ID   URE2_KLULA              Reviewed;         389 AA.
AC   Q96X43; Q6CQ56;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Protein URE2;
GN   Name=URE2; OrderedLocusNames=KLLA0D19624g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; AF260776; AAK51642.1; -; Genomic_DNA.
DR   EMBL; CR382124; CAH01029.1; -; Genomic_DNA.
DR   RefSeq; XP_453933.1; XM_453933.1.
DR   AlphaFoldDB; Q96X43; -.
DR   SMR; Q96X43; -.
DR   STRING; 28985.XP_453933.1; -.
DR   EnsemblFungi; CAH01029; CAH01029; KLLA0_D19624g.
DR   GeneID; 2893111; -.
DR   KEGG; kla:KLLA0_D19624g; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; Q96X43; -.
DR   OMA; KFFQNQP; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:EnsemblFungi.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:EnsemblFungi.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:EnsemblFungi.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0032447; P:protein urmylation; IEA:EnsemblFungi.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:EnsemblFungi.
DR   GO; GO:0010044; P:response to aluminum ion; IEA:EnsemblFungi.
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; Reference proteome.
FT   CHAIN           1..389
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186008"
FT   DOMAIN          147..231
FT                   /note="GST N-terminal"
FT   DOMAIN          240..389
FT                   /note="GST C-terminal"
SQ   SEQUENCE   389 AA;  44395 MW;  CF4C33F844FBFB65 CRC64;
     MQQDMQNGGP GNTISNLSSA LRQVNLGNSN TTTDQSNISI DFNQQQLLEE ANQGSINAYN
     AQQQQQEHLQ QQAQQQQLHM QQLQQAQQQQ AQQQAHQQQQ QVHQVQHQHV QQDHMPIGQS
     QQQAMYQGPN PIDSSRITKF FQNQPMEGYT LFSHRSAPNG FKVAIVLSEL NMHYNTIFLD
     FNLGEHRAPE FVAINPNARV PALIDHNMEN LSIWESGAII LHVVNKHYKE TGNPLLWSDS
     LADQAQINAW LFFQTSGHAP MIGQALHFRY FHSQKVKSAV DRYTDEVRRV YGVVEMALAE
     RREALIMDLD SENAAAYSAG TTPLSQSRFF DYPVWLVGDK ITVADLSFVP WNNVVDRIGI
     NIKVEFPEVY KWTKHMMRRP AVIKALRGE