ID   NSCD_TRIRC              Reviewed;         436 AA.
AC   F2T0M1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
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=TERG_08358;
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700661; EGD92143.1; -; Genomic_DNA.
DR   RefSeq; XP_003231060.1; XM_003231012.1.
DR   AlphaFoldDB; F2T0M1; -.
DR   SMR; F2T0M1; -.
DR   STRING; 559305.F2T0M1; -.
DR   EnsemblFungi; EGD92143; EGD92143; TERG_08358.
DR   GeneID; 10377340; -.
DR   VEuPathDB; FungiDB:TERG_08358; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_0_1; -.
DR   InParanoid; F2T0M1; -.
DR   Proteomes; UP000008864; 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   Reference proteome; Transferase.
FT   CHAIN           1..436
FT                   /note="Prenyltransferase nscD"
FT                   /id="PRO_0000437922"
SQ   SEQUENCE   436 AA;  49061 MW;  AA1FA03CDAFE0AA6 CRC64;
     MTSIPIFESV SRFLPPANED VQFWWKVTGR HMACMMHEAG YPEYRQVECL LFHRFKVIPC
     LGPRPHSDTP WYKSRVGGGA ADGCPINYSW RFGTIERKPH IRNFIEPLGA LTKTPADPLN
     EVATKALLQD YSMTLPNVDL EAFWTFAPHY RPRIIEKEDM EKLAGASLLV GAEMSPDSRT
     IDIKAYMYPR VPSQTSQLLT TILPQAMRDT YGEDVCLDSL NFVHDFMTND PQGSQLALTG
     TTGIDCCKLQ ETRVKIYVIT RNTSFDHIAA IMTLGGRRSI SGELLGQLKA LWYELKGAPA
     ELPSSEQLPV QTKPDGSRNP IVVPFYFDIQ PRLALPDVKA YIDVSTSPVS DLAAAKAVVR
     HLEQHGSGQN PKAYLNVLKD ITPVEELETQ KGALAFYSVA VKKNELDITS YFNPQVYKRY
     FAHEVQLNGQ RRSVFE