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 17-JUN-2020, entry version 117. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 EuPathDB; FungiDB:SPBC1198.08; -. DR PomBase; SPBC1198.08; dug1. DR HOGENOM; CLU_029469_3_0_1; -. DR InParanoid; Q9P6I2; -. DR KO; K15428; -. DR OMA; HITIPGF; -. DR Reactome; R-SPO-174403; Glutathione synthesis and recycling. 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:0006751; P:glutathione catabolic process; ISO:PomBase. 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 METAL 99 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 133 FT /note="Zinc 1" FT /evidence="ECO:0000250" FT METAL 133 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 168 FT /note="Zinc 1" FT /evidence="ECO:0000250" FT METAL 196 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 446 FT /note="Zinc 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 //