ID A0A2T4B1X7_9HYPO Unreviewed; 2609 AA.
AC A0A2T4B1X7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PTB63211.1};
GN ORFNames=BBK36DRAFT_1183243 {ECO:0000313|EMBL:PTB63211.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB63211.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., 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; KZ680220; PTB63211.1; -; Genomic_DNA.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000241546; 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; 3.30.70.3290; -; 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; 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; 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; 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; 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:UP000241546};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2526..2600
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 456..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2609 AA; 287690 MW; 2BE54C47F24CE4E3 CRC64;
MATMEPLAII GMACQFPQEG DNNENFWKML MTGKSAMTPV PKNRFNMEGH FHPDVEHGGT
FHVKGAHFMA ADPAEFDNQF FSIPKSEVMS LDPQQRLLME NVYHALENAG IPMDKAVGSN
TSVFSSGFNH DYLQLLNSDP EIKLKYKPMG TSNSILSGRI SWFFDFKGPS LTVDTACSSS
MVAFHLGAQS LRDHESDMTV ICGVNVFTYP TDWFGMDHHG FFAGDGKSYS FDHRASGYSR
GEGVATVLVK RLSTALRDGD TIRAVVRATG LNQDGRTPGI TLPSAAAQEQ MIREVYKRGG
LDIAQTAYIE AHATGTAAGD PIEARAIANS FNTANRGSPL IVGAVKSAIG HTEGASGLAG
IIKSVMVLES AMIPPNTNFE KVNPKIPIDK WRLQLPLRPT PWPSPGLRQV SINSFGFSGT
NGHVVLQDAR YYLEEHNLLG FHKTVPYPAH ANGSITNGTG HVNGHSANGH GTANGTVNDP
TGENGDSTAD RTPLIFPVSS FDEQGVQRNA NSLATYLNDL LLSDTSSKTR KYFQDLAYTL
AAKRTAFQWR SFCLANSVAD LAKTLTADSS LAKPVRTRAT PNIAFVFTGQ GAQWYAMGRE
LLAFSTFKES IESASQYMQE LGSSWSLYDE LQRDQQSSQI DKPYLAHPSC TAIQVALVDL
LSSWNLRPTR VVGHSSGEIA AAYCAGKISR QSAWKVAYFR GHVSSKVTTN GSMLAVGLTT
SELREYLDKV DAKLPGELTL ACYNSPKNHT ISGDTAKIDE LKRILDEKDI FARKLKVKTA
YHSSHMRAVA YEYLSLLGDM EPSDADMSVD MYSSVTGARV EDAITSQYWV DNLVSPVRFT
DALLKMTLES PKSSLRVNSS NSVIQEIVEV GPHSALRSAI KETLTSHFSE NLGIGYHAVL
DRNTPGVETL LKTVGNLFSR GSVVDLALVN QGALRSPSDG QPSMIANLPP YAFNHSQTTW
YESRLSRNYR FRKYPRHDLF GAPVPDWNPE EPVWRNFIRI SEQPWLRDHV VTSSIVYPGV
GYIIMAIEAS RQIASPDLKL LGFHLKDISI KSALIVPDNK EGIEVKFSMV GMDESSLEKS
KVWRKWTVTS YNTVADNWVE HCTGYIQTQY DVSPGPIDEG LEEASEVLAS KKLLQDSVHR
CTTPTSINYD NLDTVGLHFG PLFQNLSDVV VNKGQGEVSS LITVPDVAKV MPKNFLHPHM
IHPSTLDSMM HLFIAGVLDI TDKKTLESPM VPTFIKDVRI SANIENTAGH RFRGFGVSKL
TGFQKFHSDI TIWDEKTNTE RIAVRGWSGK SLGSEVSSIE AKKLCHIVEW MPDLNLVKQP
KLKAKLASDQ ENEEYRQNVR RLQLASVLFV MLALEDLKDY PVDKLEGHFK NYYAWCIKVR
DDLHKGLLPH LDIDEWKRYM DSESLREALF SQIEEYNADG RLLVRTGKAL AAVMRKEIDP
LQLMFGQDNI LDELYRNMVE SGNLPALLKA YLEIVHHNNV NLNIMEIGAG TGSLSAPVLE
ALGPSAADEE RLLNDSAIAK YTYTDVSSAF FEKAKDKFKR WRNVLEFKTF NIENEALDQG
FEQGTYDFIF AGNVIHATAD LEKVLANLRS LLKPGGKLVM HEGIRQATIL ISGLDLLWLP
LSFGQLKGWW LSVEANRKFC PSISEREWDV MLRQAGFTGI TTVLTDREVA DIRGQSIMVA
ENNEVIGAQD ANRRVHIISS AATQSLATAL HSRITNDFGY KNCSIVGLSD LSDRELIYDT
CISLIDLERP LLADFTEQQY NDLNHLIATS DGVLWLSGDF QKDPAQYMIT GVIRTVRWER
DLDAPNLITM SVAEPRPDDD IFIESILSVF KHQFVNDIDD GSKNAEYYLK DYELLTNRLI
DAQNVNGFVH SNFAEADPKQ IPLGEAGRPI MLDTSSPGSL SALHFATDPV WARPMGENEV
EVEVRAVGLN FRDVLIAMGE HVAACLGNEA AGYVSRIGSK VTNVRVGDRV VYMNGLVDGG
CLKTYGRQSA DAVVKLPDSV SFEDAASLPC VYSTVIHGLY DIARLSEGET VLIHAAAGGV
GQAAIQLANL VGAEIFATVS TPEKRDLLIN EYGVKKDHIF SSRDLSFVKG IKRMTNDRGI
DVVLNSLSGD ALRASWDVLA PFGRFIEIGK KDAQANGRID LSPLLRQTVM ASVDLTTIMH
YKPKKLGQLI AETVRLFAEG KVKLAKPTRV LNYTQIEEAF RSLQSGKSMG KTVFKPEPTD
IVPIMPERSS PLQFDQNASY VLAGGLGGLG RSIARWMVSR GAKHLIFISR SGAASESAQE
LVQELEAAGC KVYVFACDVS DEAALSKTID DCKARLPEIK GCVQGSMVLR DSMFENMSYE
NFQAALRPKF QGSWNLHKLL PTSMDFFLLL SSATGVLGNR SQANYAAGNT YQDALATHRR
CLGLPATSID LGSILSVGYV AENKTRLKTI PTISSVLESI REDEIHLIIE YHLDRRYPGP
SQTVSGLPNV AMYKQRRMPV PSYLYLPMFR HLQSETSTAT EAVEDDPLLL IPVQLAAATK
IEEAVAVVSN GIRLKLSKLL SMAADDIDPG KSISSNGVDS LVATEFRTWL GKTLKADLPM
LDIMGTSSIL TFSEKVVSLS KLVQITASS
//
