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Database: UniProt
Entry: A0A2S6CNQ2_9PEZI
LinkDB: A0A2S6CNQ2_9PEZI
Original site: A0A2S6CNQ2_9PEZI 
ID   A0A2S6CNQ2_9PEZI        Unreviewed;       366 AA.
AC   A0A2S6CNQ2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=GST N-terminal domain-containing protein {ECO:0000259|Pfam:PF13409};
GN   ORFNames=CBER1_09444 {ECO:0000313|EMBL:PPJ61373.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ61373.1, ECO:0000313|Proteomes:UP000237631};
RN   [1] {ECO:0000313|Proteomes:UP000237631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA   de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA   Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA   Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT   "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT   mechanisms and extends production to the genus Colletotrichum.";
RL   bioRxiv 0:0-0(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPJ61373.1}.
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DR   EMBL; PNEN01000024; PPJ61373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6CNQ2; -.
DR   STRING; 357750.A0A2S6CNQ2; -.
DR   OrthoDB; 35622at2759; -.
DR   Proteomes; UP000237631; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   CDD; cd03190; GST_C_Omega_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR32419:SF23; GLUTATHIONE S-TRANSFERASE (EUROFUNG); 1.
DR   PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT   DOMAIN          42..150
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13409"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        190
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   366 AA;  42045 MW;  7F29517A6139D8D1 CRC64;
     MSTSTLPPSW HSGPEDSFHG KITADGPFQP EKDRYHLYIG LFCPFAHRAN LVVHLKQLQH
     YAGIETSIVR PYPKGNDQGW PGWRFNTSDS KDNYEGATED KLFGSKFMHE VYFKAEKEYE
     GRYSVPVLWD KKLNTIVNNE SHELLRDLQT AFNPLLPPEL ANITLYPEHF RPKIDALAPM
     LQRDLNTGVY KAGFALDQQT YEKNLPPVFA VLNLLEKLAS SNDGPYILGR ELTEVDIRVF
     CTLIRFDVAY VQHFKTNLSM IRYGYPTLHN WLKGLYWNNE AFEETTDFRH IKENYTKSHA
     GIKPRAITPV GPWPHIDKGY EEDWGGVRVG EVDHPEVKEY EKKLEEELKN AAPGSGHGGF
     SLDNFK
//
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