ID   G0VHY8_NAUCC            Unreviewed;       357 AA.
AC   G0VHY8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-FEB-2023, entry version 60.
DE   RecName: Full=Protein URE2 {ECO:0000256|PIRNR:PIRNR037861};
GN   Name=NCAS0G01350 {ECO:0000313|EMBL:CCC71022.1};
GN   OrderedLocusNames=NCAS_0G01350 {ECO:0000313|EMBL:CCC71022.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71022.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC71022.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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; HE576758; CCC71022.1; -; Genomic_DNA.
DR   RefSeq; XP_003677375.1; XM_003677327.1.
DR   AlphaFoldDB; G0VHY8; -.
DR   STRING; 1064592.G0VHY8; -.
DR   GeneID; 11528613; -.
DR   KEGG; ncs:NCAS_0G01350; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   InParanoid; G0VHY8; -.
DR   OMA; KFFQNQP; -.
DR   OrthoDB; 1404190at2759; -.
DR   Proteomes; UP000001640; Chromosome 7.
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:UP000001640}.
FT   DOMAIN          115..199
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          208..357
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          26..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         154
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         167..168
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         183..184
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
SQ   SEQUENCE   357 AA;  40919 MW;  6300BD2343E9D88D CRC64;
     MNNLNGHTNQ ISNLSNALQQ VNIDNSNTTT DQSNINFDVS SNENSNHNSQ HNSDSNILEQ
     NYSNTESNRQ EQLQQQQQQQ QQQQQQQQQQ QQQHAPFGDI EYSRITKFFQ NQPMEGYTLF
     SHRSAPNGFK VAIILSELGL QYNTIFLDFN LGEHRAPEFV SVNPNARVPA LIDHSMDNLS
     IWESGAILLH LVNKYYKETG DPLLWSDDLA DQAQINAWLF FQTSGHAPMI GQALHFSYFH
     SQKIPSAIER YTDEVRRVYG VVEMALAERR EAMVMELDTD NAAAYSSGTT PMSQSRFFDY
     PVWLVGDKLT IADLAFVPWN NVVDRIGINI KTEFPEVYKW TKHMMRRPAV VKALRGE
//