DUG1_SCHPO
ID DUG1_SCHPO Reviewed; 476 AA.
AC Q9P6I2; P78801;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cys-Gly metallodipeptidase dug1;
DE EC=3.4.13.-;
DE AltName: Full=GSH degradosomal complex subunit DUG1;
GN Name=dug1; ORFNames=SPBC1198.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-455.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP FUNCTION.
RX PubMed=19346245; DOI=10.1074/jbc.m808952200;
RA Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K.;
RT "Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces
RT cerevisiae and represents a novel family of Cys-Gly peptidases.";
RL J. Biol. Chem. 284:14493-14502(2009).
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. Has a Gly-Cys dipeptidase activity.
CC {ECO:0000269|PubMed:19346245}.
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:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13812.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAB91183.2; -; Genomic_DNA.
DR EMBL; D89150; BAA13812.1; ALT_FRAME; mRNA.
DR PIR; T42426; T42426.
DR RefSeq; NP_595077.2; NM_001020983.2.
DR AlphaFoldDB; Q9P6I2; -.
DR SMR; Q9P6I2; -.
DR BioGRID; 276203; 17.
DR STRING; 4896.SPBC1198.08.1; -.
DR MEROPS; M20.017; -.
DR iPTMnet; Q9P6I2; -.
DR MaxQB; Q9P6I2; -.
DR PaxDb; Q9P6I2; -.
DR PRIDE; Q9P6I2; -.
DR EnsemblFungi; SPBC1198.08.1; SPBC1198.08.1:pep; SPBC1198.08.
DR GeneID; 2539648; -.
DR KEGG; spo:SPBC1198.08; -.
DR PomBase; SPBC1198.08; dug1.
DR VEuPathDB; FungiDB:SPBC1198.08; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_029469_3_0_1; -.
DR InParanoid; Q9P6I2; -.
DR OMA; HITIPGF; -.
DR Reactome; R-SPO-174403; Glutathione synthesis and recycling.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR PRO; PR:Q9P6I2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; ISO:PomBase.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006751; P:glutathione catabolic process; ISO:PomBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..476
FT /note="Cys-Gly metallodipeptidase dug1"
FT /id="PRO_0000185274"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 439
FT /note="G -> D (in Ref. 3; BAA13812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52840 MW; 9C9FC76AAF752AEE CRC64;
MKMSLDKLYE VIDKKKDEFV TRLSRAVSIP SVSADVTLRP KVVEMADFVV SEFTKLGAKM
EKRDIGYHQM DGQDVPLPPI VLGQYGNDPS KKTVLIYNHF DVQPASLEDG WSTDPFTLTV
DNKGRMFGRG ATDDKGPLIG WISAIEAHKE LGIDFPVNLL MCFEGMEEYG SEGLEDLIRA
EAEKYFAKAD CVCISDTYWL GTKKPVLTYG LRGVCYFNIT VEGPSADLHS GVFGGTVHEP
MTDLVAIMST LVKPNGEILI PGIMDQVAEL TPTEDSIYDG IDYTMEDLKE AVGADISIYP
DPKRTLQHRW RYPTLSLHGI EGAFSGSGAK TVIPAKVIGK FSIRTVPNME SETVERLVKE
HVTKVFNSLN SKNKLAFNNM HSGSWWISSP DHWHYDVGKK ATERVYGITP DFVREGGSIP
VTVTFEQSLK KNVLLLPMGR GDDGAHSINE KLDLDNFLKG IKLFCTYVHE LASVSP
