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DUG1_CANAL
ID   DUG1_CANAL              Reviewed;         485 AA.
AC   Q5AKA5; A0A1D8PNX7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cys-Gly metallodipeptidase DUG1;
DE            EC=3.4.13.-;
DE   AltName: Full=Deficient in utilization of glutathione protein 1;
DE   AltName: Full=GSH degradosomal complex subunit DUG1;
GN   Name=DUG1; OrderedLocusNames=CAALFM_C504300CA;
GN   ORFNames=CaO19.11397, CaO19.3915;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 2091 / CBS 2730 / DSM 1665 / CIP 1180.79 / NBRC 1393;
RX   PubMed=18637841; DOI=10.1111/j.1567-1364.2008.00411.x;
RA   Klinke T., Rump A., Poenisch R., Schellenberger W., Mueller E.-C., Otto A.,
RA   Klimm W., Kriegel T.M.;
RT   "Identification and characterization of CaApe2 -- a neutral
RT   arginine/alanine/leucine-specific metallo-aminopeptidase from Candida
RT   albicans.";
RL   FEMS Yeast Res. 8:858-869(2008).
CC   -!- FUNCTION: Catalytic component of the GSH degradosomal complex involved
CC       in the degradation of glutathione (GSH) and other peptides containing a
CC       gamma-glu-X bond. Functions also as a dipeptidase with high specificity
CC       for Cys-Gly and no activity toward tri- or tetrapeptides (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Component of the GSH degradosomal complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AOW29838.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP017627; AOW29838.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_721825.2; XM_716732.2.
DR   AlphaFoldDB; Q5AKA5; -.
DR   SMR; Q5AKA5; -.
DR   STRING; 237561.Q5AKA5; -.
DR   MEROPS; M20.017; -.
DR   PRIDE; Q5AKA5; -.
DR   GeneID; 3636456; -.
DR   KEGG; cal:CAALFM_C504300CA; -.
DR   CGD; CAL0000193256; orf19.11397.
DR   eggNOG; KOG2276; Eukaryota.
DR   HOGENOM; CLU_029469_3_0_1; -.
DR   InParanoid; Q5AKA5; -.
DR   OrthoDB; 733473at2759; -.
DR   PRO; PR:Q5AKA5; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR017153; CNDP/DUG1.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Protease; Reference proteome; Zinc.
FT   CHAIN           1..485
FT                   /note="Cys-Gly metallodipeptidase DUG1"
FT                   /id="PRO_0000370248"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   485 AA;  53675 MW;  DB14D4579B568E62 CRC64;
     MSTSTTYEKL PLQPLFDTIE ELKPKFIERL QKAIAIPSVS SDESLRPKVV EMANFLVDEL
     KTLGFTDIQL KELGTQPPPV QDANLQLPPI VLGRFGNDPA KKTVLVYGHY DVQPALKDDG
     WKTEPFTMHY DKEKEILYGR GSTDDKGPVV GWLNVIEAHN KLGWELPVNL VVCFEGMEES
     GSLGLDELVA KEAQNYFKKV DQVTISDNYW LGTTKPVLTY GLRGCNYYQI IIEGPGADLH
     SGIFGGIIAE PMTDLIKVMS TLVDGSGKIL IPGVYDMVAP LTDKEDQLYD SIDFSVEELN
     AASGSQTSLH DNKKDILKHR WRFPSLSLHG IEGAFSGAGA KTVIPAKVVG KFSIRTVPDI
     ESKKLDDLVF QHITSEFKKL NSPNKFKVEL IHDGNYWVSD PFNDSFTAAA KATQDVWNVV
     PDFTREGGSI PITLTFEKEL GVDVLLLPMG RGDDGAHSIN EKLDVSNYIN GCKTLGGYLH
     YYGKA
 
 
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