ID T0LTH3_COLGC Unreviewed; 2178 AA.
AC T0LTH3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_05047 {ECO:0000313|EMBL:EQB55056.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB55056.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB55056.1}.
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DR EMBL; AMYD01001015; EQB55056.1; -; Genomic_DNA.
DR STRING; 1237896.T0LTH3; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OMA; YCRGDGC; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000015530; 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 Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 381..813
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1664..1738
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1787..1864
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1629..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1862..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2178 AA; 236930 MW; EA135DB2C8AA3D46 CRC64;
MADKMSYLLF GDQSLDTHGF LAEFCRSGNP STLAKTFLEQ AGQALREEID GLGKLERSKL
PTFLTLRQLN ERYHAQSIKH PGIDSALLCI TQLAHYIDRT EKEPQDVCLH DQTFFMGLCT
GLFAAAAIAS TPSVSTLIPL AVQVVLMAFR TGTHVGSLAE RLSPPVGQSE PWTHILPGLK
EPEAKEALFN FHESNYIPVA SQAYVSAVSA SSLAISGPPA TLKALDDQNV FGVKSTAIPV
YGPYHAAHLH GTADIEKILR LDDPKVTEVL EKSKPRSAIM SGTKGIWFAE TSTKSLLQAV
AHECLVDVLQ FQKGIDGCIE TARDFEGSTC LVIPFGPTHN AETLQKTIKD RTQLDVIVRP
GPKIQRESYN SKIGNHGSAG KCKLAIVGMA GRFPDAASHE KLWELLAKGL DVHRVVPADR
FPVATHYDIT GKAVNTSHSQ YGCWIENPGY FDPRFFNMSP REAFQTDPMQ RMALTTAYEA
LEMCGYVPNR TPSTRLDRIG TFYGQTSDDW REINAAQEVD TYYITGGVRA FGPGRINYHF
GFSGPSLNID TACSSSAAAL NVACNSLWQK DCDTAIVGGL SCMTNPDIFA GLSRGQFLSK
TGPCATFDNG ADGYCRADGC ASVIVKRLED AIADKDNVLA VVLGTATNHS ADAISITHPH
GPTQSILSSA ILDDAGVDPL DVDYVEMHGT GTQAGDGTEM VSVTNVFAPA DRKRPADRPL
YLGAIKSNVG HGEAASGVTA LCKVLMMMQK NAIPPHVGIK KEINKTFPKD LSERNVNIAF
HLTPFKRRDG KPRRIFVNNF SAAGGNTGLL LEDAPHFKPA EVDARNVQVI TVTGKSKAAM
IRNAERLVAW MEQNPQTPLS HVAYTTTARR IQHYWRMNVA ASDLPEAQRL IKDRLKENFS
PISTQQPKVA FMFTGQGSHY AGLGKDLYAH YRVFRDSIDE FNQLAQIHGF PNFLPLIDGS
ESDVTKLSPV VVQLGLCCFE MALARLWASW GIKPSAVMGH SLGEYAALNA AGVLSASDTI
YLVGARAQLL VEKCTAGTHA MLAVTGPVDA VMEVLGSQSE AVNVACINGP RETVLSGAST
KVSEISSTLG AAGFKCTQLK VPFAFHSAQV DAILDDFETL ARSVSFEVPQ VPIISPLLGK
MVENEPINAA YLRNHARDAV NFLGGLVHAQ QSGSIDEKTV FLEIGPHPVC ANFVKSSFGI
SSIAVPTLRR NESTYKVLSN TLCTLHTAGI NLDWDEFHRD FSDCTRLLDL PTYSFDEKNY
WLQYTGDWCL TKNRGPAAVK APLQIEPAKP KLSTTSVHAI TNEDVKGDIA IIETETNLSR
PDTRPLVEGH LCNGAPLCPS TLYADMAMTI CDYAYKMLRP GTEDIGLNVA NVEVPKTLIF
DEKIDAHILR TTVTANAALG YADVSFHTGE GSKKVEHAHC KVVYGSTEQW ADEFERVTYL
IKGRVDALEE AERQGKASKI GRGLAYKLFN ALVDYDPKYQ GMEEVILDSK SCEATAKVTF
QTTDKDGSFF FNPYWIDSCC HISGFIINGT DAVDSREQVF ISHGWGSLRF TEKLDPKKSY
RSYIRMQPVK GTKMMAGDAY VFDGDRIIGV AGDVRFASIP RKVLNMVLPP RGRALAGAAP
APAAAAAKAA PAKAAPKEKA GKEKGTKQVT ASNLKTVNAK LAKRSVVQEV FDILAKEVGV
THDELADNIA FTDLGCDSLM ALTVSGRMRE ELDIDIDSHA FVEYPTIGAF KAFLAQFETA
DRKDSYVQDS GDSSGSVSET PELESDSNVT TPYEESDRSV KGEGDDEASG DLQNILRDTI
ATEMGVEVDE IVAAPDLAAL GMDSLMSLSI LGTLREKSGM DIPNDLFVTN PSLLEVEKAL
GIGPKPKPKA APPKPAPVRR EPKVQPTKEI NTHPGNTTAS ITKPPPPKEI VDNYPHRKAT
SILLQGSTRT ATKNLWMVPD GSGCATSYTE ISQVSSDWAV WGLFSPFMKT PEEYKCGVYG
MASKFIEAMK ARQAKGPYSL AGWSAGGVIA YEIVNQLTKA GETVDNLIII DAPCPITIEP
LPKSLHAWFA SIGLLGEGDD EAAKKIPSWL LPHFAASVTA LSNYTAEPIP KDKCPNVMAI
WCEDGVCHLP TDPRPDPYPT GHALFLLDNR TDFGPNRWDE YLDINRFRTR HMPGNHFSMM
HGDYAKMLGQ FIREAVCE
//
