ID A0A0C4E1E8_MAGP6 Unreviewed; 2562 AA.
AC A0A0C4E1E8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=MAPG_06208 {ECO:0000313|EMBL:KLU87206.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_06208T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU87206.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU87206.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU87206.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU87206.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_06208T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_06208T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_06208T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_06208T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; ADBL01001492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADBL01001493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876970; KLU87206.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4E1E8; -.
DR EnsemblFungi; MAPG_06208T0; MAPG_06208T0; MAPG_06208.
DR VEuPathDB; FungiDB:MAPG_06208; -.
DR eggNOG; KOG1202; Eukaryota.
DR OMA; HMFLEAI; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000011715; 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: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; 3.40.47.10; -; 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; 2.
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; 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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 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; 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 SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT DOMAIN 8..496
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1878..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2562 AA; 278689 MW; ECE836897BDA5EF7 CRC64;
MAYDMPPNEP VAVVGSSCRF AGGVDSPSKL WDLLEKPRDL SRPVPADRFN VDGFYHPNGE
YHGTTNSTRG YWLEGNHRVF DTSFFSITPK EAETIDPQQR LLLEVVYESL ESAGYDLKQY
AGKKVSVFAG IMTADFDTLC QRDDLLGSQY LATGNARSII SNRISYFYDF QGPSMTIDTA
CSASLVALHQ AVLSLRSGES VMACVAGANM MLAPEQFIVE SSLHMLSPSG RCRMWDAGAD
IMLPTPASSD LGINGYFSQF SSVSRVFGTR QNISMSDTIF NDGYARGEGA ACLLLKPLSR
ALTDGDVIQA IVRETGVNSD GRTKGITMPN PTAQAALIRD TYARTGLDPS REDHRCQYFE
AHGTGTHAGD PREAAAIADA FFSAGDTRFD HDSMPKFPPL KRKRLLVGSV KTVVGHTEGA
AGLAGVLKVI QAMKHETIPP NLHLKTLNPS VKPFYNDLEI PVSATPWPDA EQGHPLRASV
NSFGFGGTNS HAILERYTPS IHNSVGVHFS PAGAESVSPT IPQKVQQDRF PLPLVLSANS
QHSLYLMVEK YRDFLARKVD EFSSPQLFST LLRRLYTKQG PFPFKLAITA DTVTDAIEKL
YQLLLGASTS KHPQLGTRAA AIRQPLSPDG RFRVLGVFTG QGAQWATMSR DLLLNCDRYS
RSISELDAVL RSCPDPPDWT LEHEILADPS ASRVNVAAIS QPLCTALQIA MVDLLSTVGV
SFHSVVGHSS GEIGAAYAAG FIDARSAILI AYYRGKFASL AGPRGASGAV AEDGTTTVSK
QSGGMVAVGL SRTEAEKLCI QEKYAGRIVL AASNSPSSVT LSGDFDAVNE VQKELEAEGK
FARVLAVDTA YHSHHMARPA LEYSNALRAC GITPAPKMAG GRETRWFSSV NGGSGAFDAA
AEIQATYWVD NMTRPVLFRE ALEKALDGDG YFDLAIEVGP HPQLKGPAIQ TIEATTVSGS
ETKMPYLGVL DRKKGDSAAF SDFLGSLWTI FGPPAAGVGA AIACSKSEGV RPDELPTYPW
DHSQVHYRES RISHQYSHRT HAPHELLGVR TRDDSEFEMR WRNILKLETI PWIEHHKFQG
QALLPASAYC VMALDAARVL LNGRPAALVE LQDVEFVNGI TIEPGTYGVE VLFTLSVSSL
SKDSSSRSHS NNPQEIEAKF TVSSAYADGA TPLRQNFSGR MRIELGTPSA DALPPRPSLQ
PETMAVSPDG FYKMMAGLDL GYTGPFRGIE KIERRFNFAS TTLPKIHPED TTTLKVSPAM
LDTCFQACFS AFSSPGDRAL WTPFLPRSIS KVRFNLAVCD RNQEELDQKT WVDAHLTDFR
PISKQGAATI TGDMAIYNSK GQMEVQVESM VVASFAATKP EDDYELYLHT VMQVDAEDEI
VGVQPFDLDS AEEEHRVLEE SFERVTSFFY KTRGANSSIS QLRRASAMAS FEPPPFVAKG
LASSPWPRET HDSLREFTES SRYPVALELL SSLAAKLPSP VLAPMIPGVK MEAQTLLSFQ
KHIQMVTCQI AHRYPRMHVL GVTDPNLYLE EHILAGLGSS FLRFTTVGAD ERFDRRVLRN
MPQTIRDKIV ENNDLLLSGN GTAAAYDMVV LSTSVMEPGQ AAAVLKVIRR LMKPGGFLLI
IHATTTANPL RDNIGQCASR PLVGSPSVVG NNGAPTPPDW PDALEDSGFV RGPANADQSF
PPGYSLIVRQ TECADKRMLR LPFGPAGPGP LGAVAVDTPT RKAVFDRLTS QLLVVGGGSH
QTSGLPEKVA GLVEASCGNA VYVARAFDDI DPADIANCTA AIVLADLDSP VLFGMTEERL
ETLKALMRPD MRILWVTNTA GSSDSSTEQS ASFGFARTLI AEMPSLALQM LDLDTLDGDV
ATTIVESFAR LCQQASMSSD SSSSSSSSSS SSSSSGDDSD NMLWSYEHEV HIKNGRRLVP
RVLPYQPAID RVNSARRIIT RPVNTAEKSV EVVPIQFSDG SVHYEARSAD FKVESTTTTT
TTSPIPVQVL YSALNPVSEH GGFRYVSVGR TLEHHGEGRA VVFFSSKNAS LVHVESRDVY
DAPREGVLNS SLFITCLVRA LRAKILCRAL EHRAAIRPRA TEYSMVLVDP EPSLLESLKA
TVSPATPWQR VITAITPRKE LADASTDYIY AHTRSSPQTL KDLLPTSADF VVNCSADYEA
YARRIAGCLL PKGSSQYIPC WYECASSLAL EGIYRPRDVE HTTAAAIDVA ADLMLTVGIW
DTATLATVSV PQLLERSNIT ALSSSPDVIL DWRAERTVAI SPAPSPADKQ LLRPDRTYVL
VGITRDLGQS LCQLFVDLGA RYLVLASRNP PAVGSLRWVR ALRARGVTVA VETLDVTDLD
SVRCFADRLR RKFPPVAGVV NGAMVLEDRV FAQMTLDTLD RVMRPKTVGS QNLDAVFDDD
DLDFFIMTSS FAAVGGHAGQ ANYAAANMFM NALAADRRRR RGRPASVLNI GVIYGLGLHS
TQHRGRAHVP QVPESRASWP RGPQQEKGCR QWASTKALVK RKIPKPALAP RVAGRLGRLA
RFCCWECRTR ECELSIIGMT RAEGPENVAA LPAHDLSTIS SS
//
