ID A5DX61_LODEL Unreviewed; 356 AA. AC A5DX61; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 22-FEB-2023, entry version 85. DE RecName: Full=Protein URE2 {ECO:0000256|PIRNR:PIRNR037861}; GN ORFNames=LELG_01948 {ECO:0000313|EMBL:EDK43769.1}; OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; OC Lodderomyces. OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43769.1, ECO:0000313|Proteomes:UP000001996}; RN [1] {ECO:0000313|EMBL:EDK43769.1, ECO:0000313|Proteomes:UP000001996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996}; RX PubMed=19465905; DOI=10.1038/nature08064; RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., 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., Brunke S., Costanzo M.C., RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M., RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R., RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J., RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., RA 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. {ECO:0000256|PIRNR:PIRNR037861}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037861}. CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|PIRNR:PIRNR037861}. 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; CH981525; EDK43769.1; -; Genomic_DNA. DR RefSeq; XP_001527119.1; XM_001527069.1. DR AlphaFoldDB; A5DX61; -. DR STRING; 379508.A5DX61; -. DR GeneID; 5234205; -. DR KEGG; lel:LELG_01948; -. DR VEuPathDB; FungiDB:LELG_01948; -. DR eggNOG; KOG0867; Eukaryota. DR HOGENOM; CLU_011226_14_1_1; -. DR InParanoid; A5DX61; -. DR OMA; KFFQNQP; -. DR OrthoDB; 1404190at2759; -. DR Proteomes; UP000001996; Unassembled WGS sequence. DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. 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 {ECO:0000256|ARBA:ARBA00023063, KW ECO:0000256|PIRNR:PIRNR037861}; KW Reference proteome {ECO:0000313|Proteomes:UP000001996}. FT DOMAIN 113..197 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 207..356 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 60..85 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..85 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 356 AA; 40631 MW; D122A1AB5CB1C856 CRC64; MSNEQNRQLN NANNNLHNPS NPHTISNLSA GLKSVSIADQ QQNDLNLKLL QQQLQNEAAA AGRGVGGLST HNDHHQQQQQ QLQQQQQQQQ QQQQQQQQQQ SRITQFFQNQ PTEGYTLFSH RSAPNGFKVA IILSELNLPF NTIFLDFNDG EQRAPEFVTI NPNARVPALI DHYNENTSIW ESGAIILYLV SKYIKENNGE CSLWSDNLVE QSQINSWLFF QTSGHAPMIG QALHFRYFHS VPVPSAVERY TDEVRRVYGV VEMALAERRE ALIMDMDVEN AAAYSAGTTP LSQSRYFDYP VWLVGDRATV ADLSFVPWNN VVDRIGINLK VEFPEVYKWT KYMMRRPAVI RALRGD //