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
//