ID A0A428PMU6_9HYPO Unreviewed; 2298 AA.
AC A0A428PMU6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP54_009944 {ECO:0000313|EMBL:RSL54340.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL54340.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL54340.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL54340.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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:RSL54340.1}.
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DR EMBL; NKCI01000112; RSL54340.1; -; Genomic_DNA.
DR STRING; 1325734.A0A428PMU6; -.
DR Proteomes; UP000288168; 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; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR013120; Far_NAD-bd.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF40; STERIGMATOCYSTIN BIOSYNTHESIS POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 367..802
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1633..1711
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1752..1827
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1598..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2298 AA; 251647 MW; DCC363962198496A CRC64;
MTDTLNLYLF GDQTFDIKPH LQNLFQQRDH LFLQDFLTKA YNAIRVEMYR LPGKVRSDLP
RFTCQEDLLR WDESGKRCIA LDMAMTTLYH LGTFISQAGI SSYDAQSSRV VGLCTGAFAA
AAISCSSFTA DLIPMAVYSV IAAFRTGMLV TDVARRVDQS QDLDQSWALL VPGSKSAAAV
EKFCKESNLP LTSRPYISAY TPNGITISGP PKTLAQLISS PSFKGLTSKS IPIFGAYHAP
HLYSQMDAKK IVASLSYNAA TALSEQIPLL SSTDVKLEER SFATLLEDAV AQALVHPLHW
SSILGDIQAC LQDVSPEQFS VVPIGSTADH LIYTALKQTP LRSLVPNTHG QSRQYVPDVG
PEPASKKPKL AIVAMSGRFP GAKDNEAYWD LLLQGLDVHK PVPSLRWDAQ THVDPTGKTK
NTSATPFGCW LDDPAEFDAR FFNISPREAP QIDPAQRLAL MTAYEAIEQA GIVPDATPST
RPDRVGVFYG VTSNDWMETN SAQGIDTYFI PGGNRAFIPG RINYFFKFSG PSYAVDTACS
SSLAGIHLAC NSLWRGDIDT AIAGGTNVLT NPDFTSGLDR GHFLSRTGNC KTFDDGADGY
CRGEGVATLI IKRLDDALAE NDPILGVILG AYTNHSAESE SITRPHVGAQ RAIFSKILSE
AAVDPYTVSY VEMHGTGTQA GDATEMASVL DTFAPPLVNN KKARSDEQAL FLGSAKANIG
HGEAASGASS VIKVLNMMQK NMIVPHCGIK TKINHKFPTD LLQRNVHIAL KPTSWERKNG
PRRVFVNNFS AAGGNSALLL EDAPPKVDRP ATVDSRVQFP IAVTAKSGSA LQGNMRSMLK
FLKENPEVSL GELSYTTTAR RIHHQHRVLL NGPTTEDICK KIEAALQNNT GVNRPKSAPS
VVFTFTGQGA QYPGMGKQLF EESSFVRSEL IQLDQIAQSL GFPSMLPVIQ SEEQDIGIFA
PTAVQLASVC LQITLSKLWA SWGIYPAAVV GHSLGEYAAL NVAGVLSDTD TLFLVGKRAQ
LLEQKCTRST HSMLVVKGSE EEIAEVLKGN EYETACINSP IETVLAGTNE QVADLKELLT
ASAMKSTLLK VPYAFHSSQL DPVLSEFQEI AAGVTFSKPN VPVLRPLDGT VVDHCDSFGP
EYLANHSRQS VNMLGALSTA YRDHVITDRS MILELGPHPA ITGMIKAVLG QQVTCIASLQ
RGRQPWDVLC AALKGLYDAG ANISWAEYQA DFEGSQSVVA LPAYSWDLKD YWIQYVNDWS
LRKGDAPIII NNAPRLESTT IHSVVEESGD SKKTHMIVEA DISRKDMSPL VQGHEVDGIP
LCTPSVYADM ALTLGRYLLE RYQPQQKENL IDVSDMTISK ALILRGDGTK QPLQAHLDAD
WATQSATIKF MTFDNKRNLQ KHSECVVRFR DHSLQKTLQD KATSVKQKMQ ALRNGIATGE
TARYNRAMVF RAIRPLARFH DDYRAIDEII LNSPTYEASS RLSFGSIKRD GNFHTHPAII
DSLTQGCGFA MNCNDDTDLD VEVFMNHGWG SLQMFEPLQF DKSYTTYTQM RPGEDKLWHG
DVVIFDGDRV VAFFGQIAIQ GVPRRVLKVI LSLESGKKTQ PQRPVQNKTP TISVSAPVNG
PSAVQKLTLP LEKVQPSRIS TALSIIAEES GIDVADLTDG TNFSDVGIDS LLGLTISARF
REELDVDLDF NALFFDHPTV KDLKMFLMGS DDDGSATSSS NASDSGLESP PSGLITGAVT
PDVHEDFANP FEVDFLRALD IISEESGVAR EELDDDTNFA DCGVDSLLSL VITSRFQEAF
GLDVGHETLF LDCQTVGDLK EMLMREMGGK PPVPSVPISK PVFLPVPEVV QAPPTKTIAV
NSTHSDTANL DARQKAIDEL VQKYTAGFSA PTSTPSAGLP ADNEKVVLIT GATGGLGSHL
VFSIAQLEDV KTVICLNRDN REEPETRQYK AMREKGIRFP ENLKHKLRIF QTDTSKPHLG
LDKSDYDSLV GSVTHLIHNA WPMSAKRPLS GFESQFQVFR NLVDFGNETA SLRPESFKFS
FQMVSSIGVV GQYGLAAGQT GKIVVPEQSA TVDSLLGNGY AEAKWGCERM LDETLHKYPN
RFRVMVVRLG QIAGSKTSGY WNPMEHFGFL IKSSQTLNAL PDVDGALNWT PVNDIADTLS
DLVLSDRTPH PFYHIDNPVG QQWRDVNAIL SDALRIPNLV PFKDWLQLVR QAPQQDNPAA
LLADFLENTY LRMACGGLVL DVKNTLEHSK SLRAVGPVSE VVTRKYIHIW KEIGFLKTTA
EDKAGFEAER LRLWGPRV
//