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Database: UniProt
Entry: A0A0G2F8Q0_9PEZI
LinkDB: A0A0G2F8Q0_9PEZI
Original site: A0A0G2F8Q0_9PEZI 
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
//
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