ID   NSCD_TRIVH              Reviewed;         442 AA.
AC   D4CZZ3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Prenyltransferase nscD {ECO:0000303|PubMed:23758576};
DE            EC=2.5.1.- {ECO:0000305|PubMed:23758576};
DE   AltName: Full=Neosartoricin B biosynthesis protein D {ECO:0000303|PubMed:23758576};
GN   Name=nscD {ECO:0000303|PubMed:23758576}; ORFNames=TRV_00387;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=23758576; DOI=10.1021/sb400048b;
RA   Yin W.B., Chooi Y.H., Smith A.R., Cacho R.A., Hu Y., White T.C., Tang Y.;
RT   "Discovery of cryptic polyketide metabolites from dermatophytes using
RT   heterologous expression in Aspergillus nidulans.";
RL   ACS Synth. Biol. 2:629-634(2013).
CC   -!- FUNCTION: Prenyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of neosartoricin B, a prenylated anthracenone that
CC       probably exhibits T-cell antiproliferative activity, suggestive of a
CC       physiological role as an immunosuppressive agent (PubMed:23758576). The
CC       non-reducing polyketide synthase nscA probably synthesizes and cyclizes
CC       the decaketide backbone (By similarity). The hydrolase nscB then
CC       mediates the product release through hydrolysis followed by spontaneous
CC       decarboxylation (By similarity). The prenyltransferase nscD catalyzes
CC       the addition of the dimethylallyl group to the aromatic C5 (By
CC       similarity). The FAD-dependent monooxygenase nscC is then responsible
CC       for the stereospecific hydroxylation at C2 (By similarity).
CC       Neosartoricin B can be converted into two additional compounds
CC       neosartoricins C and D (By similarity). Neosartoricin C is a
CC       spirocyclic compound that is cyclized through the attack of C3 hydroxyl
CC       on C14, followed by dehydration (By similarity). On the other hand,
CC       neosartoricin D is a further cyclized compound in which attack of C2 on
CC       C14 in neosartoricin C results in the formation of the acetal-
CC       containing dioxabicyclo-octanone ring (By similarity). Both of these
CC       compounds are novel and possibly represent related metabolites of the
CC       gene cluster (By similarity). {ECO:0000250|UniProtKB:A1D8I8,
CC       ECO:0000250|UniProtKB:F2S700, ECO:0000269|PubMed:23758576}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23758576}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; ACYE01000020; EFE44836.1; -; Genomic_DNA.
DR   RefSeq; XP_003025447.1; XM_003025401.1.
DR   AlphaFoldDB; D4CZZ3; -.
DR   SMR; D4CZZ3; -.
DR   EnsemblFungi; EFE44836; EFE44836; TRV_00387.
DR   GeneID; 9581673; -.
DR   KEGG; tve:TRV_00387; -.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..442
FT                   /note="Prenyltransferase nscD"
FT                   /id="PRO_0000437920"
SQ   SEQUENCE   442 AA;  49719 MW;  E3A3EA51A86C8361 CRC64;
     MSITTTMTSV PIFESVSRFL PPGNEDEQFW WKITGRHMAR MMHEAGYPED RQVECLLFHR
     FKVVPCLGPR PHSDTPWYKS RVGGGAADGC PINYSWRFGT SDRRPHNRNF IEPLGALTNT
     SADPLNEVAT KALLHDYSMT LPNVDLEAFW TFAPHYRPRI IEKADMEKLA GASLLVGAEM
     SPDSRTIDIK AYMYPRVPSQ TSQLLTTILP QAMRDAYGED VCLDSLNFVH DFMTKDPQGC
     QLVLTGTTGI DCCKLQDTRV KIYVITRNTS FDHIAAIMTL GGRRPISEEL LGQLKALWYE
     LKGAPAELPS SEQLPVQTKP DRSKNPIVVP FYFDIQPRLE LPDVKAYIDV STSPVSDLAA
     ANAVVCHLEQ HGSGQNPKAY LNVLKDITPV EALETQKGAL AFYSVAVKKN ELDITSYFNP
     QVYKRYFAHE VQLNGQRRSV FE