ID   URE2_CANMA              Reviewed;         328 AA.
AC   Q8NJR0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Protein URE2;
GN   Name=URE2;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B4430;
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).
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}.
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; AF525172; AAM91945.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJR0; -.
DR   SMR; Q8NJR0; -.
DR   OMA; KFFQNQP; -.
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.
FT   CHAIN           1..328
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186006"
FT   DOMAIN          86..170
FT                   /note="GST N-terminal"
FT   DOMAIN          179..328
FT                   /note="GST C-terminal"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  37345 MW;  A611CDCFB25F2726 CRC64;
     MNMSDQRIPQ NTGDNSNNSN SNNNNNNNNN THTISNLSAG LKSVSLTDQQ QNEVNLNLLQ
     QQLHRESSNQ QQQSRITQFF QNQPAEGYTL FSHRSAPNGF KVAIILSELN LPFNTIFLDF
     NNGEQRAPEF VTINPNARVP ALIDHFNENT SIWESGAIIL YLVSKYLKEN GECSLWSDNL
     IEQSQISSWL FFQTSGHAPM IGQALHFRYF HSCPVPSAVE RYTDEVRRVY GVVEMALAER
     REALIMDLDV ENAAAYSAGT TPLSQSRYFD YPVWLVGDRA TVADLSFVPW NNVVDRIGIN
     LKVEFPEVYK WTKYMMRRPA VIRALRGD