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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
 
 
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