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Database: UniProt
Entry: A0A2G8RNP9_9APHY
LinkDB: A0A2G8RNP9_9APHY
Original site: A0A2G8RNP9_9APHY 
ID   A0A2G8RNP9_9APHY        Unreviewed;       368 AA.
AC   A0A2G8RNP9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=GST C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50405};
GN   ORFNames=GSI_14436 {ECO:0000313|EMBL:PIL23127.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL23127.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL23127.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL23127.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
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:PIL23127.1}.
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DR   EMBL; AYKW01000068; PIL23127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8RNP9; -.
DR   STRING; 1077348.A0A2G8RNP9; -.
DR   OrthoDB; 35622at2759; -.
DR   Proteomes; UP000230002; 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; 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; SFLDG01206; Xi.1; 1.
DR   SFLD; SFLDG01148; Xi_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT   DOMAIN          218..344
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        241
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   368 AA;  42123 MW;  64E184E53F841407 CRC64;
     MMIQPRSFLR IQPFRHHLAR PINTAPPGRS PILQHAYTPL TTPTLHLRTM ATRDVSHLSD
     ISKGKVETDG SFKRKASSFR NFIEKGGEFA PEKGRYHLYV SYACPWATRT LIVRKLKGLE
     DFIDVSVVSP KMGGNGWPFA NVDAFPGADV DPLYGSSHIK DLYLSAKPDY DGRFTVPVLW
     DKQKKTIVNN ESSEIIRMFN TVFNDQLPAD KAKLDLYPAP LRKEIDELNE WVYDTVNNGV
     YKSGFATTQQ AYEVAVVPLF QSLDKLEKIL QGKNYVIGDR LTEADVRLFV TIVRFDPVYV
     GHFKCNLHTI RDGYPAIHLW LRKLYWNNDA FSSTCNFDHI KTHYYWSHPH INPHRIVPVG
     PIPNILPL
//
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