ID A0A0A1UND4_9HYPO Unreviewed; 2486 AA.
AC A0A0A1UND4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EXU95975.1};
DE Flags: Fragment;
GN ORFNames=X797_010933 {ECO:0000313|EMBL:EXU95975.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXU95975.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXU95975.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXU95975.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU95975.1}.
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DR EMBL; JELW01000058; EXU95975.1; -; Genomic_DNA.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000030151; 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: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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 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; PF13489; Methyltransf_23; 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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 10..441
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2486
FT /evidence="ECO:0000313|EMBL:EXU95975.1"
SQ SEQUENCE 2486 AA; 269372 MW; A05395A5896DE161 CRC64;
MDTDNSEWAS EPIAVIGMSC KFSGGASNPD KLWDLMASGK TGWSEIPKER YNLEGVYHAN
HERNSTTHVK GGHFLDDDVA AFDAAFFNYS AEMAQAVDPQ FRLQLESTYE ALENAGLPLS
QVMGSQTSVF AGVFTHDYQE GIIRDEDGLP RFNVVGTWSP MSSNRISHFF DFRGASMTLE
TGCSTTLVAL HQAVHTLRNR EADMSVVTGA NVMLNPDTFK AIGSLGMLSP DGRSYAFDSR
ANGYGRGEGV ATIVIKRLSD ALAANDPVRA VIRETALNQD GKTDTITTPS GAAQVELMRE
CYRRAGLDPR GTQYFEAHGT GTPAGDPIEA GAVAAVFAGG QGRDDKEHYL RIGSLKTNVG
HTEAASGLAA VVKGVLCLEK GLIPPTVNYE RPNPKLKLDE WRLKVVRMME QWPDSLVDGP
RRMSINNFGY GGANAHVILE SADPWTSTSG LDLEPVSGRH SKNGNKGHVN GNGYTNGSHD
TNDATDDAKV LVLSARDERA CQQMVSDLKA YLEKHRSLGH EDSEQLLRNL SYTLGERRTL
FPWVAAHQVR LDKDGGLDAA IQALESPRFK PGRRAPDRPR IGMIFTGQGA QWYAMGRELL
ASYPVFRQSI EEAEAYLRAL GADWSLLEEL QRDAKTTRVH ATKISIPVCV ALQVALVRLL
EAWGITPSAV ASHSSGEIAA AFAVGALTHR QAMAAAYYRA VLVADETQHA PGAARGAMAA
VGLGVEAVQS YLNMLTTGNG KAVVACVNSP QSVTISGDAD AVQEMEDLCK QNGVFARRLR
VQQAYHSHHM DPFAEAYRER LRVEMARDVV QGDKQRVQAA KKELGAVFSS AVTGGRITDI
KEIASPDHWV GSLVQPVEFV DAFTEMVLGD PDDPTGRSVD LLLEVGPHTA LGGPIREILS
LPEFEGIELP YWGCLVRDEH AGDSMRSAAI NLFRQGQPLI MDQINFPVPA YDGESPLVLT
DLPSYPWNHT MRHWLESRVN RAIRERSQPP HELLGMPVAG HDPSTAVWRR TLRVTETPWV
RDHMVQGAIV YPGSGYICLA IEAARQMEKA AGATDRDKSG GTISGFRLRD VHFLFALVIP
DSADGVEIRT TLQPVPEREI GARGWRRFEV SSVTPDNRWT LHAKGMVMVE QEAAAPETAE
RRPLSTYTRH PDPQDLFANL RARSVYHGPL FQNTTKIIQD GREPRSVCDI TIRHEASSDT
DPVEAAQNTL LHPITLDAIV VAFYSALPSV GALQEDPKLP RSVASMWVSS NISRESGRTL
RCDTRLLHED AQSGIADMTV VDGQTDATVL KIQGVELASL GRGSGRTARQ HAAVPSKWEQ
GVCSKLVWGP DLSLRNPLAL AQIKKELVHA GSDAEADKAR SLQRLCSYFA HDALQSLTSE
DVARLQEHPH MAKYHAWLRE LTKAAKNCAL DEPEKRQEYI AAAAPQGIDE EWVCRLGPLL
PSILRGELHV DQVSGPLLNE YHANAMRRSV ALGQLSALLC KIAHKNPGAR VLQIGAGAGA
LATRRMLETL GTPKTPMVAS WHITEPSWDS LEDARAQLAD WTHLLAFDQL DIGQSPAKQK
FTPGSYDVVV AFHALRATKN AAIAAANVRS LLKPGGTFLF ADVTKDQVDV DFTFGLLPSW
WQGEEECDHP TLTTSSWDRV LRDAGFSGAD LEIRDSESDI IHTNSVIMST LPLAKDQKPD
LGRAHHRESF VVVISSKAPP PPGFVDLLSR RIQALTGAGS LAPEHLVLEQ SSSDTYKAKT
CVFLGEIDEP ILADLDAVRM EGLRAMVSQC SGLLWVTTGG TVASEAPERA AHQGFLRVLR
NEYIGRRLLS LDLDPAHAAE RWSSGGEVAV SAIVQVLEEG FGRSNTEAGP AEFEYAERDG
VLQVPRYYKD EQCNDMVAGP LVPSWGEVLP VVKDDKGSID AVASIPLEPL FQEDVTLRLE
VGIPGHLDTL AFLHHEENDE ALTPELVETY PPGLRGIITR VGAEAQEKGY NVGDRVMALL
AGASFASHAR VPWHGVIQIP YGMDFVKAAS LPLAFTLAYA GLVDTARLSA GQSVLIHAAA
GAIGQAAIML AKCLGVTDIY ATAGSQEKRD LVQREYGIPA ERIFTSRDAS FATAVLAATK
GRGVDVVLNS LPGPLLQASL DAIAPLGYLI EIGKKDIESN SLVALESFSR GISLVSLDAP
TLLRRGPGVG RALGEMVRLI EEQALKPVHP VAVYPMQDAQ AAFRFVQTGA QMGKVVLSAG
PDELVHAVPR PKGVTARVRL QADASYLIVG GVGGIGGSVA HWLVAHGARN LILLSRAAGD
LDLDVNNNTH GALFVRELRE AGCRVKPVSC DIALASSLTT ALRACEDDGF PPVRGVIQGA
MLLRDAVLEQ MTLDDWRGGL RPKVFGTWNL HTEFSQPDSL DFFVMLSSVS GVVGITSQAN
YAAGGSYEDA MARWRQSRGL PGVAIDLGPI SDIGYVSTTA KVAERLRKDG DFAMLDEDTV
LRALHAAVLH PLGARSQIIV GLNSAP
//
