ID   LUC7_FUSSX              Reviewed;         219 AA.
AC   A0A6J4B5J2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Glutathione S-transferase-like protein LUC7 {ECO:0000303|PubMed:32043422};
DE            EC=2.5.1.- {ECO:0000250|UniProtKB:S0EHD0};
DE   AltName: Full=Lucilactaene biosynthesis cluster protein 7 {ECO:0000303|PubMed:32043422};
GN   Name=LUC7 {ECO:0000303|PubMed:32043422};
OS   Fusarium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=29916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=RK97-94;
RX   PubMed=32043422; DOI=10.1080/09168451.2020.1725419;
RA   Kato S., Motoyama T., Futamura Y., Uramoto M., Nogawa T., Hayashi T.,
RA   Hirota H., Tanaka A., Takahashi-Ando N., Kamakura T., Osada H.;
RT   "Biosynthetic gene cluster identification and biological activity of
RT   lucilactaene from Fusarium sp. RK97-94.";
RL   Biosci. Biotechnol. Biochem. 84:1303-1307(2020).
CC   -!- FUNCTION: Glutathione S-transferase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of the mycotoxin lucilactaene
CC       and the lucilactaene-related compound NG-391 that act as cell cycle
CC       inhibitors with potent growth inhibitory activity against malarial
CC       parasites, moderate growth inhibitory activity against cancer cells,
CC       and no activity against bacteria and fungi (PubMed:32043422). Within
CC       the cluster, LUC5, LUC6, LUC2 and LUC1 are sufficient for lucilactaene
CC       production (Probable). The roles of the other LUC members are yet
CC       undetermined (Probable). {ECO:0000269|PubMed:32043422,
CC       ECO:0000305|PubMed:32043422}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; LC515193; BBQ09585.1; -; Genomic_DNA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..219
FT                   /note="Glutathione S-transferase-like protein LUC7"
FT                   /id="PRO_0000454640"
FT   DOMAIN          3..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          90..219
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   219 AA;  24623 MW;  2412FB75F8219D9D CRC64;
     MAPFGRLYSF MPNGRVFKIL AAATLNGLEI EITPYQHMVD NKTPEFRAKF PAGKVPAFEG
     ADGLLLPESD AIAQYLAQSG PYSEQLLGRD AATSAKIRQW ISFFDGEVYP HMLDLVIWRV
     GIAPFDQSTE TKALARLEFA LDVLEKHLDG RKWLVGDELT LADLTGASSL LWAFMHIIDA
     SERKRFPSVV AWYLRTIETE EVKEVFGPPN LIDVKRVHE