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Database: UniProt
Entry: A0A317VN51_ASPEC
LinkDB: A0A317VN51_ASPEC
Original site: A0A317VN51_ASPEC 
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
//
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