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P53871

- DUG3_YEAST

UniProt

P53871 - DUG3_YEAST

Protein

Probable glutamine amidotransferase DUG3

Gene

DUG3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activityBy similarity

    GO - Molecular functioni

    1. amidophosphoribosyltransferase activity Source: SGD
    2. omega peptidase activity Source: SGD
    3. peptidase activity Source: SGD

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. glutathione catabolic process Source: SGD
    3. proteolysis Source: GOC

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33202-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glutamine amidotransferase DUG3
    Alternative name(s):
    Deficient in utilization of glutathione protein 3
    GSH degradosomal complex subunit DUG3
    Gene namesi
    Name:DUG3
    Ordered Locus Names:YNL191W
    ORF Names:N1410
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL191w.
    SGDiS000005135. DUG3.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 357356Probable glutamine amidotransferase DUG3PRO_0000203401Add
    BLAST

    Proteomic databases

    MaxQBiP53871.
    PaxDbiP53871.
    PeptideAtlasiP53871.

    Expressioni

    Gene expression databases

    GenevestigatoriP53871.

    Interactioni

    Subunit structurei

    Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3.1 Publication

    Protein-protein interaction databases

    BioGridi35642. 5 interactions.
    DIPiDIP-3956N.
    IntActiP53871. 4 interactions.
    MINTiMINT-501795.
    STRINGi4932.YNL191W.

    Structurei

    3D structure databases

    ProteinModelPortaliP53871.
    SMRiP53871. Positions 46-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 260259Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DUG3 family.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0121.
    HOGENOMiHOG000256686.
    KOiK07008.
    OMAiMHNGGIS.
    OrthoDBiEOG7QNVX7.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR017932. GATase_2_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR026869. Put_GATase_2.
    [Graphical view]
    PfamiPF13230. GATase_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53871-1 [UniParc]FASTAAdd to Basket

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    MCRFLIFKGK QPIRLSHLLT RPAHSIINQS FDSRLRLDRR RPMNGDGFGV    50
    AYYPLDTELS EDGPCLFKAI TPAWNNQNLS TLAEKTKSDL VFAHVRASTY 100
    GVLSETNCHP FTYHSLCFMH NGGISNFKGI KRKLLNHIKD EYLNFIQGST 150
    DSECAFALFL DTLDKLGYDP KKQDGDFGNV ALRKAMLRTI DYIRDWTKEA 200
    NKDEAHVEPS LLNFAVTDGS TVVVSRYITS KTDEAASLHF SCGSSFVETS 250
    PGEYRVERLD RNQDVIMVAS EPLTFERGDW TAVPTNSILT IKKQTILLHP 300
    IIDEYYQEDP LYLRSSTLAE SKGLMGSIPL AKAVEKNVPP LEREGRTRPP 350
    TAVAHIA 357
    Length:357
    Mass (Da):40,181
    Last modified:October 1, 1996 - v1
    Checksum:iAFAAEFE7152CFE1A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71467 Genomic DNA. Translation: CAA96085.1.
    AY692717 Genomic DNA. Translation: AAT92736.1.
    BK006947 Genomic DNA. Translation: DAA10362.1.
    PIRiS63146.
    RefSeqiNP_014208.1. NM_001183029.1.

    Genome annotation databases

    EnsemblFungiiYNL191W; YNL191W; YNL191W.
    GeneIDi855530.
    KEGGisce:YNL191W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71467 Genomic DNA. Translation: CAA96085.1 .
    AY692717 Genomic DNA. Translation: AAT92736.1 .
    BK006947 Genomic DNA. Translation: DAA10362.1 .
    PIRi S63146.
    RefSeqi NP_014208.1. NM_001183029.1.

    3D structure databases

    ProteinModelPortali P53871.
    SMRi P53871. Positions 46-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35642. 5 interactions.
    DIPi DIP-3956N.
    IntActi P53871. 4 interactions.
    MINTi MINT-501795.
    STRINGi 4932.YNL191W.

    Proteomic databases

    MaxQBi P53871.
    PaxDbi P53871.
    PeptideAtlasi P53871.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL191W ; YNL191W ; YNL191W .
    GeneIDi 855530.
    KEGGi sce:YNL191W.

    Organism-specific databases

    CYGDi YNL191w.
    SGDi S000005135. DUG3.

    Phylogenomic databases

    eggNOGi COG0121.
    HOGENOMi HOG000256686.
    KOi K07008.
    OMAi MHNGGIS.
    OrthoDBi EOG7QNVX7.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33202-MONOMER.

    Miscellaneous databases

    NextBioi 979577.

    Gene expression databases

    Genevestigatori P53871.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR017932. GATase_2_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR026869. Put_GATase_2.
    [Graphical view ]
    Pfami PF13230. GATase_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae."
      Ganguli D., Kumar C., Bachhawat A.K.
      Genetics 175:1137-1151(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiDUG3_YEAST
    AccessioniPrimary (citable) accession number: P53871
    Secondary accession number(s): D6W0Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7300 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3