ID   URE2_CANAL              Reviewed;         344 AA.
AC   Q96WL3; A0A1D8PHB4; Q59LH8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein URE2;
GN   Name=URE2; OrderedLocusNames=CAALFM_C204710CA;
GN   ORFNames=CaO19.155, CaO19.7794;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
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 (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Darlington;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; AF260777; AAK51643.2; -; Genomic_DNA.
DR   EMBL; AF525173; AAM91946.1; -; Genomic_DNA.
DR   EMBL; CP017624; AOW27495.1; -; Genomic_DNA.
DR   RefSeq; XP_710606.1; XM_705514.2.
DR   AlphaFoldDB; Q96WL3; -.
DR   SMR; Q96WL3; -.
DR   STRING; 237561.Q96WL3; -.
DR   PRIDE; Q96WL3; -.
DR   GeneID; 3647795; -.
DR   KEGG; cal:CAALFM_C204710CA; -.
DR   CGD; CAL0000198677; URE2.
DR   VEuPathDB; FungiDB:C2_04710C_A; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; Q96WL3; -.
DR   OrthoDB; 1231780at2759; -.
DR   PRO; PR:Q96WL3; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0003714; F:transcription corepressor activity; IGI:CGD.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; IGI:CGD.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IGI:CGD.
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..344
FT                   /note="Protein URE2"
FT                   /id="PRO_0000186004"
FT   DOMAIN          102..186
FT                   /note="GST N-terminal"
FT   DOMAIN          195..344
FT                   /note="GST C-terminal"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  39136 MW;  09D18470BF36C0CD CRC64;
     MMSTDQHIQQ NMNDNSNNSN NSNNNNTNNN NNNQSVNVNV NNTNNNTQTI SNLSAGLKSV
     SLTDQQQNEV NLNLLQQQLH QEASTQQQQS RITQFFQNQP TEGFTLFSHR SAPNGFKVAI
     ILSELNLPFN TFFLDFNNGE QRTPEFVTIN PNARVPALID HYNDNTSIWE SGAITLYLVS
     KYLKENGECS LWSNNLIEQS QISSWLFFQT SGHAPMIGQA LHFRYFHSCP VPSAVERYTD
     EVRRVYGVIE MALAERREAL IMDLDVENAA AYSAGTTPLS QSRFFDHPVW LVGDRTTVAD
     LSFVPWNNVV DRIGINLKVE FPEVYKWTKH MMQRPAVKRA LRGD