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Database: UniProt
Entry: A0A2P5I6I4_9PEZI
LinkDB: A0A2P5I6I4_9PEZI
Original site: A0A2P5I6I4_9PEZI 
ID   A0A2P5I6I4_9PEZI        Unreviewed;      2032 AA.
AC   A0A2P5I6I4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:POS78118.1};
GN   ORFNames=DHEL01_v203496 {ECO:0000313|EMBL:POS78118.1};
OS   Diaporthe helianthi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=158607 {ECO:0000313|EMBL:POS78118.1, ECO:0000313|Proteomes:UP000094444};
RN   [1] {ECO:0000313|EMBL:POS78118.1, ECO:0000313|Proteomes:UP000094444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7/96 {ECO:0000313|EMBL:POS78118.1,
RC   ECO:0000313|Proteomes:UP000094444};
RA   Baroncelli R.;
RT   "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL   Submitted (SEP-2017) 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:POS78118.1}.
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DR   EMBL; MAVT02000212; POS78118.1; -; Genomic_DNA.
DR   STRING; 158607.A0A2P5I6I4; -.
DR   InParanoid; A0A2P5I6I4; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000094444; 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; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF54; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 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; PF00550; PP-binding; 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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094444};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..424
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1951..2028
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2032 AA;  221675 MW;  831E10665650743D CRC64;
     MEDDPIAIVG MAVRLPGGVL NTDDFWDLMI NKKSGLIPIP KERWNIDGSW SAEPRWGTIQ
     NRDCYMFDSN VQLNRFDTSF FTCGKLESDR MDPMQRQLLE ITRECLDSAG ESKTRGEDIG
     CYVGTFSSDW QDDQSMDPHA SGIYRGSGYL DFFQPNRISY EYGWTGPSLL IKTGCSSSMV
     ALHLAAEAVK NGSCSSAMAL GCNIMTSVLT SIVFTETGVL SPSGKCKTFD SLADGYGRGE
     AVNAVYIKKL SHALRDGNPI RAIIRGSGTN NDGRSLGIMT PNDIVQEKLI RQVYKNAGIS
     DLSKTAFFEC HGTGTPTGDP LEASAVARIW GPHGGVLMGA VKPNVGHSEG AAGLTSVIKA
     VLALEHKVIP PNIYLEDPSP RIPWASAHLR VPTEPEAWPL DRYERVSVNS FGVSGSNAHI
     IIDSYDSFER GQRCNSPDSE TDSGVFIPDL PSNRLLLFSA SHPESLDKQV QLHKDYLKKH
     PDQVDNLAYT LAFHREHLGY RSYVVADSQG GFETGQVPIS TSRVNRRLVF VYTGQGAHWA
     GMGKSLITSN QAFRSSIQRL DRFLQSLPEA PAWTLEEELM KEDPISSKVG QRGYSHPCAT
     AVQIALTDML FSLGLRPGAV TAHSGGEAAA AYATGAITAE AAMAIAYFRG VVIKGENVPK
     GTMAAVSLGP KAVEPFLIPG VVVGCENSQL STTLSGDPVC IQHCVDQIGR RHPDVKYKIL
     NLETSFHSPW LQPLTGIYRE LMRPYVKDTG SPSCPHFSSV TGQMITSADF GLEYWVENFL
     LPVKFNSAMR NILESDPNNT FVEIGPHPAL RTPVHEILRD FPGASCEYVT TLERQQDSSH
     SLLLLAGRLF SLGVDDVDLG GIIPKARVIP DLPTYPWHHQ AVHWYEPRNA ARFKHRRYPR
     HQLLGSRVLE GNDIEPAWRN TLDIKEAGWL NDHVVNGSMV FPATAYVAMV GEAMRQVAGG
     VRPFTVRDVS FTTGLVLLKD KRVEFYTRLI PEGATYDEDG DAWYNFKIMS SDGEHWVSHC
     SGYIRSGAEI SPDAETLVEL GHEKATKGLA RHIDTETWYR GASKIGVDWT GMFRGLEDMR
     ASVTAEEATA SVFDSYEDSD AYASHPAMLD QLLQINLVAL TNGLMRNFDK IHLPTKLGRL
     AVFASQELDM HVFGEAADPT PGDDSEVRDK IFHAVMLSQQ GRPVAVLEGL SISELPVAKR
     RGAGDKLLGS HFTCDTDLTM LDSVTRRTLN LNSSVDGTPP PSDQNVVEDV HRAVYLFGWK
     YPDADILEIG DACLGVGSAV HVLDALRPDP RRRYFKSYTY ACTDAEALGE TEASLAAEGL
     ADVMAVSAED MSLVVRGVDL VVASLSSLLV EDESVQEELQ ELSTMLRPWG RVIVHYDSTD
     PENFEKMREL ACEKLEELGF AVFSGTDMSF TLAQLPQPAA LSQTVTVLTT NNEQGLLSAE
     QLGQVFKNYD CKVNIVFEVP ENTEPGNIVI SLLDLHSPTF YSLDEASFHP FMTKLTGLRG
     SLIWVTPSAL TSCSDPRSAM AHGVVRTARM EGGVDVTIVE VDEPSKSASS LGEALWKISQ
     SLSSRRSGGS LDADFDYIIT DGVVQIPRMQ WFDLCDFQAQ HDDSRQVPTL ASGPGEVDTT
     MSLSQGNMPK ATAQSLQRSL FRDDATYVLV GGTGGIGRSV ATWMAENGAR SFVFLSRSAA
     SPEHEPFLGE LESYPGCRVQ AISGDVSDMN DVERALSLAP ENLPVAGVVQ LSLVLCDNGL
     KTMTFDQWQK AIKPRVHGTW NLHKATESLP LDFFLIFGSG GGITGYFGQA NYSASNTYLD
     ALVEYRHGLG LPASLIDVGV VGDMGYLTGH DGHSAAFRSA GYLFLTERDV LAAAEVAVAH
     SNDRGPLHSF CLGAVPDMPL AEPGNRINWK RDVRFGVAHY LFGAGERAKH RETPGRGGYE
     DGGAPGDGFN LLNIADLATS DPNNPKWRDP ATIEGLANAL CEALAEILMQ PVDGFSVRTS
     LPSLGLDSIV SIELVDWIHR NFRVAMTSIE VTQCSSLLHL SGNIVEKLIG SA
//
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