CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006860
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable di- and tripeptidase DUG2 
Protein Synonyms/Alias
 Deficient in utilization of glutathione protein 2; GSH degradosomal complex subunit DUG2 
Gene Name
 DUG2 
Gene Synonyms/Alias
 YBR281C; YBR2018 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
762EQSVEQVKRDLKAYLubiquitination[1]
Reference
 [1] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269
Functional Description
 Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. 
Sequence Annotation
 REPEAT 18 57 WD 1.
 REPEAT 68 107 WD 2.
 REPEAT 235 274 WD 3.
 REPEAT 282 322 WD 4.
 REPEAT 362 405 WD 5.
 REPEAT 608 651 WD 6.
 ACT_SITE 522 522 By similarity.
 ACT_SITE 586 586 Proton acceptor (By similarity).
 METAL 520 520 Zinc 2 (By similarity).
 METAL 553 553 Zinc 1 (By similarity).
 METAL 553 553 Zinc 2 (By similarity).
 METAL 587 587 Zinc 1 (By similarity).
 METAL 853 853 Zinc 1 (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease; Reference proteome; Repeat; WD repeat; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 878 AA 
Protein Sequence
MYDSRGVALH SELIHRWNHA FSILSIVAFP KKRLLFAGSQ DSKILVFDLP TYNLIHTIRL 60
GESQEETHTR SSVLCLTGSE DENFLFSGGA DSLVRIWSIG EKTIRDDFLP VTEIATVYSV 120
TDIGDIFSLA YLDSLETIVF GCQNASLLYV ENLIQKIEKK SSDGVENINK LPHRRYDKFF 180
DSLGPTGYSS NSLSQTSLTS LQENCGAAII EVPSENIIKY AHYGFIYSIN KLCPRFNQLL 240
EKSSRTSGAE HIISSAGDGI SKLWEFSKDK GQNTVKISLI NDKIDNEDSV ISQTIEFPFL 300
YCGLTDGIIK IWDLNTQQII STLKTKHESD VISISVYMDH VFAIDESGIT HFYQNQVNHW 360
NPQQGKILSS EIFSKSNAGS VSLLTGGSDG SLTLWDITSL LSAVPLSSNS PINASSTLQT 420
TNLWAAYQSA SLNNEEMLNT LRELISFQTV SQSKDTTNTL SLRRCAIYLQ QLFLKFGATN 480
SQLFPLPDGG NPVVFAYFQG NGKVSQVKGA KKKRILWYGH YDVISSGNTF NWNTDPFTLT 540
CENGYLKGRG VSDNKGPLVS AIHSVAYLFQ QGELVNDVVF LVEGSEEIGS ASLKQVCEKY 600
HDIIGKDIDW ILLSNSTWVD QEHPCLNYGL RGVINAQIKV WSDKPDGHSG LNGGVYDEPM 660
VNLVKIVSKL QNEQNEIMIP NFYSPLKDLT EEEYQRFQKI TELANIDENT TVQDLITNWT 720
KPSLSMTTVK FSGPGNITVI PKSVTMGISI RLVPEQSVEQ VKRDLKAYLE ESFKQLKSQN 780
HLEIKVLNEA EGWLGDPTNH AYQILKDEIT TAWDVEPLLV REGGSISCLR MLERIFDAPA 840
VQIPCGQSTD NGHLANENLR IKNWSNLTEI LSKVFNRL 878 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0008242; F:omega peptidase activity; IGI:SGD.
 GO:0006751; P:glutathione catabolic process; IDA:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
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. 
Pfam
 PF07687; M20_dimer
 PF01546; Peptidase_M20
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS
 PR00320; GPROTEINBRPT.