ID   NSCD_ARTGP              Reviewed;         436 AA.
AC   E4V2N3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
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=MGYG_06589;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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; DS989827; EFR03595.1; -; Genomic_DNA.
DR   RefSeq; XP_003170603.1; XM_003170555.1.
DR   AlphaFoldDB; E4V2N3; -.
DR   SMR; E4V2N3; -.
DR   STRING; 63402.XP_003170603.1; -.
DR   EnsemblFungi; EFR03595; EFR03595; MGYG_06589.
DR   GeneID; 10025842; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_0_1; -.
DR   InParanoid; E4V2N3; -.
DR   OMA; TGIDCCK; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000002669; 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_0000437921"
SQ   SEQUENCE   436 AA;  49123 MW;  6488C2DA4DD9893B CRC64;
     MASLPIFDSV SRFLPLTNED EQFWWRLTGQ HMARMMHEAG YPEDRQVECL LFHRFKVVPC
     LGPRPHSDIP WYKSRVGGGA ADGCPINYSW RFGTADRKPH IRNFIEPLGT LTNTPADRLN
     EVATKALLQD YAMTLPNVDL ELFWTFAPHY RPRIIEKADM EKLAGASLLV GAEMSPDSRT
     IDIKAYMYPR VPSQTSQLLT TILPQAMRDA YGEDVCLDSL NLVRDFMTSD PQGSQLTLTG
     TTGIDCCKLQ DTRVKIYVIT RNTSFDHISA IMTLGGRRPI SKELLSQLQT LWYELKGAPA
     ELPSSEQLPA QTKPDGSKNP IVVPFYFDIQ PRLALPDVKA YIDVSTSPVS DLAAAKAVVR
     HLEHHGSGQN PQAYLNVLQD ITPVEELETQ KGALAFYSVA VKKNELDITS YFNPQVYKRY
     FAHEVQLNGQ RRSAFE