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Database: UniProt
Entry: A0A166B9Q7_9AGAM
LinkDB: A0A166B9Q7_9AGAM
Original site: A0A166B9Q7_9AGAM 
ID   A0A166B9Q7_9AGAM        Unreviewed;      1739 AA.
AC   A0A166B9Q7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Ketoacyl-synt-domain-containing protein {ECO:0000313|EMBL:KZV64746.1};
GN   ORFNames=PENSPDRAFT_756992 {ECO:0000313|EMBL:KZV64746.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV64746.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV64746.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV64746.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV424640; KZV64746.1; -; Genomic_DNA.
DR   STRING; 1314672.A0A166B9Q7; -.
DR   InParanoid; A0A166B9Q7; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009403; P:toxin 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; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
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; 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; 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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..454
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1275..1351
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1375..1449
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1739 AA;  189369 MW;  FE538F60E4A327E0 CRC64;
     MSTYNQAAVF DPAVPAEHAI PAAPHHESIA IVGMAVNMPG APDASRLWGI LEHGINTVAE
     IPGHRFKVSN YEEADTGRAA RTMKARTGNF IDDPEGFDAA FFKISPREAR SMDPQARILL
     HTAYEALEDA GYVPSATPSF APETFGCYVG VATGDYTQNL RKDIDVYYST GTLRAFLSGR
     ISYVFKWGGP SVVLDTACSS SMVSIYQACR ALTSHDCNAA MAGGVNVITS PDMFLGLDRG
     HFLSPTGQCK AFDASADGYS RGEGCGLFVL KRLSDALAEN DNILGVIRGV EVNQSGLAHS
     ITHPHAPTQA RLFRRLLERS GVNASRVNVV EAHGTGTQAG DPNELESIRN VLSVGRDAEN
     PLHVTSVKAN IGHLEAASGA ASLAKLLLML KHGTIPRQIS LCNLNPRVTN LVRDHIVIDR
     EQVPWQPVHE GERRMALLNN FGAAGSNTAL LLEEYVADPV CAPDTASTFV FGISAKSPET
     LLRLRDAYVQ WLQRDEHQDT RLVDIAYTAT ARRIVYDYRF AVTASSKKEL VEKLTTSNSA
     SPSRVPKKIA FVFSGQGGKY RGMGSTLYRT SSLFREIVDE CHSFLVDSGF PGVLQVLYPK
     RSPADISQEE EFEINQSAIF VLEYGMARLW LSWGVEPAAV VGHSLGEYVA QVVSGVLLLK
     DALTLIANRV RLMVTQCATG STSMLAVNVG RSELEGILAS SSSFADLSIA CCNSPTDTVV
     SGPVRALKEL KVHLDSEVHV KHVMLSVPFG YHSRAMDIIF PDLLAMGQRV TVRPPSIAIV
     SNVLGQVVMP GTQGVFTPDY YARHCSDPVR FEQGITSLCQ ANGFDDISVW IEIGPHSSTL
     PMLKAHPLVR DDAVLIPSLR RKQDAWATLS SALAQLYLTS NTIRWRDTFT HVDARCTHLP
     AYPWSKTKFW VAFEEDSLAT GALTTNSKPL GTALVQKHAM LHRWVRSPNL ESEPTAVFEA
     PVASLARAIT GHKVGGVALC PASVYGELAL AGIDAATERL GLVTDDFVVT LRDTEFTRPL
     IFDAGIERKV YTSITLASGD TGSWHVSSRV DERSEDVHSV GTFKRQPNKK IVTKFTRAAP
     MVLRQIAVVQ AALDAESFST RTVYDIIFPR VVEYGNEYRT IRSLRISSDG MEGYAVVQLP
     DDHDRQRFVI HPTFLDTLFH VAGFAANIRG DKGDAYICSR VEKIMALPQL VDPAARYGVY
     FRNIWFSEER TILAESYAIE LDGQRRVVAH VKGIHFRRVL LSGLERSFTF AAGGHARPPL
     HRNERYLSST HKPSQSTVEA ETIVKQLVAK TCDIPNIDPF VDLDTYGVDS LMSIEICHKL
     IQAFPTVALD ANVLQSCTTV AQLIEAVVRR LPACLQTATP PSTTSVATRS QPQSVATSAD
     ARAIIATTLG VSVYELADEV DLDALGLDSL TAIEATMALQ TAFARSLPKT LFESVKTVKD
     ALDVISYTTR STDIGNATQF ALTPPHTPAH DALEPMLIAP ETRARLTKSL RLDEIPVLLQ
     AGTGTPLFLV HDGSGVVSYL KRVEPLGRAL WGLNNPHFLD GTSWDSLETM AGAYARQILE
     TIGGTGPVIL GGWSFGGVVA FEAARQLRAL GAPVRGVLLI DSPPPRGHVP FDDTLITAIA
     SADGRSPTND LTRLVSRQFE LSSRLLGAYG ANALEGPFEE RVVLLRSREG YRTVNHEVQV
     PQWIADRTDT GVVVDGWEEM LGYRIKVLPI PGNHFEVFAP QTMAQLSETI AGAADYLDE
//
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