ID A0A2T4AC38_TRIHA Unreviewed; 2498 AA.
AC A0A2T4AC38;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB54616.1};
GN ORFNames=M431DRAFT_553585 {ECO:0000313|EMBL:PTB54616.1};
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:PTB54616.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB54616.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB54616.1,
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.
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DR EMBL; KZ679680; PTB54616.1; -; Genomic_DNA.
DR STRING; 983964.A0A2T4AC38; -.
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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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; 3.
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; 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; 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:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 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; 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; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..401
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2399..2476
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2498 AA; 276635 MW; 0A2F2E290DBB5D17 CRC64;
MRWALSSYAD PQNRYNVDAF YHPNADHGGT VNFRGGHYLQ QDISAFDAPF FSISPDEAKT
MDPQQRLLLE VVYEGFENAG IPMSKYVSSR TACFVGAFTR DYEGLLGRDP ENLSAYQATG
NGMAMLSNRV SWFYDLKGPS MSLDTACSSS LTAFHLACRS LQHEEAEMAV VAGSNLFYNP
DQMVPSTAMR FLSPDSKCYS FDHRANGYAR VEGLGAVIIK RLSSAIRDGD TIRAVVRGTG
VNQDGRTPGI TLPSQEAQRS LIRETYAKAG LELGQSRYFE AHGTGTAAGD PLEAGAIAAT
FAEARTKDDG EPLIVGAIKS NIGHLEGSSG LAGLIKTILV LETGNIPPNI WMEKVNPKIP
AKQWKLKFPT SNTPWPSSGL RRASINSFGY GGSNSHVILD DAYHYLQQHG LECRHNTVLS
PGVPLNGVNG THTNGDLHNG TPMNGTDLTP ANLFLWSASD QKGIERVPIR SSQEPNIGFI
FTGQGAEWQG MGKALYSRYP IFADSLRAAD VYLRESLGAT WSLLDTFLDD ENTTRIHDPA
ISQPLSTALQ VALMELLSSW GLAPSRVVGH SSGEIAAAFS AGIISRECAW GIAYYRGEAV
VEAVSSEGTT NTGAMMAVGA SEQVTLQYIA RLEESSKILV VACVNSPTNV TVSGDEDMVD
KLKLLLDEEG IFSRKLHVKA AYHSPYMNRV SEAYRAKLET LDVASSGQKN KIDMFSSVTG
TMADKASVAI SDYWVSNLVS PVLFHQSSRA MCTQRPTKKG ITIGSQESPL DILIEVGPHS
ALQGPMKQTM AAESNLKGMQ YFSMLSRSRS AIETALQLAG NLYKYGSKLD FQFINSPGSQ
EMLVDLPSYA WNHENKYWCE SRMSKGFRFR KFPRHDILGA PVSDWNPLEP QWRNVLRVSE
NPWLVDHMIT DVVLYPAAAS LVMAIEASRQ LADVTRTISG YQLREITLHE ALAIPKTADG
VETMFCMRPH GDNSFGGSAT WNEFHVYSYS EEYEWREHCR GLVSVEYETQ PTDSPGKESE
VEAEARELQE LVKGAETRCQ KELGRKQMYD HYESIGLQYG PTFRAIHNIR YTDNEAIGKR
ELIGNIKNPD LKAIMPNGYY HQPVIHPITL DNLLQLLLPA MGRGIASLDE PIIPTLIGKL
WVSASISVDA DYSFSGYGNA RWMSAREARG WGVLMNEARQ SPWVILRDSV SKVVHSADFS
TAPQATQNRQ VGSFNIAWQP DVDFVDTKHL IQLSGDTKQK DWTTETHDLE LLGISYIKET
LAALEQDSRI NLPEHLEKYV AWMRFQAERF GQGEEQEVDR VALEEKVEAS SVDGQAMTRV
GRNLGRILKQ ETGFLELLAE DQLLDRFYEF AIGSETLHQH LATYLDTAAF KNPDMNILEI
GAGTGSATKT ILNALTGEGM VRIARYMYTD ISGGFFDKAK EKFQDWIDIM TYKTLNIEVD
PVEQGFELNK YDVIVASHVL HATARLDVTL DNTKKLLKPG GKLILVEITN PDLLRSPFLF
GLLPGWWLSK EKNRKWGPTI TADEWNNLLQ RHGFEACDHI IKDMEDPSLH QASILVSTYM
PDRQVSGTDV VVATSPSNPQ EALASEVQDR LQQQGQTATI LPFTSIRKHD IARKLVICIA
ELYDTMIHKL KEDEYADLQH MVGAASAIVW VTKGGTFTTE NPLSALSNGF GRNVRAEREG
YRFVRLDLEE DVVVESAADS ITKVYMRLST SPAITENEYA VKDGNLFISR LVHDDQFAET
FTSLYAKPET QLVPFTKDNR ALKLDISSPG TLSTFHFQDD DVYGVELGPN EIEVKVKAVG
LNFKDVMIAM GQLSDTWLGN ECSGVITRVG KDVSEFTVGD RVCSVGVGTF RTFYRDDARL
FQRIPEHMSF AEAAALPLVY WTAYYSLFEL ARLKKGESVL IHAAAGGVGQ AAIVLSQLIG
AEIFVTVGTA EKKHFLMETY NIKEDHIFSS RDLSFAKGVM RLTNQRGVDV VLNSLSGEAL
RQSWELMAPS GRFIEIGRRD IDLNRRLDMS VFARGATFPS VAVVLKDNRD MVGRILREIM
DLAREKKISP AKPLNLFPYS KMEVAFRFMQ AAKHIGKIIL EPHDDDVVPA LPPMKMPQYF
DENASYLISG GLGGLARSMV RWMVDKNLKN VILCSRSGPN SDKGKATAKE LRERGVNATI
YACDVSNAVE LAAVLEDCAR KMPPIKGCIQ AAMVLRDSTF ENMSYADFQE PLRSKVPGTW
NLHSMLPDTL DFFVILSSSS GINGTRGQAN YAAGNTFQDA VAHHRVSQGQ HAIAIDLGFV
LSVGYVAEGG NAEIDNNLSA WGFMGIREEE FLAIIEYCVN PNTPRPTPTT CQVVTGIENP
ALMRAKGLEK PYYFKDPFFS HLQIANREEN SSALGGDDQE RELTAQTIAA LRSVKSLDEA
AGLIRVAFVA KLCKVLSINQ DDLDVNKPLY TYGVDSLVAV VIRYWLFRDY HADVPVFDIM
GGSTITGLSL KIAAKTKFVD KSLIEMEEQD RLGVEAEE
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