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Database: UniProt
Entry: V2WU81_MONRO
LinkDB: V2WU81_MONRO
Original site: V2WU81_MONRO 
ID   V2WU81_MONRO            Unreviewed;       845 AA.
AC   V2WU81;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ESK85112.1};
GN   ORFNames=Moror_3606 {ECO:0000313|EMBL:ESK85112.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK85112.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK85112.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK85112.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK85112.1}.
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DR   EMBL; AWSO01001141; ESK85112.1; -; Genomic_DNA.
DR   RefSeq; XP_007855576.1; XM_007857385.1.
DR   AlphaFoldDB; V2WU81; -.
DR   STRING; 1381753.V2WU81; -.
DR   KEGG; mrr:Moror_3606; -.
DR   HOGENOM; CLU_000022_16_6_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          18..440
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   845 AA;  90582 MW;  5780246DC80C1B68 CRC64;
     MVSTSFSIAR PSYAITDPHA MAIVGISIAA PGGVDDGLDT EEFYEFLKSR GSGIITVPKD
     RWNAEAYHGT QPGKVVTTKG GFIPNFTLGD PQEFGITPAE AAQMSCSQTA ALHQAFNALQ
     RSGVDYRGTN TGVYIGCAGG GPPFDMDITE AGAYYMTGTS LAINANRISY VFDMTGPSMP
     VDTACSASLT AMHLAVQAIR NGECDQAVVA GVNVILSPLE TSSFSQLGVL SPDGISKSFD
     EDANGYARGD VVGAVVIKRH DLAVKDHDRI LATLVGSALT SCGSLMGSLT TPSPDAQTQA
     IKNAYADAGL VPSQADFVEL HGTGTIVGDQ IEANAAGACF SEGRDGREIV IGSVKSNVGH
     GEMGAYMSSL VKVVMMLDRK QLLPNGYFKK PSSKINFEKY NLRVPIKVED FVAHDRKQGL
     IASISSFGFG GSCGHTVLRE HDARPVLADY HGLNSAPYLF AVGGLTPRGV NSLIESYKAD
     YADVNPALLS EHLGSRARQS SWRSYAVGDS LSQVKFTEPV MVPKRAAPLI FCFSGQGPQH
     WQQGRDLFMK YSVFRESILA SDKIHTEYAG KSFLANSGLF LPNPPPDSIL AKSLSWPADM
     ISISIAFFQI ALFDLLIYLG LKPDAIVGHS IGETAVMYAS GAMSREMIVK IAIARGGALC
     LVDNNGGAMA AISGCDEQTI QDYINAVVEL SDNPRAGVTD SLYIAARNSP TDFGVSGAEY
     LVDALTSYID QWVSGVMARK LRVGTAVHSP YVDPCEAQYR QELYRIFSSY PGPHKPSIPV
     MSTVTAEFVK DEYTVDYLWD NMRQPVRFSD AIPKLMDKFG ESTTFVEIAP HPVLSQVCVF
     SLLHS
//
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