ID A0A166Y5J7_9PEZI Unreviewed; 2566 AA.
AC A0A166Y5J7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Polyketide synthase (Beta-ketoacyl synthase) {ECO:0000313|EMBL:KZL77283.1};
GN ORFNames=CT0861_03058 {ECO:0000313|EMBL:KZL77283.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL77283.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL77283.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL77283.1,
RC ECO:0000313|Proteomes:UP000076552};
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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:KZL77283.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIV01000008; KZL77283.1; -; Genomic_DNA.
DR STRING; 708197.A0A166Y5J7; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
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; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 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; PF00326; Peptidase_S9; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 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; 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; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 424..840
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1682..1759
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1763..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2566 AA; 283041 MW; 42A7FBA432F84DDF CRC64;
MRPSKEQQHC SFLCLLVFGP QAQLSPNDLV ELRSLLVSNA LLSRLLTAVQ ELPNFWSRLV
RFDPELARVP GESCLRGLAE WLAHAGSFPY HPSELPVTLA FPLNFLFQMT QYGCFIQSMN
KNNTQRMILE SLEDGGVQGF CVGFLSAITV ASSLSEKELV ETAIRALRLA VCIGAYVDKD
AIYSRSACVS VRGRHTHAET QKKVADILQK FPKAYISAVT DETSMTITTF CRELSELTEA
LRGAGFLVQG VPINGRFHSA AYVVEVDRLV DFFEHASDLR FPESDHLRVA VRSATDGKVV
NQGDLVRHIL ENTLLRRVEW YNTLKLATAS LPPGQKCIAL AGISTHFPPS LSAKPDIQLF
SLRSLADAQT IMMQEPHVEG LSGHHTPPRT PPGHAHDNSV LSLADYCDRH PSTRGEFVQS
AFPSHSVAIV GMAGKFPGAS SVDELWELIS TGRSTVNSAP DRIGLSHLPD DTSQVRWWGN
FLDEHDTFDH KFFNKSPREA MACDPQQRKL LEVVYEALES SGYHSADARS DPTDYGCYIG
AVMNNYATNT SCHLPTAYAM MGTSRAYLSG AVSHHFGWTG PAMTIDTACS SSLVAIHTAC
RAIAAGDCSR AIAGGTNIIT CPYDYRDLKA AGFLSPTGQC KPFDAGADGY CRGEAVCVVV
LKLLSAAIEE NDHILGVIVG SATNQNPKDG PIVVPNAKAQ ASLMREVLEM SKVLPEDVTF
VEAHGTGTGV GDPIEVQSLR EAFGGQRRTS TLYFSSIKGN IGHAEAASGA AGLAKAILMM
RHGQIPPQAS YQSLNPKIPA LKPDEMAIPR QLIPWNPRER IACVNNYGAA GSNSVIVVRE
APFIELGRKG PNINTSQPSR WPLILSASSK ISLSTYSQKL LDWMRHTDSA DFSDAHFPDI
LFNLAHRANH ALEHHVSTSV SDVSDLELTL SAIASGGDSI ITAPSQSQPV VLVFGGQEGR
FVGLSEAVYK SAQIFRHHLD TCQNILLNLD YEGFYPAIFQ QAPISELVVL HTALFAVQYA
CAKAWINCGL KVEAVVGHSF GQFTALCVSG VLSLSDALKL VAGRASLVEK HWGSEPGAMI
ALQADRQKIT EILERLGSRA GYVEIACLNG PRNHVVVGSS KAIRHLENFV SGKEQPQGSI
STQRLEVTHG FHSRFTEALL PYLEDLADEL EWKSPTIYLE VCSETQNDQT PDRRLIVEHT
RRPVYFQQAV ERLMKKYPRA TWLEAGRGLS ATQLVRACAQ HPDRHSFLAP QLTTPNAQDS
LVDVTVRLWR NGHAVQYWPF HRTQRWQYQY LSLPPYQFQK TRHWLPYVRS VAGSGDSTST
QPKEAKHHQF ISLISGDKST EARFRISTRS NRFRALVAGH IMCGYAVVPA SAYIEVASRA
ALTLQGDLQA TIWTPTVEDL VMQAPIALGP DQTPADITLT MRHLENPWPS WSFSITVKPD
LENDQGPVQG HETTTGTVKL HQRTDSQIAR ELKRFDSLVG NHRWEQTMSH QDAEGMHGKH
IYRAFSQVVE YSEAFRGIKS IACLGSEAAG TVKIFPNSED PPDQRLTDTP MVDSFMQFGG
FLVNYFNETA SPDSLFVCHR VQRVQVGPAF TPDGYEWSVL ANMTAVDQGS LSVDVYVSET
RSRKIVFTAL GMDFTKMSRA SFKRIVGGPA RDADSLRVTT CTKAERQAND GLITQTTQKT
PKNLLSKRTE ILRITASIAD IAENELSGET SLADIGIDSL GATEMISDIT SALNVKIDLA
TFLLFPNIDT IISHVDSQLG VQPEAENDAV NSSSAENTKG LGELRSLEND TVPKSRGEAQ
EVIKGTSPKR YNKFKPDSLM LPATTSIRKS FDDVRLSFDE LGAANQALDY WSKIYPDDVR
LILAYTTDAL KTLGCDLRAL GPGETVSEVV GVLPRHRQLM RRLYRFLEDE NVIETSGTGV
FTRTNKIFEA TTGEQIFQQI VGKYPLNAAI RHLLQAVGPH LAACLIGDKD ALQILFGNRS
NKKWLEGLYL EWPMLVTATQ LLGNFLCHAF TENHGSELRP GPFHILEVGA GTGGTTRHIV
DLLKRRGIQF EYHFTDISAS LVQKARTSFA DVDSMSFGVL DVEQEPTSEL TNAFHVIIST
NCIHATRDIA CSLANMRKML REDGALALVE MTAPRPLYVF DVIVGLLEGW WLFEDGRSHA
LADVERWEQA FTEAGFREVL WSDGETLEAK TVRVICGFQN SGAPQSRLDT AKNQGGLANV
RIQEVAYKTA GSQEIHADIY CPLNANPTKG MPIALMIHGG SHIIFYRKDI RPPQTRIMLE
MGLLPVSLDH RLCPETRLVD GPMVDVCDAV EWATTKLPHI ELVNPDIRPD PNNVVVVGWS
SGGQLALSTG WTAVERGIRP PNAILAFYCP TDYESDWWQK PIQPFGAEYR GEEYSVLEGV
QDEPITNYGI IGAWEPLSDP RIRTDSRSRI VLHMNWKAQT LPIIIGGLPS KRRAVSERPD
VEDWNVLPQP PVEEIRRCSP LAQVRRGNYA TPTFLVHGMA DDLIPWQQSL CTVEEMRTQG
IDARLVLVPD GPHICDASHD PESAGWQAVL EAYQWLGNHA FPHSHD
//
