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Database: UniProt
Entry: A0A2P8A3Z7_9PEZI
LinkDB: A0A2P8A3Z7_9PEZI
Original site: A0A2P8A3Z7_9PEZI 
ID   A0A2P8A3Z7_9PEZI        Unreviewed;       221 AA.
AC   A0A2P8A3Z7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=B9Z65_2569 {ECO:0000313|EMBL:PSK55180.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK55180.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK55180.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK55180.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003494}.
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:PSK55180.1}.
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DR   EMBL; NHZQ01000067; PSK55180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8A3Z7; -.
DR   STRING; 40998.A0A2P8A3Z7; -.
DR   Proteomes; UP000243723; Unassembled WGS sequence.
DR   CDD; cd03053; GST_N_Phi; 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; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43900:SF98; GLUTATHIONE S-TRANSFERASE 2; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 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:UP000243723}.
FT   DOMAIN          2..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          96..221
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   221 AA;  24987 MW;  B12C1091FCADEB85 CRC64;
     MAPIKLYGML QSTCTQRVIL TCSELSIAYE LIEVNMMKGE HQALSYTSAH HPFGRVPALE
     DDDVKLFESR AICAYLLAKS ALSGGTAKVS DVNGKSPVAL GKFQEAASVE YSYFDPAMKG
     LAFEKMFKGF MGKGEADQEV VETLTAQLKK TLDLYEQRLK GQDYLTGKDF TLIDLYHVPW
     VAFMPRIGLE NEITSRPNFE AWWKRINERQ SWKDLQVKMA H
//
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