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
//