ID   URE2_ASHGO              Reviewed;         354 AA.
AC   Q8NJR2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Protein URE2;
GN   Name=URE2; OrderedLocusNames=ABL195C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8717 / IMI 31268;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AF525170; AAM91943.1; -; Genomic_DNA.
DR   EMBL; AE016815; AAS50576.1; -; Genomic_DNA.
DR   RefSeq; NP_982752.1; NM_208105.1.
DR   AlphaFoldDB; Q8NJR2; -.
DR   SMR; Q8NJR2; -.
DR   STRING; 33169.AAS50576; -.
DR   EnsemblFungi; AAS50576; AAS50576; AGOS_ABL195C.
DR   GeneID; 4618831; -.
DR   KEGG; ago:AGOS_ABL195C; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; Q8NJR2; -.
DR   OMA; KFFQNQP; -.
DR   Proteomes; UP000000591; Chromosome II.
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..354
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186003"
FT   DOMAIN          112..196
FT                   /note="GST N-terminal"
FT   DOMAIN          205..354
FT                   /note="GST C-terminal"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39044 MW;  B8ECBEB2979F3329 CRC64;
     MQQEIRNSNT PNTGSGNPVS NLSSALRQVH LGNSNTTTDQ SNISIDYTSR APQQQPLDEL
     SRGAAGGPAA GGGPEGSNMV GASSAAQVTA FGGPSVVDSS RITKFFQNQP MEGYTLFSHR
     SAPNGFKVAI VLSEMGLNYN TIFLDFNLGE HRAPEFVAIN PNARVPALID HSLDNLSLWE
     SGAIILHLAN KYYRETGTPL LWSDNLAEQA QINSWLFFQT SGHAPMIGQA LHFRYFHSQK
     VPSAVERYTD EVRRVYGVVE MALAERREAL IMDLDSENAA AYSAGTTPLT QSRFFDYPVW
     LVGDHITIAD LSFVPWNNVV DRIGINIKVE FPEVYKWTKH MMRRPAVIKA LRGE