ID A0A395NIX6_TRIAR Unreviewed; 2375 AA.
AC A0A395NIX6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RFU75979.1};
GN ORFNames=TARUN_6263 {ECO:0000313|EMBL:RFU75979.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU75979.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU75979.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU75979.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU75979.1}.
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; PXOA01000395; RFU75979.1; -; Genomic_DNA.
DR STRING; 490622.A0A395NIX6; -.
DR Proteomes; UP000266272; 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; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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 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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 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; 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; 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 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:UP000266272};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2293..2367
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2375 AA; 259015 MW; B03EDBA043D38EA2 CRC64;
MDDIAIIGVA LRFPGDATSP QKLWDVLERK ESQWSEFPKD RLNIDGYYHP SNQRLGSISF
RGAHFLKDDI SAFDAPFFSI PTEEANAVDP QQRMLLEISY EALENAGIRK EDIDGSDAAV
YVGSFVKDYE YISLRDQNWG PQYAATGNGI AIMSNRISYF FNLHGPSMTV DTGCSSSLIA
VHLAAQSLRT GETSLALAAG TGMILAPDTM LPMTALNFLS PDGKCFTFDS RANGYGRGEG
VGVVVMKRLS DAIRDNDTIH AVMRASCINQ DGRTKGITFP SKDAQISNIR AVYASAGLDF
DQTGYIECHG TGTQAGDWQE LQAISETIAS VRSTDNPIIV GSVKTNVGHL EGAAGIAGLI
KGVLALERGR IPPNINFIKG NPKIDFENWK VKVPTEMLDW PVPGIRRVSV NSFGFGGSNA
HVVVDEAPGY LLEKGLRANH SSMDTIITGS GRALAEQKPE VRLFCFSAND NPGVARVMNS
HVPFLESDQA DTTDWLRNYS YTLGCRRSNL EWKAFILAES TTELVAKIRE FDSNYVTRSL
LKKQPKIGFI FCGQGAQWAQ MGKDLMSFNV YCTSLKEASC FLQIALGSRF DLLEEILREA
ESTRISDPEI SQPATTALQV ALVDLLKSFG TQPNYVFGHS SGEIAAAYAS GAISRYDAWK
IAYYRGLAAA SIPVRAPKLI GGMMVVGMST EEVSAYLASI NKSAQLACVN SPRSITISGQ
ADAIEFIASD LRKRNIFNKV LNVKVAYHSS HMRLVEHDYA DALNDIVANK CFEGVKMFSS
VTGKQVIGNE LNARYWADNM VSPVQYVAAL QSLMSLPAEA RPDMLIELSP GAALRSPTTD
ILAAISNVSN TIYHSVLERK QNGCVTLLNL IGTLWSKGYP VNMKNVVSKG YQQDSLRCLS
NLPSYSWDHS KKYWHETDMS LENRLREYPR MDLIGARVVD SIAPFEPRWR GFLRISENPW
IQDHQVQKTV VYPASGMVAM VLEGAKQLAK GTQDLLGYEL VNMKIEKAMT IPDTAFGLEV
SLNIKNDSTN TGDHSKIGVK SFAIYSRLQG RSWDRHASGS LRFHYKVGNW QAAFRSYESR
YDAMSEICKE TIIPRQLYEH LDSVGMNYGP LFQNIVDVRK SNDSCVSRVK IPDTKSKMPC
KFEYPHLLHP ATLDSMIQTL LAIQPLPMVP VFIKSLFVAA NLGNAESGAD FTGYSLASAT
GIRNAEATVV MKQTAISQSN VIIEGLRFAA LHSPSPQEGG FLPSNRNLCS QIIWNEDGNF
ARPNSYSEQV AILAHKYSGL SILHVGGGYQ LSQATLKAVA PDTDTTPRLL RYTIVEGEGD
DTASRVLASV ENTQLQPFIE KISDISGVKN DYHLIVVCNH AEVDIGKLKG KLKAGGVLLT
QATTSEEPHK QETSEVSTAH CQENENAQKS IDNHVSKDDG AFVNYIEGES EIVLEVYRNN
RPSPLNRPVI FLTPQEITTE VQGFIDAINR FKETNDLSFD ASLMTVDKVL EDQTALTGKV
IVSLLEFSGI QSHDNAIFDW KQNDFDCFYA LQHRARNILW ITRGAHMSCT NPRGSPILGL
ARTLVSEDPL KSVVTFDLAG ESELDNPIVV KNMLSLLDTT FGSRLASVQD TEFAEDAGKI
YIPRLTTIRS INRIIEGGNL SGQFSQKPFA DSRGLELTIS SPGISDDNLY FIKTELQDLG
VDEVEIAFKE APLSFLDLEV VLGRATESTI GADVRGQITR VGSEVRGLSP GDNVAALVAD
GSIKNSLRVK SQFVRRVDTE VVLSFLVSAY FALVHIGRAR RGRKVLIHAG ASAFGLVGVD
LAVAIGAEVF ATVAAPEVHL QREVLKRHGV SEDHILEADS GLFVTALLGA TDGSGIDCVY
NPTLEAFEEQ FDCVRKCGSI IRFASKSMAP TSSRLPPTSV TVVNWDLHQL LTEDPEFVVD
LLELATQFIK NGDYKPSLSA ELKQVFDIGA LKDGLLHLQQ TPHVGYASLS LAETGTSTVP
VLNEDTTKSL QESLESGGTY VLAGGLGGLG RSISELLVNN GARHLAFLSR SGASSDAAKS
FIDSLRLRGV NAQAYVVDIC NETSLNDFFK DVLTMEMPPI RGVFQCAAVL RDSVFENMTF
NDWNEAIKPK THGSWNLVHA ISAAGHDPFY IFLASSSGVI GNRGQANYAA GNCFQDSFAR
YLQQQGKHAV AIDLGPVLGA GMLAENEDIL DTLRSNGFFG IPHEDFLTVI KHAITGEMAP
GLSTPAQITV AVGTGGINAQ INAADPYWTR TALYSYLNLV DIAPPNLSVN GDATSKDMKP
MLASAASIEE ATSIIRAGLS VMLAKAMSML PSEIDMNKSL NAYGVDSLVA VTIRNWILNN
CGVQLSVFEI LSESPIAEMT NAIVEKGGYG GGKME
//
