ID   FUS3_GIBF5              Reviewed;         210 AA.
AC   S0EHD0;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Glutathione S-transferase-like protein FUS3 {ECO:0000305};
DE            EC=2.5.1.- {ECO:0000305};
DE   AltName: Full=Fusarin biosynthesis protein 3 {ECO:0000303|PubMed:23932525};
GN   Name=FUS3 {ECO:0000303|PubMed:23932525}; ORFNames=FFUJ_10056;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   INDUCTION.
RX   PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA   Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA   Tudzynski B.;
RT   "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT   fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL   Mol. Microbiol. 77:972-994(2010).
RN   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA   Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA   Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT   "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT   insight into the complex regulation and fusarin biosynthetic pathway.";
RL   Chem. Biol. 20:1055-1066(2013).
CC   -!- FUNCTION: Glutathione S-transferase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of the mycotoxin fusarin C
CC       (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC       sufficient for fusarin production (PubMed:23932525). The other FUS
CC       cluster members are not essential for fusarin C biosynthesis
CC       (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC   -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC       GLN1 (PubMed:23932525). Moreover, components of the fungal-specific
CC       velvet complex VEL1, VEL2 and LAE1 act also as positive regulators of
CC       expression (PubMed:20572938, PubMed:23932525). Finally, expression is
CC       induced under acidic conditions in a PACC-independent manner
CC       (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC       ECO:0000269|PubMed:23932525}.
CC   -!- DISRUPTION PHENOTYPE: Does not alter fusarin C production
CC       (PubMed:23932525). {ECO:0000269|PubMed:23932525}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; HF679031; CCT73262.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EHD0; -.
DR   SMR; S0EHD0; -.
DR   STRING; 5127.CCT73262; -.
DR   EnsemblFungi; CCT73262; CCT73262; FFUJ_10056.
DR   VEuPathDB; FungiDB:FFUJ_10056; -.
DR   HOGENOM; CLU_011226_3_2_1; -.
DR   Proteomes; UP000016800; Chromosome 9.
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   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..210
FT                   /note="Glutathione S-transferase-like protein FUS3"
FT                   /id="PRO_0000437367"
FT   DOMAIN          1..74
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          80..206
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   210 AA;  23160 MW;  9659BA9CA2488B7D CRC64;
     MPNARVFKIL AAAKLNNIAL EIPAYQHGVT NKSAEFLLKF PAGKVPAFEG PDGFCLVESD
     AIAQYVAQSG PQASQLLGQD AMSSAKIRQW ISFFAEEIYP TVLDLVMWRV GLGAFDETTE
     TKALTQLVYG LSVLEKHLGT GALLVGDKLT LADLTGASTL LWAFMHIVDE PMRQQYPNVV
     AWYLKVVQNE EVEEVFGKPN FIEKRRLGAK