ID A0A1S8A8Y2_ROSNE Unreviewed; 1417 AA.
AC A0A1S8A8Y2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:GAW26385.1};
GN ORFNames=SAMD00023353_3000160 {ECO:0000313|EMBL:GAW26385.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAW26385.1};
RN [1] {ECO:0000313|EMBL:GAW26385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAW26385.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF977475; GAW26385.1; -; Genomic_DNA.
DR STRING; 77044.A0A1S8A8Y2; -.
DR OMA; FDAGYWA; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000054516; 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; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; 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; 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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516}.
FT DOMAIN 44..466
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1417 AA; 153278 MW; DE0210B7A9E59205 CRC64;
MSSDSEPIFV GNSAAESDSS SVVFMNQAEE CIESFTVGLA SLNDDPPVIV GAACRLPGNI
TTPSGLWDFM VAEKSAQGPV IPERYNIGGF YHPNGSRSGS SNVPGGYFIN EDLRRFDNGF
FGINNLEATY MDPQQRKLLE LVYECLESSG TPMKSLSGSL TGVYVGNFSV DYQPNQTRDP
DYIHRYTSSG SGATIMSNRI SHVLNLHGPS FTIDTACSSS IYALHQALNA MRVGDCDSAI
VASANMVLSP ELHIMAAKSG VLSPTGTCHT FDASADGYGR AEAVNAIYIK RLSAALRDGN
PIRAVIRGSA VNASGRTPGI SLPSGEQQEA VIRKAYYNAG LNFSETDYVE CHGTGTPVGD
PIEVNAIGKC FAPREGAPLL IGSVKSNVGH SEGASGLTSI LKVVTAFENG KIPPSQGVVK
LNPKLILKER NIKVATAVEE WPRSIRRASI NSFGYGGANA HLILESAESY LGQAILQRSI
TVNGITSDEQ KLLVLPVSAS TTSSLEARVK QISQAVSEHN DLETLRNLAH TLTNGRDDLR
HRGFLLAHAG GKIEPVDETA TTKSINTLPF GFVFTGQGAQ YAGMAKELLI QNEHFRNTIR
TLDLVLKNLP APYAPDWTLE QTLLDGPSVS RINEVTRSQP ICTAVQIGLV DLLRTWGIQP
SSVVGHSSGE IGAAYAAGLL SLSQAILVAY YRGYAVGTMR SKGSMIAAGL NVEAANQLIE
DKGFSAHVRV ACVNSPDSVT IAGSSEGIEA IRAELVSQNK FARKLETGGR AYHSHMMEEI
GPLYQQLLIP LFNEHEKTGA QAEAKMYSSV GFSAEGLRIL DSSTNMAAYW RQNLEQPVQF
SAALSSLVAG GKVHLIEIGP HAALKGPIKQ IRTSLGLDTM ALPYSSTLTR NQDADVCMKN
LAGGLFTYGH TLSWSRINGL PESGLKILHN LLPYPWDYTA GILWSEPRSS LEQRNRKHIR
HELLGTVALT GNDIDFTWRN LLKPSEMPWI QDHKLEDQVV FPGAAYLAMA VEGVSQIKGV
RGKPAAQLAF EFQNVSITAA LHVPDENDAA AADLELHTTM TPRKRSGGSN SVDWYDFSIS
SWRSGETKTH CTGSVRLAEP VTSTGDDSIT VQNTEHYDDW QASRWYKQWA EEGFCFGPHF
QSLIRFRADN SLTRREAIGT VNLVPALNGG GDTDYPVHPI TIDAAIQAAI WSTTAGKLRT
LKAWFPVFIS ECRIQPPQDY DTGFEAEIHT RSEETGVSSR MMAATLRDGR GAPVVAFKNA
RIALFTGKKV EPADENSPLD IFMRRQPTLR VNWKPDVLRL GADAGAPLKA HISAFVGGQH
PDLQDDAALA VVSALLDLAG HKNPRMRVLE LGGDALGYKA RQWLGVLDKE TAFPRCRSWH
SGAVDEDGEY SIEDGGDDGP YDVLLVPTVS ETCPCQF
//
