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URE2_SACBA
ID   URE2_SACBA              Reviewed;         345 AA.
AC   Q8NJR6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Protein URE2;
GN   Name=URE2;
OS   Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS   eubayanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YJM 562;
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}.
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DR   EMBL; AF525166; AAM91939.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJR6; -.
DR   BMRB; Q8NJR6; -.
DR   SMR; Q8NJR6; -.
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..345
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186010"
FT   DOMAIN          103..187
FT                   /note="GST N-terminal"
FT   DOMAIN          196..345
FT                   /note="GST C-terminal"
FT   REGION          22..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  39297 MW;  F8A71C8BB4AE3E91 CRC64;
     MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFP SGVNSNNSVQ NSNNGRNGTQ
     NNNNENSIKD TIEQHRQQQQ AFSDMSHVEY SRITKFFQEQ PLEGYTLFSH RSAPNGFKVA
     IVLSELGFHY NTIFLDFNLG EHRAPEFVSV NPNARVPALI DHNMDNLSIW ESGAILLHLV
     NKYYKETGNP LLWSDDLADQ SQINAWLFFQ TSGHAPMIGQ ALHFRYFHSQ KIASAVERYT
     DEVRRVYGVV EMALAERREA LVMELDTENA AAYSAGTTPM SQSRFFDYPV WLVGDKLTIA
     DLAFVPWNNV VDRIGINVKI EFPEVYKWTK HMMRRPAVIK ALRGE
 
 
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