ID A0A0C4DP36_MAGP6 Unreviewed; 2320 AA.
AC A0A0C4DP36;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KLU82516.1, ECO:0000313|EnsemblFungi:MAPG_01588T0};
GN ORFNames=MAPG_01588 {ECO:0000313|EMBL:KLU82516.1};
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_01588T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|EMBL:KLU82516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82516.1};
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 [2] {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 [3] {ECO:0000313|EMBL:KLU82516.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82516.1};
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_01588T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_01588T0};
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_01588T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_01588T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; ADBL01000384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876966; KLU82516.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4DP36; -.
DR EnsemblFungi; MAPG_01588T0; MAPG_01588T0; MAPG_01588.
DR VEuPathDB; FungiDB:MAPG_01588; -.
DR eggNOG; KOG1202; Eukaryota.
DR OMA; CRMPGNV; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000011715; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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: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; 3.40.47.10; -; 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; 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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 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; 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.
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:UP000011715};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 133..557
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2237..2314
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2320 AA; 250730 MW; BFD6FB615A324B7F CRC64;
MAPGAWLPDS PGDSPTSETA ANGGFLNGYW ARLRGAAAAR LGTGLQTSTN GHDSSHHPDD
HSSGDTNGHA NGVASDHVND NGNNQVNGDS RGDAPRVSGA APRTTAGAEP TSGLRNGAAT
NGHGPAAAPK TSTAPIAIVG MSCRMPGNVS SADEFWELLS RNRSGFSEIP KERFNPASFY
HPNPGKGGCY TPVGGNFLKC DLRDLDAPFF GLTEKEAISM DPQQRLLLEC TFEALENAGI
PKHHIVGKDV GVFIGGSFPE YESHLFRDSD TIPMHQATGC AYAMQSNRIS HFFDLRGPSF
TSDTACSSSM VAVHLACQSL RAGESSLALV GGCHLNMLPE FWISFSTCRL LSDSGKSMAF
DNRGNGFGRG EGCAMIVLKP LEQALRDNDA IRAVIAGSGI NQDGKTPGIT MPNGDAQETL
MRQVYHNFNL NPRDCGFVEA HGTGTKVGDP IEATAIHKVF GKGRTAREPL LMGSVKSNIG
HLEGASGIAG ILKGAMMLER SFVLPNHDFK SPNPKIPWKE WKLKIPPMQR PFPRDKKYVS
VNNFGFGGTN AHVVLEAAPF RMKEELTAKE LDKQPKLIVF SANDKTALQA TLKNTVIYFE
RRPEAFEGAL MRNVAYTLGQ RRSLLPWRAA IHARDSLSLV EALNGGQATL HKEMESVRIG
YIFTGQGAQW WAMGRELYPQ YPVFADSLDR ADRCLASLGS GWSLLEELAK SESSSLVSEA
HISQPSCTAI QLALVDLLQN WGVKPTAVAG HSSGEIGAAY AAGIISFESA VKIAYHRGRL
IPVLREKFPE LKGRMMAVGG SKDEVQHLID GLDKSQVRIA CFNSPSSLTI SGDEVALAAL
EKVVEQKQMF NRRLVVDVAY HSHHMDLVAK EYRAALADLA DLPAPVSSSV RFHSSLDGRL
VDGKELQPSY WVNNLTCPVR FSEAVESMLQ PTGGFKTGVN ALVELGPHSA LQGPIKQILK
AVGGPAAKTT YDSALIRKRN AIDTALELAG SLFTKGVNLD LGAVNFPKPG IAPALQTDMP
RYPWNYQNKY WQESRMTARH KQRSQPRSDI LGVEAIYSND LEPTWRNIIR LDDLPWLRQH
KIQSLVMYPM SAFIVMALEA TSQRAASKDR RIGSFEMRDV TIVKPLIVQE DDIEVTTTLR
PHQESTLVSS DVWDEFRICS YSHSVGWTEH CVGLVATRAH DTNDVDAARQ RLDSKMMLRT
AASAVQDSEP VGVGAEQMYG VMAEAGVAFG PAFQGLKDCE ASSTHATAKI HVGDLSKEMP
SEYLSSPLIH PCVIESLIGM YWPVLSSGHS KIATVYLPSA VSRVSISTEA IEVSNAAGRS
FRAYSSVDFG QGASKPAQVT TMAAPSDHET EPLIVLEGLV VAPILDGETQ AEADVPRELC
YKLEWEPWPE PAHGTSEGLN GAPMNGESSP EPFRSLSVVI AHDDSVLQRC VAQELAAALE
QLVGTPPDMG QLSAVEPEGK ILVFLSELDT ILLSTLSASQ FELLQRALTK AEGCLWVVRG
AYTNSTSPEA NMVTGLSRSI RSETGMRFAT LDLDGQKPLV EERISSAIMR VFREVFGPDA
TSTSELEFME REGAFFTPRI INDDEMNAFV KQQTNPSALE DAPFAGDGRQ LRLSIKTPGA
LETLHFVDDP VVGGPLTGGQ IEIDIRAMGM SFRDVMAVRG QTGDDPGYEV SGVIASVGPE
AAGFVVGDRV AALVQGGYAS KVRTPVRNVF KMRAEMTFEA AATLPLAYCT AYYSLFELGR
LEQRESVLIH SAAGPVGQAA IVLARTAQAT IFATVGTAEK KALIMEKYGI PDEHIFYSRR
TAFGNAIRQA TGGKGIDVVL NSATGDTLRE SWECLNEFGR LIDIGRRGGP SKTRLEMTSA
SKNSSFISLD LFAVAAEKPR VIERMIREVS RLLDLGEIRP LTPVTVFGIS EVETALKKMQ
SARLAGKLVV VPQPGEVVKA TRSRRANRLL RADATYILVG GTGGLGRSMA RWMVGNGARH
IALVSRSGST EGKVQELREE LEKSGAEIVV HKCNVVNRDE VDDLLTNRLK SMPAVRGVVH
GTMVLHDVLF EKMTWEQYVM VIEGKVQGAW NFHHALADQA LDFFVAISSA AGAVGNRGQA
AYAAANCFLN AFVQHRLSLG LPASSIDLTM VSDAGYLAED AERLAEVARN LGSDSICESE
VLALLGAAIE GRLASTCNNH TITGMRITPA VQPFWTSDAK FKHLRLAMEA QAAQREGGNS
GAISFGVAAK AAQSLEEAEA AVCRGLVDKI STVLMLEPKD MDVTRSLSHY PLDSLVGIEI
RNFIAREFEA NMQVMELLSS GSIQALAKAV CAKSKLISFT
//
