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 28-JUN-2023, entry version 95.
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 GeneID; 3636456; -.
DR KEGG; cal:CAALFM_C504300CA; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_029469_3_0_1; -.
DR InParanoid; Q5AKA5; -.
DR OrthoDB; 177966at2759; -.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 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
//
