ID DUG1_SCHPO Reviewed; 474 AA. AC Q9P6I2; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 30-NOV-2010, entry version 57. 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 (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] 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 RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] 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 RT Saccharomyces cerevisiae and represents a novel family of Cys-Gly RT peptidases."; RL J. Biol. Chem. 284:14493-14502(2009). CC -!- FUNCTION: Catalytic component of the GSH degradosomal complex CC involved in the degradation of glutathione (GSH) and other CC peptides containing a gamma-glu-X bond. Has a Gly-Cys dipeptidase CC activity. CC -!- COFACTOR: Zinc or manganese (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). Component of the GSH CC degradosomal complex (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the peptidase M20A family. 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; CAB91183.1; -; Genomic_DNA. DR RefSeq; NP_595077.1; NM_001020983.1. DR ProteinModelPortal; Q9P6I2; -. DR SMR; Q9P6I2; 2-472. DR STRING; Q9P6I2; -. DR MEROPS; M20.017; -. DR EnsemblFungi; SPBC1198.08-1; SPBC1198.08-1; SPBC1198.08. DR GeneID; 2539648; -. DR GenomeReviews; CU329671_GR; dug1. DR KEGG; spo:SPBC1198.08; -. DR NMPDR; fig|4896.1.peg.943; -. DR GeneDB_Spombe; SPBC1198.08; -. DR HOGENOM; HBG690347; -. DR OMA; ESFHKGI; -. DR OrthoDB; EOG92Z66C; -. DR PhylomeDB; Q9P6I2; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-003182-MONOMER; -. DR ArrayExpress; Q9P6I2; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_Spombe. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_Spombe. DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR017153; GSH_degradosome_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; PS00758; ARGE_DAPE_CPG2_1; FALSE_NEG. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Dipeptidase; Hydrolase; Manganese; KW Metal-binding; Metalloprotease; Protease; Zinc. FT CHAIN 1 474 Cys-Gly metallodipeptidase dug1. FT /FTId=PRO_0000185274. FT ACT_SITE 99 99 By similarity. FT ACT_SITE 165 165 Proton acceptor (By similarity). FT METAL 97 97 Zinc 2 (By similarity). FT METAL 131 131 Zinc 1 (By similarity). FT METAL 131 131 Zinc 2 (By similarity). FT METAL 166 166 Zinc 1 (By similarity). FT METAL 194 194 Zinc 2 (By similarity). FT METAL 444 444 Zinc 1 (By similarity). SQ SEQUENCE 474 AA; 52581 MW; 1F221F1FD9942298 CRC64; MSLDKLYEVI DKKKDEFVTR LSRAVSIPSV SADVTLRPKV VEMADFVVSE FTKLGAKMEK RDIGYHQMDG QDVPLPPIVL GQYGNDPSKK TVLIYNHFDV QPASLEDGWS TDPFTLTVDN KGRMFGRGAT DDKGPLIGWI SAIEAHKELG IDFPVNLLMC FEGMEEYGSE GLEDLIRAEA EKYFAKADCV CISDTYWLGT KKPVLTYGLR GVCYFNITVE GPSADLHSGV FGGTVHEPMT DLVAIMSTLV KPNGEILIPG IMDQVAELTP TEDSIYDGID YTMEDLKEAV GADISIYPDP KRTLQHRWRY PTLSLHGIEG AFSGSGAKTV IPAKVIGKFS IRTVPNMESE TVERLVKEHV TKVFNSLNSK NKLAFNNMHS GSWWISSPDH WHYDVGKKAT ERVYGITPDF VREGGSIPVT VTFEQSLKKN VLLLPMGRGD DGAHSINEKL DLDNFLKGIK LFCTYVHELA SVSP //