(data stored in ACNUC8465 zone)

SWISSPROT: C5DD52_LACTC

ID   C5DD52_LACTC            Unreviewed;       359 AA.
AC   C5DD52;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Protein URE2 {ECO:0000256|PIRNR:PIRNR037861};
GN   OrderedLocusNames=KLTH0B08360g {ECO:0000313|EMBL:CAR21713.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21713.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21713.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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|PIRNR:PIRNR037861, ECO:0000256|SAAS:SAAS01088318}.
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DR   EMBL; CU928166; CAR21713.1; -; Genomic_DNA.
DR   RefSeq; XP_002552151.1; XM_002552105.1.
DR   STRING; 381046.XP_002552151.1; -.
DR   EnsemblFungi; CAR21713; CAR21713; KLTH0B08360g.
DR   GeneID; 8290991; -.
DR   KEGG; lth:KLTH0B08360g; -.
DR   HOGENOM; HOG000125742; -.
DR   InParanoid; C5DD52; -.
DR   KO; K00799; -.
DR   OMA; KFFQNQP; -.
DR   OrthoDB; 1231780at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
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   Gene3D; 3.40.30.10; -; 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   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   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD52.
DR   SWISS-2DPAGE; C5DD52.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nitrate assimilation {ECO:0000256|PIRNR:PIRNR037861};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN          117..201
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          210..359
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          169..170
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   REGION          185..186
FT                   /note="Glutathione binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   COILED          51..92
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         129
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
FT   BINDING         156
FT                   /note="Glutathione"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037861-1"
SQ   SEQUENCE   359 AA;  40922 MW;  6F8571645F36FDF2 CRC64;
     MVGEKQTSVG GSVSAAVSNL SSALRQVNLG NSNTTTDQSN INIDFHNRMN RQQLMGEAQR
     NNLNAQQAEE LLRQQEAHQQ QQLQQAQQQQ QQQQQYVGPA QIDSSRISKF FQNQPEEGYT
     IFSHRSAPNG FKVSIVLSEL NLQYNTIFLD FNIGEHRAPD FVAINPNARV PALIDHSMDN
     LAIWESGAII LHLVNRYYRE TGEPLLWSEN MGEQAHITAW LFFQTSGHAP MIGQALHFRY
     FHSQKIQSAV DRYTDEVRRV YGVVEMALAE RREALIMELD TENAAAYSAG TTPLSRSRFF
     DYPVWLVGDK ITVADLSFVP WNNVVDRIGI NIKLEFPEVY KWTKHMMRRP AVIKALRGE
//

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