ID A0A395NR88_TRIAR Unreviewed; 2226 AA.
AC A0A395NR88;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RFU78582.1};
GN ORFNames=TARUN_3625 {ECO:0000313|EMBL:RFU78582.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU78582.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU78582.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU78582.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU78582.1}.
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DR EMBL; PXOA01000201; RFU78582.1; -; Genomic_DNA.
DR STRING; 490622.A0A395NR88; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..401
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2137..2217
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1227..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2226 AA; 242056 MW; 78D013461431A059 CRC64;
MSSLNQEDMA QEDLMPIAIV GMACRLSGGV STLDDFWTML SRSRDGWRPM PEERFLKAHF
LLVDPQQRHL LECTYEALEN AGLPKNAVAG SNMGVFIGGA SSDYRLGTLK EVDQIPMFDA
TGNHQSIQAG RISYYFNLHG PAFSADTACS SGLYALHLAV QSIRSGESDS AIVAASSLYL
QPHDMVSMAG LGLFNEHGKT FAFDHRAKSG FARGEGTGCL ILKPLHQALA DNDKIRSVII
NSGTNQDGKT AGLTNPSGDA QERLMRDVYA RAGISPDDTG YVEAHGTGTR IGDPIEANSI
YRVFGAGRTK RMPLYMGSVK SNVGHLENAS GIISIIKASM MLEKGFILPN VNFEKANDAI
PLDEWNIKIP TSIRPWPRDK RFISVNSFGF GGSNAHVVLE KVPPSYADLP LDSQNKIPRL
FVLSAHDEGA AKRVAEQLGV YIEQHPEVFQ KRLVRDMAYT LGERRSHLQW RIAITASSCD
GLAKALNGMG AAPAVISEEP RVAFVYTGQG AQWAGMGKEL MESHPIFANT IKACSDYLQE
IGAEFSLLEE LAKGSKESLV NEAHISQPAC TAIQLGLTSL LESWGIRPAA VIGHSSGEIG
AAFATGAIGL EEAMSVAYWR GKVSSELRLK HPNLRGAMLA VGAGAEEVRN IIKTKGLQKV
TVACENSPNS VTASGDEEDV DRLAAELESR SIFNRKLRVT MAYHSAHMQL VAEDYKAAIK
YVTSKATSDV EFYSSLNGSK LDSTSCLGPS YWVDNLTKPV LFSPALKELY LGSKPNVIIE
IGPHSALEGP IKQILKTVSP QAALAVKYLP SLIRNQHATS AALNCAGSLF VKGYPINLKM
INLPYEGVRV PTIVTDFYPY PWSEHKYWFE PRSAKQLRQK PFPRHDLLGL LEDSYSEIEP
KWKNVISTDD VPWLKDHRMQ SLATFPLAGY ICMAVEAASQ RAQMRGIPSE QINGFRLREI
QVSKALILDD GAPYEMIFSL KPYAEGTRSY SNEWDEFRIS SWTSSRGWLE HCSGLVGIKK
IAPANPVSAA ILSASSARRQ QIMATNCDQL PLEGFYAELE TRGAGYSGVF RISLDADVRI
RGQYSTAALT VPDTATVMPS SYETASIAPA AFVDLLFQLT FPILGAGSGE MPSLFMPSAV
KDIDISSSLP NKPGDRVQVV AHGCPNFAAP GPVDFFIDSW YGDSIEPVAK ISGFRMTPVN
GDIDEGVSPR SICYKVQWES LDGIKKQIDR KENKNGAIEN NHESSSSASP IKVTSNTRND
HISDSTKCHA NGYRRPDKTC EEVNGNSVER SSRNDTNGEF AVDSLPGNLS DADFVIISHH
GRSNALVGTL FDLLELRTTK RPRLVGFSDV VPESTSCYIC LSEIDEPLLA NMTAETFEGM
QNLLTTCQSM LWVTSGAYRF AESPEGNISQ GLLRTVRSEA SKPVASLDLD PHSKLDAQAT
AELILRAIKV STATNEDGAP VDYEFAEEGG NLVVPRVVKQ DDMNLAIFHD IEASAAPPYM
QPFEQPGRRL AVAVGTYGAL DSLYWKDEHE MPLGPLDVEI KVACTGMNFK DVVIAMGQVP
SPYLGVECSG TISRVGSRVG SLKVGDRVCA MSLGAYGTYS RCLASSAAVI PDGMSFKVAA
SIPVVYCTAY YGIMDLARLE YGEKILIHAA SGGVGQAAIQ LAQMVGAEIY ATVGSADKKQ
LLMEVYGIPD SHIFYSRDIS FGPAIREATG GDGVDVVLNS LAGDLLRETW ECLAPFGRFI
ELGKRDITVN TRLEMAKLEY NCTFSSVDLT LVAAERPKIM ERTFASVMRL LENKTITPIG
PITPVSIQDV EGALRKLQSG KTTGKLVVTH SGRSQVKATH PAPRSDMLEH DATYLIIGGT
GGLGRSITRR MVRRGARHII LLSRSGKVTD ELSMLMKESR KLGASLYVMP CDVADEKNVK
ALVDELQDDL PPIRGIIHAA MVLRDVLFEK MTFEDYEAVV RSKISGAWHF HNALINTPLQ
FFIVLSSVAG IVGNRGQAHY SAANTYLDAL VLYRRRKGLA AASIDLAAVE GVGYLAENAA
KMSQVMRNLS DNTVGEAEVL ALIESAMTGK VDCFCQGQVI TGMGFDNASS LPYYASDARF
SHLRDALLAT SADADTASGS ENLTICQQLR RCITVEEAQD MVTLGLRHKL GAILMLPEEV
MAARQGNTSI TAFGLDSLNA IELRNWIGKE LQAHLQVLEL LTSGRVADLA ALVLRKSRIE
GVWTQK
//
