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Database: UniProt
Entry: A0A0D2FLT8_9EURO
LinkDB: A0A0D2FLT8_9EURO
Original site: A0A0D2FLT8_9EURO 
ID   A0A0D2FLT8_9EURO        Unreviewed;      2368 AA.
AC   A0A0D2FLT8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Z518_06497 {ECO:0000313|EMBL:KIX02947.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX02947.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX02947.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX02947.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847479; KIX02947.1; -; Genomic_DNA.
DR   RefSeq; XP_013270083.1; XM_013414629.1.
DR   STRING; 1442369.A0A0D2FLT8; -.
DR   GeneID; 25294568; -.
DR   VEuPathDB; FungiDB:Z518_06497; -.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000053617; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 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; 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; IPR011032; GroES-like_sf.
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; 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; IPR029063; SAM-dependent_MTases_sf.
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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2279..2360
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2368 AA;  259606 MW;  527D05919C0C740C CRC64;
     MGSLAHDNPV PADIAVIGLA CRFPGGASNT QNFWDLLYQQ KATYADFPRS RDNASTFYQE
     GDKINATGSQ KGHFLQQDVS AFDAPFFGIT GQEAKAMHPT ARLLLEVTYE AFENAGLAIE
     QLAGSNTSCY VGCSEPDLAG TILYDPESPT TYKTTTSLSL LSSRISWYYD FRGPSLTLDT
     GSSSGLVALH LACQALGAGE SKLAVVSGAN LILNIEYATV FANPDRFCQE TSSKSFAGGA
     VCHGRGEGVA SILLKPLNDA LRDGDPIRAI IRGTGVNQDG HTIGATVPNS NSPAELIRST
     YDSAGLDFSH TVYLEAHGTA RRMGDAFERT AVARSLGYSR KEGRNLLVGS VTSNIGNLEG
     ASGLASIVKS ILMLERGIIL PNVHTENTVN PRCSVDLKLA TPTSCIRWPL NSPRRVSVHN
     LGSGGTNAHA ILDDATEYLT IRGLQDSSSL SPWVSKNATQ PRLFVFSAHD EAALRRMKKQ
     YADYLESYMT TAGSKFQVKE SAFLDQLAFT LSERRSRFDW KTHVVASSIK ELRTQLSSST
     VRLGRSSTSN PQVAFVFTGQ SENWARMGVG LFRYPAFKKS ILDADEHLKE AFDCDYSFIE
     ELKRDDKGIE THLAAISHPM STVLQVALVD LLRSWNIIPA GVVGHSSGEI GAAYAYGVIS
     REDAWTIAYW RSKLCSELTA ESTPPKEAML AVALSKDAVQ EHLSTISHGQ LVIACVNSPS
     SVTISGKETA IGQLHEKLSA SSVFCRQLKV PNAFNSHHME QISQRYLEKI STIRPKSPMS
     ARNIVMVSSV AGEVIEPRAL APEYWVRNLV SPVKFSDAIE KLFKNKNFDF LLEVGPDSTL
     KGPLRQIMRD LNIQNVTYKS IISSGEDAIS SAANSAGMLY TQGFPLCVTA INMIDTRLKP
     MTDLPPYPWN HSLKYCIESQ MSSSCPAGGC RRHDILGSVA LGSNELEPKW RNLLRVSEQP
     WIQDHVVRGE TIYPAGGIVA MAIESVKQIA NKVESIEKIH LKNVHIPKVI VIPDNEAGIE
     CSLQLRRPSS TGSPWTNWWE FSVLSSLDHQ KPEQIAFGLV KVQYKSDDIP SWEIQKTQTV
     KMLRGDYQKA KLLCTRRINP KDFYEAEKQA GLNYGPCFQG LTDVSTHSRR CCFKISAPIT
     RGSMPGRVES PYTIHPVSIE IMFHSLLAAL GGNIDSNFHT VAIPVSFDSM TVAMELPVGE
     NSKFHGHCEA IKEDSGEVVG DVFVSDRSWV EPKVLIRGVH FRKLPPATTP SRPICPWKAP
     FGTLAWKPDI HLCQNQSLED YLSQTELVLD LVAHKNPDMS ILQLGGSLSM TRSILSVLAT
     DPEDTSRFSN LVAADTNSAI AQDFEDKFRD WGSKLSFIKL NEDLDLQGQT LSPGSFDLII
     TGATFSNNMQ KTRFLQDVQG LLKNGGVFLI LESFTDITKT KGWESVVIQS GLQPIGMLQS
     DDDEVKSVTT ALCVTVKAYT EVQKKLSDVI YIVQPPNLTE KMSEIGQSVI RRFSSSSMPA
     QIVEWPPDPA KLKEQPVISL LELTRPFLIN ISSRDFEMMK TIVQGSSSFL WVSMGSEPMM
     TVGMGFFRVL RNENPKLNVR FLLFEEMAGR QPDELAGNIF KVMTSSNPDG EFIQMDGQLC
     INRWSPDKGI SRITTDQGGV VLEAMALEES QTPLRIHAEG SGQEQSWYFV AENELSGHPA
     PGEVDIVTRA VVLSNQDSTA SSPEPIKEFS GIVKSVHKDC PRFKPGDRVY GCQPAPYRTV
     YRVKERFCQQ ILGDDPFEKA ASRPITFGTA YYSLVKIANL QYGQTVLIQA ASTAVGQAGV
     QIAQAQVAVV FATVRTEEES LLVEKLGIPR ERILNDADPE LCTTISRLSG RKGFDVILNI
     SKDGEDLGDL WRSVASFGHL ISAAAANQLK GPDLDMAPFQ KGCSFAVVDM NLIYRENPTL
     MAEISKDLGR YLATSSLRPI EPTRVYSSEQ ISDAFKSTKS QDMSPGTTIV SFNPQDELRI
     HPTARNPLHL QKEASYVLVG GLGGFGRHLA RLLVDHGARH MVFLSRSALM AANAQAVVDE
     IAARGVITKV FVCDISDETT LSKVVEQCRN EMPPIRGVIQ STAVDNDSLD RKTTHELWLD
     ATRIKIRGSW LLHKLLPRKM DFFVLVGSTK RMFGNRTQAS HAAVNTFQHA LAQYRRHQGL
     AGAAVDLGPM LGEKFVAEKD GSTNILNLEA PSLSEAELQA IMVAAMTGSY GSNPTPVPLV
     TGLPTGGLLH RQGLDGPSYY SDPRFSFLKK MDFGQNVREE ISGEENEESS LAKRLRACQS
     LEEASKEICS AMCEFLGEEL QTGAENLEIN SSLYSNGADS LLAVEMRSWL LRQMGAEISL
     GDMLSGHSIS ELADKIATAS TLIPAGVK
//
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