ID E9EIL3_METAQ Unreviewed; 2571 AA.
AC E9EIL3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EFY84249.1};
GN ORFNames=MAC_09711 {ECO:0000313|EMBL:EFY84249.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY84249.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY84249.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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DR EMBL; GL698644; EFY84249.1; -; Genomic_DNA.
DR RefSeq; XP_007816051.1; XM_007817860.1.
DR STRING; 655827.E9EIL3; -.
DR GeneID; 19254022; -.
DR KEGG; maw:MAC_09711; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR InParanoid; E9EIL3; -.
DR OMA; WHVYARH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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; 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; 2.
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; IPR001509; Epimerase_deHydtase.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF14; ITERATIVE POLYKETIDE SYNTHASE AFOE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 434..858
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1697..1771
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1656..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2571 AA; 280879 MW; 277CFDFF8F022F8D CRC64;
MGGMAYLKPQ EATMLLFGPQ AFSSSKLLEK IRNTLSSDSS EKQCILDTVA ELPQHWSSLI
ERIPRINGVV PGEKHLADLA SWLQQGPLDE YKLERLPNLV LTPLVILAQL TAYWRYLEIN
KPEKATSGAE NDLQANLVSK RNSRDGSPLQ TIGFCTGLLS AFAVASAKDQ ADLEKYGAVA
VRLAMLVGGL VDAQEAWNVE FGQGPSKSYA TAWHNAQERQ ELNRITDSLF PQAYISVLYD
ESRATVTITQ QAVPAFLQAT KDSGITVAEV GLRGRFHSPS KDFLTLTDTL VELCNSTTLL
RFPSSSELAL PTYTNDVVDG RPVGSTTDVK GLTLTEIALR AILVKRCNWY STLAAVQANL
RNDVAFLSFG PDRCVPPTLA RQLGSRLVEF YDLDLDGEVP QHLSSVLDPD AHLLHQQQSQ
SQPQPQTQPR DESDNAIAVV GMSIKVAGAD DLDEFSQMLR IGKSQHEEIT SERLMMDTLF
REGDKDPKRK WYGNFIRDVD AFDHKFFKRG PREALTMDPQ QRLFLQASYQ AVEQSGYFAE
TTSSSPVRDK NHVGVYLGAC AGDYEHHAAG HTANAFTATG NLKSFIPGKV SHYFGWTGPS
MTFDTACSAS AVAIHTACRN LLSGECTAAL AGGVSTITNF LWHQNLAGAS FLSPTGQCKA
FDDAADGYCR AEAIACVFLK KASDALADGN TTLGYIPSTA VYQNQNCTPL FVPNSLSLSQ
LFTDVIKKAH ITPYDVSVVE AHGTGAPVGD PAEYESVLQA LAGPTRSKPL VLGSVKGHVG
HSEGASGVVS LIKIIMMMQE GYIPPQASFT KMSHYIKTSP TDMMEVSTSL RPWNEERKIA
LINNYGASGS NASMIVSQSH YNSSGQASSF IRGSGVNNAP FPFLITGFDA RSITAYTAKL
LAFLKAREKT SVSLADVSFS VNRQSNRTLQ YGMMFSCHSM SELEEKLSMP DKSVAPVQAV
RPVVLCFGGQ VSTFVGLDQN IYRSISVLRH HLDQCDAIMR SLGLSSILPD IFSRSSITDP
VKLQSMLFAL QYSCAKSWMD SGLEGKIVSV VGHSFGEITA LCVSGVLSLL DAAKLVVSRA
KLIRDDWGPD PGAMIAVEAD EETVYKLLAE ANRRYEGEYP ASIACYNGPR SFTLAGSTRA
IDAVAETIPQ LGSIKSKRLN VTNAFHSTLV GPLMSRLEEP RTTLQLSGSK LDQPPLSHMA
SRALAGMVKP DAHHFQALSL TNTEKGIHGL TDATLSLWKQ GLRVSFWGHH PLQTTEYATL
LLPPYQFDKV RHWMELKSPL KAITEAAAAM AATAGPVVIQ PQQSVDERLL GLWSLTAYEQ
NESPKKARFR INTGSDKYKK YISGHLIAQT APICPATLQV DMAIESLFSL NPHWTASSMQ
PVVLDMSDHS PLCVDPTKTT WLEFDSLNDS ASVWAWKIFS TSSTGSNETH VEAKLHIRSP
DEAAYQTEFG RFERLVTHSQ CTAVLNLPDD DDVDILQGRN VYPAFSDVVD YGELYRGVRR
VVGRAGECAG RVVTKHNGES WLDVPLSDSF SQVGGLYINC MTDRPASDMF IATGCEMAMR
SPRMARLGKD EVPGSWHVLT RHHRQGEKVY TSDVFVFNAT TGMLTELMIG ITFARVAKAS
MSKMLTRLTG DESVLKIKPS QAQAALTTTV AAPVPFHPTQ QPQVLDKSAT ETSASQKTSS
QKKGTESGVS AVKPSRPDVT NDLRNLVANI SGVEPHEIEL DTEMAELGID SLMGMEVARE
VESVFKCTLD QTELMEATSL RKFVVCLNNA LYGPGYDNAA DESVGTDKDD DFSSQGASDN
TPTGTGATTP SVPDIKPNAI HDVPSVKPAA TATVAPPVET SLKIASSAIL KAFGDVKMFT
DQEIRSFKLD RIHRAVLAGS NRLCTALVVE QFEKLGCELR AASPGQVLNR VPFQPQHERL
MEFVYKFLEK DTRLIDIDEF TGQITRTSIP VPRKASGAIF AELLQAFPEF AVANKLTNYA
GNHLADVLTG KTDGIRVIFG SLEGRDLVQS LYLDHSFNRM QYGQMRDIIQ HLTQMLPRDQ
GPLKILEVGA GTGGTTCVLA PMLASLGFPV EYTFTDISPS MVANAKRKLN KEYPFMRFAV
HDIERPPAGE LVGHHLVIGS NAVHATHNLV TSLANVRKAL RPDGFLMMLE MTESAPFIDL
IFGLLEGWWL FDDGRKQAIV SAEHWERDLH ASGFGHVDWT DGSLPENRYQ KVIIALASGT
QSERLPCPMP EDACEPAQGL RDVVAHEAEA NRLMSKHIDA FAAPRLLCSG KTQGAILRDG
HDAVVLVTGA TGSLGSHVVA RFAEEAAVKT VVCVNRKTGT PVTQRQAEAF SSRAKLGLPA
EEYAWLAHNV TLIVYNAWPM SGTRPVKAFE QQFQALRNLL DLARDIADTR GHDSGFRVGF
QLVSSIGVVG EAGKARVPED RVPFSATLLW AIARPNRFRT MVVRPGQIAG SRKSGFWKPI
EHFAFLVKSA QTLRAWPDFD GVLQWTPVDA AAGVLVDLCR VAQLHNAPEP YPVYHVDNPV
GQPWKEMNLV LADALGIPAE GIVPFRYWVD MVRRSPLPAE TDNPAARLMT F
//