ID   URE2_CANGA              Reviewed;         355 AA.
AC   Q8NJR5; Q6FP16;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Protein URE2;
GN   Name=URE2; OrderedLocusNames=CAGL0J07392g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=37A;
RX   PubMed=12177423; DOI=10.1073/pnas.162349599;
RA   Edskes H.K., Wickner R.B.;
RT   "Conservation of a portion of the S. cerevisiae Ure2p prion domain that
RT   interacts with the full-length protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Plays an important role in the cellular response to the
CC       nitrogen source. URE2 gene plays a major part in the repression of GLN1
CC       and GDH2 genes by glutamine, and is required for the inactivation of
CC       glutamine synthetase. URE2 gene product may catalytically inactivate
CC       GLN3 in response to an increase in the intracellular concentration of
CC       glutamine (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AF525167; AAM91940.1; -; Genomic_DNA.
DR   EMBL; CR380956; CAG60979.1; -; Genomic_DNA.
DR   RefSeq; XP_448028.1; XM_448028.1.
DR   AlphaFoldDB; Q8NJR5; -.
DR   SMR; Q8NJR5; -.
DR   STRING; 5478.XP_448028.1; -.
DR   EnsemblFungi; CAG60979; CAG60979; CAGL0J07392g.
DR   GeneID; 2889591; -.
DR   KEGG; cgr:CAGL0J07392g; -.
DR   CGD; CAL0129812; URE2.
DR   VEuPathDB; FungiDB:CAGL0J07392g; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; Q8NJR5; -.
DR   OMA; KFFQNQP; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EnsemblFungi.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:EnsemblFungi.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:EnsemblFungi.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0032447; P:protein urmylation; IEA:EnsemblFungi.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:EnsemblFungi.
DR   GO; GO:0010044; P:response to aluminum ion; IEA:EnsemblFungi.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017298; Ure2.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PIRSF; PIRSF037861; Prion_URE2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Nitrate assimilation; Reference proteome.
FT   CHAIN           1..355
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186005"
FT   DOMAIN          113..197
FT                   /note="GST N-terminal"
FT   DOMAIN          206..355
FT                   /note="GST C-terminal"
FT   CONFLICT        55
FT                   /note="N -> S (in Ref. 1; AAM91940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   355 AA;  40397 MW;  5CD40F1D37AC12AA CRC64;
     MGDSRNTGTI SNLSSALRQV NIGSGQDQKN INYEFSNGLN NNVNDNGNHN LVNTNEDNVN
     KDGSINTNMM SRQVPIQHTH GSQLLQQERM NEQQFNPMEY SRISKFFQNQ PMEGYTLFSH
     RSAPNGFKVS IVLSELGLQY NTIFLDFNLG EHRAPEFVSV NPNARVPALI DHGLENLAIW
     ESGAILLHLV NKFYKETGNP LLWSDDLADQ AQINAWLFFQ TSGHAPMIGQ ALHFRYFHTQ
     KIESAVERYT EEVRRVYGVI EMALAERREA LIMELDTDNA AAYSAGTTPL SQSRFFDYPV
     WLVGDKLTIA DLSFVPWNNV VDRIGINIKV EFPEVYKWTK HMMRRPAVIK ALRGE