ID A0A364KR68_9EURO Unreviewed; 1776 AA.
AC A0A364KR68;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAO66038.1};
GN ORFNames=BHQ10_002050 {ECO:0000313|EMBL:RAO66038.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO66038.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO66038.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO66038.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO66038.1}.
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DR EMBL; MIKG01000002; RAO66038.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364KR68; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000249363; 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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 1.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
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:UP000249363};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 404..839
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1701..1775
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1776 AA; 194652 MW; E856B101A091DA82 CRC64;
MTLRPNTTPS DSQGDFVKLK LAYFSNEFPR DDLHDLLRLL WSRSKDRTHP ILANFIDEAT
LAIREEIRLL PNALRTLIPP FQTIFNFADY PELRKGQLSG SIDGVLLVAV ELATFIGYYE
SHPDQFDFDS ANSFLAGLGI GLLATTAISL SSTLADIPVA GAEVTRLAFR LGVLVDDISI
NLQQRDWSSP DTPDSWAYVI PNVEADVVQK ELDIIHAKEK APEASKIFIS ALSQTSVTVS
GPPARLKNVF RVSDFFRDRK FISLPVFSGL CHASHIYDEK HVREVVRKSP LDSSFKYSPG
IPIFSTSTGR PFEASTATEL FERVIHEILT QKIQWEKVVD GIIENANNSG TVDVQVLVFR
VSLPIHDLVE AVKTHLPQAN ATTDELISWA HEGSLSISPR GSLQSKIAIV GMSCRLPGGA
TDTESFWELL EKGLDVHKKI PADRFDVDSH YDPAGKRVNA SHTPYGCFID EPGLFDAPFF
NMSPREAEQT DPMQRLALVT AYEALERAGY VANRTESTNL HRIGTFYGQA SDDYREVNTA
QEISTYFIPG GCRAFGPGRI NYFFKFSGPS YSIDTACSSS LATIQAACTS LWNGDTDTVV
AGGMNVLTNS DAFAGLSHGH FLSKTPNACK TWDSQADGYC RADGIGSIVL KRFEDAEADN
DNILGIILGA GTNHSADAIS ITHPHAGSQS YLSREILSAS GINPLDVSYV EMHGTGTQAG
DKEEIQSVSN VYAPITGNRR HSKQPLYIGA VKANVGHGEA VAGVTALLKV LLMFDKEMIP
PHVGVRNGIN PTFPKDLDKR NLHIPFEKTP WIRDPGRKRI AAINNFSAAG GNTTLLIEEG
PIREVTAVDP RSTHVVAVSA KSKGSLKRNL ERFITYLGKN PGASISNLSY SSTARRYHHN
YRIAVGTSDI QELKKQLNFH LNKVDSHKPI PNTGPPSVVF AFTGQGSSHK SSDLALFKQS
PVFRSHILTL DGLAQKQGFP SFVPSIDGSF LKDHKHSPVV VQLALLCTEI ALAKYWGSLG
IKPDVVIGHS LGEYAAMHVA GILSANDAIF LVGKRAQLLQ EKVAIGSHKM MAVRASVEQI
QDAAGDKSFE IVCINGPKET VLSGTSEEIQ AIYEPLQVAG YKTHILDIDF AFHSSQTDPI
LDDFEEIARS STLFQEPHVP IISPLLERVV FDDKTIDAKY LRQSTRQTVN FLSALRFAKD
ISIIDETQVW IEIGPHPVAT SFVKATLPSV NVTVPSLRRD EDNFFTLAHS LAALHVAGVQ
INWSEFHRPY ESALRLLDLP TYAWNDKNYW IQYNGDWALT KGNTFYNAEK GLAAAKTTPV
VSSSLRTSTV QQIIEESFNG SAGKVTMQSD LMQPDFLAAA YGHKMNGCGV VTSSIHADIA
YTLGEYLHKK LIPNTKTVDI NVANLEVSKG LVARKNTSVP QYIQVSLSTA DIHSGVAVLK
WYNVQTNGMI AEPFATANIF YGNSNQWLDS WIPVTHLVQG RIEALERLAA EGVANRFSRT
MAYTLFASNL VDYADKYRGM QSVVLHQLEA FADVKLTEEK SGTWTVPPYF IDSVAHLAGF
IMNVSDAIDT KRDFSVTPGW SSMRFAKPLI ARSRYRSYVR MIPTTEDTNV YLGDVYILQD
DVIIGMVGGI KFRRYPRLLL SRFFSAPDEA GTAAAAIAPK PVISTPAVTV VAEPAKPDPS
PEILQPSSTA PALGVNSIDS DSTAAKAMLL VANEAGLELD DLKDEASFAS LGIDSLMSLV
IAEKFREELG ITVGGSLFLE YPTVGDLRAW LVEYYS
//
