ID   NSCD_TRIEC              Reviewed;         436 AA.
AC   F2PWS6;
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=TEQG_05347;
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97;
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; DS995747; EGE06344.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PWS6; -.
DR   SMR; F2PWS6; -.
DR   STRING; 63418.F2PWS6; -.
DR   EnsemblFungi; EGE06344; EGE06344; TEQG_05347.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   Proteomes; UP000009169; 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_0000437918"
SQ   SEQUENCE   436 AA;  49026 MW;  71DA1FB354E43BAD CRC64;
     MTSVPIFESV SRFLPPANED EQYWWKITGQ HMARMMHEAG YPEDRQVECL LFHRFKVIPC
     LGPRPRSDTP WYKSRVGGGA ADGCPINYSW RFGTADRKPH IRNFIEPLGA LTNTPADPLN
     EVATKALLQD YSMTLPNVDL EAFWTFAPHY RPRIIEKADI EKLAGASLLV GAEMSPDSHT
     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