GenomeNet

Database: UniProt
Entry: M7UIQ4_BOTF1
LinkDB: M7UIQ4_BOTF1
Original site: M7UIQ4_BOTF1 
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
//
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