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Database: UniProt
Entry: A0A395NUD1_TRIAR
LinkDB: A0A395NUD1_TRIAR
Original site: A0A395NUD1_TRIAR 
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
//
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