ID   URE2_KLUMA              Reviewed;         404 AA.
AC   Q8NJR4; Q8NJR3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Protein URE2;
GN   Name=URE2;
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 1 AND 2).
RC   STRAIN=B4425;
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; AF525168; AAM91941.1; -; Genomic_DNA.
DR   EMBL; AF525169; AAM91942.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJR4; -.
DR   SMR; Q8NJR4; -.
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..404
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186009"
FT   DOMAIN          162..246
FT                   /note="GST N-terminal"
FT   DOMAIN          255..404
FT                   /note="GST C-terminal"
FT   REGION          110..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         25
FT                   /note="N -> S (in allele 2)"
FT   VARIANT         77..81
FT                   /note="Missing (in allele 2)"
FT   VARIANT         107
FT                   /note="Missing (in allele 2)"
FT   VARIANT         126
FT                   /note="P -> A (in allele 2)"
SQ   SEQUENCE   404 AA;  46664 MW;  D4C6112E5677CE7E CRC64;
     MQQDMHNGGT GNTISNLSSA LRQVNLGNSN TTTDQSNIAI DFNQQQLMEE VNQNSMNAFN
     IQQQHQQQQE NVQKQQEQQQ QQLQQQQQQQ QQQQQQQQQQ QQQQQQLQQQ QQLQQHHHHQ
     QRQQHPNNNV QAGTSQQQML FQGANSIDSS RITKFFQNQP MEGYTLFSHR SAPNGFKVAI
     VLSELNMHYN TIFLDFNLGE HRAPEFVAIN PNARVPALID HNMDNLSIWE SGAIILHVVN
     KYYRETGTPL LWSDNLADQA QINAWLFFQT SGHAPMIGQA LHFRYFHSQK VKSAVDRYTD
     EVRRVYGVVE MALAERREAL IMDLDSENAA AYSAGTTPLS QSRFFDYPVW LVGDKITVAD
     LSFVPWNNVV DRIGINIKVE FPEVYKWTKH MMRRPAVIKA LRGE