ID   DUG2_YEAST              Reviewed;         878 AA.
AC   P38149; D6VQS6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 199.
DE   RecName: Full=Probable di- and tripeptidase DUG2;
DE            EC=3.4.-.-;
DE   AltName: Full=Deficient in utilization of glutathione protein 2;
DE   AltName: Full=GSH degradosomal complex subunit DUG2;
GN   Name=DUG2; OrderedLocusNames=YBR281C; ORFNames=YBR2018;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091861; DOI=10.1002/yea.320100007;
RA   Holmstroem K., Brandt T., Kallesoe T.;
RT   "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT   II from Saccharomyces cerevisiae.";
RL   Yeast 10:S47-S62(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17179087; DOI=10.1534/genetics.106.066944;
RA   Ganguli D., Kumar C., Bachhawat A.K.;
RT   "The alternative pathway of glutathione degradation is mediated by a novel
RT   protein complex involving three new genes in Saccharomyces cerevisiae.";
RL   Genetics 175:1137-1151(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Component of the GSH degradosomal complex involved in the
CC       degradation of glutathione (GSH) and other peptides containing a gamma-
CC       glu-X bond. {ECO:0000269|PubMed:17179087}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Component of the GSH degradosomal complex composed of at least
CC       DUG1, DUG2 and DUG3. {ECO:0000269|PubMed:17179087}.
CC   -!- INTERACTION:
CC       P38149; P38149: DUG2; NbExp=2; IntAct=EBI-21176, EBI-21176;
CC       P38149; P53871: DUG3; NbExp=5; IntAct=EBI-21176, EBI-29079;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; X76053; CAA53644.1; -; Genomic_DNA.
DR   EMBL; Z36150; CAA85245.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07396.1; -; Genomic_DNA.
DR   PIR; S44543; S44543.
DR   RefSeq; NP_009840.3; NM_001178629.3.
DR   AlphaFoldDB; P38149; -.
DR   SMR; P38149; -.
DR   BioGRID; 32975; 63.
DR   ComplexPortal; CPX-325; Glutathione hydrolase complex.
DR   DIP; DIP-1612N; -.
DR   FunCoup; P38149; 114.
DR   IntAct; P38149; 8.
DR   MINT; P38149; -.
DR   STRING; 4932.YBR281C; -.
DR   iPTMnet; P38149; -.
DR   PaxDb; 4932-YBR281C; -.
DR   PeptideAtlas; P38149; -.
DR   EnsemblFungi; YBR281C_mRNA; YBR281C; YBR281C.
DR   GeneID; 852584; -.
DR   KEGG; sce:YBR281C; -.
DR   AGR; SGD:S000000485; -.
DR   SGD; S000000485; DUG2.
DR   VEuPathDB; FungiDB:YBR281C; -.
DR   eggNOG; KOG2276; Eukaryota.
DR   HOGENOM; CLU_008535_0_0_1; -.
DR   InParanoid; P38149; -.
DR   OMA; HATVCVD; -.
DR   OrthoDB; 7832001at2759; -.
DR   BioCyc; MetaCyc:G3O-29201-MONOMER; -.
DR   BioCyc; YEAST:G3O-29201-MONOMER; -.
DR   BioGRID-ORCS; 852584; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38149; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38149; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0061672; C:glutathione hydrolase complex; IDA:ComplexPortal.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008242; F:omega peptidase activity; IGI:SGD.
DR   GO; GO:0008233; F:peptidase activity; IGI:SGD.
DR   GO; GO:0006751; P:glutathione catabolic process; IDA:ComplexPortal.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd05677; M20_dipept_like_DUG2_type; 1.
DR   FunFam; 2.130.10.10:FF:001401; Dug2p; 1.
DR   FunFam; 2.130.10.10:FF:001543; Dug2p; 1.
DR   FunFam; 3.30.70.360:FF:000029; Dug2p; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR051458; Cyt/Met_Dipeptidase.
DR   InterPro; IPR017149; GSH_degradosome_Dug2.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR020472; WD40_PAC1.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF8; DI- AND TRIPEPTIDASE DUG2-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PIRSF; PIRSF037237; Peptidase_WD_repeats_DUG2; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Dipeptidase; Hydrolase; Metal-binding; Metalloprotease; Nucleus;
KW   Protease; Reference proteome; Repeat; WD repeat; Zinc.
FT   CHAIN           1..878
FT                   /note="Probable di- and tripeptidase DUG2"
FT                   /id="PRO_0000051469"
FT   REPEAT          18..57
FT                   /note="WD 1"
FT   REPEAT          68..107
FT                   /note="WD 2"
FT   REPEAT          235..274
FT                   /note="WD 3"
FT   REPEAT          282..322
FT                   /note="WD 4"
FT   REPEAT          362..405
FT                   /note="WD 5"
FT   REPEAT          608..651
FT                   /note="WD 6"
FT   ACT_SITE        522
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        586
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         553
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         553
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         587
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         853
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   878 AA;  98071 MW;  A24C10BB4E94C344 CRC64;
     MYDSRGVALH SELIHRWNHA FSILSIVAFP KKRLLFAGSQ DSKILVFDLP TYNLIHTIRL
     GESQEETHTR SSVLCLTGSE DENFLFSGGA DSLVRIWSIG EKTIRDDFLP VTEIATVYSV
     TDIGDIFSLA YLDSLETIVF GCQNASLLYV ENLIQKIEKK SSDGVENINK LPHRRYDKFF
     DSLGPTGYSS NSLSQTSLTS LQENCGAAII EVPSENIIKY AHYGFIYSIN KLCPRFNQLL
     EKSSRTSGAE HIISSAGDGI SKLWEFSKDK GQNTVKISLI NDKIDNEDSV ISQTIEFPFL
     YCGLTDGIIK IWDLNTQQII STLKTKHESD VISISVYMDH VFAIDESGIT HFYQNQVNHW
     NPQQGKILSS EIFSKSNAGS VSLLTGGSDG SLTLWDITSL LSAVPLSSNS PINASSTLQT
     TNLWAAYQSA SLNNEEMLNT LRELISFQTV SQSKDTTNTL SLRRCAIYLQ QLFLKFGATN
     SQLFPLPDGG NPVVFAYFQG NGKVSQVKGA KKKRILWYGH YDVISSGNTF NWNTDPFTLT
     CENGYLKGRG VSDNKGPLVS AIHSVAYLFQ QGELVNDVVF LVEGSEEIGS ASLKQVCEKY
     HDIIGKDIDW ILLSNSTWVD QEHPCLNYGL RGVINAQIKV WSDKPDGHSG LNGGVYDEPM
     VNLVKIVSKL QNEQNEIMIP NFYSPLKDLT EEEYQRFQKI TELANIDENT TVQDLITNWT
     KPSLSMTTVK FSGPGNITVI PKSVTMGISI RLVPEQSVEQ VKRDLKAYLE ESFKQLKSQN
     HLEIKVLNEA EGWLGDPTNH AYQILKDEIT TAWDVEPLLV REGGSISCLR MLERIFDAPA
     VQIPCGQSTD NGHLANENLR IKNWSNLTEI LSKVFNRL
//