ID A0A135U5N4_9PEZI Unreviewed; 2181 AA.
AC A0A135U5N4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KXH55672.1};
GN ORFNames=CNYM01_12118 {ECO:0000313|EMBL:KXH55672.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH55672.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH55672.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH55672.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH55672.1}.
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DR EMBL; JEMN01000839; KXH55672.1; -; Genomic_DNA.
DR Proteomes; UP000070054; 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; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 381..813
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1666..1740
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1789..1866
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1630..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2181 AA; 237364 MW; 867FB445E5C60950 CRC64;
MADMMSYLLF GDQSLDTHGF LAEFCRSGNP STLAKTFLDQ AGQALREEID GLGKLERSKL
PTFLTLRQLN ERYHAQSIKH PGIDSALLCI TQLAHYIDRH EKEPQDVSVH EHTFFMGLCT
GLFAAAAIAS TPSVSTLIPL AVQVVLMAFR TGTHVGSLAE RLSPPVGQSE PWTHILPGLK
ESEAKEALTN FHESNYIPVA SQAYVSAVSA SSLAISGPPA TLKALEDQNV FGVKPTAIPV
YGPYHASHLH GTADIEKILR LNDPKVAEIL AKTKPRSAIM SGTKGIWFAE TDTKSLIKAV
THECLIDVLQ FQKGIEGCIE TARDFEGSTC LVIPFGPTHN AETLSKLIKD KTQLDVTVRP
GPRIQRESYN SPIGNHGSSG KCKLAIVGMA GRFPDAASHE KLWELLSKGL DVHRVVPADR
FPVATHYDIT GKAVNTSHSQ YGCWIENPGY FDPRFFNMSP REAFQTDPMQ RMALTTAYEA
LEMCGYVPNR TPSTRLDRIG TFYGQTSDDW REINAAQEVD TYYITGGVRA FGPGRINYHF
GFSGPSLNVD TACSSSAAAL NVACNSLWVK DCDTAIVGGL SCMTNPDIFA GLSRGQFLSK
TGPCATFDNG ADGYCRADGC ASVIVKRLDD AVADKDNILA VILGTATNHS ADAISITHPH
GPTQSILSRH ILDEAGVDPL DVDYVEMHGT GTQAGDGTEM LSVTNVFAPA DRKRAADRPL
YLGAVKSNIG HGEAASGVTA LTKVLMMMKK NAIPPHVGIK KEINKGFPKD LSERNVNIAF
HLTPFKRRDG KPRRIFVNNF SAAGGNTGLL LEDAPLVATA EADPRSVQVV TVTGKSKAAM
IRNAERLVGW MEQNPETPLA HVAYTTTARR IQHYWRMNVA ASDLPEAQRL LKDRLKENFT
PISTQQPKVA FMFTGQGSHY AGLGKDLYAH YHVFRDSIDE FNQLAQIHGF PSFLSLIDGS
EPDVTKLSPV VVQLGLCCFE MALTRLWASW GILPSAVMGH SLGEYAALNA AGVLSASDTI
YLVGARAQLL VQKCTAGTHA MLAVTGPVDA VMEALGAQAD AVNVACINGP RETVLSGAAA
KISEISSHLG TAGFKCTQLK VPFAFHSAQV DPILDDFETL ARSVSFDMPR VPIISPLLGK
MVEHEPVNAA YLRNHARDAV NFLGGLVHAQ QSGAVDEKTV WLEVGPHPVL ANFVKSSFGI
STIAVPTLRR NEPTYKILSN TLCALHTAGI NLDWDEFHRD FTNCTRLLDL PTYSFDEKNY
WLQYTGDWCL TKNRGPSAVK APLQIEPARP KLSTTSIHAV TNEDVKGDIA LIETETNLSR
PDTRPLVEGH LCNGAPLCPS TLYADMAMTV ADYAYKMLRP DTENIGLNVA NVEVPKTLIF
NEKLDAHILR TTVTANATLG YADVSFHTGE GAKKTEHATC KVVYGSTEQW ADEFERVSYL
IKGRIDALEE AERQGKASKI GRGLTYKLFT ALVDYDTKYQ GMEEVILDSK TCEATAKVSF
QTTDRDGNFF FNPYWIDSCC HISGFIINGT DAIDSREQVF ISHGWGSMRF TEKLDATKTY
RSYVRMQPVK GTKMMAGDAY VFDGDRIIGV AGDVKFQSIP RKVLNMVLPP RGRAAAGAAP
AVAAPAPKAA APAKAAPAKE KSGKEKASKQ VTASNLKAVN AKLSKRSVVQ DVFDILAKEV
GVTQDELADN IAFTDLGCDS LMALTVSGRM REELDIDIDS HAFVEYPTIG AFKVFLGQFE
SPDRKDSYVQ DSGDSSGSVS ETPELESDSN VTTPYEESDR SVKGDAEEED CDDLQHILRE
TIATEMGVEV EEIIAAPDLA ALGMDSLMSL SILGTLREKS GQDIPNDLFV TNPSLLEVEK
ALGIGPKPKA AAAPKPAKAA PVARREKVEP TREINTHPGN TTASITKPPP PREIIDNYPH
RKATSILLQG STRTATKNLW MVPDGSGCAT SYTEISQVSS QWAVWGLFSP FMKTPEEYKC
GVYGMASKFI EAMKARQPKG PYSLAGWSAG GVIAYEIVNQ LTKAGESVEN LIIIDAPCPI
TIEPLPKSLH AWFASIGLLG EGDDDNKKIP SWLLPHFAAS VTALSNYTAE PIPKDKCPNV
MAIWCEDGVC HLPSDPRPDP YPTGHALFLL DNRTDFGANR WDEYLDINKF RTRHMPGNHF
SMMHGDYAKQ LGQFIREAVC E
//
