ID E9EI51_METAQ Unreviewed; 2488 AA.
AC E9EI51;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EFY84397.1};
GN ORFNames=MAC_09549 {ECO:0000313|EMBL:EFY84397.1};
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:EFY84397.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY84397.1,
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; GL698629; EFY84397.1; -; Genomic_DNA.
DR RefSeq; XP_007815889.1; XM_007817698.1.
DR STRING; 655827.E9EI51; -.
DR GeneID; 19253860; -.
DR KEGG; maw:MAC_09549; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_1_1_1; -.
DR InParanoid; E9EI51; -.
DR OMA; THLACNA; -.
DR OrthoDB; 20296at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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 InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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:UP000002499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 523..598
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 616..1039
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2002..2077
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2488 AA; 267587 MW; A756522C5DD9FA66 CRC64;
MSGISDHDYQ VLVNEFNATD DISLLGSRLD QLFEKVVDRF PDNIAVIHNE NEVTFTELNT
SANTLSRGLA RRGLQQGDVV GLAVSRSIDL IVVMLAVLKL GAAYVPIDPS FPAERINQMV
EDAGLKLILL SDRPTKGLAC WTDLCLSVAD ARDGSITDAT NLGTEIQSRD LAYVIYTSGS
TGRPKGVEIS HGAAANFLSS LRKHEPGCNE HDRLLAITTI SFDMSALELL LPLVSGSAMI
IANTSAVKDP RELISLMVRH KVTILQATPA TWTMLLESGW KGNPRLSKVI CGGEPLSRQL
ADRLLAVADS VWNVYGPSET TYGSVGRVGE GDIVVGNPVA NGRIYVLDDN MLPVPIGCEG
EVYIGGGSVS NGYRNKTGLT RSRFLTNPFH GGVFFRTGDL ARFIGPGKLQ VIGRIDGVVK
IRGHRIDVGD IEAVLVQHVN VSEAVVISRD DRLVAYCVLH APCHDATSLG SILRPWVAER
LPAYMLPTFF VQMDALPLSP SEKVNRKALP DPIEAMQNQT MTQPTSELEQ QIQAIWSDIL
GHDRVGIEDN FFNIGGDSVR IIRMQAALEN QLHRPVPTPK LFEHYTIKAL AAYLTGTSKD
NKQDLQTVSR TFAGSHEDIA IVSMACRLPG GVATPEALWQ LLQSGGETII DVPKDRWDAD
KLYSADPNID GTSYCRRGGF LDSIYSYDAS FFGISPREAQ AMDPTHNLML ELCWEGFERA
GYTRDQLSGS PTGVFLGVSN NGTTNSTPPD LKGYSITGSA SATMCGRLSY TLGLQGPSLV
VDTACSSSLV ATHLACNALR QGECSMALAG GVSLLTTPGI HIEFSKLRGL SADGRCRAFS
DDTDGTGFSE GAAIIVLKRL SDARRDGDDI HAVLRGTAVM HGGSSAGLTA PSGPGQVALI
RNALARAAME PGDIDYIEAH GTATKLGDPI EATALAEVFG TERSGLDPLR IGSAKSNLGH
TQAAAGVVGL LKVVLSMKHN TLPRTLHVSE PMTAVDWKRA NMELVLENRP WLPNSNRARR
AGVSAFGIGG TNAHVILEES PTPAIEETGD ATLPSLPATL PFVLSGQNDS ALRAQAEKLR
LHIKSGDGKD SRLSDVAYSL ATSRSHLHRR LVVTAADQAE TLERLASVSS GSINSLNMNE
VGSPTLAMLF TGQGSQLPGM GKDLYAVYPV FRDALDEIAA RFTDLELPLL DIMWAESGSQ
SAALLSRTDF AQPALFALEV SLWKLWQSWG VKPDFLLGHS VGELAAAHVA GVLDLSDACR
LVMTRGRLMQ AIPRHGKMAS LEASSAEVTA AIQELKQHDR VEIAGYNTPS QTVISGDVEA
VEAILVHMAG LGRKTKLLDT SHAFHSFHMN GMLDDFKTVA QNIRFSSPKT RIISSMTGRL
AEAGELERPE YWVQQARNPV RFSDAFQKLA SQGANVFLEL GPSSMLCGLG AACLADPSQV
SAALWLPSLK PNMDGPSVIQ NSLGELHVRH VPVNWAAYFE PFDCKRVILP TYAFQRENFR
PTNKAGWFGV ISPSTGVDDA VPRVEDMMFE INWRRVETKN IQPRGAWGLF CPSGETLWTK
EAQRALSAAG IQLVPVSRLQ EADQLDGLLS LWDSDADTVQ MAHNFTALAL AQLHEAIRTG
FAVPMVWVTR HAVGAGADDR PVSIGAGPLW GLMRAARSEH PELRLRLIDD DEETKCATLS
LALMLADLTE LAVRREQLLM PHMERASRAA PPPVGQPFVR AGGAVLVTGG LGDLGSLVAR
RLATAHGVCD LVLVSRQGTN SPGADGLVAE LAELGAKATI VGCDLADLDS LGSVMQLFTP
DRPLRGVIHA AGVVDSGTLS SLTPHKCATV FAPKVDGLWN LHQLTKDMDL DLFMMFSSIS
GVIGLPGLAN YAAANSFIDS LAYLRRAQGL PASSVAYGTW AGDGMATTLV PTTRAHLSQL
GLGFLPPEAG LEIFEQAVRQ GRALTVAAVL DLQRLKAYYE EQGGVSPLLH SMLGETKVRK
PVNEAVNLRE VLADAAPEQH DSIVLHMVQA TIAKALGYTK TEDVDASRPL QELGIDSLTA
ILTRNHLATL TGMALPPNIA LLYPNLKSLS EFLLCRLLGE VESSASSPSE TDGATSSTPT
SAASYVDMAD IRRGVLDSTF QFDNAASSGV PEAVFVTGAT GFVGAFMAHE FLKRGISAYC
LVRASGFQEA QERMIKTLKQ YSLWRPEYEP LLVAVAGDLS QPLLGLDEVV FDDLANRADA
ILHSGALVDW MRPLEDYIGP NVLGTHEVLR LASCGRGKAV HFISTISTLP IHAGYGLAEH
DREHGYGTSK YLAERMIVAA RFRGAKASSY RLPFVAASAA SGHFRLDRGD FLNNLVTGSL
ELGAFPVINA DLSSVLPVDY LCGTIAAIMT EDQGRVGEDY DFANPQAPTF KHFFALMCAV
GGSKEMLPFG EWHRRALEYA AAHPKSPLAR ITTVIDGYTD ETAGSLMSGS PVGKHVLGLD
AYQAPPLDEE YVRRYVYCIE AARAKTRT
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