ID A7TM75_VANPO Unreviewed; 398 AA.
AC A7TM75;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 22-FEB-2023, entry version 78.
DE RecName: Full=Protein URE2 {ECO:0000256|PIRNR:PIRNR037861};
GN ORFNames=Kpol_529p22 {ECO:0000313|EMBL:EDO16642.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO16642.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480420; EDO16642.1; -; Genomic_DNA.
DR RefSeq; XP_001644500.1; XM_001644450.1.
DR AlphaFoldDB; A7TM75; -.
DR STRING; 436907.A7TM75; -.
DR GeneID; 5544801; -.
DR KEGG; vpo:Kpol_529p22; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_1_1; -.
DR InParanoid; A7TM75; -.
DR OMA; KFFQNQP; -.
DR OrthoDB; 1404190at2759; -.
DR PhylomeDB; A7TM75; -.
DR Proteomes; UP000000267; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR037861};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT DOMAIN 156..240
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 249..398
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT COILED 86..132
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 168
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT BINDING 195
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT BINDING 208..209
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT BINDING 224..225
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
SQ SEQUENCE 398 AA; 45870 MW; 7987EE7B48FAE98E CRC64;
MQSNLNPDEI NRNSNKNGVN VSQLSSALRH VNISNSNTTT DQSNIHFESS GRENVLQTHP
QQQYQSQEVH LEDMIHPISV QQQVSNQNLN EQQVRQQQAQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQN QEMFNAAFNP NQNSRITQFF QNQPMEGYTL FSHRSAPNGY KVSMVLSELG
LNYNTIFLDF SSGEHRAPEF VSVNPNARVP ALIDHGLDNL GIWESGAILL HLVNKYYKET
GEPLLWADNL SDQSQINAWL FFQTSGHAPM IGQALHFRYF HSQKIPSAIE RYTDEVRRVY
GVLEVALAER REAVVMELDT ENAASYSAGT TPISQSRFFD YPVWLVGDNI TIADISFLPW
NNVIDRIGIN IRVEFPEVYK WTKNMMRRPA IIQALRGE
//
