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}.
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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
//
