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P43616 (DUG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cys-Gly metallodipeptidase DUG1

EC=3.4.13.-
Alternative name(s):
Deficient in utilization of glutathione protein 1
GSH degradosomal complex subunit DUG1
Gene names
Name:DUG1
Ordered Locus Names:YFR044C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides. Ref.8 Ref.10

Cofactor

Zinc or manganese. Ref.10

Subunit structure

Homodimer. Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3. Ref.8 Ref.10

Subcellular location

Cytoplasm Ref.6 Ref.8.

Disruption phenotype

Accumulation of Cys-Gly dipeptide and enhanced GSH toxicity. Ref.10

Miscellaneous

Present with 22300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase M20A family.

Biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for Cys-Gly (at pH 8.0 and in the presence of 20 µM manganese ions)

KM=0.8 mM for Cys-Gly (at pH 8.0 and in the presence of 200 µM zinc ions)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-5137,EBI-5137

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Cys-Gly metallodipeptidase DUG1
PRO_0000185275

Sites

Active site1041 By similarity
Active site1711Proton acceptor By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1371Zinc 1 By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1721Zinc 1 By similarity
Metal binding2001Zinc 2 By similarity
Metal binding4501Zinc 1 By similarity

Amino acid modifications

Modified residue4511Phosphoserine Ref.9

Secondary structure

.............................................................................. 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43616 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3E53773A945F5EBC

FASTA48152,871
        10         20         30         40         50         60 
MSHSLTSVFQ KIDSLKPQFF SRLTKAIQIP AVSSDESLRS KVFDKAKFIS EQLSQSGFHD 

        70         80         90        100        110        120 
IKMVDLGIQP PPISTPNLSL PPVILSRFGS DPSKKTVLVY GHYDVQPAQL EDGWDTEPFK 

       130        140        150        160        170        180 
LVIDEAKGIM KGRGVTDDTG PLLSWINVVD AFKASGQEFP VNLVTCFEGM EESGSLKLDE 

       190        200        210        220        230        240 
LIKKEANGYF KGVDAVCISD NYWLGTKKPV LTYGLRGCNY YQTIIEGPSA DLHSGIFGGV 

       250        260        270        280        290        300 
VAEPMIDLMQ VLGSLVDSKG KILIDGIDEM VAPLTEKEKA LYKDIEFSVE ELNAATGSKT 

       310        320        330        340        350        360 
SLYDKKEDIL MHRWRYPSLS IHGVEGAFSA QGAKTVIPAK VFGKFSIRTV PDMDSEKLTS 

       370        380        390        400        410        420 
LVQKHCDAKF KSLNSPNKCR TELIHDGAYW VSDPFNAQFT AAKKATKLVY GVDPDFTREG 

       430        440        450        460        470        480 
GSIPITLTFQ DALNTSVLLL PMGRGDDGAH SINEKLDISN FVGGMKTMAA YLQYYSESPE 


N 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."
Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.
Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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]"The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae."
Ganguli D., Kumar C., Bachhawat A.K.
Genetics 175:1137-1151(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, SUBCELLULAR LOCATION.
[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-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases."
Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K.
J. Biol. Chem. 284:14493-14502(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION, COFACTOR, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50617 Genomic DNA. Translation: BAA09283.1.
AY692702 Genomic DNA. Translation: AAT92721.1.
BK006940 Genomic DNA. Translation: DAA12487.1.
PIRS56299.
RefSeqNP_116702.1. NM_001180009.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G1PX-ray2.55A1-481[»]
ProteinModelPortalP43616.
SMRP43616. Positions 1-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31202. 23 interactions.
DIPDIP-6492N.
IntActP43616. 2 interactions.
MINTMINT-640305.
STRING4932.YFR044C.

Protein family/group databases

MEROPSM20.017.

Proteomic databases

PaxDbP43616.
PeptideAtlasP43616.
PRIDEP43616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYFR044C; YFR044C; YFR044C.
GeneID850605.
KEGGsce:YFR044C.

Organism-specific databases

CYGDYFR044c.
SGDS000001940. DUG1.

Phylogenomic databases

eggNOGCOG0624.
GeneTreeENSGT00390000009682.
HOGENOMHOG000216709.
KOK15428.
OMADYALVCD.
OrthoDBEOG7ZD249.

Enzyme and pathway databases

BioCycYEAST:G3O-30491-MONOMER.
YEAST:MONOMER3O-4.
SABIO-RKP43616.

Gene expression databases

GenevestigatorP43616.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
InterProIPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF037242. CNDP_dipeptidase. 1 hit.
ProtoNetSearch...

Other

NextBio966481.
PROP43616.

Entry information

Entry nameDUG1_YEAST
AccessionPrimary (citable) accession number: P43616
Secondary accession number(s): D6VTS7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references