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 28-JUN-2023, entry version 103. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EnsemblFungi; C2_04710C_A-T; C2_04710C_A-T-p1; C2_04710C_A. 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; 1404190at2759; -. DR PRO; PR:Q96WL3; -. DR Proteomes; UP000000559; Chromosome 2. 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; IGI:CGD. DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IEA:EnsemblFungi. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0008104; P:protein localization; IGI:CGD. DR GO; GO:0032447; P:protein urmylation; IEA:EnsemblFungi. DR GO; GO:0006808; P:regulation of nitrogen utilization; IGI:CGD. DR CDD; cd10293; GST_C_Ure2p; 1. DR CDD; cd03048; GST_N_Ure2p_like; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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 PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1. DR PANTHER; PTHR44051:SF3; TRANSCRIPTIONAL REGULATOR URE2; 1. 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 SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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 //