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Database: UniProt
Entry: Q6RKE5_COCHE
LinkDB: Q6RKE5_COCHE
Original site: Q6RKE5_COCHE 
ID   Q6RKE5_COCHE            Unreviewed;      1450 AA.
AC   Q6RKE5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AAR90274.1};
GN   Name=PKS20 {ECO:0000313|EMBL:AAR90274.1};
OS   Cochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris
OS   maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5016 {ECO:0000313|EMBL:AAR90274.1};
RN   [1] {ECO:0000313|EMBL:AAR90274.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C4 {ECO:0000313|EMBL:AAR90274.1};
RX   PubMed=14676319; DOI=10.1073/pnas.2532165100;
RA   Kroken S., Glass N.L., Taylor J.W., Yoder O.C., Turgeon B.G.;
RT   "Phylogenomic analysis of type I polyketide synthase genes in pathogenic
RT   and saprobic ascomycetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15670-15675(2003).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; AY495661; AAR90274.1; -; Genomic_DNA.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF24; NON-REDUCING POLYKETIDE SYNTHASE APTA-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 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; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          79..510
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1373..1450
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          118..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  159676 MW;  0D9D4E3F714E3978 CRC64;
     MNKIHIDNVV DDIVETLDLP SVSQQQQSLF AFRNSVILRT MMKNVENKCD GRITFTQRDL
     IKWTKRDESE AETPMSPKGS KLAVVGMXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXTHFDPTG QIQNTTQTSY MNHIDSPGLF DAGFFNISPK EAEQMDPMHR LALVTVYEAL
     EMSGYSPNRT RSTSSPRVGT YHGQASDDWR ELNASQNIGT YAVPSGERGF ANGRINYFFK
     FNGPSFNMDT ASSSGLAAVN AACSALWAGD VDIAIAGGLN VITDPDNSVS SEGSLFVSCG
     TMQSLGRAAD GYCRADGVGS VVIKRLDDAL ADNDKILATI LAANTNHSAD AISITHPHAP
     KQAQNYQRVM SQAGFSPLDV SYVELHGTGT QAGDREEAKS VSHIFAPVAP RRKKKYRLRL
     GAVKSNIGHG GVAAGIASFI KVLLMYQKSA IPPQIGVKKL NPTLPPDLEE RTIGLNWEYV
     EWPRPKTGSR LAIVNSFGAH GGNTTVLLSD GPVPSPVITD PRPSFPLTIS ARSKNSLKMN
     TETLLQYIND HEDAQLGDLS YTLTARRIHH PFRLATSVKD ISQANKFLSI EIEKMEQQQW
     VSTVPLKAPT VAFTFTGQGA FYVGMCSQLY SHCSSFREDV QRLDRLSQSF NLGFDSAIPI
     IDGAAGYSDT VDPVASQLAI VLVELALAHY WATLGIKPSM VMGHSSGEFA ALAVAGVISE
     LDALYLTTAR AKLMAKHCQV GTDTMLAVRC SIDRLEELLA GREQDYELAC INGESDLVIS
     GAKTQIQDLA SILATAGLKS TALNVPYAFH SVQMDPILES FAQLAENVTF KAPQIPVVSP
     LLAECIFDGK TLNHEYLRRA TREQVEVVGA LDAAQELGIA DADTVWIDIG PHMIAGGMVR
     NILTPNIVVP SVKRDEDNFS TLVSSLVTLH RAGVTPVWNK YFREHERAHQ VFHLPTYRWN
     DKTYWIPYLG TWTLDKAHIK ENLDKARQNK ALSGISGMGS KLKTSTIHSI VSETVGESTV
     SLVTLSDLLD HAFLEAVEGH RMNNHGVASS SIWADMAFTV GRYLHGLGYP KEKDFHMNVR
     DMEILYTQVA RSRKDGPQLI QLEATLDIHA RSVTIFLYNV SQDGIRDAKY YGSCKIQFEE
     AATWSKNWKR LEHLVRQRIQ ALDQLAIEGL ASKINRNMAY TLFKNVVTYA DHYRGMRSVV
     LKDYEAFADV TLNPDELGVW HTPPHWIEVC HLGGFILNGS DASNTDDFFY VTPGWETFRL
     ARPPHPGASC RSYVQMVSSE EDPKFWTGDV YILQGDTIIG MIGQMKFRQI NRILMDRFFS
     PSEIHGTAHA SSTSSKVKTI VPAAAGPVAK RTTPTIVHPA PVSVTAEKAE PANEENSLIA
     GAIDLILKET GVDASELKDD TTFMQIGVDS LMSLVLVEKF KNILKMEIKS SLFIECETVG
     VFKEWLEENQ
//
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