ID M7U225_BOTF1 Unreviewed; 2585 AA.
AC M7U225;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative polyketide synthase protein {ECO:0000313|EMBL:EMR80653.1};
GN ORFNames=BcDW1_10746 {ECO:0000313|EMBL:EMR80653.1};
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:EMR80653.1, 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; KB708113; EMR80653.1; -; Genomic_DNA.
DR STRING; 1290391.M7U225; -.
DR HOGENOM; CLU_000022_6_2_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite 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; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013120; Far_NAD-bd.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 395..811
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1657..1734
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1612..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2585 AA; 285641 MW; 47AF72B5A9D6A69C CRC64;
MTTMIDPRSG LGADPVLLLF GPQALKFDAE SFKKLCIRER PHYQWVLETV TALSSEWNDI
SKANPSLQHY NGMEKLEQLK AWVSRGEISK HHSSFPLPNI LLSPLVVITQ LIQYWDFLIV
ALPDLKDADE LLTSITTNAE TLGLCTGMLS AFAVACSSSI KELQQYGAVA VRLAMLTGAF
VDAKEELVGL GEAAVSFSLS LNPTDSGIAL KEALRQFPEA YISLLTDEKR MTITTSEQTA
SSLIPQLKLA GIQATKLVLR GRFHWAKHQE DIESLIQSCT PKFQLPDASK MALPSRSNTG
GKYLMAGKLH EIALRSILVE QSQWYKTFSV AYSSHLLSSN ASCICFGTES CVPPTIARQL
GSRLIQVGGI DLSTSQLPGE LLGTHRTNAF ANIPDERVAV VGMACQLPGA EDLEEYWKIL
SSGKSQHTEI PQERFSMETA WREADSERKW FGNFVENYNT FDHKFFKKSP REMASTDPQH
RLMLQIAYQT VEQSGYFGSL NADKHIGCFL GVGNVDYEAN VACYPATAYS ATGNLKSFVA
GKISHYFGWT GPSLTIDTAC SSSSVSIHYA CRSILSGECN SALAGGINII TSPNWYHNLS
GASFLSPTGQ CKPFDAKGDG YCRGEGVGAV LLKKLSSAVA DGDQVLGVIS STGVYQNGND
TAITVPISDS LSDLFLHVLH KAKLEPKDIS VVEAHGTGTP VGDPAEYKGI QRVFGGPDSS
HKVSLTSVKG LIGHTECASG VASLLKVILM VQEGFIPPQA SFTSVNPNLG LTPDDKIEIS
AQLKPWEVEF RAALINNYGA SGSNASMVVT QAPKLISQIP SKLPSNRTYP FWFCGNDEHS
LRAYITKLLG FLRSQGTPGK DLSTSNLSFQ VSRQSNRSLD WALIFNCNSS SELQDKLAAH
LKGEKSITAI RTPSTRPVIL CFGGQVSTYV GLNQEIYDTI PLLRRYLDQC DAIFISMDLG
SIYPDIFQKS PVQDIVKLHS ILFALQYSTA KCWIDCGIKV AAAIGHSFGE LTALCVSNAL
PLKHAIEMIT GRAHLIQQKW TAERGCMMAV EADAANVNAL LAKSKNVAIA CYNGPRSFTL
AGTGKAIDSL EEMAKSDPTF SGVKLKKLNV TNAFHCHLVD PLMEDLEKFG MKLVFREPDF
PLETATEYEF TDKRDEKFVA RHLRSPVFFH HAVQRIAKKH PDATWLEAGS NSTVTTMASR
ALGSSGASSS HFQPINITSD NSFNFLAEAT SRLWKEGLRV LFWAHHPVQA SSYTPVILPP
YQFEKSKHWM DLKKAPKLEP LVVKTQTKEL PKGLTTFVGY QDEANHSALF QVNTKTERFA
RLVSGHVMAS VAAVCPGIFQ MELALDALMS LRPEFANLSF RPELQRMQHY HPLVPDDSKL
VWIEAISQDP QHLVWDWKIV ATKKIGSAST QHTSGAFAFR PANDTQLQAE LEGYERWVSR
KRCIRLLERR DADDVLQGRN IYRGFSQIID YKELYRHVNI IVGKDDESAG RVTKTHIAEP
WLDSILTDCF CQVAGIFVNL MTDRSDMTEG GIFVCDGIGR WFRSPKMGPD TQLDHWEVFA
LHHPESEKKY ISDVFVFDPR DGSLVEVILR ISYQWVAVDG IRKALSAPAP SGHHLPTVTP
APSQTSTPAP TLAPALVNGW KPQEKKKKKE KKVAVKQQRP DVIGKTREII CNLSGLEPDE
VKDNSDLIEL GIDSLMSMEL TREVNAAFQC LLDTAQLMDL TDFQSLVICI QTMLGLDSQE
LGNISEAHDT ASGESGEETA TNGTMNRKIN GVNSVVKGSA LSASIVLDAF QKASKATDEF
IVNGHLGTYY NEIMPKSTEL CVIYILDAFE VLGVNIRATA PGHKIERVPY LPKHQQLMNL
IYDLLCKDAR LIDINGSEII RTAVAPPTKS ADALLGELLR NAPVHAAEHK LTKLTGERFA
DCITGKADGL QLIFGTPEGR EIATDLYAKS PINGIWIQQA EYFLETLVAG LPKDGEPLCI
LEMGAGTGGT TIKMVQLLAR LGIPVKYTIT DLSSSLVVAA RKRFKQYKFL EFKVLDIEAA
PDSSLLHSQH IVLATNCVHA TRNLTISTTN IHKILRPDGF LLLIEMTEQV PWVDFIFGLL
EGWWLFNDGR QHALQPPTYW EKILSSVGFG HIDWTRGNRP EANIQRLIIA LADGSRYDPV
PKPHPPTAQM VLTKNTVRQT AIDVYAYEYS KEFFFEPRNL ISYPVHPSNE KYCVLVTGTT
GSLGSHIVAY FAQLPEVETV VCLNRLSMVD ATLRQQQSFA LRGISLDKIS MSKLRVIETD
TAKSMLGLPK STFQYLTDNV THIVHNAWPM SLTRTVSAYE SQFKVMRNLI ALSSEATSQR
PAPFKLGFQF ISSIGVIGYY PLWTGKVLAP EESMPVDSVL PVGYADAKLV CERMLDETLH
RYPEHFRPMA VRIAQIAGST INGYWNPVEH FASFLKSSQT LNILPDLKGT LSWCTVQDVA
ATLGELLISN TPPYPIYHIE NPSRQPWPDM IMVLANELGI PSNNIVPFDE WLSRVRRFPG
STNDNPAGQL VEFFDKHFVR MSCGGLILDT VKSQEHSKTI RSTGPVSIDL VRKYILSWKS
SGFLS
//
