P38149 (DUG2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable di- and tripeptidase DUG2
EC=3.4.-.-

Alternative name(s):
Deficient in utilization of glutathione protein 2
GSH degradosomal complex subunit DUG2

Gene names

Name:	DUG2
Ordered Locus Names:	YBR281C
ORF Names:	YBR2018

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	878 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Ref.6
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3. Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.4 Ref.6.
Miscellaneous	Present with 1940 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase M20A family. Contains 6 WD repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat WD repeat
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione catabolic process Inferred from direct assay PubMed 22277648. Source: SGD proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.4Ref.6. Source: SGD nucleus Inferred from direct assay Ref.4. Source: SGD
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW omega peptidase activity Inferred from genetic interaction Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 878	878	Probable di- and tripeptidase DUG2		PRO_0000051469
Regions
	Repeat	18 – 57	40	WD 1
	Repeat	68 – 107	40	WD 2
	Repeat	235 – 274	40	WD 3
	Repeat	282 – 322	41	WD 4
	Repeat	362 – 405	44	WD 5
	Repeat	608 – 651	44	WD 6
Sites
	Active site	522	1	By similarity
	Active site	586	1	Proton acceptor By similarity
	Metal binding	520	1	Zinc 2 By similarity
	Metal binding	553	1	Zinc 1 By similarity
	Metal binding	553	1	Zinc 2 By similarity
	Metal binding	587	1	Zinc 1 By similarity
	Metal binding	853	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	200	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P38149 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: A24C10BB4E94C344	FASTA	878	98,071
	10 20 30 40 50 60 MYDSRGVALH SELIHRWNHA FSILSIVAFP KKRLLFAGSQ DSKILVFDLP TYNLIHTIRL 70 80 90 100 110 120 GESQEETHTR SSVLCLTGSE DENFLFSGGA DSLVRIWSIG EKTIRDDFLP VTEIATVYSV 130 140 150 160 170 180 TDIGDIFSLA YLDSLETIVF GCQNASLLYV ENLIQKIEKK SSDGVENINK LPHRRYDKFF 190 200 210 220 230 240 DSLGPTGYSS NSLSQTSLTS LQENCGAAII EVPSENIIKY AHYGFIYSIN KLCPRFNQLL 250 260 270 280 290 300 EKSSRTSGAE HIISSAGDGI SKLWEFSKDK GQNTVKISLI NDKIDNEDSV ISQTIEFPFL 310 320 330 340 350 360 YCGLTDGIIK IWDLNTQQII STLKTKHESD VISISVYMDH VFAIDESGIT HFYQNQVNHW 370 380 390 400 410 420 NPQQGKILSS EIFSKSNAGS VSLLTGGSDG SLTLWDITSL LSAVPLSSNS PINASSTLQT 430 440 450 460 470 480 TNLWAAYQSA SLNNEEMLNT LRELISFQTV SQSKDTTNTL SLRRCAIYLQ QLFLKFGATN 490 500 510 520 530 540 SQLFPLPDGG NPVVFAYFQG NGKVSQVKGA KKKRILWYGH YDVISSGNTF NWNTDPFTLT 550 560 570 580 590 600 CENGYLKGRG VSDNKGPLVS AIHSVAYLFQ QGELVNDVVF LVEGSEEIGS ASLKQVCEKY 610 620 630 640 650 660 HDIIGKDIDW ILLSNSTWVD QEHPCLNYGL RGVINAQIKV WSDKPDGHSG LNGGVYDEPM 670 680 690 700 710 720 VNLVKIVSKL QNEQNEIMIP NFYSPLKDLT EEEYQRFQKI TELANIDENT TVQDLITNWT 730 740 750 760 770 780 KPSLSMTTVK FSGPGNITVI PKSVTMGISI RLVPEQSVEQ VKRDLKAYLE ESFKQLKSQN 790 800 810 820 830 840 HLEIKVLNEA EGWLGDPTNH AYQILKDEIT TAWDVEPLLV REGGSISCLR MLERIFDAPA 850 860 870 VQIPCGQSTD NGHLANENLR IKNWSNLTEI LSKVFNRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae." Holmstroem K., Brandt T., Kallesoe T. Yeast 10:S47-S62(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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].
[5]	"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].
[6]	"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.
[7]	"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-200, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76053 Genomic DNA. Translation: CAA53644.1. Z36150 Genomic DNA. Translation: CAA85245.1. BK006936 Genomic DNA. Translation: DAA07396.1.
PIR	S44543.
RefSeq	NP_009840.3. NM_001178629.3.
3D structure databases
ProteinModelPortal	P38149.
SMR	P38149. Positions 237-270, 317-401, 423-872.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1612N.
IntAct	P38149. 5 interactions.
MINT	MINT-399156.
STRING	4932.YBR281C.
Proteomic databases
PaxDb	P38149.
PeptideAtlas	P38149.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR281C; YBR281C; YBR281C.
GeneID	852584.
KEGG	sce:YBR281C. sce:YBR285W.
Organism-specific databases
CYGD	YBR281c.
SGD	S000000485. DUG2.
Phylogenomic databases
eggNOG	COG0624.
HOGENOM	HOG000183136.
KO	K14262.
OMA	YGHYDVI.
OrthoDB	EOG4WT0JN.
Gene expression databases
Genevestigator	P38149.
GermOnline	YBR281C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.130.10.10. 2 hits.
InterPro	IPR020472. G-protein_beta_WD-40_rep. IPR017149. GSH_degradosome_DUG2. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. PF00400. WD40. 1 hit. [Graphical view]
PIRSF	PIRSF037237. Peptidase_WD_repeats_DUG2. 1 hit.
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 4 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971733.

Entry information

Entry name

DUG2_YEAST

Accession

Primary (citable) accession number: P38149
Secondary accession number(s): D6VQS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program