ID A0A2T3ZD55_9HYPO Unreviewed; 2429 AA.
AC A0A2T3ZD55;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB42734.1};
GN ORFNames=M441DRAFT_166252 {ECO:0000313|EMBL:PTB42734.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB42734.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB42734.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB42734.1,
RC ECO:0000313|Proteomes:UP000240493};
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.
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DR EMBL; KZ679260; PTB42734.1; -; Genomic_DNA.
DR STRING; 1042311.A0A2T3ZD55; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000240493; 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: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; 3.40.47.10; -; 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; 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; 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; IPR025714; Methyltranfer_dom.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 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; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF13847; Methyltransf_31; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000240493};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..413
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2346..2423
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2429 AA; 264559 MW; 11A469C8BF550626 CRC64;
MACRLPGGIK SPKDLWDFLL EGRDGRSRVP KTRFNIDGYY SPTKRAATAI TEHGYFLDES
VDLGALDTSF FSMTRTEVEY LDPQQKLMLE VARESLDDAG EVGTKGSNIG VYVGSFGQDW
YDILAREGLR QNSYTIVASH DFMLSERISH EMDLKGPSLT IRTACSSSLV GLNEACMAIA
KGDCESAIVG GTSLILAPDV FTRLSYQGVL SPDGSCKTFS ADANGYGRGE AVVSVYIKSL
SAALRDGNSI RSVISGSATN FDGKTNPLTT PSASAQELLI RKAYEHAGIE DIGKTGLFEC
HGTGTYAGDP IEAEAIASVF GEKGIYVGAV KPNLGHSEGA SGLTAVLKAT LALEHRIIPP
NIKFSPLNPR IPFEKAKLRI PEQPTKWPAD RDDRVSINAF GVGGANAHVI VESAASWLAS
HQKPRPTGSE TTKAAEPQLL LFSANTAQSL KDLVSKYQIL LSETSLDVAN VAYTLANRRE
HFTNRSFAIA TKDKFDVAAS VTAQKDGSTP PSVVMVFTGQ GAAWPQVGRT LLLSNTTFSH
TIDLLDKHLQ HLGAIWSLKE ELLKPARTSR VFEAEFSQPL CTALQLALVD TLAAVGIKPA
AVVGHSSGEI GAAYAAGALT AEEAITVAYL RGTATKHKTQ HGGMAAVGLG WDDIQEYLVP
RVVTACDNSP SSVTISGDAD KLETVIAAVK QAHPDVPTTT LKVEQAYHSH HMLAFGQAYY
QAMVNCGVVG RTPTVPFFSS VTGELLTSSK ISPLGPSYWQ ANLERPVLFR SAVTNILKSA
AIINPVFLEL GPHSALAGPL RQILTSESSG ASYVSSLVRR QNSAENLLQA IGKLYMLQAS
IDFKSISPTG SCLPDLPAYP WDHSRRHMFE SRVTKEWLGK KYPDHTLLGG RVPESTDLEP
VWRNLLQVDT TPWIVDHKLG DNIVFPLAGY VAVAAEAARQ VSGIDDGVSF RNIAVSSALV
LNDDAPTEII TTMRRKRLTD SQNSEWWEFG IASHNGHVWT KHASGEVKGE TFDKMQQLDD
TEEELPRKVD STKWYDSTAR QGITYGPTFS GLENIKSSTG WPNKSTATMK NNKWGDEAQH
HLHPIILDTY YQLMSCALHD GLDRDFRRTL AARIDSMIMF RCSEDNLKIA VRSEPTQEGY
IAYGSVSAGS KIVLKVDGSH STLFEEAEAG DKSSIPITAR TEWVPHVDFI DRNSLIKSRP
DQETIMPLIN QLSQLVISLA SRATIKTQVL APHLIKYKKW LHEQAPSGID TLDSATLTQS
IQLLIDKLQA TSAGHAAAAI VAVSSNIEAL LSGEKTVLEV LNSTGSLDSF TEFLREHDDG
NYLRCIGHSK PNISILEIGA GLGEKTSKII KYLSRADGQP LYSQYVVVDA SSGLVNAARE
GLKGVPNLEF ITLDVSRDLA EQGFEDRQFD VIVAANIAST GNILQDSLRN LYRLLRPHGK
LILEESRPGL SWAKFVLGLL PRWWAHASDM DRVGEPFIGP ERWQDELAGA GFAVVDHIKP
DSEHWTNSVL IATPQHLNTP DKHITLLSLT DMTQPSLIVQ ELENRGYKID RILLGETPPA
DQDVLAILEE EQPFFENLDA EKLSQFKTLL TDLGSAGLLW VTRPSSIGVT DPRYAQVIGL
VRTLRSELSI DIATVETDRI ETPLGAIYLA DVVSKFLARG DDGALGPDLE YAIHKDQILV
NRIFPFSLEQ DLIVSQASAE AVVTQTIPGR LNTITWSTLS PTAPKDDEIE VEVYASGVNF
RDVLVGMQII PGRHEPKFGY ETTGIVRRVG PRVTKLTVGD RVVGVGARTF TTVITSREVY
YEKLPDHINF VEAACIPTIF LTVVHGLRDL GRLERGQSVL IHSGAGGVGL AAIQVAQMLG
AEIYTTVGSE NKVKYLMDTF HLPRNRIFNS RNESFVQDLL RETNGKGVDV ALNSLAGELL
HATWKCVGRW GTMVEIGKRD LIGNAQLDMG PFLASRNYCC IDIDQMRSER PEMISRLLQS
VMDSFAKGFL KPIRIDRVFS GSEVLEALRY MQQGKHMGKI VLEIREPSGK LLVDNVDATK
KSGAEFDEAA SYLLVGGLGG LGRSISVWMV QRGARNLSFL SRSAGSGEHD ADFVREIESM
GCTVQLVKGD VTNAGDVTRA VDGVLAPLKG IVQMSMVLRD QMFDGMSIED WNAVTKPKVQ
GTWNLHNATL SKGIDLDFFL LFSSLSGIVG QVGQSNYASA NTFLDAFVQY RARHNLPCTA
IDLGAMKGVG YLSENTELLR KMQGTGWSVV QETELLGALD LAMMTPATRN QRKKANSFGD
TFLLGLVPTV PLNSPSSSSR LKRDVRMAIY HNIDAGNHLK AGSAPDGLRA FLASVKQDPS
VLKTSEAVEI LAVEIARKLF SLLLAEDAEI DITQNTADLG LDSLVAVELR AWWKLNLGFD
ISTLDMLSLG TAEALGKRAV DGLIALHGP
//
