ID A0A319E552_9EURO Unreviewed; 2466 AA.
AC A0A319E552;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ketoacyl-synt-domain-containing protein {ECO:0000313|EMBL:PYH98773.1};
GN ORFNames=BO71DRAFT_480073 {ECO:0000313|EMBL:PYH98773.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH98773.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH98773.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH98773.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ825808; PYH98773.1; -; Genomic_DNA.
DR STRING; 1448320.A0A319E552; -.
DR Proteomes; UP000247810; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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; 1.
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; 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; 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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF48; HIGHLY REDUCING POLYKETIDE SYNTHASE SDGA; 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; PF08242; Methyltransf_12; 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; 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; 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:UP000247810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2370..2445
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2466 AA; 272296 MW; BDD5AFA54A088D5C CRC64;
MASLEPVAII GTGCRLPGSA SSPSKLWDLL HHPRNVASKA PSDRFSHDAF YHPDGHHGTS
SSPESYFLTE DIWAFDAPFF NISHAEAESM DPQQRLLLEV VYESLERAGL KMESLRGSNT
GVFCGLMNTD YNNIISHDLD EIPTYTSSGT AASMLSNRLS FFFDWRGPSM TIDTACSSSL
VALHQGVSAL RSGDCRMAVV VASNLILSPR EYIASSKMHL LSPTGRCRMW DEDADGYARG
EGVASVILKR LSDAIASGDP IECIIRATGI NADGRTMGLT IPSSIAQSQL IRSTYASVGL
DPQLRPEDRC QFFEAHGTGT QVGDPQEASA IYESLFGHPS LPDDVLYVGS IKTVIGHTEG
TAGLASVIKA SLSVQQGIIP PNMHFSCINP MIVSFTSRLR VPTQPLPWPN LSSGSPRRVS
VNSFGFGGSN AHAIIESYTP PENFNLGHGF SPQILPFTFS AATENSLTNV MERYAEFLQD
NPQIDLIKLA ESLTKRRSAF RHRVILTAVS SEALQSKIQA ELERRKSTSS SSSIVSRAND
APKQVLGIFT GQGAQYPQMF WDSISASPQA LVWMAELQES LDTLPSQYRP SFSMTKELST
PKPFSRLHEA AISQPIRTAI QIIQVNMLRA LRIEFSAVVG HSSGEIVAAY AANAITAKDA
IRIAYLRGLV IEQAIINGPS GAMLAGGIPW KEARALCDEG GFSGKVAVAA SNSPVSVTFS
GDTDAVQDLE WMLRSLDLTV NRIVVDTAYH SHHMVPCAAP YLRYLESSDT RAYPLSTKWF
SSVYKGKQLQ IEDINPQYWV ENMLRPVLFS QAVTAALADN PDLSLVIEIG PHPTLKGPVL
QTLSEIKHID AEIPYFGLAE RGSDSIEVLA RAIGLIWAYL EPNIDIQRYL SLFGKSYESH
IIKHMPTYPF DKKRSYQFIS RLTKARMHRS DPPHPLLGVL SPETGDNEWR WRNYLSRAEL
EWLHGHRIQS QLVFPATGYI AMALETAAAI ARDKSLRLVE IDEMLINRAL PIPNDMSGVE
TIFKVEQISS EDNVVLGAFT CYASFSGVLK TCASGKLTIT IGKQDAMLLP PQSLAPLVSR
PVDIDNFYAS LERLGLGYSG LFRGLQVLTR HTNGSMGMIS NSDMTSSLLL HPAIVDSSLQ
ALLAAMVSGQ LHTLHVPVSI EHIAINTMFC KHGSVETRNQ LVIETLLHDV NPNGATGDIS
TFDIDGHGVY QIEGFHVAPL TLPEDRAIFS EVVWGPLLPQ TIQSDMYEDF ELQKDLYLAE
RCALLYIRDA RNCISSEEHK HLDSYRSRIV AWMDRVLSMT SDGIHSICRP EWLEDNMEDI
LEMSSVSSKD WTSLHIAGRK LVGFITGNTK MTESLCKEEH SDQLYDDPFE IKLKNSQLAT
FVEQIAFRFP RLKILEIAAG KSSATESILN KLNRSYHSYT FTGISPTSFT EMQTVLSDYE
DRLLYQELDI NQDPAEQGFK EHSYDLVIAA GTLYITKGLV QTLTNIRRLL KPGGYLVARV
GTNTDTNRLA LMFGQFENWR YDGAEGRRRS PVMCIKEWER LLEKTGFGGF QAILPAGRLE
FDSIIVSQAI DDRIQLLRDP WKSSKILSDR VLLIGGATET TANIMQDLRA FLTPQFDRLV
VASSLELLDL QDTFGWCVLS LTDIDTPVYQ NLADARFSGL KMLMNNASEL LWVTAGPESG
QPYWSMSKAM VHCMAYENPQ STFQYLNIPD RREVSAQTLA TNFMRLIHTA MENDHSLDTF
VNSTELELQL VQGSLKIPRI HMSDSMNQRY SANHRVVKDY VDLQRTILEV VPPSGRHREF
ALCERVQSEN HVEEHHRQLR VYYSTMTALK LDGIGFLHLI LGRDTRDKTR WLALCDRHAS
EIAAPLRWCW QVPDFLCESA EPKFLMKTAA SLIALQVINQ GRPDTSLLVH GADALSPSIR
DALSALVLIR NIRLYFSTSV HSTHPQDDML FIHERSSSRA LSRLLPDDIS VVARCQGAEC
GVYTRIEALF PDAMTIDIAS LGRISSSLFK FSDPITAGQT FLTACGVALQ LGKSQVVDLL
SVQDIFEYAP GSNQLKILDW SHPGQVPVLV QTASSMVSLS AHKTYLLVGM TGDLGQSVCQ
WMIGRGARAV VLGSRTPSVD PQWIKEMATL GAQVLPMAMD VTNRESICHV RDTICSQMPP
IGGVVNGAMV LKDCLFAQTT LEDMKSVLAP KVEGSIFLNE IFGNRDLDFF ILFGSAAGPL
GNVGQTAYSA ATGFMSALIQ QRREQGLVGS IIHPGLIKGV GYFARADRTR QDTIEKNTGT
PHLTEQDLHE LFAEGILAGR PDSGRNPEVI AGYKVIDPAE NPNALWLRNP KAWSLVNPST
HSISRVSSSD DSISMKIQLE SARSMDGVIE AIAEGFIKEV RSKLQLSDDE SLTGAAALTE
LGVDSLVAIE LRQWFVKELS VDIPVLQIIG GSSIRDLSRL AASKLSTEYV PNIDKSGSQQ
RLVPDS
//
