ID A0A162P5G3_9PEZI Unreviewed; 2272 AA.
AC A0A162P5G3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KZL86703.1};
GN ORFNames=CI238_08741 {ECO:0000313|EMBL:KZL86703.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL86703.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL86703.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL86703.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL86703.1}.
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DR EMBL; LFIW01000383; KZL86703.1; -; Genomic_DNA.
DR STRING; 1573173.A0A162P5G3; -.
DR Proteomes; UP000076584; 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:UP000076584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 474..906
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1757..1831
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1880..1957
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1711..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1834..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2272 AA; 247829 MW; 04D3F35D8CE0CC91 CRC64;
MGRFSRTPFN PLPLPSMCSM LQFRYPSAMT LTAELRNSGD GLLLDWCAHL TRPVSSPSQS
YKFKTRSRHP GILFLLEHRE PHHLGNLCRR SFKMADMMSY LLFGDQSLDT HGFLAEFCRS
GNPSTLAKTF LDQAGQALRE EIDGLGKLER SKLPTFLSLR QLNERYHAQS IKHPGIDSAL
LCITQLAHYI DRTEKEPQDG APHDHTFFMG LCTGLFAAAA IASTPSVSTL IPIAVQVVLM
AFRTGSHVGS LAERLSPPVG QSEPWTHILP GLKESDAKEA LTNFHESNYI PVASQAYVSA
VSASSLAISG PPATLRALED QNVFGVKPTA IPVYGPYHAS HLHGTADIEK ILRLNDPKVV
EVFAKSKPRS AIMSGTKGIW FAETDTKSLL KAVAHECLID VLQFQKGIEG CIETARDFEG
STCLVIPYGP THNAETLSKL IKDRTQLDVQ VRHGPRIQRE SINSPIGNHG SSGKCKLAIV
GMAGRFPDAA SHEKLWELLS KGLDVHRVVP ADRFPVATHY DITGKAVNTS HSQYGCWIEN
PGYFDPRFFN MSPREAFQTD PMQRMALTTA YEALEMCGYV PNRTPSTRLD RIGTFYGQTS
DDWREINAAQ EVDTYYITGG VRAFGPGRIN YHFGFSGPSL NIDTACSSSA AALNVACNSL
WVKDCDTAIV GGLSCMTNPD IFAGLSRGQF LSKTGPCATF DNGADGYCRA DGCASVIVKR
LDDAIADKDN VLAVILGTAT NHSADAISIT HPHGPTQSIL SRHILDEAGV DPLDVDYVEM
HGTGTQAGDG TEMVSVTNVF APADRKRPAD RPLYLGAVKS NVGHGEAASG VTALTKVLMM
MQKNAIPPHV GIKKEINKTF PKDLSERNVN IAFHLTPFKR RDGKPRRVFV NNFSAAGGNT
GLLLEDAPHL KSPEADPRSV QVVTVTGKSK AAMIRNAERL VGWMEQNPQT PLSHVAYTTT
ARRIQHYWRM NVAASDLPEA QRLIKDRLKE NFTPISTQQP KVAFMFTGQG SHYAGLGKDL
YAHYRVFRDS IDEFNQLAQI HGFPSFLPLI DGSESDVTKL SPVIVQLGLC CFEMALARLW
ASWGIRPSAV MGHSLGEYAA LNAAGVLSAS DTIYLVGARA QLLVQKCTAG THAMLAVTGP
VDAVMEALGT QAEAVNVACI NGPRETVLSG AAAKISDISS HLGTAGFKCT QLKVPFAFHS
AQVDPILDDF ETLARSVSFD RPQVPIISPL LGKMVENEPI NAAYLRNHAR DAVNFLGGLV
HAQQSGSVDE KTVWLEVGPH PVLANFVKSS FGISSVAVPT LRRNESTYKV LSNTLCALHT
AGINLDWDEF HRDFSECTRL LDLPTYSFDE KNYWLQYTGD WCLTKNRGPS AVKAPLQIEP
ARPKLSTTSI HAVTNEDVKG DIALIETETN LSRPDTRPLV EGHLCNGAPL CPSTLYADMA
MTVADYAYKM LRPDAEPVGL NVANVEVPKT LIFDEKLDAH VLRTTVTANV ALGYADVSFH
TGEGSKKTEH AHCKVVYGST EQWADEFERV SYLIKGRIDA LEEAERQGKA SKIGRGLTYK
LFTALVDYDT KYQGMEEVIL DSKTCEATAK ISFQTTDKDG NFFFNPYWID SCCHISGFVI
NGTDAIDSRE QVFISHGWGS MRFTEKLDAS KTYRSYVRMQ PVKGTKMMAG DAYVFDGDRI
IGVAGDVKFQ SIPRKVLNMV LPPRGRAAAG SAPAAAAPKA AAPSKAAPAK EKSGKEKATK
QVTASNLKAV NAKLAKRSVV QDVFDILAKE VGVTHDELAD NIAFTDLGCD SLMALTVSGR
MREELDIDID SHAFVEYPTI GAFKAFLGQF ETPDRKDSYA QDSGDSSGSV SETPELESDS
NVTTPYEESD RSVKGDGDEQ DCGDLQSILR DTIATEMGVE VDEIVAAPDL AALGMDSLMS
LSILGTLREK SGMDIPNDLF VTNPSLLEVE KALGIGPKPK PAPAPKPAKA APAPRREKVE
PTKEINTHPG NTTASITKPP PPREIIDNYP HRKATSILLQ GSTRTATKNL WMVPDGSGCA
TSYTEISQVS SQWAVWGLFS PFMKTPEEYK CGVYGMASKF IEAMKARQPK GPYSLAGWSA
GGVIAYEIVN QLTKAGESVE NLIIIDAPCP ITIEPLPKSL HAWFASIGLL GEGDDDNKKI
PSWLLPHFAA SVTALSNYTA EPIPKEKCPN VMAIWCEDGV CHLPSDPRPD PYPTGHALFL
LDNRTDFGPN RWDEYLDINK FRTRHMPGNH FSMMHGDYAK QLGQFIREAV CE
//
