ID A0A0G2F8Q0_9PEZI Unreviewed; 1713 AA.
AC A0A0G2F8Q0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:KKY31072.1};
GN ORFNames=UCDDA912_g08996 {ECO:0000313|EMBL:KKY31072.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY31072.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY31072.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY31072.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY31072.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY31072.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY31072.1}.
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DR EMBL; LCUC01000417; KKY31072.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2F8Q0; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000034680; 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 CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
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; 1.
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; IPR020807; PKS_DH.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
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; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..384
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1223..1300
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1354..1431
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1307..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1713 AA; 186874 MW; 79BE67EA2FF13C2B CRC64;
MAGRFPDAAS HEKLWELLEK GLDVHRVVPA DRFPVATHVD PTGKAINTSH TPYGCWIEKP
GHFDPRFFNM SPREAFQTDP MQRMALTTAY EALEMSGYVP NRTPSTRLDR IGTFYGQTSD
DWREINAAQE VDTYYITGGV RAFGPGRINY HFGFSGPSLN IDTACSSSAA AMNVACSSLW
ARDCDTAIVG GLSLIVKRLE DAEADQDRIL AVILGTATNH SADAISITHP HGPTQSILSS
AILDEAGVDP IDVDYVEMHG TGTQAGDGTE MLSVTNVFAP PERKRPADRP LYLGAVKANV
GHGEAASGVT ALCKVLMMLQ KNSIPPHVGI KGEINKGFPK DLSDRNVNIA FHTTPFKRRD
GKPRRVFINN FSAAGGNTGL LLEDAPRLDP ATEDTRSHHV ITVTAKSKAA MIRNAERLVA
WMQEHPNTPL SHVAYSTTAR KMQHYWRMNV AVSDLSEAQN AIQDRLKEQF SPVNTQQPKV
AFLFTGQGSH YAGLGKEFYA NHAVFRQSIN EFDHITRIHG FPSFMPLIDG SEQDMTKLSP
VVIQLGLCSF EMALARLWAS WGVQPSVVLG HSLGEYAALN IAGVLSVSDT IYLVGARARL
LMEKCTAYTH AMLAVQGDVD TVKEALGEKG QCVTVACING PRETVLGGEA AQMTEISYQL
SAAGFKCTQL NVPFAFHSAQ VDPILEEFEA LAQSVKFNTP KVPVISPLLG KIVESERVDP
AYLRNHARDA VNFLGGLVHA QQSGAIDEQT VWLEIGPHPV CANMVKAAFG VATIAVPTIR
RNETSYKTLS TSLCTLHSAG LNMDWSEFHR DFPSSVRILD LPSYSFDEKN YWLQYTGDWS
LTKNRGALTT GPAAIEPTKP KLSTSSVHSI ISEEVKGDLV TVETESNLSR EDLRLVVTGH
LVNGAPLCPS SLYGDMAMTI CDYAYKLVRP DADNIGCNVA HMEVPKSLIF DDSIEKHVLR
VKATANVAAG YADLVFSTGE GAKKTEHANC KVFYGRTEEW ASEFERADYL IKGRIESLKA
AEKIGQASKI GRGLAYKLFT ALVDYDRRYR GMEEVILDSD TCEATAKVVF QTSEKEGSYN
FSPFFIDSLC HISGFIINGT DAVDSREQVF ISHGWGSMRF IETPVAGKDY RSYIRMQPVK
GTKMMAGDVY VFDGERLIGI TGDIRFQAIP RKVLNIVLPP RGAATTGARP APAAISAAKP
AAKSVPVKEK KMLTPTNLSH VNKKLASVVS QVMEILAKEV GVSHDELADN IAFADLGVDS
LMGLTVSGRI REELDLDIDS HVFVEHLSIG SFKSYLQQFE KPGAAEILSS GDSADSSSET
ETPELMDSES DVTTPDDESE SMEIKGENDS KDGAGNARLR SAVRETIASE MGVEVEEIIA
APDLANLGMD SLMSLSILGT LREKTGRDIP SDLFVSNPSL KDVERSLGIN EAPKKPALPK
PAVKLAKFEA PQLSPSQKLL PPSMVTATIP KPPRPSRIVD DFPNRKASSV LLQGSHRTAT
NHLFMVPDGS GSATSYTEIS NVSPSWAVWG LFSPFMKTPE EYHCGVYGMA TKFIEEMKRR
QPAGPYNLAG WSAGGVIAYE IVVQLTQAGE RVDNLIIIDA PCPITIEPLP AGLHAWFASI
GLLGDGDEKR IPGWLLPHFA ASVTALSNYT AEPIPKEKCP NVMAIWSDFG PNRWDEYLDV
NKMTMRHMPG NHFSMMHGDL AKQLGSFLKE ALL
//