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Database: UniProt
Entry: A0A428PMU6_9HYPO
LinkDB: A0A428PMU6_9HYPO
Original site: A0A428PMU6_9HYPO 
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
//
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