GenomeNet

Database: UniProt
Entry: A0A423VMW5_9PEZI
LinkDB: A0A423VMW5_9PEZI
Original site: A0A423VMW5_9PEZI 
ID   A0A423VMW5_9PEZI        Unreviewed;       345 AA.
AC   A0A423VMW5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=GST N-terminal domain-containing protein {ECO:0000259|Pfam:PF13409};
GN   ORFNames=VSDG_07293 {ECO:0000313|EMBL:ROV92340.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV92340.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROV92340.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROV92340.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
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:ROV92340.1}.
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; LJZO01000038; ROV92340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423VMW5; -.
DR   STRING; 252740.A0A423VMW5; -.
DR   Proteomes; UP000284375; 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; IPR040079; Glutathione_S-Trfase.
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   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          46..150
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13409"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        47
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        191
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   345 AA;  39374 MW;  B6AC992ACFB88BF8 CRC64;
     MTSVRPTPTP VAEHLAGSTQ SWHGKITPDG PFKPEKDRYR LYIGLFCPFA HRANLVRHLK
     GLQDVIPVTV VKPYPKGDDE TGWPGWQFPS TDDEYPGANP DPIFGAKYVH ELYFKADPQY
     KGRYSVPVLW DTKTGTIVNN ESAELLRDLQ TGFDSILPED KAKLTLYPEH LRSKIDDISA
     WMQRDLNIGV YKAGFARTQE AYDKNVPVVF AALNKLESII AENGGPFIMG KELTELDVRA
     YATLVRFDTV YVQHFKCNLG TIRHDYPQIN NWLKKLYWNV PEFRKTTDFK HIKENYTKSH
     SDINPFAITP MGPWPDVEEG YEADLSKVKT GGVKMPLVLE LERKL
//
DBGET integrated database retrieval system