ID E3RIL8_PYRTT Unreviewed; 2587 AA.
AC E3RIL8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFQ94415.1};
GN ORFNames=PTT_07891 {ECO:0000313|EMBL:EFQ94415.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94415.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94415.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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DR EMBL; GL533333; EFQ94415.1; -; Genomic_DNA.
DR RefSeq; XP_003297473.1; XM_003297425.1.
DR EnsemblFungi; EFQ94415; EFQ94415; PTT_07891.
DR KEGG; pte:PTT_07891; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001067; 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:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; 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; 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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..452
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2504..2582
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 477..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2587 AA; 284779 MW; EEFF312139082C8B CRC64;
MGDFQPEDVE AFNNENMEGK VPLGEGPEPI AIVGMACRWP GGVSNPSQLW DMLQAKRSGY
SEFPEDRFNI DGWYHPEQQR PGSFFTRGGF FLEENPRLFD HNFFGMSPLE TRTADVAQRK
LLEVTFEAFE NAGIPWEDFY GSKTGVYVGN FCSDHQNMQF RDADYPLPYM ATGGDTTILS
NRVNYTFDLK GPSVTMNTAC SSSMYALHLA INGIRNGDCD GAIVAGSNII LEPASQIFIS
KLGAISPTSI SHTFDASADG YARADGFGSL YLVPLSRALT EGHNIRAVIR GSAISANGRS
DGISHPSAIA QEAVIRQAYI NSGHLDPAET DYFECHGTGT PVGDPLEVAG IGKVFAQHRG
TLPLLIGSVK PNLGHSESAS AMASIMKVIL AIERDVIPPT RGITKLNPNI DFEGTRTEVV
QEMRPWPRPN LKRASINSFG YGGSNAHVIL EHPSSAVAEY ISRQSTSRTL PRRTLSLYTG
EPNSSNIHEN GTTTNSEPER PLLFVFSAKD ETALQKNVAA IAQSSSKFHV SDLAYTLISK
RSRFSHRSFA VATAEDLGSQ LAGGLAIQKI KNRESTCQIC LVFTGQGAQW PNMGRDLFHN
FPVFRDSIRR QDAVLSVLPG RPKWTIEDVV AGDLGSSVHE PAISQTVCTS LQIALVDLLL
SFGIQFSGTV GHSSGEIAAT YAAGKLSAAE AVTMAFYRGY VVGKNSRTGT MLAVGIGYPE
IEDYLGDFSQ DLVVAAINSP SSTTISGRTP AIEALSERLS SEAIFNRILK TGGNAYHSPD
MALLGSEYER LATEGMEVVR GLQLEMKTLP PVFWVSSVHP WKDTSAFVVS PKYWRKNLES
PVQFNEAVRQ LQLRAGQAFQ MAIEIGPHAA LQGPLKQIFE STKAQGIQPP SYTHALSRGK
DDVSSILVMA GRLFQEDCQI DLEAVNSFSD SNSLRTPRIC LDMPTYSYSY GPIIYHENRI
NKEWRLRKRL RHDLLGVKQP ASSHLSPSWR NILRVRDVPW LADHKLIPQV IFPGAGFLAM
AAEAFSQHYE DTTEGANNWT GISFRNVAIT STLEIPDDEL GVEVILSMQP SALESSNSQS
THWFDFQITA LKVNTTVWVQ CCSGSVGAEK SNRESDAVVD ISASGFVPND MKQWYRRFEE
LGLGYGEAFQ GLNNLLVTKD GCRASINLDP SANIMKLESA YRIHPATIDA CLQLALIASH
GGNVESAKSA FVPVMIDSLS IWNVTPARYL ETGIAIASGA RKGPRGLYAK SQLISETGEI
LMDMGFLKCI SYQGPGNFEE DAHVSKNPLF RLCWKPDIDR LPDDQAKILF PVAECQDKAI
PVLRHLEELA AYMIISISEE YRSSMDAVLA EEHVNFVSWT HRYHTRAADG KTNFGLDALD
KTHDERAKRI EEICEYLGHD PEMLLMKQIY DNRAMVLTGK MSSAEIARND DLLENIWQSS
ITFDRAYEQL THLVDLCAHK NPHLRILEIN AGMGLGPTGR LLSKLESATD FKRYKDYTLT
SKSPSFITGA QERFAASKSI LYNVLDIDRD PQEQGLEAQY DLVIASRTLH ATDVLSRTVQ
NCRKLLKEGG KLVVVEMTRP LDVAGMLSGT FPGFWRGHDD CRPDGPFVEE ARWHHEFATN
GFSGIDLCLN DYPKGFDIAS VMMTTATEPT AYLNGHATVK EAITILGNDD QRLFSQQLIN
HLDHDRYHIT YASLIDNIPP QGSHVISLLD LEDSTNILEE EASFVSFKEI VRRSSSLLWL
TKSDMLEQTS PTAGLNIGLL RTLPHEMPHI KISQLCLGSD YATQSSVFDH IKAISTELVH
QSSEGEAENY YTLQKDVLHV SRVVPDTLMN AQYRIQEEIG TDLISQRWSE LGPMKVAFGQ
AGLLSTLHFE KDDDMHKPLA EGWVEIRTEA IEINMKDLAV ATGRFDLNTY SLTCCGIVTK
LGAGVNSLVV GDRVCGMAPG NFGNFVRTSA VSVQKFDKKD KPEQVASLPV SYITAVYSLM
HLARLQKGEK VLIQSATSAL GMALIRIARH LGGDIYVTVG ASQKADVLVE QFGISRERVF
ASRDHNTWRQ LREAGGMDVI LSSSSGEHMQ ESWRCVAPMG RFIEMGRLDV INRGKLAMEV
FERNATFSSF DIGLMHQQKP EFIGSLMEEV AALYRKGIVK SIDVITTFEV SQLEKALVFM
GKGTHVGKVV VTYTNPDSVV QVLPSASQAS FDPDAAYILT GCSGLGVGYT IISWLIARGA
RHLYFMSRSG APPPTFLGNE EVRCISIKCD VTIKDELDLA LAPIKAERQV KGVVHAAAVF
EDVNFESMTY AQLRKVIDPK VRGTINLHEA TLDQPLDFFT MTSSIVSVVN TATQSSYSAA
NSFQDAFARF RRARNLPALS LAMGMISDVG FASRRPDVQR SLQRNGVYGT TQEDLTKLLD
IAFTVPRADS VDRFDPWSDA HLLQGLEPVK IYQLDPNAEF IWSSDPRFSR LVRAIADLRE
LRQLAVSGGA TKSAAGLGEL QARAVALRDT QSGGVQSSDQ IQAELRELAQ AVLVERVAKL
LFLPAADVDV DEDLTTFGID SMVGAELRGW LMKSFGLGVT FGQLVARGMK IRVLVGLVVE
KLTSPRG
//