ID   NSCD_ARTOC              Reviewed;         436 AA.
AC   C5FM58;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=MCYG_03599;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
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 (By similarity).
CC       Neosartoricin C is a spirocyclic compound that is cyclized through the
CC       attack of C3 hydroxyl on C14, followed by dehydration (By similarity).
CC       On the other hand, neosartoricin D is a further cyclized compound in
CC       which attack of C2 on C14 in neosartoricin C results in the formation
CC       of the acetal-containing dioxabicyclo-octanone ring (By similarity).
CC       Both of these compounds are novel and possibly represent related
CC       metabolites of the gene cluster (By similarity).
CC       {ECO:0000250|UniProtKB:A1D8I8, ECO:0000250|UniProtKB:F2S700,
CC       ECO:0000305|PubMed:23368997, ECO:0000305|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; DS995703; EEQ30780.1; -; Genomic_DNA.
DR   RefSeq; XP_002848093.1; XM_002848047.1.
DR   AlphaFoldDB; C5FM58; -.
DR   SMR; C5FM58; -.
DR   STRING; 63405.XP_002848093.1; -.
DR   EnsemblFungi; EEQ30780; EEQ30780; MCYG_03599.
DR   GeneID; 9229415; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   OMA; TGIDCCK; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000002035; 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   InterPro; IPR012148; DMATS-type_fun.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; 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_0000437916"
SQ   SEQUENCE   436 AA;  49240 MW;  EEC22A9D92DD2C1B CRC64;
     MSSLPMFDSV SRFLPTANED EQFWWKLTGR HMARMMHEAG YPEDRQVECL LFHRFKVVPC
     LGPRPHSDKP WYKSRVGGGA ADGCPINYSW RFGTSDRKPH IRNFIEPLGA LTNTPADPLN
     EVATKALLRD YSMTLPNVDL ELFWTFAPHY RPRIIEKADM EKLAGASLLV GAEMSPDSRN
     IDIKAYMYPR VPSQTSQLLT TILPQAMRDA YGEDVCLDSL NLVRDFMTND PEGSQLTLTG
     TTGIDCCKLQ DTRVKIYVIT RNTSFDHIAA IMTLGGRRPI SEELLNQLRA LWFELKGAPA
     DFTSSEQLPA QTKPDGTKNP IVVPFYFDIQ PRLALPDVKA YVDVSTSPVS DLAAAEAVVR
     HLERHGSGQN PKAYMNVLQD ITPVEELETR KGALAFYSIA VKKNELDITS YFNPQVYKRY
     FAHEVQLNGQ RRSAFE