ID   DHC1_ALTCI              Reviewed;         477 AA.
AC   A0A0N7D483;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Polyketide synthase-related protein Dhc1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000305};
DE   AltName: Full=Dehydrocurvularin biosynthesis protein 1 {ECO:0000303|PubMed:26493380};
GN   Name=Dhc1 {ECO:0000303|PubMed:26493380};
OS   Alternaria cinerariae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Sonchi.
OX   NCBI_TaxID=216837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 11784;
RX   PubMed=26493380; DOI=10.1002/cbic.201500428;
RA   Cochrane R.V., Gao Z., Lambkin G.R., Xu W., Winter J.M., Marcus S.L.,
RA   Tang Y., Vederas J.C.;
RT   "Comparison of 10,11-dehydrocurvularin polyketide synthases from Alternaria
RT   cinerariae and Aspergillus terreus highlights key structural motifs.";
RL   ChemBioChem 16:2479-2483(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 11784;
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Polyketide synthase-related protein; part of the gene cluster
CC       that mediates the biosynthesis of 10,11-dehydrocurvularin, a prevalent
CC       fungal phytotoxin with heat shock response and immune-modulatory
CC       activities (PubMed:26493380). The highly reducing polyketide synthase
CC       Dhc3 is responsible for biosynthesis up to the tetraketide stage
CC       (PubMed:26493380). The non-reducing polyketide synthase Dhc5 then
CC       conducts four additional chain extension cycles, producing the
CC       unreduced part of the nascent octaketide from C-1 to C-8 in 10,11-
CC       dehydrocurvularin (PubMed:26493380). The role of Dhc1 in 10,11-
CC       dehydrocurvularin biosynthesis has not been identified yet
CC       (PubMed:26493380). {ECO:0000269|PubMed:26493380}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:26493380}.
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DR   EMBL; KT271470; AKQ49199.1; -; mRNA.
DR   AlphaFoldDB; A0A0N7D483; -.
DR   SMR; A0A0N7D483; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..477
FT                   /note="Polyketide synthase-related protein Dhc1"
FT                   /id="PRO_0000438391"
FT   DOMAIN          34..112
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          161..322
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          410..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   477 AA;  51984 MW;  9BDEE7D09C8FA3F0 CRC64;
     MPKTPNGKLD RKSIAALLLR NAKRDMNGVV NDVEKMTVRE GELRLLWERV LPTLGDLRLG
     PSSDFFMCGG NSMLLMKLQK AIKETTGIRV STKDLYESST LRAMTHCVFD RANRADDDAA
     PIDWAVETSL PASLQTQIQD LATSSPPEAG GHGTNGTEVL LTGATSFLGS HLLRSLLSSP
     RVKKVHCVAV PADEQATLFS HDTRIVCYSG TLLSPTLGVT PQERRTLEQS VHVIVHAGAH
     GHCLNRFDSL RAPNLQSLHF LATLALPRCV TILFLSSSRV VLLSGDTAPA PASMRSYPPA
     VDGKDGYTAS KWAGEVFLEN LVAHVENVAS SASSPSVFWR SSLNVEVHRA CTLVSESAPN
     SDAMNAILRH SLDMRCAPRL ERAEGYLDFA PMESIVAKIT VHAVEMATAV QQQQQQQQRQ
     SQPPRDDAAD GSPTERARGL RIAITLAVSS RPWATLGRIW RGRMVGDPKN WIYKSGL