ID   URE2_DEBHA              Reviewed;         308 AA.
AC   Q6BM74;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Protein URE2;
GN   Name=URE2; OrderedLocusNames=DEHA2F07744g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89036.2; -; Genomic_DNA.
DR   RefSeq; XP_460697.2; XM_460697.1.
DR   AlphaFoldDB; Q6BM74; -.
DR   SMR; Q6BM74; -.
DR   STRING; 4959.XP_460697.2; -.
DR   EnsemblFungi; CAG89036; CAG89036; DEHA2F07744g.
DR   GeneID; 2903499; -.
DR   KEGG; dha:DEHA2F07744g; -.
DR   VEuPathDB; FungiDB:DEHA2F07744g; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; Q6BM74; -.
DR   OMA; KFFQNQP; -.
DR   OrthoDB; 1231780at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro.
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..308
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186007"
FT   DOMAIN          66..150
FT                   /note="GST N-terminal"
FT   DOMAIN          159..308
FT                   /note="GST C-terminal"
SQ   SEQUENCE   308 AA;  34996 MW;  E3A5570EDC3D311E CRC64;
     MTNNNSNSNN NQTISNLSAG LKSVNLADQQ QNEVNLNLLQ QQLQNEATTQ QSQSRISQFF
     QNQPTEGYTL FSHRSAPNGF KVAIILSELN LPFNTIFLDF NNGEQRAPEF VTINPNARVP
     ALIDHFNENT SIWESGAIIL YLVSKYLKDN GECALWSDNL IEQSQISSWL FFQTSGHAPM
     IGQALHFRYF HSCPVPSAVE RYTDEVRRVY GVIEMALAER REALIMDLDV ENAAAYSAGT
     TPLSQSRYFD YPVWLVGDRA TVADLSFVPW NNVVDRIGIN LKVEFPEVYK WTKYMMRRPA
     VIRALRGD