ID   URE2_SACPA              Reviewed;         359 AA.
AC   Q7LLZ8; Q96X44;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Protein URE2;
GN   Name=URE2;
OS   Saccharomyces paradoxus (Yeast) (Saccharomyces douglasii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=27291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YJM 498;
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 [GENOMIC DNA].
RA   Fernandez-Bellot E., Baudin-Baillieu A., Cullin C.;
RT   "Prion characteristics of the URE2 protein of various yeast species.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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; AF525165; AAM91938.1; -; Genomic_DNA.
DR   EMBL; AF260775; AAK51641.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7LLZ8; -.
DR   BMRB; Q7LLZ8; -.
DR   SMR; Q7LLZ8; -.
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..359
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186012"
FT   DOMAIN          117..201
FT                   /note="GST N-terminal"
FT   DOMAIN          210..359
FT                   /note="GST C-terminal"
FT   REGION          39..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  40658 MW;  A077EE2DEDA329C7 CRC64;
     MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS AGVNNNNNNS SSSNNNNNNN
     NNAQNNNSGR NGSQSNDNGN NIKDTLEQHR QQQQAFSDMS HVEYSRITKF FQEQPLEGYT
     LFSHRSAPNG FKVAIVLSEL GFHYNTIFLD FNLGEHRAPE FVSVNPNARV PALIDHGMDN
     LSIWESGAIL LHLVNKYYKE TGNPLLWSDD LADQSQINAW LFFQTSGHAP MIGQALHFRY
     FHSQKIASAV ERYTDEVRRV YGVVEMALAE RREALVMELD TENAAAYSAG TTPMSQSRFF
     DYPVWLVGDK LTIADLAFVP WNNVVDRIGI NIKIEFPEVY KWTKHMMRRP AVIKALRGE