ID A0A2V1D8V3_9PLEO Unreviewed; 2520 AA.
AC A0A2V1D8V3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:PVH94495.1};
GN ORFNames=DM02DRAFT_721263 {ECO:0000313|EMBL:PVH94495.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVH94495.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVH94495.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVH94495.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805532; PVH94495.1; -; Genomic_DNA.
DR STRING; 97972.A0A2V1D8V3; -.
DR Proteomes; UP000244855; 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:InterPro.
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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF08242; Methyltransf_12; 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; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..477
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2438..2514
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2520 AA; 273976 MW; D279C4CFFA765EDF CRC64;
MAPDLNLLKD PASGAPSEVS GEAGFVKNGN FSSMDSSASE PNGTNGTTKG MNGHGSRPEL
KPVAICGMAM RLPGGVRSAE DFWDLLYNGR DARGPVPADR YNAAAFDNSL GGHGAIPPKE
GYFLDEDLST IDTTFFSVGK TELEKVDPQQ RQLLEVTREC FDSAGEVDYR GKDIGCYVGT
FSEDWLYSAS KETLANGGYT MTGHADLMIA NRVSYEYDLQ GPSIVVKTGC SASFIALHEA
FRALQSGDCS GALVAGTSLI MGPTTTAAMF SEGILSPEAS CKTFDASADG FARAEAITCV
YVKLLEDAVR DGNPIRAVIR NTGTNSDGKS AGLMAPNGKA HESLMRKVYL EAGLKPGETG
YVECHGTGTA TGDPIETNAV GNVFSEHGVY IGSVKPNIGH SEGSSGISSL IKSVLILENK
IIPPNIKFNQ PNPKIAFAEK KLTVPTQPTP WPTDRKERIS INSFGIGGAN AHLILDAYDA
PRDAKNVSES EGPHLLLYSA NTQASLQRQI KSIATYHDSN SKHSTTDLAY TLGLRREHLL
HRAFSIVPRP GKDSSSLGSP SPAVKASAAT NKLVMVFSGQ GAQWAGMGAD LIQDDQAWRD
DIRSMDRVLS SLIHPPVWTI EEELLKSPEH SLVNRAQLSQ PLCTALQIAQ VNALSRSGIF
PAAVVGHSSG EIAAAYATGA LSMAEAITIA YYRGLVTKKQ TMQGAMAAVG LSAAETQEFL
GDGVVVACEN SPSSVTISGD ADKVAAVLEA VRRENSSVLA RLLKVDMAYH SHHMKALAEH
YRNLMDAELQ EKGWEKHTPL IPMHSSVHGG IIDTGKQLGP TYWINNLISP VKFHTAVESI
LEQFSSTLFV EVGPHSALAG PLRQICGGKG RPCTYVPTMV RGTSGQESFL SAMGQLYQQA
VPIKLESIFE KGKVLHDLPT YEWDHSASFW HESRVSKDWR FRAFPNHVLL GVKIPESTSV
LPVFRNMINL EDVPWLADHK VRSDIVFPFA GYCCMAGEAI RQITGMDQGY ALRHVRALSA
LVLAENKPVE IVTTLQRHQL TDSNDSDWYD FTISHHAGAA WVANCRGQVR AIDRPTEAAL
KYPEPLPRKV KASRLYSALS RSGIVYGPEF RNLEDISASP AEKIAVSSVV PRKDHQTAPF
LFHPATMDSC FQLFIAAIAH GAGRNLSTTA VPTCIEEIEV HHTSDDMTCR AWCLDEERDI
GIDCTANGAC LLRVRGMELS GLGDEDDQPS MLGAGELDHN AAAHLEWLPD FDFTDVSKTF
KTLPAMPFEV RLQEEMTFLC ILDSAERLEG LEACNWHFDK FREWLDVEIA IARDGKYPVL
EPEHVSDLMR LPKADRDRKI RELYAQLSAV SAKWAIAECT MRIWEKIDLI FTGKSSTLDI
LMEGNVLTKI YDAISIGHGE FVRLLSNSKP NLRILEVGAG TGGTTEMILR DLTASGGEAA
YANYTFSDIS AGFFTQATER FSYAPNMEYK VFDISKDPFE QGFKPDFYDL ILAPNVVHAT
ANLNVTLGNL EPLLKADGLL VLTELSAVLR TPNYTFGNFD GWWLSEDDRP WQPYIDVDRW
DLELKAAGFS GVDTAVFDAP LPERCCAAIV SRPARNVSRT GTDRITVSII LSLEQAQYTV
DTVQLGDALP EKQDVLCTLD LEAPFFDKIT ASQLAAFQAF NTHQQTGGQK VLWLMPPTQI
RCKNPRGAQT IGLVRTIRAE MGLALFTLEI DVEEPEFFDL VRKVMSKVQR SDDVEQTLEP
DREFAVDQGV IKIGRYHPFS LEKELQAQQE KDTVDVVKKL SITKPGLLDT LGWSGEERPV
SIGPDEVEIQ AKSIGLNFKD VVLAMGIISA GPGDDIPLGL EVAGAISRVG SNIKHLAVGD
RVIALSPGGC AATSTILSAA VCAKIPAKLS FEDAATLPIC YATAYQSLVK VGHLEEGQSV
LIHSAAGGVG HAAVNIARML GVEIFATVGS DEKVEYLETK IGIPRDHIFH SRDESFYSGI
MQATNGRGVD VVLNSLSGEL LHTTWQCVAE FGKLIELGKR DAVGSGKLEM RPFLASRSYC
CVDLSHLTKD KPDRAGALLR NILALYRNDW VKPIAPTAIF DAEDAAAAFR HLQNGDHIGK
AVLRIPENAS NLATTSKKAA APLRLDGNAA YLLTGGLGGL GKSIATWMAE RGARSLIFLS
RSAGATPEDE ALREELRAVS CSVSYIKGEV QDRATVERAI AAADGKPIRG VLHLAMVLRD
VAFNKMTIEE WTAAVSPKVD GAWNLHHALE GQPLDFFFLA SSLNTVVVNP GQSSYCAANT
FLEAFVQYRR DQGQPASVLN IAPVDDVGYV ADNVHAFKNM KAQGICSLGE ASFLRFLELA
LLEPVTAGDN SNCKSEHVPS WKTKDQIIMC LRSEMDLDDP NNPTTWRRDR RMGTYHNIRS
NAAGDAGASS NSSNLLKAFL GKAVIQPEIL QEEASIVFLA QQIGRKALDF MLRELEEGEE
VDVSLSLQEI GLDSLMAIEL RRWWKQAFGL EVSVLEILGS GVLAGLGKVA ADSLFLKYTA
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