DUG2_YEAST
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 03-AUG-2022, entry version 183.
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=4; 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; 57.
DR ComplexPortal; CPX-325; Glutathione hydrolase complex.
DR DIP; DIP-1612N; -.
DR IntAct; P38149; 7.
DR MINT; P38149; -.
DR STRING; 4932.YBR281C; -.
DR iPTMnet; P38149; -.
DR MaxQB; P38149; -.
DR PaxDb; P38149; -.
DR PRIDE; P38149; -.
DR EnsemblFungi; YBR281C_mRNA; YBR281C; YBR281C.
DR GeneID; 852584; -.
DR KEGG; sce:YBR281C; -.
DR SGD; S000000485; DUG2.
DR VEuPathDB; FungiDB:YBR281C; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_008535_0_0_1; -.
DR InParanoid; P38149; -.
DR OMA; IDNKAEP; -.
DR BioCyc; MetaCyc:G3O-29201-MON; -.
DR BioCyc; YEAST:G3O-29201-MON; -.
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:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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:SGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF50978; SSF50978; 1.
DR SUPFAM; SSF55031; SSF55031; 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
