ID A0A2T4BD16_9HYPO Unreviewed; 2636 AA.
AC A0A2T4BD16;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PTB67224.1};
GN ORFNames=BBK36DRAFT_1158065 {ECO:0000313|EMBL:PTB67224.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB67224.1, 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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ680211; PTB67224.1; -; 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: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; 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; 2.
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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013120; Far_NAD-bd.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-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; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000241546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 389..814
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1686..1760
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1764..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2196..2215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2636 AA; 289057 MW; 96588546C024757A CRC64;
MAASSIRTLL MFGPGAMSLN EAYFANILSF VSTDSASQWA LAAIRDIESH WASLCEAVPK
LQHTPGVGHA QKLAEWLRTG TLSPGSTIAS LPNALLGPLV VIAQLVEYLQ HVDSISASGL
RGGEGFQVPS ASDAETVGCC LGVFSALVLS SSSSWAEFCH NAAAVVRVVF VLGALSDAQD
ASDASGPSVS LIAFWRGGQS LSDLKKALER FPEAYISVLY DENRVTVTTS TRTVAALKNH
LQKVGITTNE TEFHGRFHAG QLYKAELEAF LLYCKRFPTF QLPDASCVVV PTRVNSEDIV
TSQESLLEIA CRAFLVSQFD WIKTFRSAVS STLQNRASRI IEFGPERCVP PTLLRRLNSQ
VTHFDFEESI KRTKANLSQD QELPAGVAEN DIAVIGMACK VAGADDVNEY WELLLQGKSQ
HRELIPNDRF VMETPFRPSE AGNEKKKWFG NFMSDHDAFD HKFFKKSPRE ALHMDPQQRL
MLQAAYQAVA QSGYYNVNMN VHGPTKVGCY IGVVANDYEN NISHTTPIAF SATGALRSYI
AGKVSHFFGW TGPAMTVDTA CSASTVALDL ACKAILSGEC SAALVGGTNF YSTPMFFQNL
AAGSFLSTTG QCKPFDAKAD GYCRGEAVGT VFLKKLSQAI ADGDQVLGVI SATAINQNRN
ETPIFVPNSP SLTNVFRTAI QKSGLDAKDI SVVEAHGTGT PVGDPVEYDS IRQVFGGSVR
AGQDALQVGS VKGLIGHTEG ASGVVALIKI LLMLQRGQIP PQASFDSINP SIKYSASDNL
EITKTPLPWN QEFKAALINN YGAAGSNASV IIKQSPAQLS KPPPPVIDSE TEVLLSKDGA
GDSQKVPFFL SGLDEKAILA YAQKLRQFVN SHDNLDIQDL AFSINRQSNW SLGRGSVFSA
GSIVELDEKL ASIDTFPIRS SQPPVILCFG GQVSTFVGLD YQLFTKSAIL RRHLDQCDSV
CKSIGAGSIY PRIFQSDPID DPSILQPLLF SMQYSSAMSW IDCGIVPAKL VGHSFGELTA
LCISGVLSLQ DGLKLVYGRS KIIKESWGAE KGSMLAVESD LEELEGLLST VNASLQEGKA
TIACFNGPRS FTVAGSSAAI DAVQKAISST QPALKHKRLN VTNAFHSVLV ERLKPELEAL
GRQLTFALPQ IPLERATHSR KVDKLSAVYV ADHMREPVYF HHAVERITKE YPEAVWLEAG
SNSTITSMAS KALGLPKAST FQPFNVTNNN KALSQLTDVT MNLWKAGLRV SFWPHSRAQT
YEYKHIILPP YQFEKHRQWL EFKPPQALQV AVQTAPSTEA GNGTQQQQPV GLYILLDRGT
DKYRFRINTA AAQFVDAMSS HAVANTQTCP VMFETDLAIQ ALVSIHPELA DTSKLDPQIY
NVVNREYIHD TSAELFILFE RLGHDENSWL FKVTSKGKDS GEILHMSGQL HFQASDDARS
RLEFGRFDRF ITHDRCLQVL ESSGRSDEVI QGQTIYSVLS SSDVHYGQRL RGLQRIVGRS
NESAGRVVRR RSGKSFVDFA LGEVFTQVGS IWANCIAQNL RNTKKRTVYM ATGIEQWSKS
SKVLEKFSQR LYDNDPELEW HVLAQHKRNA SDDSFTTDIF VFDAASGNLE EVILGIRYAP
VSLNQPLSGS TTTTAAVPVV NRYVPSSTPF VPVPVSTTSK QTSVPQPQEV IKKPVKAAAP
KRDIKAELWL RLRPVLADIS GLEPDEIQPT DALADIGIDS LMGMEMAREV ETTFNCTVEQ
SELLSIVDVP GILKFLQSTL GDEDVNDSSE SMSTASSDAN VHSPPTSGSE MASPNLKVSF
GSSDGASDLP ASAVLEAFGE SSSRTDYFLK ARGCAGYLDG VSQKQTRLCL VLTAAAFKQL
GCDLEAAKPG EVLQPVPFVE RHRRFHQYLY SMLEETRIIN IDGDVMTRTA IPLPSQSADA
ILQDLMRRHA DNGSSHQLAY NVGSRMADVL SGKADGPQLI FGDAKNRELV ANFYGELPFN
KLYFELMADF FTRLAAKLKL SSSQHGAPTL KILEMGAGTG GTTKVLVPVL AKLGIPLEYT
FTDLSPSLVA QAKRRFKEYP FMKFAVHDIE QPPSDPELVG SQHVVIASNA VHATHSLRDS
AQNIRKFLRP DGFLMLLEMM RTLHWVDVVW GTLEGWWLFD DGRTHAIVNE QRWEKELLAS
GFKHVRWTDG KLPEVHVQRV IIALAGDADG DLSNIPTLTS STLEDEEEHH GSKLDAEERK
RVANTYVEST IRDFAIPRYA GPTLNTEPGS GACVLVTGAT GSLGSHLVAH IASLPSVDTI
YCLNRPRPGK KGQEDQSRDP LSRQLEVLAS KSIELSEAEI GKLRVIETDL PLPQLGLDES
QYEQLLNNVT HIVHSAFPVN GLRSLKQNES QLTLMRNLVD LAAGVSARRP TEFKFTFQFI
SSLSAVGMYP KVHGEKRVPE QQWDVDSALP NGYGEAKVIC ERVLLETLGQ HPDRFRAMTV
RLGQLSGSMK TGYWNHMEML SFLFKSAQTL RALPDVDGAV SWLHLEDASA SLADLLLRDA
PTCHAVYHLD NPQTRDWKDV IPVLADALDV PSSHIVPFKE WLRRVRAYPG EDPWDNPSAK
AMDFFEHKFK HMSCGGVTMA TDNALEHSAT LRAVRPVSDE LVHKYIQAWK DSGFLR
//
