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Database: UniProt
Entry: A0A225AMD8_9EURO
LinkDB: A0A225AMD8_9EURO
Original site: A0A225AMD8_9EURO 
ID   A0A225AMD8_9EURO        Unreviewed;      1880 AA.
AC   A0A225AMD8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:OKL58418.1};
GN   ORFNames=UA08_05979 {ECO:0000313|EMBL:OKL58418.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL58418.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL58418.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL58418.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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:OKL58418.1}.
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DR   EMBL; LFMY01000009; OKL58418.1; -; Genomic_DNA.
DR   RefSeq; XP_020118539.1; XM_020268732.1.
DR   STRING; 1441469.A0A225AMD8; -.
DR   GeneID; 31005735; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000214365; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR032088; SAT.
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; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
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.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214365};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          395..820
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1801..1878
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1635..1654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1780..1801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1637..1654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1784..1801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1880 AA;  205284 MW;  54D205BF0EB4E6E3 CRC64;
     MESKLLDAAR PSAAFFCPQN KPPKPKYLDT IRRYLRSNTL LAPFRVAILD SLSTTWEILA
     DAHPGIAAMT QGPRYIQHFH DWIAATESPV TSSQMEWTEI MSGLISLPLL TIMQIVQYFQ
     YLEARQIRHK QFVEEIRVGG AQGYCGGLLP AAAIAASRNE EEVVKNAGIA LRLSLAIGAY
     AELGDDPDTP GPTTVVLRTK YLGQAGEIVA KFPGTYISAI TDPETISIVG PTKVVEDLRV
     YAESQGLKAT KLHLRGKVHN PENAELCKEF IELCEKYPDL LLLPTPAALQ TSMRSNKTSK
     ELRHSGIITS LSLEVLESTL ANRCEWYDLL SVMADKLDET GKEHTFALFG TGRKNCVPLA
     PFEQKQQRIS KLDIATYVEK LDIPRDGRTL DQYPENAIAI VGAGCRLPGA NSIDELWDIL
     SSGTSRVEKL RPSRFDLSTI SRGTVGPDAK QTSRRELYGN FLDDVESFDS NFFGVSPREA
     MYMDPQQRLL LETAYEALDA SGYLRTHRRD DFDNVGCFIG ASYTEYLENT SSYNPTAYTA
     TGTIRAFQSG RISYHFGWSG PSEVIDTACS ASLVAVNRAC KAIQSGECPM ALAGGVNVIT
     GVNNYFDLGK AGFLNTTGQC KPFDATADGY CRADGIGLVA LKSLRQAVAD GNDVLGVIMG
     VGTNQGGLSP AITVPYYRAQ ISLFKNVVKQ SGLKPGQISY VEAHGTGTQV GDPIEISSVR
     EVFGGSQRSD FVNLGSLKAN VGHSETAAGI GSLMKVLAML KHGKIPPLAG FKTLNPKIPA
     LEPDFLRIPT EVKSWDVSFR AACVNSYGAA GSNSALICAE APRMTAMATA SLSHIKTNED
     EALQYPILIS AINNASLKAN ASKLASYIRQ NRGEQDLRIA DIAFTLYDRR KHHRVQWNGE
     AHDLEALAQK LDQVEEGVEV PTTPKSVVLA FSGQSKQTIG LDASWYVSFP RLRHYIDLCN
     NTIMRLGYSA ILPAVFASDP VEDVVALQCG TFAVQYACAK CWIDAGVKVD AAVGHSFGEL
     TALAVTSVLS LEHALKLVAA RASLMQTKWG PQRGTMLAVE ASVETARQII STVNRSLEIA
     CYNAKTSQVL VGTDSDIELV ERLITTDARF KGTRLARVKT SHGFHSVFTE PLLEELDLVA
     QALDFKTPSI PLETCTEVPA EVDEQTIDAS RIVQHTRTPV YFGDAVARLE SRLGPCVWLE
     AGSDSPIIPM VKRAVQNPSQ HTFLKLKAKD TARPTDIISQ TSISLWQEGI SASFFAGFYS
     SPSGAEGSIA FKQIWLPPYQ FQRTRHWLQY MDVVTEERKI SEARIRSASP NGSVIQQPHS
     PSMRLVTARR RDSTSWSSLE FAIHTETSRF TDIVSGHAVR DQPLCPASMY MECVVMAAQM
     VEPSVSVKSL TFQNLSFQGA LGINYSRDVS LLLEGDGEYL AWNFTVRSTV KDSKGRPTTH
     AKGRFSVSSH IDFQLYERMI ADRMNEILVH PQSERLMAGR AYTLFSRVVN YADTLRGITE
     ITILNNRHAV AEVSRPKVAV STTESTAAGV CDTVTLDTFI QVVGLLINSS ETCPADEVFI
     ATGIDSIIMQ DCDFSDSQSD SWKVYAMATT RSESHVAGDM FVFTKEGKLI FTGSGVQFSR
     FPIAKLEKVL EGIGMNSGAK SPSSNDNNKR GLSTRRSSDY LIQTNGNAKP AVNGHAFKPN
     MTVEIDDQTL VAQDSVSMRP SVIKSAMIKN DSNLGTLGLD SLSKLEFVNQ LRAEFGNEIS
     SQNDFAQVAL LYNKLFANDS PVNGKPVHVG HVEHVDEIEL DGPSSPSTEH TPPALRGVGS
     QSQLRIRQRI LELIAENSGE AIGNIGDEVS LQDIGIDSLS VIELKEAFED AFGIQFGDWD
     FGLHLTVKEL LDFVASSGAA
//
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