ID A0A2W1ERK0_9PLEO Unreviewed; 2279 AA.
AC A0A2W1ERK0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KAF7576126.1, ECO:0000313|EMBL:KAI1519982.1};
GN ORFNames=Ptr86124_000350 {ECO:0000313|EMBL:KAI1519982.1}, PtrM4_003660
GN {ECO:0000313|EMBL:KAF7576126.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:KAF7576126.1, ECO:0000313|Proteomes:UP000245464};
RN [1] {ECO:0000313|EMBL:KAF7576126.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:KAF7576126.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1519982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1519982.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1519982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1519982.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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:KAF7576126.1}.
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DR EMBL; NQIK02000001; KAF7576126.1; -; Genomic_DNA.
DR EMBL; NRDI02000001; KAI1519982.1; -; Genomic_DNA.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 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; 3.40.366.10; 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; 2.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..446
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2191..2268
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 502..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2279 AA; 249814 MW; 8EA06CC5066EDFB4 CRC64;
MKAPATSQAP LKATSDVEDI VEPIAIVGFG FKFPQDITNT ESLWKLLMER RSTMTEIPKN
RWNIDGFYKE HGHRPGTVKN RGGHFLADDP ARFDAPFFSI QPAEAECMDP QQRLLLETSY
HALENAGIPM QSAMGTRTSV HVGCLLQEYS QISQRDAQMP GDYRIVGSSG LAMLANRLSW
FYDFSGPSMT VDTACSGGLV ALHLACQELL TGNVNMSLVC GNNLCLLPDS TALLSSLNMM
SKDSVCYSFD ERASGYARGE GFGVLVLKRL SQAITDGDTI RGVIRSTGCG QDGNTPSITS
PSQTAQERLI RETYARAGLS LDETRYFEAH GTGTPVGDPC EAAAINSVFS SRTPEEPMYV
GALKSNMGHP EGASGIAGVI KTLLVLENGI IPPNVYPERI NPAVTLAGPN LRFPLEPVVW
PTNGIRRASV NSFGYGGTNA HVVIDDALSF LNERGLHSRH CTRALQSIQE HCVADQEAST
IIDDTPGSTD CERLEHERQR YDSITSIGGP EPKTESLSTN ETPSRATSET EDENIRLTEA
FNSSPKLLVV SGFDERAVRR SVTALQRWMQ DHIVDDNRVQ GLEDLAYTLA EKRTSFPWNT
VCVAPSESTP HLAWPVPMRM RQRVDVCFVF TGQGAQWHGM GRELLAYETF RDSMLQADRF
FKALGSEWSL MDELYNKNKE ESAINQPELS QPICTALQVA IVDLLTSWKL GARASVGHSS
GEITAAYTSK AISRESAWMI AYFRGLAVAI TQNITSFQGA MIAVQAPLDV WEHLMTEQNA
AYPSDRVSIA CYSSPRSFTV SGSHDAIHRL VDMLKEASIE VHILKINVAY HSQHMQPVAG
VYSKLLRGID CGEQTENQPL FVSTVTGDSL GETDELRTAQ YWNRNLTGAV KFSTALDTIC
KHQDASSYFF LEIGPHSVLR SPLGEILKAH DRDVTLDYAS VLRRDRSSSI TALECAGKLY
TIGASIDIAA VNKSSGPSPK FLTSLPGYQF EDKKKYWLEG RTSIQYRQTK FVHHELLGSR
TPDWNEHEAR WTNRILLEQS PYLKDHMING MCLMPAAGML VMAIEAVRQF YGERATRATG
YKLRDVTFTK AMTLSGDPRG TEIQFTLRPA NLDPRDELPG SLWDHFSLYT YEDEGWHLCC
AGSISIDYHE ATGGSEILEE KKCNMNLALE ECGNEIDSGE IYGAFNQAGL AYGPTFRGMC
NVKWDKHSQA TGTIGLRDWE AQARFDYSDT HLIHPAALDT ILQLTFPAYS IYAKDSSATT
VPTGFSNAWF SAGLATASCN RQEVHVHAKV SGRGFRNKLF TVTAAFAGTQ DPCFFGELET
STIGRSVAPS PEKSHRSLYR IEWQSADFDS IALDSELPAT LTSTIRVVFD DANELQTSLA
RAIYEKFLVH HGPQALIPWN VATESDVADT TCVFLPGLDG TFLQCLEEED LEKVKFLLAT
TKSLIWVTFQ HHAVNENPTE GLVSGLVRTL ATESEDYRLV SVNLNVQNGL DSASVNIENA
LKALIHQQTD PEDEYCEIDD SLCTPRVVDD DELANQALPS EQSVQYVEKP WSELDNPKLT
IGAAGILNTL HYEQSSDYDN AIAADDVVVE IKATGLNARD LLVAIGQVHD EVFGSEIAGV
VVRVGSSSTR FKVGDRVFGV ATSGVMQVVH CKSFQLREIP ASMSFHEAAA FPVAYCTAYY
ALVEGARIKN NNSILIHHGV SATGQAAIKI AQLYGCTDVL VTVNSVGEAN FLKNQCGILE
SHIFIAEERN LAHRICHLTD ERGVDVVLGS PGVLQQSWPC IAPFGRFIDI GEKDVFVSTA
NGSKQIAIPP STQNISFTRV NFQELAQSTM FTGIFEQVLL LITDSNVGPP QPLTVFKQSE
IEQAFRALQE EKLVGKVVVE MKGEELVEME VAPNASEPLF RADASYLVAG AFGGIGQSIT
RWMVENGAKH LILPSRSLVE GTDCVRLQFV NELRTQGAIV HAPVCDIANA SQLESTLNSL
SSMPAVAGCI QAAMSMHDSS FAKMTIAQWH ESLAPKVSGS WNLHTLLPRN LDFFVMLSSS
TGIMGSFGQA NYTAGNTYQD NLALHRMRNG QRAHTLALSM VTGVGYVAQN EQVQSLLRVR
GMLEEVSLND IYALLRFCCD AERVDASTIG PNIITPLTLP ADLRALNIVA PLGSTRPIYH
YLDTLPARIK PSPTAQNSTS HLLSSATSLA QATDIVVSAI QTQLSSLLVV AKEDIDPQRA
IYRYGVDSLV AVEMRNWFSK AVGADVATSE IMSDVSIWLL GVKVAGKSRF VAEGVREGT
//
