ID M7UIQ4_BOTF1 Unreviewed; 2159 AA.
AC M7UIQ4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Putative polyketide synthase protein {ECO:0000313|EMBL:EMR86678.1};
GN ORFNames=BcDW1_4687 {ECO:0000313|EMBL:EMR86678.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR86678.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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DR EMBL; KB707850; EMR86678.1; -; Genomic_DNA.
DR STRING; 1290391.M7UIQ4; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009403; P:toxin biosynthetic 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; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 393..826
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1661..1742
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1787..1864
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1745..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2159 AA; 236072 MW; 2996DB694AC0CF8E CRC64;
MSFLIFGDQS LDTHTFLTDF CQHGRPSMLS RSFLEQAGSA LREEIDRLPS LQRNTIPEFS
TILELNKLYH AGTIKNPAVD SALLCIAQLS QYIDRHEKEH GDSTIPSETC LVGLCTGLFA
AAAIASSPSI SQLIPIAVQV MLMSFRTGAY VAALANRLDS RPELPESWTY VVPAAQENEV
NSILGDFHKE NVRCNFLILP VIANSTKETP ILNQAYISAT TSKSIAISGP PSTLKSLFAS
EAFQAKPVSI PVYGPYHAAH LRSSLNVEQI LHLKDKKVRD VLGNLKTRFP VISCTTGTWY
TEQEPELLLQ AILLEMLTEP IIFNKILQGC VQKGKDFQGR ECLIIPFGPT SAAKVLAAVL
ESQTELDITL RSPQSGNQQA AKQKTSMEVS PGKCKLAIVG MAGRFPDAAS HEKLWELLEN
GLDVHREVPK DRFDVATHFD PTSKIRNTSH TPYGCWIENP GLFDPRFFNM SPREAYQTCP
MQRLGLATAY EALEMAGYVP NRTHSTKLDR IGTFYGQTSD DWREINAAQD VDTYFITGGV
RAFGPGRINY HFGFSGPSFN IDTACSSSAA ALQLACTSLW AGDCDTAVVG GLSCMTNPDI
FSGLSRGQFL SKNGPCATFD HDADGYCRAD GIGTVIIKRL DYALADKDNV LAVILGSATN
HSADAVSITH PHGGTQEILY KRILNNAGVD PNDIDYVEMH GTGTQAGDGT EMKSVTNVFA
PADRKRRPDQ PLYLGAVKAN VGHGEAASGV TALIKCLMML QKNAIPPHVG IKKTINQGFP
KDLAERNVHI AFKNTPLPRK KSGAPRRIFV NNFSAAGGNT GLLLEDAPDL PFRKADPRST
HVIAITAKSK SAMLNNAERL ISYLERNRDI NLADLAYTTT ARRIQHKWRM TVTASEVSEV
SPALKSKLHE QFIPVLPEPP KVAFLFTGQG SQYAAMGREL FENSCLFKET IMEFDNLATI
LGFPSFISLI DGSVTDAQGL SPVVVQLSIV CLEMTMAKLW ESWGVKPSVV IGHSLGEYAA
LNVAGILSAS DTIYLVGRRA QLLVERCTAG THAMLAVQGS RLAVTEALNE TGTSVNIACI
NSTRETVLSG EAAEVSSVSD KLCNSGFKCT QLKVPFAFHS AQVEPILDQF EKLATSVHFG
REKIPLISSL FGRCLNESED IDAAYLRNHA RQPVNFLDGL VSAQSSGVID EKTVWIEVGP
HPVCLGLIKA TVGTSTIAAP SLRRNESAYK TLSNSLSVLH TAGLEIDWNE YHRDFNDSVH
LLNLPTYAFD DKNYWIQYAG DWCLTKGQLP NKTSLQLEPP KPKLSTSTIH TVVSEHIDGD
VAVVTAQSDL ARADLRGVVT GHLVNGAMLC PSSLFADMSM TLCEYGYKLL RPDVKNLGVD
VGRMKVPKSL IADPDGKSQV ITLTATINAA NGRADLIFST GTDKTRVEHA NCQVYFGDTE
EYHADFQRTA YLIQSRIDWL QEAERSGKAS KINRGLAYKL FAALVDYDQK YQGMEEVILD
SMKMEATSRV VFQTTEKDGT FRCSPYWIDS VAHISGFIVN GSDAVDSREK VYISHGWDSL
KFSEPLSADK TYRSYVRMQQ RKDKTMAGDV YVFDGDTIIG MVGGLAFQAI PRKVLNMFLP
PVGVATAVST KPSHALREPQ ASKASNSKTV KKAQVTKANL SKVNEKLMSI TSQVMDILAA
EVGVKHDELV DNVAFTDLGA DSLMALTVCG RLREEMDIDI NSNEFINHPT IGAFKSFLSQ
FEGKPSVAYS EDPSSPVTTP SPGESVHDPQ DDSEFTDPSD DDISTIGAID SLGDVIRVTI
AEEMSVDVLE VASCPDLASL GMDSLMALTV LGRLREKTGL SLPPDLFQVN QTIRDIEKAL
KVEAPSKPKP KPKSKAPSDQ PRLSKPTASI AKPSMQSIPQ RIANSILLQG NLRKASKYLW
MVPDGGGSAT SYIEIPALSS DVAVFGLNSP YMKTPEEFTC GVVGMATHYI KEMKRRQPTG
PYTLSGWSAG GVIAYEIVSQ LTKNDEIVDK LILLDSPCPD IIEPLPSSLH RWFAEIGLLG
DGDPSKIPEW LLPHFAASVQ ALSTYMPEAI DPKKVPQVMA IWCEDGVCKL PTDPRPDPFP
YGHAQFLLDN RTDFGPNIWD KYLGNEKFVT RHMPGNHFSM MHTPHIKLLG DFMREALTM
//