ID   NSCD_TRIT1              Reviewed;         436 AA.
AC   F2S700;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 33.
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=TESG_06703;
OS   Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=647933;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112818;
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).
RN   [3]
RP   FUNCTION.
RX   PubMed=23368997; DOI=10.1021/ol303435y;
RA   Chooi Y.H., Fang J., Liu H., Filler S.G., Wang P., Tang Y.;
RT   "Genome mining of a prenylated and immunosuppressive polyketide from
RT   pathogenic fungi.";
RL   Org. Lett. 15:780-783(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,
CC       PubMed:23368997). The non-reducing polyketide synthase nscA probably
CC       synthesizes and cyclizes the decaketide backbone (By similarity). The
CC       hydrolase nscB then mediates the product release through hydrolysis
CC       followed by spontaneous decarboxylation (By similarity). The
CC       prenyltransferase nscD catalyzes the addition of the dimethylallyl
CC       group to the aromatic C5 (By similarity). The FAD-dependent
CC       monooxygenase nscC is then responsible for the stereospecific
CC       hydroxylation at C2 (By similarity). Neosartoricin B can be converted
CC       into two additional compounds neosartoricins C and D (PubMed:23758576).
CC       Neosartoricin C is a spirocyclic compound that is cyclized through the
CC       attack of C3 hydroxyl on C14, followed by dehydration
CC       (PubMed:23758576). On the other hand, neosartoricin D is a further
CC       cyclized compound in which attack of C2 on C14 in neosartoricin C
CC       results in the formation of the acetal-containing dioxabicyclo-octanone
CC       ring (PubMed:23758576). Both of these compounds are novel and possibly
CC       represent related metabolites of the gene cluster (PubMed:23758576).
CC       {ECO:0000250|UniProtKB:A1D8I8, ECO:0000269|PubMed:23758576,
CC       ECO:0000305|PubMed:23368997}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:23758576}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; GG698521; EGD99349.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2S700; -.
DR   SMR; F2S700; -.
DR   EnsemblFungi; EGD99349; EGD99349; TESG_06703.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000009172; 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..436
FT                   /note="Prenyltransferase nscD"
FT                   /id="PRO_0000437917"
SQ   SEQUENCE   436 AA;  49052 MW;  71DCC3C354EB9EAD CRC64;
     MTSVPIFESV SRFLPPANED EQYWWKITGQ HMARMMHEAG YPEDRQVECL LFHRFKVIPC
     LGPRPRSDTP WYKSRVGGGA ADGCPINYSW RFGTADRKPH IRNFIEPLGA LTNTPADPLN
     EVATKALLQD YSMTLPNVDL EAFWTFAPHY RPRIIEKADI EKLAGASLLV GAEMSPDSYT
     IDIKAYMYPR VPSQTSQLLT TILPQAMRDA YGENVCLDSL NFVHEFMTKD PQGSQLVLTG
     TTGIDCCKLQ DTRVKIYVIT RNTSFDHIAA IMTLGGRRPI SEELLGQLKA LWYELKGAPA
     ELPSSEQLPV QTKPDGSKNP IVVPFYFDIQ PRLALPDVKA YIDVSTSPVS DLAAANAVVR
     HLEQHGSGQN PKAYLNVLKD ITPVEELETQ KGVLAFYSVA VKKNELDITS YFNPQVYKRY
     FAHEVHLNGQ RRSVFE