ID A0A165QAD1_9APHY Unreviewed; 307 AA.
AC A0A165QAD1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KZT69209.1};
GN ORFNames=DAEQUDRAFT_727121 {ECO:0000313|EMBL:KZT69209.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT69209.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT69209.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT69209.1,
RC ECO:0000313|Proteomes:UP000076727};
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; KV429060; KZT69209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QAD1; -.
DR STRING; 1314783.A0A165QAD1; -.
DR OrthoDB; 35622at2759; -.
DR Proteomes; UP000076727; 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; IPR040079; Glutathione_S-Trfase.
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; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01206; Xi.1; 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:UP000076727};
KW Transferase {ECO:0000313|EMBL:KZT69209.1}.
FT DOMAIN 144..281
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT ACT_SITE 41
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT ACT_SITE 178
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ SEQUENCE 307 AA; 35451 MW; CDB02A16D2713F33 CRC64;
MKTGQDGSFD RKPSQFRSWI EKGGKFEPEK GRYHLYVSYA CPWATRTLIM RKLKGLEDFI
DVSVVSPHMG QHGWPFASAD AFPGTDDDPL YGAQHIKDLY LRVAPDYDGR FTVPVLWDKH
THTIVNNESS EIIRMFNAAF NHLLPADKAQ LDYYPEHVRK EIDDVNDWVY DTVNNGVYKS
GFATSQAAYE KAVYPLFASL DRLEKLLTGK HYLVGDQLTE ADIRLFVTIV RFDPVYVGHF
KCNIRTIRDG YPAIHSWLRK LYWTVPAFKE TCNFEHIKTH YYWSHPTVNP HRIIPVGPVP
DILPLDA
//
