ID   G8C1Y3_TETPH            Unreviewed;       385 AA.
AC   G8C1Y3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Protein URE2 {ECO:0000256|PIRNR:PIRNR037861};
GN   Name=TPHA0O01950 {ECO:0000313|EMBL:CCE66161.1};
GN   OrderedLocusNames=TPHA_0O01950 {ECO:0000313|EMBL:CCE66161.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE66161.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE66161.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
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).
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; HE612870; CCE66161.1; -; Genomic_DNA.
DR   RefSeq; XP_003688595.1; XM_003688547.1.
DR   AlphaFoldDB; G8C1Y3; -.
DR   STRING; 1071381.G8C1Y3; -.
DR   GeneID; 11530566; -.
DR   KEGG; tpf:TPHA_0O01950; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_1_1; -.
DR   OMA; KFFQNQP; -.
DR   OrthoDB; 1404190at2759; -.
DR   Proteomes; UP000005666; Chromosome 15.
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:UP000005666}.
FT   DOMAIN          143..227
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          236..385
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          23..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         155
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         182
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         195..196
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         211..212
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
SQ   SEQUENCE   385 AA;  43897 MW;  4DC3C3549C2655B5 CRC64;
     MQNTNIGNVS QLSSALRHVN INNNESAGNM NKNGSNEILF GGNDMINNNG DNDKNNIMQQ
     QLNQQQSNQQ NGTEQQQDQQ LQQGHHTNAH QQVHLEDMLH PFTIQQQQQQ QQAQQQAQNI
     LGSEYNPAQH SRITQYFQNL PVEGYTLFSH RSAPNGYKVA CALSELGLQY NTFFLDFATG
     EHRAPEFVSL NPNARVPALI DHSLENLGIW ESGSIMLHLV NKYYKETGDP LLWSDNLAEQ
     SQINSWIFFQ TSGHAPMIGQ ALHFKYFHSQ KIPSAIERYT DEVRRVYGVL EVALAERREA
     LVMELDTENV ASYSAGTTPI SQSKFFDYPV WLVGENITIA DLSFLPWNNV IDRIGINIRV
     EFPEVYKWTK HMMRRPAIIQ ALRGE
//