ID A0A319E110_ASPSB Unreviewed; 2428 AA.
AC A0A319E110;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PYI03687.1};
GN ORFNames=BO78DRAFT_374507 {ECO:0000313|EMBL:PYI03687.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI03687.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI03687.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI03687.1,
RC ECO:0000313|Proteomes:UP000248423};
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; KZ826377; PYI03687.1; -; Genomic_DNA.
DR STRING; 1448318.A0A319E110; -.
DR Proteomes; UP000248423; 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; 3.30.70.3290; -; 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; 3.40.50.720; 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:UP000248423};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2343..2418
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2428 AA; 263793 MW; 17BB66A0978F5328 CRC64;
MTRAEPIAII GTGCRFPGSA STPSRLWELL QNPPNVASKP PSDRFNIDAF YQAGKARPGM
TNAPESYFLQ EDVRTFDAPL FKISPAEAAS MDPQQRLLME VVYESLERAG LQLQRLQGSS
TGVYCGFMNY DYGQLLNADT SALHPFLLSG TAPSVLANRL SYFFDWRGPS FVLDTACSAS
LTAMHLAAEA LQNGDCSLAV AAGSSLLLSP DPYIGESQMQ MLSPTGRSRM WDEGANGYAR
GEGVAALVLK RLSDAVADGD PIECVIRSTG INCDGRTKAL TMPNGEAQLE LIRSTYARAG
LDPLRPEDRC QFFEAHGTGT PAGDPQEALG IAGAFFNEDS PADDILYAGS IKTVVGHTEA
TAGLAGVIKA SLAIQHGVIP PNLHFNQLSP LVAPHASHLR IPTQALPWPE LPPGVPRRVS
VNSFGFGGAN AHAILESFTR PNQIMTHREP TIPGILPFVF SAASETSLTA VLQQYVEYLD
ACPTMELLDL ATSLLSKRSS LSHRLIITAD STESLREKLK GEIRQRPGDA SSTITRRLGT
EPKRMLGVFT GQGAQWPQMG LDVISQFSQA AGWLQELQQS LDTLPAEYRP TFTLLDELSA
PEAISRLNTA AVSLPLRTAL QVIQVRILRS LGIEFAAVVG HSSGEIAAAY AAGRLTAGEA
IRVAYLRGVA AQYAGAPGES GAMLAVGISL DQAEALCSEA PYAGRVCVAA VNSPASVTLS
GDSELISELE WLFESLEQSP RRLRVDTAYH SHHMIPCADP YIQAMEDCQI EGLQGLSATK
WYSSVFDDRV MENLDVQYWS DNMLRPVRFS QALTAAMKDI PELDIIIEVG PHAALQGPTL
QTLSSIKSDN ADVPYIGLAN RKSGGIEALA RAVGSFWAYL GAETLDVLPY VQLFSPSIEL
EYLSDLPTYP FDHSQKYWGV PRLSTARLNR RLPIHPLLGS ITPETGEAEW RWRNYLRVQD
LEWVDGHQVQ SQVVFPATGY LVMALEAAHV IANGRPLHLV EINDLAIDRA ISVPDDAPGM
EILFTFYQTD GNQSKLSGAF TCQASFDGTF SCCASGRMEV AFGEPDAALL PSRGAPTAGL
RSVDSDHFYG ELEKLGYGYD KLFRTLQDIK RRKDVASGTI PALDRDDDST LLLHPATLDT
GLQALIATIG HPGDGQLSGL YLPTKIARTT INPAFCRTTG NTFHGPFGVD AALSGIENAG
MRGDIDLFTS EGDGVVQIEG AQIAPLSRPI IDSFAEEVWG PLLPSATLSS AVGTPDFHCT
RREGDRLALL YLRDTQQQLT AEDRQQLDWH RGRYVEWMDW VLARVRAGSH PLYPAQWLEG
DTATVLSPEV KNANEVNATG LNVVGVNLLG WLRGQTSIME ELRRDDLLGR LYREGHEVKT
MTRNLAGIVG QLAFRFPRAK VLEVGAGTGS ATRKVLSQIG RDYHSYTYTD ISAAFFEEAQ
SAFIDHEDRF TYEVLDLERD PTAQGFQEHA YDLVIASNVL HATQSLNKTM THVRRLLKPG
GRVAILELTD TESLTFSLIY GVFEGWWLGE PDGRKWGPLL SIDGWDQVLR TSGFGGLETV
SPPEEAQLFG LSAFTAQAVD DHIQRLQHPL SVLAAGQYPD LIMLGGATPA TEHLISGVRN
LVAPFFGRIT HMATLEAFAA PSDASLPVIL TLTDMDQPCL QGLTTDRLRS LQALVGSARK
LLWVATGTPG QDPYVGMTKG LLRCQAYENP HALFQHLTIR DPNAVSSPEL IVATALMRLA
HIEVGNDYTL ANSTESPEWE LLVENDGTVK IPRMQSSSAM NHRLLSSRGF PSPEPIEPQN
ARVQILSDDG KFALASCPPK SSLKETANEH FVHIRVHYAT LFGVCIDGTF LHVVLGRNEK
TQARAVALSV DHASAVLTPV SWCWDVPSWL PEGDEASFLY QVSMALVARH LVSKTPANSM
LLVHEASRAL QESVAAIASL KGVRSRFMFA TFAPETDVRI QSSLPPTVAT YGVQTFYGAP
STPANGVMPA KDALVSACLL AEQRVGSQPA VATISPEDIR TYSSSSSRFE IVDWVHSGPV
LAYSPSASSL VDLSAHKTYL LVGMTGDLGR SVCHWMITRG ARSLVLTSRS PNIDPQWLED
MSAIGARVVV MAMDVSDRSS VLKVHGRIRA ELPPVGGVVN GAMVIRDVLF AEMSLEDVVQ
VLKPKVEGSL ILDELYQDDS LDFFILMGSF AGVFGNFNQT AYAAAAEFMQ GLVHQRRLRG
QVGSIIHPGE IRGVGYVARM DPHLIDVMTQ NIGHLILSER DLLESFAEAV LAGRPDSSRA
PVIISGLAMT DPAVYPDVLW YSNPLLWPYI EYFQQSEVLE ANQEQVPIKV QLQSAGSLVE
AAEIIATGFR IKLRRKLHLP MDGELPGTAL LTELGVDSLV AVDLRVWFVK ELGVDMPVLQ
LLGGSSIDAL ARSAAERFDP GLLSLVQA
//
