ID   H0GCX2_SACCK            Unreviewed;       878 AA.
AC   H0GCX2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Dug2p {ECO:0000313|EMBL:EHN08463.1};
GN   ORFNames=VIN7_0422 {ECO:0000313|EMBL:EHN08463.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN08463.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN08463.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN08463.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHN08463.1}.
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DR   EMBL; AGVY01000005; EHN08463.1; -; Genomic_DNA.
DR   HOGENOM; CLU_008535_0_0_1; -.
DR   PhylomeDB; H0GCX2; -.
DR   Proteomes; UP000009009; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR   CDD; cd05677; M20_dipept_like_DUG2_type; 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; 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; 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; PS50082; WD_REPEATS_2; 2.
PE   3: Inferred from homology;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          66..99
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          383..399
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          628..774
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   878 AA;  98235 MW;  6396B3A7915D4B2D CRC64;
     MYDSRGVALH SELIHRWNHA FSILSIVAFP KKRLLFAGSQ DSKILVFDLP TYNLIHTIRL
     GESQEETHTR SSVLCLTRSE DENFLFSGGA DSLVRIWSIG EKTIRDDFLP VTEIATVYSV
     TDIGDIFSLA YLDSLETIVF GCQNASLLYX ENLIQKIEKK SSDXVENINK LPHRRYDKFF
     DSLGPTGYSS NSLSQTSLTS LQENCGAAII EVPSENIIKY AHYGFIYSIN KLCPRFNQXL
     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
//