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