ID   A0A2G5IEA1_CERBT        Unreviewed;       950 AA.
AC   A0A2G5IEA1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Polyketide synthase PksJ {ECO:0000313|EMBL:PIB02793.1};
GN   ORFNames=CB0940_11777 {ECO:0000313|EMBL:PIB02793.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB02793.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIB02793.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIB02793.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIB02793.1}.
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DR   EMBL; LKMD01000099; PIB02793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5IEA1; -.
DR   OrthoDB; 3149897at2759; -.
DR   Proteomes; UP000230605; Chromosome 10.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   PANTHER; PTHR24096:SF428; DIDEMETHYLASTERRIQUINONE D SYNTHETASE TDIA-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
FT   DOMAIN          572..652
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   950 AA;  105192 MW;  ECE9770A8D402B43 CRC64;
     MIKMASTVQT LLDLLRQSAE SGTDAGIVAY PLHNTVEARR ITYSQLLSEC RRRASLLARQ
     RGFTRGGIIL LQFNDHLDNI VWFWTVLLAG CIPALSSPLP NDLDQRRQHL DHLNKLFDAP
     ICLTRQTSFA DFAVCPSLSL LAIDAIEAQT SNNDKHIDYL PIPTPTPSDL AALMLTSGST
     GNAKAVELTH QQILSSISGK DSVTKLHNNS PPISLLNWIG LDHVAALTET HLLAMYRNLN
     QIHIQPPDIV SDPLLLLRMI TKHRVARTVA PNFLLAALLK SIEQADEKEL DSIDLSTLTQ
     FVSGGEANPV KLCAKLDEVL QKFGAPAGVL QPAFGMTETC AGCTYNVESP EMDVESGMDF
     ASLGKPVGGF EVRVIGRGEE EDSTEQLGQR GILQIRGPMV FSRYYNNPIA TAEAFTEDGW
     FDTGDEAIID SAGRLHLVGR IKDQIRINGV SIVASDLESQ LNALSLSGAQ DGFFAAFGYR
     STPTSDESLA ILYLPTWTED DIQRQTTHSA IVQSVMRSHG IAPYVLPVDN TILQKSTLGK
     LSRGKLRRAL EQGKLRSYEQ ANAAKSASVA VEPRNELEAR LLRIFREALE HSLDLSTLDI
     VTPWFNLGIT SIQLIRLKRK IELGLELAEV PLVKLLKCST IEELAVELQP RRRRDSVTDL
     DVEIEEEAPS AAYDPVVKLR TQGSKAPLWL FHPGVGEVLV FIDMAKEVTD RPVYALRARG
     FDPGEGFFNS IEEAVDTYYR AIKKQQPHGP YALAGYSYGA MLAFETAKRL NNDGNGNQVQ
     FLASFNLPPH IKFRMRQLDW RACALHLGHF LGLLHDPDLD DNPGGTGPAD HASTVKAIFD
     NAPQQRLSEL SLTPANFQHW ANLAHEMQSM ARDYEPGGRV SKMDVFYCHP LAVVAQSKQE
     WLDNHLSRWN DFASDVRCHE VGGEHYTMID TNHVQSFMET FTKALSDRGV
//