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Protein

Cys-Gly metallodipeptidase dug1

Gene

dug1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Has a Gly-Cys dipeptidase activity.1 Publication

Cofactori

Zn2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Zinc 2By similarity
Active sitei101 – 1011By similarity
Metal bindingi133 – 1331Zinc 1By similarity
Metal bindingi133 – 1331Zinc 2By similarity
Active sitei167 – 1671Proton acceptorBy similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi196 – 1961Zinc 2By similarity
Metal bindingi446 – 4461Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-1614635. Sulfur amino acid metabolism.
R-SPO-174403. Glutathione synthesis and recycling.

Protein family/group databases

MEROPSiM20.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Cys-Gly metallodipeptidase dug1 (EC:3.4.13.-)
Alternative name(s):
GSH degradosomal complex subunit DUG1
Gene namesi
Name:dug1
ORF Names:SPBC1198.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1198.08.
PomBaseiSPBC1198.08. dug1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Cys-Gly metallodipeptidase dug1PRO_0000185274Add
BLAST

Proteomic databases

MaxQBiQ9P6I2.

Interactioni

Subunit structurei

Homodimer. Component of the GSH degradosomal complex.By similarity

Protein-protein interaction databases

BioGridi276203. 16 interactions.
MINTiMINT-4704004.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

HOGENOMiHOG000216709.
InParanoidiQ9P6I2.
KOiK15428.
OMAiCNVKFMI.
OrthoDBiEOG092C1SDA.

Family and domain databases

CDDicd05676. M20_dipept_like_CNDP. 1 hit.
Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR017153. CNDP/DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P6I2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMSLDKLYE VIDKKKDEFV TRLSRAVSIP SVSADVTLRP KVVEMADFVV
60 70 80 90 100
SEFTKLGAKM EKRDIGYHQM DGQDVPLPPI VLGQYGNDPS KKTVLIYNHF
110 120 130 140 150
DVQPASLEDG WSTDPFTLTV DNKGRMFGRG ATDDKGPLIG WISAIEAHKE
160 170 180 190 200
LGIDFPVNLL MCFEGMEEYG SEGLEDLIRA EAEKYFAKAD CVCISDTYWL
210 220 230 240 250
GTKKPVLTYG LRGVCYFNIT VEGPSADLHS GVFGGTVHEP MTDLVAIMST
260 270 280 290 300
LVKPNGEILI PGIMDQVAEL TPTEDSIYDG IDYTMEDLKE AVGADISIYP
310 320 330 340 350
DPKRTLQHRW RYPTLSLHGI EGAFSGSGAK TVIPAKVIGK FSIRTVPNME
360 370 380 390 400
SETVERLVKE HVTKVFNSLN SKNKLAFNNM HSGSWWISSP DHWHYDVGKK
410 420 430 440 450
ATERVYGITP DFVREGGSIP VTVTFEQSLK KNVLLLPMGR GDDGAHSINE
460 470
KLDLDNFLKG IKLFCTYVHE LASVSP
Length:476
Mass (Da):52,840
Last modified:July 11, 2012 - v2
Checksum:i9C9FC76AAF752AEE
GO

Sequence cautioni

The sequence BAA13812 differs from that shown. Reason: Frameshift at position 424. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391G → D in BAA13812 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB91183.2.
D89150 mRNA. Translation: BAA13812.1. Frameshift.
PIRiT42426.
RefSeqiNP_595077.2. NM_001020983.2.

Genome annotation databases

EnsemblFungiiSPBC1198.08.1; SPBC1198.08.1:pep; SPBC1198.08.
GeneIDi2539648.
KEGGispo:SPBC1198.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB91183.2.
D89150 mRNA. Translation: BAA13812.1. Frameshift.
PIRiT42426.
RefSeqiNP_595077.2. NM_001020983.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276203. 16 interactions.
MINTiMINT-4704004.

Protein family/group databases

MEROPSiM20.017.

Proteomic databases

MaxQBiQ9P6I2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1198.08.1; SPBC1198.08.1:pep; SPBC1198.08.
GeneIDi2539648.
KEGGispo:SPBC1198.08.

Organism-specific databases

EuPathDBiFungiDB:SPBC1198.08.
PomBaseiSPBC1198.08. dug1.

Phylogenomic databases

HOGENOMiHOG000216709.
InParanoidiQ9P6I2.
KOiK15428.
OMAiCNVKFMI.
OrthoDBiEOG092C1SDA.

Enzyme and pathway databases

ReactomeiR-SPO-1614635. Sulfur amino acid metabolism.
R-SPO-174403. Glutathione synthesis and recycling.

Miscellaneous databases

PROiQ9P6I2.

Family and domain databases

CDDicd05676. M20_dipept_like_CNDP. 1 hit.
Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR017153. CNDP/DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
PROSITEiPS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUG1_SCHPO
AccessioniPrimary (citable) accession number: Q9P6I2
Secondary accession number(s): P78801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: July 11, 2012
Last modified: September 7, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.