ID A0A2T4AS51_TRIHA Unreviewed; 2676 AA.
AC A0A2T4AS51;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB59880.1};
GN ORFNames=M431DRAFT_536358 {ECO:0000313|EMBL:PTB59880.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB59880.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB59880.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB59880.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; KZ679675; PTB59880.1; -; Genomic_DNA.
DR STRING; 983964.A0A2T4AS51; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000241690; 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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 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; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; 2.
DR PROSITE; PS00606; KS3_1; 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:UP000241690};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 482..904
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1795..1869
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1905..1982
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1872..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1892
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2676 AA; 288663 MW; B24E914983E3DE0C CRC64;
MSTHGLYHQV RWTTATLSEK PIQFGKVVFL AGEGEHDKIL SAYQSQLAEE GHKTAIARDV
EQIASLLTPD AIVVHLPQAV NDKYGVYEAA TKSCTSLIAA AQMLQHTQAN GDTAHKLFSV
ITKDSGISEL SYAPLYGLAR AMKMEIPDLF GGLIEEDEGR FPLSAIKYAQ GFDVVQVSNG
VAHTARLQPF QDIETKGAGI KPSLDPKGTY LITGGTRGIG LETATWMGER GARNIVLVSR
RGLPVLNNEE KDADTDALAK RIDHLRTLGA IVHVLAIDIS KPDADLTLRQ ALDNLALPPV
KGVIHTAGVA GYRTLERCTP SEVDNDIAPK VMGALHLDKL FPPGTLDFFI LTSSVGQLVG
FPGQLSYAPS NSFLEGLAAR RRRQGDNSTS IQWTCWDGVG MMAQSKSATR MITTGMQAKG
LAIISKEEAL AALDGIFSLK SDHVAVVRVL ELKKGDPPRH PVLWDITPRT GDEKITPTSY
PKHAVAIVGM ACRTAAGDTA DDLWQAISSG KSMFRDLDPK RFPDAASKSE KMVGNFLRDT
ESFDHQFFKK SKRESAALDP HQRLLLETTY HALESAGCFG EDQQQEAETH DVADGGEITG
CFIGMNAPDY PLNLACNPSS PYTGFGMLRS FVAGRLSHHF GWTGPSQTID TACSSAMVAI
HQACRAIQVG ECTRAIAGGA NLITNTALFD ALRTGGFLSK TGPCKTFDAR ADGYCRGEAV
GVLVLKPVAR AIRDGDDIHA VLLSTGNNQN INNTSITNPV LKSQKALFRD VLLRAGVSPA
AVSYVEAHGT GTRAGDPVEV EAIRQVLGGP DRRNTLHVGA VKPNVGHSEG ASGAISLIKV
LLMMKHGKIT PQAQFQTLNP NIPALEPDRM AISTSLKEWR DDLRLALVSS YGASGNNAAT
VVAPPPPRSS SSPSLLESNT ANASVSKFPI FISAGSKSSL LAYFAKLKSQ IDRDASTPEF
VRHLAYTLAK KQNRQLQHVF STTVTSGKYY ALHSNVLNFH GLATKSPTQV NDLQTQLADP
ESHITTATPK PKSIVLLFSG QNGTAVPPAK ALYESSVLFK SYIDECEEAM KSLGLPSLFP
AVLEGVQESD DLVLRHAAMF AIQYSSGMSW IASGVKPQAI SGHSFGEWAA LTVSGAITLK
DGRASLIAKL WGDDTGSMVA IEADLVGTGT TPAQNMQRFN EQHPDVKLDI ACYNGPNNYV
VAGRTSDIDL LEAHLIERKA SGEKLRFKVL RGMHAYHSVM ADPIVDEAAV LSASVTFKDP
IYPFESCHED SWTGPGPNVI ARNTRGAVYF GKAISRIVDR LGSCTFLEAG FGGPIIALAR
NAIPQAQAQD QHGFVPINGK DPVRSLADAT VALWKNGHTN VQFWPFHRSQ GASYVPVHLP
QYQFEKHNHW LDYTPLGGAG KKQGGEAPLS GLCPHCHQDI SDYPYIEQDK SQNQRAGEYV
FKVDTRSRRY HELVKGHIVV GSSLCPAAIY LELAAHAVAL LNPGKNAETT VDAIKINAPL
GVDSKRSVRL TLAKKTGSAW DFKLASFKDN EKPTSHATGV ISLTNGSKSG SESSDRHMWD
RLSTLLDDDT DTEALRGAMI YKVFSKMATY SPPYKGLKYL VGKQGKEGAG DIHMPPSDLD
ASAMTPNKSI ADPVVMDNFL QVPGIFVHSL RDAGEEEETN GEMSYICTGM DSVGPLSALK
GSARYRAYTR IVHEDSKETI LDVFGFDKNT RKLVWSARGL KFSRVPRISL AKVIAGANPG
TSVEIKESPV KAPSRPAEVQ TFTPKSSYQS PPAAITAAPI APKKPKAKKS GQKSVFVLGG
VQQLLSKSLD IPVEDIIESA TLEELGTDSL VTSEILASIS DIFKVDISND EFTKIVDVAS
LCAFISARVG GGSDDTGAEL DSSEEEEEYQ QPEPAFEPTV ETVSKPSSAW RDPIFAILSH
SLDVPIEEIQ MDSNLEDLGA DSLVASEIIS NLNDAFNVDI SNSEFSSLVD VASLCKLIGA
TLGVDSAQTP TSSGSHGQSA SINDISMTPY TGATTPAAAE KSTLERSGGR ITHTAFQQIR
RNFDVHAKDT KFTGYWDQVY PPQLETVAAF ITEGFAKLGC LIENFKRGEK LPALQGTLAK
YHREVPRLWD ILEEAGIVEK TKAGDYVRGA APLHDPNVKS AVELSADLIA RFPQYASTHG
LPDLLGPHLA ECLSGKADAV SLLFGSDKGR LLLEDFYANG PDLLATTRVL CDFISAAIHL
QASDGEPFRI LEVGAGTGGT TKHLVPLLQA TGLPFSYTFT ELSPSLLARA KKTFKGVQGM
DFRKLNIEEE PPQELLGKYH VVVSSNCVHA TRNLNVCLTN IRKMVRPDDG AVALVELAQK
LAWYDLVWGL LDGWWLFDDG RSYALQSPWA WEKVMNDSGF AHVDWSEGAT RESRGVRVVC
GMVAEPEKQC SAKATSTLLH RGSRASGGRN VFLAPDGFGS GAVFGALGPL LSSAEEVSVY
ALNSPFLKNK PDALNVPTIE ELAAIYVGEI KRRQPEGPYL LGGYSVGGVV AYEAARQLLE
DGNEVEKLFL IDTACPTFAS TLPDSLCEFL DSIAQGKNGE SSRGKVVEND HFTLARQQVA
AYKVSKLPGR KLPQAVLVSA REGADKQDTV RRPEVKPEEQ RITEWFLDDR VDGGSLGWDE
LLGSVSVVRA DGNHFSMMTP AKVNTWASTL ADLLGP
//
