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Database: UniProt
Entry: A0A0A1TSH6_9HYPO
LinkDB: A0A0A1TSH6_9HYPO
Original site: A0A0A1TSH6_9HYPO 
ID   A0A0A1TSH6_9HYPO        Unreviewed;       266 AA.
AC   A0A0A1TSH6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=VHEMI09982 {ECO:0000313|EMBL:CEJ94452.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ94452.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ94452.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000710};
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
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DR   EMBL; CDHN01000007; CEJ94452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TSH6; -.
DR   STRING; 1531966.A0A0A1TSH6; -.
DR   HOGENOM; CLU_011226_14_0_1; -.
DR   OrthoDB; 1404190at2759; -.
DR   Proteomes; UP000039046; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 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:UP000039046};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEJ94452.1}.
FT   DOMAIN          18..104
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          111..235
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   266 AA;  30411 MW;  CEDA0AFD3076C97A CRC64;
     MTSRIRQFAS QFITMATKSD ITLYTVNTPN GIKASILLEE LGLPYKVHAI KMGENEQKEP
     WFLEINPNGR IPALTDSWDD GKPIRIFESG SILQYLVDRY DKENKVSYPA GSREHWETTN
     WLMWQMGGLG PMQGQANHFK RYAPEKIEYG INRYVNESRR LYRTLDDHLA KSSSGFIVGD
     RLTIADISCW GWIAIAKWSG LDIDEFPNVK KWLFALRERP GFKKGASVPT PHTAFDFFDL
     TEEELEAKAA PSRAWIQKGM AADAKK
//
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