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Database: UniProt
Entry: A0A166K2Q0_9AGAM
LinkDB: A0A166K2Q0_9AGAM
Original site: A0A166K2Q0_9AGAM 
ID   A0A166K2Q0_9AGAM        Unreviewed;      1945 AA.
AC   A0A166K2Q0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:KZP21464.1};
GN   ORFNames=FIBSPDRAFT_919578 {ECO:0000313|EMBL:KZP21464.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP21464.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP21464.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP21464.1,
RC   ECO:0000313|Proteomes:UP000076532};
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).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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DR   EMBL; KV417547; KZP21464.1; -; Genomic_DNA.
DR   STRING; 436010.A0A166K2Q0; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000076532; 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: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; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; IPR049551; PKS_DH_C.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
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; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          375..802
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1615..1692
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1945 AA;  211648 MW;  CE81A4C86E95012E CRC64;
     MSSRHPDVPV FSGQGTDFAN AARTYAQGVR DASTPAGSVL LAACFDAFRE ELSALSVEQR
     VKSEIRLGEQ PHIYTGIDLL APSVQAVNNP ITSGARLFLF QVLRSSSSQS RFRDALLSPD
     TETKSLGVLG FSSGVLAACV TASSLSLPAY ISYSIQAFRL QEYRRNVLIN MDSTASQLPW
     SVAVFGLDQR ALEGLIADFG TRNGFRPTIT AVTAPELLTV SGHPVELQSF CASLPSSCTL
     HSTNLSTLYH SATHLASARQ KILEDALLRN IRFPELSDLA APIRSTYTGE LISNTTPGSL
     VELVVDMLLM QPVNWNLAVA SLKLAAGNSA FRLANYGPGL GLMRITERAL EGTASVAVDM
     TLECEGKSNE RNAKHEPIAI VGMAVNMPGA PDKVKLWEAL EKGVNMCTEI PESRFRVSDY
     ASSSNLQSGR SMRAHTGNFI SSASAFDAKF FKISPREARS MDPQQRILLQ VAYAALENAG
     YVPDSTPSFQ RDSMGCFVGA ATRDYAENLR SDIDVYYSTG TLAAFLSGRI SYVMQFGGPS
     VTVDTACSSS TVAIYQACRA ISTGDCRAAI AGGVNVITSP DMMLGLDRGH FLSPTGQCKA
     FDASADGYSR GEGCGMFVLK KLSDAVAEND TILGVIRSIE VNQSGMASSI THPHPPSQIK
     LFRKVMENAG IDPSRVGVVE AHGTGTQAGD PCEMESIRAV FSVNRLTQHP LHVTSIKANL
     GHLEAASGAA GLAKLLLMFQ HQTIPRQILF SELNPEIAPL GLDHTVISTS HVRWPSTRGS
     NRFALLNNFG AAGSNAALLL EEYQDGSPAA VEFHEHVMLG ISAKTEKALM DMRSGYITWL
     QKPDNAKIAL SDIAYTVTAR RQIYPHRLAL SVCDRQELVE QLTTAIPIHV SNTADGVVFV
     FSGQGSQYIG MGASLYRTCP LFRQHIDECN SILIDANFSS ILSIIMADED AEDIGLSRDA
     TLEAYQTSIF AIEYSLAKVW MSWGISPVAV VGHSIGEYAA LVTAGVLALQ DALRLVARRV
     QLMLEKCSPQ ASGMLAIKLP AASVARSDML EDLSIACYNS GEQCVVSGAI DKLKILKARL
     DGGGYKSVIL DVPFGYHSSA MHPLLGDLKK AAERVCFSAP HIPVASNVLG KVVFAGDASV
     FNAEYIVRHC REPVLFEQAI TALLNVSTAA NAAAWIELGP DATVLPMLRS HPKFPLSLLL
     GSLRKGTDAW RVISGSLEKL YLSNVNVLWR EVYAHKSSVN CVDLPSYPFD TTEYWIDFQE
     EMLHSSIQPA FPASSSPKYT MLFSWSQYPL QSNERTAIFL TPIAELAEFI NAHSVGGFPV
     CPASVYLEQM YAGAALVVEN LAMGDGCITL RDVEFVKPLV YVENIACMVK TRVSLPFGGL
     GSFTISSSYL TGDENDVIHA QGSIILKLTA DIDQKFARHL PALCRQIAAV TQPLEGAQPQ
     MFSARTVYKL IFPRVVDYGE IYQAIKSLTI DPTGMEGSAT IQFPPRAKRP NELYFLHPVF
     FDAMFHVAGF VANLQGEPND AYICTGMGSV RIAHGIIDEA ASYSIYCCNS WIAEEEIMFA
     DIYALQLNGP RKIVAHIKGL QFRRVRLDAF KHVFPLVKQV TQVIAETCLI DSALIHPNVD
     LSSLGEIFGS VLGLRIDDIN ENADLESLGL DSLTTIEAVD CFKHQSGHDI SPDIFQTYNT
     IRAIQIFLSE SSQGTHAAQF TEKSNCGPRL NRIQVSSRGA PLFLVHDGSG MVDYFNRMPS
     LGRDVWTIPN PHFGKDAIWP WEDLESMAQE YTGYVTSVSS GPVLVGGWSF GGVVAFEIAR
     QLLKGGTDAR VLLIDSPSPI NHVPLDECLI ESITNANMRS TVSSMSWMIR AQFRFNSKSL
     GMYKPLLSDG PFPKIILLRS REGFHPCGIN NVPRWLSERG DPHDVVAGWE ALVECPVRVR
     DIPGHHFEPF SPSNVRRPRF MRTSN
//
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