ID A0A395NQ76_TRIAR Unreviewed; 2337 AA.
AC A0A395NQ76;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RFU78094.1};
GN ORFNames=TARUN_4155 {ECO:0000313|EMBL:RFU78094.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU78094.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU78094.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU78094.1,
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:RFU78094.1}.
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DR EMBL; PXOA01000235; RFU78094.1; -; Genomic_DNA.
DR STRING; 490622.A0A395NQ76; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 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; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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 26..414
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2251..2335
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2337 AA; 254965 MW; EBF10EB4CD41E6C4 CRC64;
MAINDSGIEA PQRSAWPKST REPNAQDPIA IVGMACRLPG ENTSPTKLWE FLKRGGIASN
KVPENRFSIK GHYDGSKKPG TMRPPGGMFL ENIDLADFDA SFFGISTAEA ISMDPNQRQM
LEVVYEAMEN AGITLEQVSD APVGCFIGSF ASNYHDMQNR DPEDRPASIE IGIGRAILAN
RISHALNIKG PSPEHVMDTG PIRMAHSPTG YCHTFDIKAD GYVKAEAVSS VILKRLDDAI
RDGDPIRAII RGSTTNSDGR TPGIASPNPV AQAAAVRTAY ANAGIKDLGL TTYLECHGTG
TQAGDPLEVK GVSSVFSQFR SEDSPLVIGS VKSNLGHSEP SAGLSAVLKV VLALEHGIIP
GNPTFETPNP NIDFRGLRVR ATRSAIPWPE AAFRRASINS FGYGGTNSHL ILDDLAALED
VKPSHISSYV TGDEEDLLEA EEEYKPHIIV LSANSEQSLR GYVDALDQHL SNLEVKVDLP
NLAYTLSERR SRHFHRAYAV VRSKDSIEPN AFTYGKLSSD APKIGFIFTG QGAQWPQMGK
ELVETFPVAR EILSQLDAAL QELPTPPPWS LLNELVEARS AEHLRQPEFS QPLVTALQIV
ILEILQGWDI EATAVVGHSS GEIAASYAAG YITKEEAIKV AYYRGYSAKH SKSTGSTGVG
MMAVGLGAVD ATPYLEGLQD QVQIACYNSP KSVTLSGAVP ALETVKERIT KDGHFARLLQ
VDLAYHSKFM TEIGADYEKL LEKNFKPLES KNKAAVMFSS VTGDTMGATA NARYWKDNMT
SAVRFDEALQ AMLSKSDAPN FLIEIGPSGA LAGPVSQIRA ALGAKANNVK YTKALNRGTD
SILALYGVAG SLFVEGASIS LTKVNQEADS PKPKVIFDLP NYVWNHSTKY WHENDASRDW
RFRKYPHHDL LGTKVFGAPW HSPSFRKILK LEQLPWLRDH KMGTDILMPA SGYISMAVEA
LYQTSQALQP VEGVERASQL CYRLRNVTFD KALVLEDNVD TKVMFTLTPH PGTGNPWYDF
KVASSRGDDL WLTHCVGLIR LSDPAANEPA SVEDVTPLKF PTPAHMWYKA QANIGYGFGP
AFQKLIDVES LVGQRRSRAT VSLEEPEAAH SPQSHYPLHP AVLDGCFQTT QPALRAGDRS
ALDSVVVPAS IDELIINATD SRPTVGVSLG VAGYTGRGRK EEAKNYWSSC TVYDPEKRQL
LMKLSGLRCH KLDTGIELHS QHTLSRTVWR PDISYLYDDQ LISLARGSQP KIQDILDLVA
HKSPRLRVFE VNLVPGDSSS LWFDDGDRSL RRAYSAYTLA SSDAKSIINA RADYEKNGQT
SFELHDFAKS AFDAKEQKID LALIKVSSLD ENLAQLARNI RAILADGAIA LFVESEAAAD
VDSDGSSVVV VGDKGSETEE TNSFAANGFE KAATVSVDNG KRLHFVRAIQ QEEQTKRHVS
VIHLIPESRL STGLKSTLRS EGWEVTEHSA PFADLEKDSI LLILDDLVAP VLPTIEEAQW
NSIKQLVLQG YRTLWVTEGS QMNVTKPNNA LAHGLFRTIR AEDRGVSVTT LDVEYGESPS
AFASINRVLN QVLKLNPQAP VEPEFVERGG IIYVNRVVPD EPVNQFKKAG QLGGEPVTKT
LRDIRPVAML RAERLGTLDA LRYSEMSSEP VQVEPGMIEV ELHASGLNFK DIAVTMGIVP
ENEHLLGLEG AGIVRRVGAG AEQFKIGDRV AILRNGTFAN LIQTPVERAH KIPDWLSFEE
AATIPLVYLT SIYSLFDIGG LKKGQSVLIH SAAGGIGLSS IQLAQWVGAE IYVTVSTEEK
RQFLEKEFGI PRSRMFSSRD TQFASAILEI TGGKGIDVII NSLTGELLDE SWRICADGGV
MVEIGKKDIV DRNYLSMEPF DRNCSFRAVD FSYKQVTDDI IQRLLAQTFQ MVEDRHIKPI
LPITTYRFDD IPAAFAFMRS GKHIGKIVIS DGQESASVPV RPATRKLALR ADRSYIIVGG
LKGLCGSLAV YLAREGAKHI IALSRSGCSD ERSQKVIANC AALGCTVYDA AADVSDPKAV
KSVFETAAVP VGGVIQGAMV LRDRPYETMT IDDFHTTIAS KVQGTWNLHN AALAQKEPLE
FFTLLSSISG VVGQKGQANY SAANVFLDAF SQHRRSLGLA AHSVDLGVIE DVGYVAEQGG
MKQHFDDKQW TGINEAMLHR ILFYSILQQT DTINKDSADQ MITGIPVPQP ADSDLAYDAR
FSLLFGSNEG GAALQGGNSD ERDIQAFQLL RSSAPDHAVL LAAAVELTGA KFTKTLRLSD
PIEPGKSLAT YGLDSLSAVE FRNWVRLTLG AEITVLDITN ASSLFALCEK IIAKLPK
//
