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Database: UniProt
Entry: A0A165H1T5_9BASI
LinkDB: A0A165H1T5_9BASI
Original site: A0A165H1T5_9BASI 
ID   A0A165H1T5_9BASI        Unreviewed;       220 AA.
AC   A0A165H1T5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KZT58762.1};
GN   ORFNames=CALCODRAFT_432063 {ECO:0000313|EMBL:KZT58762.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58762.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT58762.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58762.1,
RC   ECO:0000313|Proteomes:UP000076842};
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).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; KV423947; KZT58762.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165H1T5; -.
DR   STRING; 1353952.A0A165H1T5; -.
DR   InParanoid; A0A165H1T5; -.
DR   OrthoDB; 1328078at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03048; GST_N_Ure2p_like; 1.
DR   Gene3D; 1.20.1050.130; -; 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; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF3; TRANSCRIPTIONAL REGULATOR URE2; 1.
DR   Pfam; PF00043; GST_C; 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:UP000076842};
KW   Transferase {ECO:0000313|EMBL:KZT58762.1}.
FT   DOMAIN          5..89
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          95..220
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   220 AA;  25274 MW;  AFDB52A7F9D3BB9C CRC64;
     MSDHKHFTLY TNVEAANGWK VAIVLRELGL TYDSVYLDFT KHEHKSPEYL KLNPNGRIPA
     LIDHENDDFV LWESDAILVY LVERYDTDHK LSAATDAERA LQNQWLFFQA SGQGPYFGQF
     FWFSFFHPEK IPSAVERYKK ETERVLSVLD SVLSKKEWLV ASKPTIADLS FVTWNNGAFA
     TIVGHDAVVD KFPAVYKWHM ALCSRPAVKS VTDLRTALQK
//
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