ID A0A2T3YX94_9HYPO Unreviewed; 2400 AA.
AC A0A2T3YX94;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB37188.1};
GN ORFNames=M441DRAFT_148855 {ECO:0000313|EMBL:PTB37188.1};
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:PTB37188.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB37188.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB37188.1,
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; KZ679268; PTB37188.1; -; Genomic_DNA.
DR STRING; 1042311.A0A2T3YX94; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000240493; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; PF21089; PKS_DH_N; 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 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; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2316..2394
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2400 AA; 260172 MW; D00BF26418C5E130 CRC64;
MQETSGPSSA FTVEDNTVCI VGMACHLPGG ITSPSGLWDY LYNKKTAQCT VPLERYDFRG
FYNKDGSRAG VMAVDGGYFI NEDVRKFDPS FFGINNLEAS YMDPQQRKLL EVVYECFENA
GLSMEDVNGT STGVYVGNFT ADYSVMQSRD TDYVHRLSAT GSGTSIMANR VSHVFNLHGP
SFTLDTACSS TIYALHQAVN AIKNGDCDSA IVAGANLVMS PEQHFGTAKG GFLSPTSACH
TFDTSADGYA RAEALNAIYI TKLTSAMKSD RKIHAVIRGT AINANGKTPG ITLPDAKMQA
AVIRKAYHNA GLSFADTDYV ECHGTGTPVG DPIEVDGIAA CFAGREGEPL RLGAVKTNMG
HSEAASGLTS IIKVALAFEH GVIPPTYGVK NINPKLKLKE RNMKVMTENE AWPRAIRRAS
VNSFGYGGAN GHVILESIGS YFVGSLASSP VSRTLTSPYE SSKGQVFVLP FSASSGKSLE
ARRKQNIETL ERTEPNDVKA LAAAMSKRQA KLRLRDFVLA SAKGDSQPSL IEMADAGDKA
SPGTQPLPFA FVFTGQGAQY ANMAKELIEN DISFLASIRD LDEVLQSLPA EYKPSWTLEQ
TLLDKPAVSK INDVTRSQPI CTAVQVALVN MLRSWGVSPT AVIGHSSGEI AAAYGAGLLT
ASEAILAAYF RGFAVGQLKS RGNMMAAGVS PDAAKALIEE LGLKEVRVAC VNAPESVTLS
GAIKDIDALQ TELQKEGKFA RKLETGGRAY HSHMMVEIGD LYESLVTPHF TTKKDGDMEA
EMFSTVGHSP DALGAVDAST NMASYFRKNL EQPVQFSAGL TKMITGDKYH LVEIGPHSAL
KGPIQQIRTG AKRDKEAVPY SPTLVRKEDA YVCLKKLAGT LFSYGHTLDW YAVNSVPRHQ
SLPVPILASY PWDYSKPLPW HEPRASVEHR HRKYIRHELL GTRATAGNGI EWCWRNIPRV
SEMPWLRDHK LGESQIVLPG AAYMSIAIEA LSQVLDIKSR LVAGESYGFE FENVNISAAF
VVPEENDAGA DSLELHTVMT QRKISTANTS GNWYEFSVSS FQSGVATLHC MGSIRVSEST
LAPKDGAVEV QEQGYEVWGM ARWYAKAKEE GLNFGPTFQS LTSLHTDGNR ISTDSISTTH
LAPPSEAANG MFYAMHPITI DACFQAAIIG GTAGVVNDLK AFIPCFISNC SIQIPKGGSA
SLGSQEVRIH TSMEKTGFAS RAVAFTLRLP DGTPAIDVPH LRMNLYTGKS PVESETSMYL
QRQPCLRIQW KPDVLRLQPG SESAIRDFIE AFSEEQSDDL NDNGALVVFA ALLDLFGHKI
PRMSVLELGQ DRQWTPKDCQ AILGKDTAFP RFKSWNDGKL GEDNKLAIEN AKSADPYDTI
LIPHLSVSKK VWSKAADEVI SQVSDNGIVI TRKTKDAVSA LQAAGFTTLE LPNETLAAVR
NAKQTGLENK EVVIVKPNQS STSIDTLADA VAAHLKKNAG VEKLSTVTIA NIETVALHDQ
VVCVSVMEME NEFLATISSE DMDLFRKITD NVSDLLWLTG ANMLSAPNPN LTLSSGLSRA
LMLEQPALRY TVLDVGADIT NPGFLNAICN NVSAALTFRY ATDDKEFIQK DGILYVSRFT
PDFELNSLFR QRMTPNDTMK LVPLGEVGPA RLSVGQVGMT DTIHFQQISE LKTTPPAGFV
DVDLRAVGLN AKDIYAINGR VETKEATTAL DFGGVVSAIG PGVEHLKVGD RVAGFIPNHF
STTERVPVQA VHKMLPEEEF TVVPTLLGVY CTALVALKDR AHLRAGESVL IHSGAGAFGL
AAITLAKHLG ATVFATVGSQ SKREYLVKEM GVPTENIFHS RNASFVDDIM TATGGRGVNV
IVNSLVGDLM HASWSCIAPF GRFVEIGKRE LIDAGKLDMR IFLKNATFTA FDLSEFFYDS
DSYYQDVVFN HTAEVVKMYR AGIIKASPIA TYDVSEIGHA YRYFGNKDRV GKVVVSMENP
NSLVQVMPAT YQSVFSPEKT YLLVGCLGGL GRSLSRWMMS RGARKFCFLG RSGCDKPSAA
ELVNRLRDAG ATVTVVRGDV SEEDHVREAV VAAAKDGPIG GVVQAAMGLS EALFSVMTNK
AWHTGIQPKW KGSWNLHNAL EGYDADLDFF LLTSSISGTC GTATESNYCA ANNFLDSFAK
WRRSQGKPAV SVGLGMISEV GYLHENPEIE AMLLRKGIQP LNEDEFLQVL DYGIAGPWSD
AEFARGVSMP SEAAHILTGL ESYGARKLMA QGFEVNNGVT EEARATILAA SLLAEKDAND
EEKSGDVGQL AAAAEWFKDV PAGAVSMLAP EASAPTMLDA ILRLTKKRFS NLILMQLDAV
DDRAPLPSFG VDSMLAAEFR TWFFNTFKVD VPFLDIVSPQ KSLHTLAEFV EEKLVTSWVS
//
