032641. Exo1.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERiPTHR11081. PTHR11081. 3 hits.
PTHR11081:SF8. PTHR11081:SF8. 3 hits.
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIQGLLPQL KPIQNPVSLR RYEGEVLAID GYAWLHRAAC SCAYELAMGK
60 70 80 90 100
PTDKYLQFFI KRFSLLKTFK VEPYLVFDGD AIPVKKSTES KRRDKRKENK
110 120 130 140 150
AIAERLWACG EKKNAMDYFQ KCVDITPEMA KCIICYCKLN GIRYIVAPFE
160 170 180 190 200
ADSQMVYLEQ KNIVQGIISE DSDLLVFGCR RLITKLNDYG ECLEICRDNF
210 220 230 240 250
IKLPKKFPLG SLTNEEIITM VCLSGCDYTN GIPKVGLITA MKLVRRFNTI
260 270 280 290 300
ERIILSIQRE GKLMIPDTYI NEYEAAVLAF QFQRVFCPIR KKIVSLNEIP
310 320 330 340 350
LYLKDTESKR KRLYACIGFV IHRETQKKQI VHFDDDIDHH LHLKIAQGDL
360 370 380 390 400
NPYDFHQPLA NREHKLQLAS KSNIEFGKTN TTNSEAKVKP IESFFQKMTK
410 420 430 440 450
LDHNPKVANN IHSLRQAEDK LTMAIKRRKL SNANVVQETL KDTRSKFFNK
460 470 480 490 500
PSMTVVENFK EKGDSIQDFK EDTNSQSLEE PVSESQLSTQ IPSSFITTNL
510 520 530 540 550
EDDDNLSEEV SEVVSDIEED RKNSEGKTIG NEIYNTDDDG DGDTSEDYSE
560 570 580 590 600
TAESRVPTSS TTSFPGSSQR SISGCTKVLQ KFRYSSSFSG VNANRQPLFP
610 620 630 640 650
RHVNQKSRGM VYVNQNRDDD CDDNDGKNQI TQRPSLRKSL IGARSQRIVI
660 670 680 690 700
DMKSVDERKS FNSSPILHEE SKKRDIETTK SSQARPAVRS ISLLSQFVYK

GK
Length:702
Mass (Da):80,162
Last modified:October 1, 1996 - v2
Checksum:i78E22F6B265DB3AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86134 Genomic DNA. Translation: AAB47428.1.
X87331 Genomic DNA. Translation: CAA60749.1.
Z74941 Genomic DNA. Translation: CAA99223.1.
S69545 Genomic DNA. Translation: AAC60570.1.
BK006948 Genomic DNA. Translation: DAA10815.1.
PIRiS62169.
RefSeqiNP_014676.1. NM_001183452.1.

Genome annotation databases

EnsemblFungiiYOR033C; YOR033C; YOR033C.
GeneIDi854198.
KEGGisce:YOR033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86134 Genomic DNA. Translation: AAB47428.1.
X87331 Genomic DNA. Translation: CAA60749.1.
Z74941 Genomic DNA. Translation: CAA99223.1.
S69545 Genomic DNA. Translation: AAC60570.1.
BK006948 Genomic DNA. Translation: DAA10815.1.
PIRiS62169.
RefSeqiNP_014676.1. NM_001183452.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FMOX-ray3.04C443-450[»]
ProteinModelPortaliP39875.
SMRiP39875. Positions 2-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34435. 112 interactions.
DIPiDIP-2421N.
IntActiP39875. 3 interactions.
MINTiMINT-553509.

PTM databases

iPTMnetiP39875.

Proteomic databases

MaxQBiP39875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR033C; YOR033C; YOR033C.
GeneIDi854198.
KEGGisce:YOR033C.

Organism-specific databases

EuPathDBiFungiDB:YOR033C.
SGDiS000005559. EXO1.

Phylogenomic databases

GeneTreeiENSGT00510000047676.
HOGENOMiHOG000112416.
InParanoidiP39875.
KOiK10746.
OrthoDBiEOG77HDQN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33579-MONOMER.
BRENDAi3.1.11.1. 984.
ReactomeiR-SCE-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).

Miscellaneous databases

PROiP39875.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR020045. 5-3_exonuclease_C.
IPR032641. Exo1.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERiPTHR11081. PTHR11081. 3 hits.
PTHR11081:SF8. PTHR11081:SF8. 3 hits.
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of Saccharomyces cerevisiae EXO1, a gene encoding an exonuclease that interacts with MSH2."
    Tishkoff D.X., Boerger A.L., Bertrand P., Filosi N., Gaida G.M., Kane M.F., Kolodner R.D.
    Proc. Natl. Acad. Sci. U.S.A. 94:7487-7492(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSH2.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Molecular cloning of a gene, DHS1, which complements a drug-hypersensitive mutation of the yeast Saccharomyces cerevisiae."
    Lee Y.S., Shimizu J., Yoda K., Yamasaki M.
    Biosci. Biotechnol. Biochem. 58:391-395(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-702.
  5. "Exonuclease I of Saccharomyces cerevisiae functions in mitotic recombination in vivo and in vitro."
    Fiorentini P., Huang K.N., Tishkoff D.X., Kolodner R.D., Symington L.S.
    Mol. Cell. Biol. 17:2764-2773(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Decreased meiotic intergenic recombination and increased meiosis I nondisjunction in exo1 mutants of Saccharomyces cerevisiae."
    Kirkpatrick D.T., Ferguson J.R., Petes T.D., Symington L.S.
    Genetics 156:1549-1557(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective cells."
    Cotta-Ramusino C., Fachinetti D., Lucca C., Doksani Y., Lopes M., Sogo J., Foiani M.
    Mol. Cell 17:153-159(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEXO1_YEAST
AccessioniPrimary (citable) accession number: P39875
Secondary accession number(s): D6W299
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 672 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.