ID W3X8Z1_PESFW Unreviewed; 340 AA.
AC W3X8Z1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glutathione S-transferase omega-like 2 {ECO:0000313|EMBL:ETS82510.1};
GN ORFNames=PFICI_04386 {ECO:0000313|EMBL:ETS82510.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS82510.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; KI912111; ETS82510.1; -; Genomic_DNA.
DR RefSeq; XP_007831158.1; XM_007832967.1.
DR AlphaFoldDB; W3X8Z1; -.
DR STRING; 1229662.W3X8Z1; -.
DR GeneID; 19269399; -.
DR KEGG; pfy:PFICI_04386; -.
DR eggNOG; KOG2903; Eukaryota.
DR HOGENOM; CLU_037263_0_1_1; -.
DR InParanoid; W3X8Z1; -.
DR OMA; PWANRAI; -.
DR OrthoDB; 35622at2759; -.
DR Proteomes; UP000030651; 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; 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; IPR047047; GST_Omega-like_C.
DR InterPro; IPR016639; GST_Omega/GSH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR32419:SF6; GLUTATHIONE S-TRANSFERASE OMEGA-LIKE 1-RELATED; 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.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETS82510.1}.
FT DOMAIN 165..314
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT ACT_SITE 199
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ SEQUENCE 340 AA; 38929 MW; 7F6763767B755AE0 CRC64;
MSSSGTKITD WVKPGDKSGE FKRPASSFRD FISTEAGAKF PPEKGRYHLY VSYACPWACR
ALIARSIKGL EDFISFSVVH WHMGEKGWRF PTSEDTDAEG ENVIPDPVPG HEKITHLREI
YFAADPDYSG RFTVPVLYDK VQQTIVNNES SEILRMLGTV FNDQLPADKA AIDLYPEALR
KDIDEVGEWT YDQINNGVYK SGFATTQEAY EKNVVKLFEA LDRVEEHLKN GKGPYYFGDV
LTETDIRVFC TLIRFDPVYV QHFKCNIRDI RSGYPAIHKW MRNLYWNDPA FKKTTNFLHI
KNHYTKSHTQ INPFSIAPVG PLPDILPLDE EVPVVKAYKS
//
