ID Q6RKI8_BOTFU Unreviewed; 1988 AA.
AC Q6RKI8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AAR90248.1};
GN Name=PKS12 {ECO:0000313|EMBL:AAR90248.1};
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559 {ECO:0000313|EMBL:AAR90248.1};
RN [1] {ECO:0000313|EMBL:AAR90248.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B05.10 {ECO:0000313|EMBL:AAR90248.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY495617; AAR90248.1; -; Genomic_DNA.
DR ESTHER; botci-q6rki8; Thioesterase.
DR PHI-base; PHI:5280; -.
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; 1.
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 234..667
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1502..1583
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1628..1705
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1586..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1721..1736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1988 AA; 216864 MW; 04467D2091DBB74B CRC64;
MGDKMSFLIF GDQSLDTHTF LADFCQHGRP SMLSRSFLEQ AGSALREEID RLPSLQRNTI
PEFSTILELN KLYHAGTIKN PAVDSALLCI AQLSQYIDRH EKEHGDSTIP SETCLVGLCT
GLFAAAAIAS SPSISQLIPI AVQVMLMSFR TGAYVAALAN RLDSRPELPE SWTYVVPAAQ
ENEVNSILGP TSAAKVLAAV LESQTELDIT LRSPQSGNQQ AAKQKTSMEV SPGKCKLAIV
GMAGRFPDAA SHEKLWELLE NGLDVHREVP KDRFDVATHF DPTSKIRNTS HTPYGCWIEN
PGLFDPRFFN MSPREAYQTC PMQRLGLATA YEALEMAGYV PNRTHSTKLD RIGTFYGQTS
DDWREINAAQ DVDTYFITGG VRAFGPGRIN YHFGFSGPSF NIDTACSSSA AALQLACTSL
WAGDCDTAVV GGLSCMTNPD IFSGLSRGQF LSKNGPCATF DHDADGYCRA DGIGTVIIKR
LDYALADKDN VLAVILGSAT NHSADAVSIT HPHGGTQEIL YKRILNNAGV DPNDIDYVEM
HGTGTQAGDG TEMKSVTNVF APADRKRRPD QPLYLGAVKA NVGHGEAASG VTALIKCLMM
LQKNAIPPHV GIKKTINQGF PKDLAERNVH IAFKNTPLPR KKSGAPRRIF VNNFSAAGGN
TGLLLEDAPD LPFRKADPRS THVIAITAKS KSAMLNNAER LISYLERNRD INLADLAYTT
TARRIQHKWR MTVTASEVSE VSPALKSKLH EQFIPVLPEP PKVAFLFTGQ GSQYAAMGRE
LFENSCLFKE TIMEFDNLAT ILGFPSFISL IDGSVTDAQG LSPVVVQLSI VCLEMTMAKL
WESWGVKPSV VIGHSLGEYA ALNVAGILSA SDTIYLVGRR AQLLVERCTA GTHAMLAVQG
SRLAVTEALN ETGTSVNIAC INSTRETVLS GEAAEVSSVS DKLCNSGFKC TQLKVPFAFH
SAQVEPILDQ FEKLATSVHF GREKIPLISS LFGRCLNESE DIDAAYLRNH ARQPVNFLDG
LVSAQSSGVI DEKTVWIEVG PHPVCLGLIK ATVGTSTIAA PSLRRNESAY KTLSNSLSVL
HTAGLEIDWN EYHRDFNDSV HLLDLPTYAF DDKNYWIQYA GDWCLTKGQL PNKTSLQLEP
PKPKLSTSTI HTVVSEHIDG DVAVVTAQSD LARADLRGVV TGHLVNGAML CPSSLFADMS
MTLCEYGYKL LRPDVKNLGV DVGRMKVPKS LIADPDGKSQ VITLTATINA ANGRADLIFS
TGTDKTRVEH ANCQVYFGDT EEYHADFQRT AYLIQSRIDW LQEAERSGKA SKINRGLAYK
LFAALVDYDQ KYQGMEEVIL DSMKMEATSR VVFQTTEKDG TFRCSPYWID SVAHISGFIV
NGSDAVDSRE KVYISHGWDS LKFSEPLSAD KTYRSYVRMQ QRKDKTMAGD VYVFDGDTII
GMVGGLAFQA IPRKVLNMFL PPVGVATAVS TKPSHALREP QASKASNSKT VKKAQVTKAN
LSKVNEKLMS ITSQVMDILA AEVGVKHDEL VDNVAFTDLG ADSLMALTVC GRLREEMDID
INSNEFINHP TIGAFKSFLS QFEGKPSVAY SEDPSSPVTT PSPGESVHDP QDDSEFTDPS
DDDISTIGAI DSLGDVIRVT IAEEMSVDVL EVASCPDLAS LGMDSLMALT VLGRLREKTG
LSLPPDLFQV NQTIRDIEKA LKVEAPSKPK PKPKSKAPSD QPRLSKPTAS IAKPSMQSIP
QRIANSILLQ GNLRKASKYL WMVPDGGGSA TSYIEIPALS SDVAVFGLNS PYMKTPEEFT
CGVVGMATHY IKEMKRRQPT GPYTLSGWSA GGVIAYEIVS QLTKNDEVVD KLILLDSPCP
DIIEPLPSSL HRWFAEIGLL GDGDPSKIPE WLLPHFAASV QALSTYMPEA IDPKKVPQVM
AIWCEDGVCN LPTDPRPDPF PYGHAQFLLD NRTDFGPNIW DKYLGNENFV TRHMPGNHFS
MMHTPHVS
//
