ID A0A3F3PJ14_9EURO Unreviewed; 2632 AA.
AC A0A3F3PJ14;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=BcPKS20, polyketide synthase {ECO:0000313|EMBL:RDH26878.1};
GN ORFNames=BDQ94DRAFT_176075 {ECO:0000313|EMBL:RDH26878.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH26878.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH26878.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH26878.1,
RC ECO:0000313|Proteomes:UP000253729};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004721}.
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DR EMBL; KZ852111; RDH26878.1; -; Genomic_DNA.
DR STRING; 1341132.A0A3F3PJ14; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000253729; 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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
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; 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; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
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; 2.
DR Pfam; PF00975; Thioesterase; 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; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 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:UP000253729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 477..877
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1775..1849
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1872..1949
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1362..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2632 AA; 284812 MW; 636A1C5F2754A2DE CRC64;
MSITQGLIHG VNWTPATVSD TPLAFQNIVF LVNPNANPEQ LPHYQQQLGE AGYTTTVVKD
AIQLESHLRS GTIVVHIPDV ARDKDGVYDA AKASCASLIA AARILSKHRV HKLFSVFATP
SEIAELGYAP LYGLARVLKM EVPDIFGGLF EVDSGSFPLK SLKYARGFDV VRISQSMPHT
ALLQPITNEP DEAVAQLRLQ TGGTYLITGG TRGMGLEIAK WMGKRGAGNL VLVSRRGLSE
GPQSSLSNDK NEALASCVKE LEGQGVTVHV LAIDLSLPEA QKTLQQAIDG LQLPPVKGVV
HAAGVAGYHT LDRCSPSDLD NTMAPKALGA LALDSIFPPG SLDFFLLTSS VGQLVGFPGQ
LTYAPANAFL DGFAVYRRRQ GDACTSIQWT CWRGVGLMAQ NKSAIRMILR GMQARGIADI
SPEEALAALE RVSQLSTDQV AVVRAVTLEA EEPLRHPILQ NITPRKSAQK SYLDYPVHSV
AIVGMSCRTA AGDTADDLWR VIQTGQTTVR EIDASRFPEA ATRKGPKLWG NFLSDPKSFD
HGFFKKSKRE SAALDPHQRV LLETTYHALE SAGWLAQEQL PETHEWSLSR DITGCFIGMN
APDYPLNLAC HPASPYTGFG MLRSFAAGRL SHHFGWTGPS HTIDTACSSA MVAIHQACQA
ILAGEWGFLS ETGPCKTFDA RADGYCRGEA VGILVLKPLS RALQDGDEIH GVLLGTGNNQ
NINNTSITNP VLESQAALYR GVLARGGITP HQVSYVEAHG TGTRAGDPVE VEGIRQVLGG
PERGSLLHIG GVKANIGHSE GASGVISLIK VLLMMKHRQI TPQANFERLN QNIAALEPDR
MAISTSLQEW RSPSGPLVAL VNSYGASGNN AAALVASPPP LLTSSASPTS LASPGTPSAW
PVLISAASKA SLSAYCQKLK EQVVQPTLRP EMGVHLAFQL ATKQNRQLDY LFATTATSLP
ELEVQLSTPD NHTMTLTTSP QPIVLLFSGQ NGNSVPAAQS LYDASVTFRK YLHRCDEVVK
SLDGPSLFPA VLDGIDGGDD IILRHAAAFA IQYSCGMTWL DSGVKPQAVC GHSFGEWAAL
TVSGTMTLEA GMKLVTGLTL MGETGRASII QKFWGPDPGS MVAIEADLVG TRTTPSQHLE
PFRRKHPKST FDIACYNGPN HYVVAGRTTD IDLLEADLQE EKSRGAKLRF KVLRGMHAYH
SIMADSIIQQ CAQLSATIPF QTPTLPFESC HKDPWTGPGT NVIARNTRGP VFFADAIDRI
VTRLGGSCTF LEAGIGGPIV AMARNALSHS LSPSQQSSHS FVAIGGKDPI RGLAEATVAL
WRNGHPFVQF WPFHAKQRES YLPVTLPPYQ FEKHPHWLEY IPPLSSDRNP QPSQPPASSQ
RSGPCPHCGK EISQYPYIAL NVTSPSQDYR LLATFRIDPR SHRYQELVKG HVVVGSPISP
AAMYLELVAH AVVQAGHMGA ASLSSEGHDI WIEALEIKAP LGLDPQRSVL LTLNRKSDGV
LAFELCSTNP FNENVAASKP TSHATGVVIV GAKNSHMPTE ATNRWARLTH LLEREPDIDA
LRGAMVYKVF STMAKYSAGY RGLRYIVGKG GESAGIISMP VDAERDERAR SPNDGIADPM
VLDNFLQVAG AFVHSLRVTD SPDDDESDMS YICTGMGSVG PLAKLPGGGS YRAYAKIQRE
DQKEVALDLL AFDTDTREVV WAVQGLKFSR VPRPSLARAL AAANPSTGEE IRGVQAKPAG
QQVASRKVMD PKVDQLLTSL SPPSHPPPPV IPQGLDILDG VRQVLSRSLD VPPDDVSKQA
TLEELGTDSL VSAEIQAGIG ERFGIDISTE EFAALTTVTD LCDLVRSRLG SDAGDSGVAM
QPSDSGDDTG DEINTEWQKT VFEILSHSLE VPVANIQLDS ALEDLGTDSL ITPEILSNIK
ESLNVELSST EFAALVDVRS LLTLLAGALG VDNARLTPAT GSSSASDTVR LDTKSMHTAF
QEVRRNFDAH AKIFQLTGYW EQVYPVQLQA VAAFILDAFE KLGCPIRTFQ PGERLPPLQE
TLPKYHREVR RLWDILQEAG IVENQEANIF VRGPAQLDCT PVKPAAQLSQ ELIAAFPPFA
STHGLPDLLG PHLAECLTGQ ADPVSLLFGS EQGRHLLEDF YANGPDLRAA TQVLCDFVSA
AISAHAQTVG GDGGEPFRIL EVGAGTGGTT KHLIPLLQAT GLPFTYTFTE LSVSLLARAR
RTTFAGTPNM EFRKFDLEAT PEPELHGRYH LVISSNCVHA TRDLRRSLQH IRQLLRPHDG
CVALVELTQK LAWYDLVWGL LDGWWLFDDG RDYALQSPWA WERAMRDSGF AHVDWSECAS
RESRSVRVVC GFTNSSPEKH QQLKAPSTLL HRATTSSTGG HNLFLCPDGF GAGAVFTALA
PHLASVPDVS VYALSSPFVA TAMDPTDLDQ VPSIEELAGI YVAEIKRRQA TGPYTLGGYS
FGGVVAFEAA RQLLEEGDIV ERMVLIDSAC PTFAHSMPFE LVQFLDAIDA TNNRGHGPVG
ASTHFTLARE QLRRYRVRPL PGPTKGLIRD VVLFSAREGV DKQDSVPRPQ VRHAEQSIVD
WFLDDRTDDS ALGWEELLDN VRVVRTEGNH FSMMMTPWVD SWGPKLANVL VA
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