ID A0A179G8R8_METCM Unreviewed; 488 AA.
AC A0A179G8R8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glutathione s-transferase {ECO:0000313|EMBL:OAQ74204.1};
GN ORFNames=VFPPC_01758 {ECO:0000313|EMBL:OAQ74204.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ74204.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ74204.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ74204.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
CC -!- SIMILARITY: Belongs to the asaB hydroxylase/desaturase family.
CC {ECO:0000256|ARBA:ARBA00023604}.
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:OAQ74204.1}.
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DR EMBL; LSBJ02000001; OAQ74204.1; -; Genomic_DNA.
DR RefSeq; XP_018150287.1; XM_018281530.1.
DR AlphaFoldDB; A0A179G8R8; -.
DR STRING; 1380566.A0A179G8R8; -.
DR GeneID; 28845524; -.
DR KEGG; pchm:VFPPC_01758; -.
DR OrthoDB; 2383386at2759; -.
DR Proteomes; UP000078397; Chromosome 1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR044053; AsaB-like.
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 NCBIfam; NF041278; CmcJ_NvfI_EfuI; 1.
DR PANTHER; PTHR34598; BLL6449 PROTEIN; 1.
DR PANTHER; PTHR34598:SF3; OXIDOREDUCTASE AN1597; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAQ74204.1}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..219
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 488 AA; 56088 MW; E24D9333B4BA6F24 CRC64;
MVLQLYIDPA SVNCHKVVAA LDYMGTPYEI KHTDYMKGEH KTAEYAKINP NATLPSATDD
GVAITQSNAI MQYAADKNGG SSAYPTDPKQ RALVNCWLHW EASGWFRSNY VYLVENILKG
ISSMAPDQET LAAEEPNWLK LANVLNDQLG KTKYVVGDDI TIADFAIMAP MHLYQIQKLP
LDKVPNIQRW IGDIEKIPAW QSSQAYVNKV FGLDSDRYVR ATLNYTKYSD DRSTEVYFYE
DERAADAHHP GDDAQEVSIH DGWDRKGEYS EDKHGFSLHE FKSTYPRDKW QDETLVKEKF
YPEVAEFVKN TVGAARVLVF DHTIRTKVNE AKKLTDESQT SQRAPVRLVH CDYTSESGPL
RVRQLLGDEA DDLLSRRVAF LNVWKPLAKV EEMPLAMCDI TSSPKEDFFK LFLRYRDRTG
ENYVMRYSPE HRWVYFPDMD ENHCIILKTY ESDESRARFV GHSAFEDPTS KPDAPYRESV
EIRTIAFF
//
