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Database: UniProt
Entry: A0A135TJV2_9PEZI
LinkDB: A0A135TJV2_9PEZI
Original site: A0A135TJV2_9PEZI 
ID   A0A135TJV2_9PEZI        Unreviewed;      2481 AA.
AC   A0A135TJV2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:KXH48441.1};
GN   ORFNames=CSIM01_04820 {ECO:0000313|EMBL:KXH48441.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH48441.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH48441.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH48441.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
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:KXH48441.1}.
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DR   EMBL; JFBX01000132; KXH48441.1; -; Genomic_DNA.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000070328; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; 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; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..447
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          304..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2481 AA;  272192 MW;  C001A3C2235F415A CRC64;
     MSTYKKPQSE PIAIVGTGCR FAGDVTSPTK LWDLLTNPRQ LSQEVPSNRF NAQGFYHPDG
     EYHGATNATQ GYFLEEDHRV WDAGFFNITP KEAEAIDPQQ RIILEVVYEA LESAGYTLEK
     YAGKKVAVYA GLMTADYDSL CQRDDITSNQ YFATGNSRAI LSNRISYFFN FRGPSMTIDT
     ACSSSLVALH QAVLSLRSGE CEMACVAGAN LMITPEQFIS EASLHMLSPT GTSKMWDVSA
     DGYARGEGFA ALFIKPLSQA LRDGDSIISI VRETGVNSDG RTQGITMPSP LAQAELIRDT
     YRRSGLDSQN PSDRPQYFEA HGTGTQAGDP REAEAISTAF FGNEANTTAE SDDTKLVVGS
     IKTVIGHTEG AAGLAGLLKV AHSMINNCIP PNLHLNTLNP SVKPFYGHLR IPVDVVPWPQ
     APTGQPLRGS VNSFGFGGTN SHAILEKYEP SIHDEVAKHF APALEAPVSP LTTTPYDAEA
     PAVGLPLVIS AKSQKSLVAV AQALRDFMVS TDKSADEVAY NLYAHRSALT YRTAISADSR
     DGVIAALDNL LSKAGSSSNP ELGVRAKLDG GEVKILGIFT GQGAQWSGMG RKLFHSSSVY
     RNTIENLEKV LKACPHPPTW SLIEELIHQE DASRINIAAL SQPLCTAVQI ALIDLLGSIN
     VSFHTVVGHS SGEIGAAYAA GVLSARDAML ISYYRGMSAY LAGGKDGQKG MMMAVGMTRA
     EASALCARDD IKGRIWVAAS NAPTSVTLSG DVDAVKALQV ELTEEKKFAR LLVVDTAYHS
     AHMERPAAQY MEDLAGCGIE PRQRNSTVWI SSVYADGTEP SIEELKGPYW KDNMVKAVSF
     YEAIDLALSS QGPFASAVEV GPHPALKGPV QQTVKAATGG ALSYAGLLDR KKDDRHAFAE
     FLGFTWNYFG TEAIDWKLLV AQSSQPGLSS SRMDLPSYPW DHSQMHFRES RIAHQYQFRE
     KGPHELLGVR TRDDTEFELR WRNILKLETV PWIQHHKFQG QALLPASAYC VLALDAAKAV
     LNGREASVVE LTDLEFMSGI SLEANTYGVE ILVSLSIAPP STKGRLAGKI IEGVFTITSC
     YADGVTPMQK NFTGNLRIYL GEPSEDALPT RDPSMAETLP ADTDSFYQMM LDIGLDYTGP
     FRALQSIDRR YNFCSATLQK FHNTDTTGLG VSPATLDSCF HSVFAAVASP GDKSLWTSFL
     PRSIEKIRFN LALCDGKPAD NASLVVDSVI TQEIPRTKTA TTKFVGDMSI YNPDGEMEIQ
     VEGLMVASFA NSKPEDDKEL YLTTVCDLDP EHEIIAADLS QEDVATERIL LEACERVARF
     YIHDDSLKDL SSSPVFFTPP ATPMSPPKAR SSETTPSPWQ QDTAETLDAY ILQSPFHHAL
     SFIRLLGENI PDVLPAMLST IIQEAKQLHR FRSHVSRVVS QLAHRYPRMR VLGLTDPETA
     LTKHVIDGFK GSFVSYTLGN ETEPDLMARV SSDAIKKKID TEHTKILDNE DNSSLQPFDM
     VVLTTSIVKG AEQRSRLKQV QSLMKPGGFL ILIHESMSPL RDRLRRAFGV RRQADMPLTP
     PEWPDLLDEC GFARVSKNAE QFFAPDFSLI VRQAESDIKQ AALSPLNSSV PKVMGHTLII
     GAQENTADLS AEVHQKLDPL CSSIDIIADL DSLQPAIFNE ISSVIFLADL DEPMMSSMTP
     ERLDLFRALM APEKVVLWAT MNSRAGNPEH AATFGFCRSM LAEIPSLKLQ MLDLDSRRDS
     SDLVAETFLR LSMKALRSAA QDGKLLWSHE NEIFMEHGKR LIPRLLPWKE GNDRVNCPRR
     LVADEVNTLK QCVEVVSAQS GDGSAVYTAN IVEETDIDDA VAIPDQSVIQ VKYSSVEVIN
     FGLKYASHVC IGKEVTSGEL CLAMTKSNSS YVTVPNSCVF QLSSSNIEPK LLLGLVLRYL
     VALSVAEDMM EQTVLLLEPD AALLECMKEV FEAKGANVIA CTTTGSKRKS YGQRYIHPYA
     SNRELKALFP ADGASVIDFL PEGSELSETV LDCLPENCEY HSRFSLLTSE HVVALGDSMD
     IEHLWETAIG KAITNVRSMN GRFSFPALES ISVPQLLDHT GSSKPFQILD WRAEREVQHI
     AKPLFGTQLL RPYKTYVLVG LTRDMGQSLC NLFFEHGARH IVLASRNPNM QPQWIDDLSV
     KGCEVRIERL DVTSIESVRA FKQRLAQEMP PVAGVINGAM VLDDRVFAQM DVETWNRVMR
     PKTVGSSNLD EIFCEADMEF FIMTSSFAAP GGHGGQSNYA AANMYMNGLA ANRRIRGLAG
     SVLNIGVIYG LGLLHRERTD IYAFLEKDGY PPISERDIHH MFLEAIVAGR PLDGQIYDIT
     TGLSRYNANR EDKLHWQIDP RFSHFTFEDD DEGAEGEGQG KQSLKEKIKA VEGGAEEVAA
     VLTEGFARYL EVVLGQGEGS VKGEHSVGEL GMDSLVAVEV RGWFWKVIER DVSVMKILGS
     ASVAKLCLEV ADGYIKEKNK A
//
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