Exodeoxyribonuclease 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39875 (EXO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Exodeoxyribonuclease 1
EC=3.1.-.-

Alternative name(s):
Exodeoxyribonuclease I
Short name=EXO I
Short name=Exonuclease I
Protein DHS1

Gene names

Name:	EXO1
Synonyms:	DHS1
Ordered Locus Names:	YOR033C
ORF Names:	OR26.23

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	702 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5 Ref.6 Ref.8
Cofactor	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 regulation	Inactivated by calcium and zinc ions.
Subunit structure	Interacts with mismatch repair protein MSH2. Ref.1
Subcellular location	Nucleus Potential.
Miscellaneous	Present with 672 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.

Ontologies

Keywords
Biological process	DNA damage DNA excision DNA repair
Cellular component	Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Excision nuclease Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gene conversion at mating-type locus, DNA double-strand break processing Inferred from mutant phenotype PubMed 18806779. Source: SGD meiotic DNA double-strand break processing Inferred from genetic interaction PubMed 20150422. Source: SGD mismatch repair Inferred from mutant phenotype PubMed 11438669. Source: SGD telomeric 3' overhang formation Inferred from genetic interaction PubMed 20808892. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD nucleus Inferred from direct assay PubMed 22842922. Source: SGD
Molecular_function	5'-3' exonuclease activity Inferred from direct assay PubMed 12531018. Source: SGD 5'-flap endonuclease activity Inferred from direct assay PubMed 12531018. Source: SGD DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MSH2	P25847	3	EBI-6738,EBI-11352
MSH2	P43246	2	EBI-6738,EBI-355888	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 702

702

Exodeoxyribonuclease 1

PRO_0000154045

Regions

Region

1 – 96

N-domain

Region

114 – 247

134

I-domain

Compositional bias

501 – 520

Asp/Glu-rich (acidic)

Compositional bias

537 – 553

Asp/Glu-rich (acidic)

Compositional bias

618 – 625

Asp-rich (acidic)

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

Magnesium 1 By similarity

Metal binding

150

Magnesium 1 By similarity

Metal binding

152

Magnesium 1 By similarity

Metal binding

171

Magnesium 2 By similarity

Metal binding

173

Magnesium 2 By similarity

Metal binding

227

Magnesium 2 By similarity

Amino acid modifications

Modified residue

372

Phosphoserine Ref.9 Ref.10

Modified residue

563

Phosphoserine Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P39875 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 78E22F6B265DB3AA
Show »

FASTA

702

80,162

        10         20         30         40         50         60 
MGIQGLLPQL KPIQNPVSLR RYEGEVLAID GYAWLHRAAC SCAYELAMGK PTDKYLQFFI 

        70         80         90        100        110        120 
KRFSLLKTFK VEPYLVFDGD AIPVKKSTES KRRDKRKENK AIAERLWACG EKKNAMDYFQ 

       130        140        150        160        170        180 
KCVDITPEMA KCIICYCKLN GIRYIVAPFE ADSQMVYLEQ KNIVQGIISE DSDLLVFGCR 

       190        200        210        220        230        240 
RLITKLNDYG ECLEICRDNF IKLPKKFPLG SLTNEEIITM VCLSGCDYTN GIPKVGLITA 

       250        260        270        280        290        300 
MKLVRRFNTI ERIILSIQRE GKLMIPDTYI NEYEAAVLAF QFQRVFCPIR KKIVSLNEIP 

       310        320        330        340        350        360 
LYLKDTESKR KRLYACIGFV IHRETQKKQI VHFDDDIDHH LHLKIAQGDL NPYDFHQPLA 

       370        380        390        400        410        420 
NREHKLQLAS KSNIEFGKTN TTNSEAKVKP IESFFQKMTK LDHNPKVANN IHSLRQAEDK 

       430        440        450        460        470        480 
LTMAIKRRKL SNANVVQETL KDTRSKFFNK PSMTVVENFK EKGDSIQDFK EDTNSQSLEE 

       490        500        510        520        530        540 
PVSESQLSTQ IPSSFITTNL EDDDNLSEEV SEVVSDIEED RKNSEGKTIG NEIYNTDDDG 

       550        560        570        580        590        600 
DGDTSEDYSE TAESRVPTSS TTSFPGSSQR SISGCTKVLQ KFRYSSSFSG VNANRQPLFP 

       610        620        630        640        650        660 
RHVNQKSRGM VYVNQNRDDD CDDNDGKNQI TQRPSLRKSL IGARSQRIVI DMKSVDERKS 

       670        680        690        700 
FNSSPILHEE SKKRDIETTK SSQARPAVRS ISLLSQFVYK GK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, MASS SPECTROMETRY.
[10]	"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 AND SER-563, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S62169.

RefSeq

NP_014676.1. NM_001183452.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FMO	X-ray	3.04	C	443-450	[»]

ProteinModelPortal

P39875.

SMR

P39875. Positions 2-297.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2421N.

IntAct

P39875. 3 interactions.

MINT

MINT-553509.

STRING

4932.YOR033C.

Proteomic databases

PaxDb

P39875.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR033C; YOR033C; YOR033C.

GeneID

854198.

KEGG

sce:YOR033C.

Organism-specific databases

CYGD

YOR033c.

SGD

S000005559. EXO1.

Phylogenomic databases

eggNOG

COG0258.

GeneTree

ENSGT00510000047676.

HOGENOM

HOG000112416.

K10746.

OrthoDB

EOG44QX8J.

Enzyme and pathway databases

BRENDA

3.1.11.1. 984.

Gene expression databases

Genevestigator

P39875.

GermOnline

YOR033C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR020045. 5-3_exonuclease_C.
IPR008918. HhH2.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]

PANTHER

PTHR11081. PTHR11081. 1 hit.

Pfam

PF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]

PRINTS

PR00853. XPGRADSUPER.

SMART

SM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]

SUPFAM

SSF47807. 5_3_exo_C. 1 hit.

PROSITE

PS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976029.

Entry information

Entry name

EXO1_YEAST

Accession

Primary (citable) accession number: P39875
Secondary accession number(s): D6W299

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents