ID A0A317VN51_ASPEC Unreviewed; 2200 AA.
AC A0A317VN51;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PWY75764.1};
GN ORFNames=BO83DRAFT_463458 {ECO:0000313|EMBL:PWY75764.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY75764.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY75764.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY75764.1,
RC ECO:0000313|Proteomes:UP000246171};
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 (DEC-2016) 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:PWY75764.1}.
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DR EMBL; MSFU01000009; PWY75764.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:BO83DRAFT_463458; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase 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:0032259; P:methylation; IEA:UniProtKB-KW.
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; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR020843; PKS_ER.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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; SM00829; PKS_ER; 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; 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; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2121..2198
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1279..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2200 AA; 239397 MW; AE335AF56CB97A21 CRC64;
MDGSPSPTDS PALEPIAIIG YSCRLPGQVS SPSDLWELCT RGRSGWTPIP KDRWSVEAFH
HPNASKPGTS NQAGGYFLGD ISRFDAPFFN VSAQEAISMD PQQRFLLECT YEAMESAGIS
REYMAGRSIG VFIGANWPDY ETNNIRDTET TPMFQATGGY PALQSNRISY MFDLKGPSLT
VDTACSSSLV ALHSAVQSLR SGECTEALVG GCHLLLTPEN SITMSMQQLL NDEGKSFAFE
ERGNSGFARG EGAGIIMLKS LSAALRNRDP IRALIAHSGV NQDGKTRGIT CPNGAAQEEL
IRRVYKEANL NPADCGFVEA HGTGTAVGDP IEATAIQAVF GKGRNARNPL YIGSVKTNVG
HLEGASGIIS VIKSAMMLER ELILPNAGYK NPNPKIPFAE WHMKVVNRTR PWPRGKRYIS
VSNYGFGGTN AHVVLQKAPS QLPQEEGTST KDKEGKRRLL LISAHDREAL RTRCKEYCIY
FEQRPEVFEN TLFGNFAYTV GSKRSHLPYR IALSATSLDD AGVQLAQMKI NPVRAIGGDG
PSVSFVFTGQ GAQWAQMGMP LMDEFPVFAA AIHRADKHLS EGLGAEFSLR EELLQTDTKS
RINMPYISQP ACTALQIALV DLLRSWGIQP VSVVGHSSGE IAAAYAAGIF DLEGALTLAY
RRGQMTELLR SKYPDLKGTM MAVGTSVEAI QPMLKTLYSG YATVACVNSP SSVTISGDVP
AIEELQGILE EKKIFNRRLI IDVAYHSDHM KKVSEAYLSA IASVQPSGAA TATFFSSVVG
DVSDPTDLSP SYWVQNLTSP VLFANALGKM SAVGSRPNLM VEVGPHSALK GPILDTLKAL
GSSVASEVGY VPTVVRKVDP SQSLLNAAGA IYVRGGTLNI NEINFPFSGT GTCNVLDDLP
RYPWQHDTVF WHHSRISEKH RFRDGQRNDI LGSEAFYSND LEPTWRNIVR LDDIPWLRDH
KMQGMIVYPI AGYISMAIEA ARTRAQRYST VAAESQFELR EVSVGAALVL TDDLDTEITI
TLRPYAEGTR GASNAWDEFR ICSWNSKRYW IDHCTGLVRV SPNKANRKRN PVVDFVELEE
SAFAKKSSEV LEAATYEIDT ENMYKVLSDV GAGYGMAFQG FGNCFSGPHH SRADLYVCDT
KSLMPKHYEA PVVIHPTLLD TLLHLTWPIL GKGRMDLETL YVPTVIKSLV IDGNISSAGH
HFPARCMGGS GRGRPEPTKF DLWMTPADSS EVLINMEGLV MTPINDTGCD NKVARDLCYQ
LQWKPLIKVE QATTGEAIQT KQSNGHSKPH AIEHVNGHGH GNYCQDNKSK DEILIVTFGD
CALAAEQVQE VISTKAIRWS TSISSLTDCD AKQKRQHVII LQTAVKTLRD LTVADFANVQ
QILLSSTNLI WVYRNDTPDS QMIVGLMRSL RSETDAKAAT LGLSAEDLER PAGPILAAMK
ALWPTGKTFS SCTDFEFITK NGELMVPRIV SDNALDEFVR KETSDDLTLE TQLFVQPGRR
FKLEIESHSA LDTLYFTDDD VEALGDDEIE IEVHATGLNF KDVAVTMGQL TQPYIGIECS
GVVTSVGKKV TNLMIGERVM ALPLGAYSTF ARCKATSATA IPETLSFEVA ASVPVVFCTA
YYALYELARL QHGVGEKVLI HAAAGGVGQA AIMLAQIASA EIYATVGSAE KKDLLISKYG
IRADHIFYSR DASFGRSIRE LTCGGVDIVL NSLAGDLLRE SWECLAPFGR FIEIGKADIT
KNTRLDMLPF ENNLSFHSVD LTKVAAYKPR LMHQLLDKVS WLLAKGFIHS VFPLSVCPIA
EIEGAFRALQ TGKSMGKTVV VPREGDRVRA VVAKTRDDIL RTDATYVVIG GTGGLGRSIA
RWMSQKGARN IVLASRRGIV DIPVQTLINA LRPSGTNIVV KACDVSNRTS LDAMLKDLED
LPPIRGVIHG AMVLRDMLFE NMHFADFQAV ADSKVSGAWN LHHALAPHPL DFFVALSSVS
GVVGNKGQAA YAAANVFLDG FMEWRRSQGL PGTSLALTAV RDAGYLATVD VARRAEILRT
IGTEGMTEAE VLALLAAALT GDLSPQTITG LASSTRQPLW PQDAKFELLA PKAYGGEEDV
ADEGISQPLH VQLTNAASKE EKVQVCYEAL AAKLAQVLVL NLEDIEPSLS VSALGLDSLV
AIELRSWIAR EARANVQVLE LLSTGTLGAV AELIVSKSGI
//