ID A0A395NUD1_TRIAR Unreviewed; 2519 AA.
AC A0A395NUD1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RFU79720.1};
GN ORFNames=TARUN_2474 {ECO:0000313|EMBL:RFU79720.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79720.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU79720.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79720.1,
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:RFU79720.1}.
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DR EMBL; PXOA01000141; RFU79720.1; -; Genomic_DNA.
DR STRING; 490622.A0A395NUD1; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; cd02440; AdoMet_MTases; 1.
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; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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; IPR013217; Methyltransf_12.
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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
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 53..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2414..2491
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2519 AA; 275445 MW; 218CB902916A74F0 CRC64;
MTASVDSPAA RNGHENHYEH INGGQRTNGN GHNGIIDETA NGRSHSNGTA EAYEPMAIIG
CGMRLPGGIE TGEAMWDFLD NKREGRCRVP DDRYNIEAFY GPGRTGHVGS QYGHYLNYLD
LAEVDTSFWS MTRQEIEEMD PQQRLALEVV YECFQSSGTT NWKGKKIGTY FGIFGEDWMT
MQAKETQHTG VYRMPGSGDF VVANRVAYEF GLEGPSMVIR TACSSSLIGI HEACLDIQRG
ECESAIVGGT SLILNPHMTI AMTEQGVLSP DGRSKTFDAS ANGYARGEGV VAIHIKKLSD
ALRDNDPIRA VIRATCTNTD GRTAGMLQPS PTAHAALMVR SHELAGLDVS RTAMIECHGT
GTPIGDPLET TAVARVFGKH GVFIGSLKPN LGHSEGASGV SSTIKAMLAL ERGLIPPNIN
FKEGNPKIPF EECRLTVPVE TTPWPADKAQ RIGINSFGIG GANAHILLES AAEMGVARPS
EATPISDTHY LLTFSASHQD SLRQTVQRHE AYLRQHPDRL TDLSYTLNAR REPLPHRAFA
VVDASALDQD LQISTFERAG DLPAMAFVFT GQGAQWATMG AELLDTNVIF RESIAQMDQA
LRHCPDPPSW TISDELRKTG KESRLMAAEF SQPCCTAIQV ALVDVLASWG VRPTGVVGHS
SGEIAAAYAS GALTRDAAIQ IAYYRGVVAK DVKSRGAMAA IGLGRSAVES LLKPGVIVGC
ENSPSSVTLS GDFNAVEETM QTIREAHPDV LVRALRVDCA YHSHHMKTVE QQYLSKIGGL
SVKKPLISFF SSVTGEVLQQ APDAAYWAAN LTSPVLFSTA VSLLAKNMTA ATVLLEVGPH
SALAGPVRQI LGAAGANKAV YASTLIRGEK AQHALLTAAG RLFQLGVELS WERIVSPGRT
LTDLPLYAWH REGPFWCESR LSQHWRFRKF PKHDILGERV AAASDFGPTW RNVLWLDHVP
WIRDHGVSGD IVFPAAGYMA MAGEAVRQLG DVDDYSYSLR EVTISNALVL HEGQPTEIIT
HLRPVRLTNT LDSVWYEFEI SALHGDRWLR HVVGQVRGGA EYERPTPAIA PRLRTVNAPH
WYGVLRRFGL QYGPRFQGLR DITADVIERA AVATIAGPSA PEAGPHESEY TMHPTAIDHA
LQLYSVAASW GQGRRFTQLV VPSYVGAVYV QSAGGKDILL QAGADVTPRG AIFGDAVGTS
GGTTVFRLEN VRMSPLADAT EARGVDPHAA VELVWKPDIR LIDNASLMYT ARDLRKPGEL
PEVERLALAC MVEGSLKLAN WSEKEITNPA NAFLAKYRAW FSAVREEALA GTYPNVPDCE
EIAAMPSDAR RALIEEIHSE TATTGAGPLA TAVYRVYHIL ESLFQGKADP LEVLLEDNLW
ARLYDIVRFV DTNNYFKVAS HFKPNMRILE IGAGTGSITG AVLETLSSQP PHRERHYYSY
TFTDISPGFF GRAKERFAAY EAVEYKVLDI SQDPLEQGFE AESFDLILAS NVIHATPSIA
TTLGNVRKLL SPTGFFFLQE LAPPFKWVNF VMGAFSGWWL GESEGRINEP YLWPDQWKPY
LEAAGFDGIS AVHHDGQFNA TMIVRPALPA VAPRITVLSH KTTRQAHVED VVKALEKKGY
GVDLRIWGQD IVPGQDVVCL VDIEKPYLQD MQLEGFSQLQ DFIRGLNGAG VLWVMGLAQV
KCTNPQYGQI LGLTRNMRTE LSIDFATIEL ETFDSAGWDA VATVLPEFQR RSITDSDTNP
VMEWVFADGF IQISRFHWTS LNDELSVPDA GAGETNGVVA RKLDIEKRGF LNSLYWKEYT
PAKPEGKSLR MRNYASGLNF KDVLISMGII DGRAIEGDGL GCEVAGIVEE VGPEVKGLEP
GDRCVSIASG SFSTHLTTSE DLCVKIPDGM SFEEAATMPT VYLTVLYSLI DKARVEPGQT
VLIHSAAGGV GIAAIQVCRY LGAEIYCTAG SEEKVNHLMK TYGIPRDRIF NSRDLTFRRD
ILQATGGKGV DVVLNSLSGE LLHASWECVA EYGCMVEIGK RDLVGKGAIA MHLFEQNRSY
IGVDFARICQ NRPLIVSRLM KQVMDLYKSG DIKPITPMTC FESTKVEDAM RFMQKGAHMG
KVVITLPKDP NELTTRAPKQ QFHCHSDASY LLAGGLGGLG QAIAIWMAES GATEKLRTLG
CNAILVAGDV TQMADIERAI ASATKPIRGV MQATLVLKDM PFLNMTFDEW QGPTLPKIQG
TWNLHSALLK HDLDFFLLFS SWSGVVGYQG QANYASANAF LDAFVQYRHA QGLPASAVDI
GAVEDVGYVS RSAHLLDHFR VTSTYVLHEE DVLESLHVMI NRSAPTLPQS TPGKKLLTPG
DYSWISKGQI AIGLRSTQRL SAPNNRSVWK RDPRMALYKN MESNDGTTAA AGNEILQQFL
GDVAQDPLLL DSEESHSLLA NEIGKMLFGF LMRDVELLNL DDSLEALGVD SLVSIELRNW
FRQRLGFEIS ALEILGSKSL LALGKHSAQM LKIKFAGGEN ATASGEQETK ARYLVAKAP
//