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Database: UniProt
Entry: A0A165QLA9_9AGAM
LinkDB: A0A165QLA9_9AGAM
Original site: A0A165QLA9_9AGAM 
ID   A0A165QLA9_9AGAM        Unreviewed;       375 AA.
AC   A0A165QLA9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KZT22578.1};
GN   ORFNames=NEOLEDRAFT_642551 {ECO:0000313|EMBL:KZT22578.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT22578.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT22578.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT22578.1,
RC   ECO:0000313|Proteomes:UP000076761};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425594; KZT22578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165QLA9; -.
DR   STRING; 1314782.A0A165QLA9; -.
DR   InParanoid; A0A165QLA9; -.
DR   OrthoDB; 35622at2759; -.
DR   Proteomes; UP000076761; 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; 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:SF23; GLUTATHIONE S-TRANSFERASE (EUROFUNG); 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW   Transferase {ECO:0000313|EMBL:KZT22578.1}.
FT   DOMAIN          78..182
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13409"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        222
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   375 AA;  42639 MW;  8CB5C89A4F6B2603 CRC64;
     MPGADSFKAD VSQRTRVYNA ESSPSYSHPT FTHYARMSSS TNSKIHEEGT ADGWHGAISP
     DGPFPPEKGR YHLYIGLFCP FAHRANLVRY LKGLTDFIDI SIVKPYPKGD EKGWPGWQFP
     KDDQEYPHAT VDKLFGSKYM HKVYFKADKE YKGRYSVPVL WDKKTETIVN NESAELLRWL
     PTAFSPFLDP EHAKLDLYPE PLRTQIDSIS EWMQRDLNTG VYKAGFAGSQ AEYDKNVIPV
     FGALNKVEGL IASSGGPYVL GKTLTELDIR LYATVVRFDT VYVQHFKCNL GTIRHDYPVI
     NNWLKNLYWN VPGFSESTDF LHIKENYTKS HYDINPKAIT PMGPFPDVEE GVDDFSKLKV
     GAVKLPAVLE YQSKL
//
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