URE2_PICGU
ID URE2_PICGU Reviewed; 301 AA.
AC A5DDU4; Q8NJR1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein URE2;
GN Name=URE2; ORFNames=PGUG_01445;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B3163;
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 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; AF525171; AAM91944.2; -; Genomic_DNA.
DR EMBL; CH408156; EDK37347.2; -; Genomic_DNA.
DR RefSeq; XP_001485774.1; XM_001485724.1.
DR AlphaFoldDB; A5DDU4; -.
DR SMR; A5DDU4; -.
DR STRING; 4929.XP_001485774.1; -.
DR EnsemblFungi; EDK37347; EDK37347; PGUG_01445.
DR GeneID; 5127596; -.
DR KEGG; pgu:PGUG_01445; -.
DR VEuPathDB; FungiDB:PGUG_01445; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_1_1; -.
DR InParanoid; A5DDU4; -.
DR OMA; KFFQNQP; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..301
FT /note="Protein URE2"
FT /id="PRO_0000295038"
FT DOMAIN 59..143
FT /note="GST N-terminal"
FT DOMAIN 152..301
FT /note="GST C-terminal"
SQ SEQUENCE 301 AA; 34109 MW; 9FB0FB73D4A76126 CRC64;
MSGAHTISHL SAGLKSVNIG DQQQNEANLN LLQQQLENEA TSQTQQSRIT QFFAQQPSDG
YTLFSHRSAP NGFKVAIILS ELELPFNTIF LDFNHGEQRA PEFVTINPNA RVPALIDHFN
DNTSIWESGA IILYLVSKYL RDNGECALWS DNIVEQSQIS SWLFFQTSGH APMIGQALHF
RYFHSCPVPS AVERYTDEVR RVYGVIEMAL AERREALIMD LDVENAAAYS AGTTPLSQSR
YFDYPVWLVG DRATVADLSF VPWNNVVDRI GINLKVEFPE VYKWTKYMMR RPAVIRALRG
D