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Database: UniProt
Entry: A0A175WJ59_9PEZI
LinkDB: A0A175WJ59_9PEZI
Original site: A0A175WJ59_9PEZI 
ID   A0A175WJ59_9PEZI        Unreviewed;      2655 AA.
AC   A0A175WJ59;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Lovastatin diketide synthase LovF {ECO:0000313|EMBL:KXX82904.1};
GN   ORFNames=MMYC01_200634 {ECO:0000313|EMBL:KXX82904.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX82904.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX82904.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXX82904.1}.
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DR   EMBL; LCTW02000006; KXX82904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175WJ59; -.
DR   STRING; 100816.A0A175WJ59; -.
DR   VEuPathDB; FungiDB:MMYC01_200634; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000078237; 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; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 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   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; 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; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
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; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2572..2650
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          453..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2451..2470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2655 AA;  286136 MW;  B3EF5410F6F131D8 CRC64;
     MSSQPDQHEP VAVVGMGCRW PGGAHDTSKF WEFLCDKVDG WKEFDDPRFS ARAFHHPNAD
     RPGGFAMKGA FLAEQDARLF DHSFFGMTSL EVETMDPSQR KLLEVTYEAI ENAGETLESV
     SGSRTGVFVG NFCLDHWMIQ SRDWDNPRPY AFVGAGTSIL ANRISYIFNL QGPSLTIDTA
     CSSSMYALHL AVNAIRAGDC DSAIVAAANW IADPGVQIAL DKLGALSASS RCHTFDARAE
     GYARGEGYGA IYLKRPSVAI AHNSPIRAMI RGSAVNSNGR TGGITRPSAS GQEAVIREAY
     RHAGGLDFHD TSYFECHGTG TYVGDPIEVA AVGRVFASVR AAEDPLLVGS VKSNLGHGEG
     ASALASVMKV VLALENGAIP PIFNLETPNP NIDFDAAKVK PVTEVTPWPA GRLQRASINS
     FGYGGANAHC IIDHVNNVLP DYVAPGVYKS TRANGATNGH ANGHTNGHTN GHTNGHTNGH
     TSGHTNGHIN GHAVGETNGH ANGQQSGNPN GKSLQHHPIV KSPQLTATPE AATRKLVLLP
     LSAHNEKSLR LNFEALSKAI DDVSLADVAY TLGARRSRFA QRSFCIVDKD SIHETLVLER
     KPVRAPLQAS NLGFIFTGQG AQWHSMGVEL FEYRVFRTAI EYLDYVLTML PNPPSWSLRS
     ILSGDCDAAF IHKAEISQAV CTAVQVGIVD LLASWSIRPS GVAGHSSGEI AAAYAAGRIT
     AAEAIVAAYL RGQAVSRNDR NGSMLAVGLG PDAVVQYVRG REDRVKVAAI NSPGSVTLSG
     EEDTIDEVSA ALTADSVFNR KLKTGGNAYH SHHMLPIGAD YVEMLRQGNE RIQELGLANP
     EHRYPHTLWV SSVTPSKATI EMDLASYWRA NLESPVRFSE AVTGLVGSED VPIHALVEIG
     PHPALKSPIE QILKAVGKAV AYSSTLKRQE DARASLLQLA GALFSLNATV DLAAVNAVDD
     TDSAGLTHGC TCTKLPPYQY TYGGLNYYES RASKEYRYRS ILRHDLLGSK VAGNAKLRPQ
     WRNLLRMKDV PWLGDHRLVP DAVLPGAGYL AMAIEAAARI YHEFPEPLKI KGFSLRNVAI
     KNSLVVPEDD YGIEVLTSME LADVATANSP AWATFSISSV GRETNEWTEH CTGSIKVELV
     DDDERKRVEQ VPTAPRLVDT RRWYRKFLEV GLGYGPAFQP LSDIHADPTS NVAVATVDLH
     TTSLKGGESR YPLHPASLDG AIQLGLIACH GGSSDEATTA FVPVQLSRLY LSNDIDEIAG
     DKCTVIARGE RRGVRGAHLD LKMLSAKGDV LLHADGLRCI SYSSAAKPAD RSFSSPFTRL
     VWKPDIRALS SRQARRLYPP PKSNVERAPA WGITNKLAHF VVLSMYQGLG KLRNSGHKPS
     GDVGHFFDWI ERKGQRDNSG LMNEARELAS KGILLQKIEE LANQAQDIME VKIAKLLHDN
     MADIFMERRT GMDVIISEDL LTPLYKSGLL MTGIYPQLHH ILASVAHSNP HLRILEIGGG
     TGGATRIAMK AFNGPNGIKA YRDYTFTDIS AGFLSAARET LADFRDMNFS VFDIEGDPVD
     QGYVEQTYDL IIACQVLHAT SNMHRTLTNC RRLLKPGGRL VLVETNQNFI VPGVVVGTFT
     GYWAGIPDGR VDAPFQSLPS WDRSLREAGF SGLDVVLDDF PEPHNTTSVI LSTVPPEAAA
     EASSATVHVL HSGKAAAPAL VEQIGKELHQ RGVTAKAATF DEAAESLTPE SRVVAFFDDE
     HLLAHASERE LTMFQRLAQN AASLVALTSC GTVKGRNPDG ALISGLLRVL QNENPASQYI
     SIDIDADNFS VEEGDGKDLA RCIVDRESEL HQGDFADEVE RNPMDREFSW HDGCMWISRH
     VPDAGFHSQH GLDPRAIKPD LLPLGSQGAV RAAFETPGVL NSLCFTPYKE LLQPLPSGFI
     DVAVAAVGLS MRDLDHWTGR VDGDHLSSEY SGIVTAVGAG VDNLKVGDLV YGLGKGQFGN
     YTRVPASLAR KLGLESDMVR MASMPLAYST AIYLLDHVAR ARKGQSVLIQ SGAKDDGLAA
     IHLAKAKGAD VFAMAETNEQ ATFLMNELGM PASHVISTPT LAALRHAAQS TSSGKFDIIV
     STTRDKLVYS FLQVLAPLGH LIELGRADSQ TSPALSLESL PRNASYSSVD PFDILVSRPD
     LGAELMQAVD NYYQKGLIQP IPKITAPDVS QMGPAIASLP SMIGKLVVSF ESPESLVRMT
     PAPPTVSFDH ESCYVITGAL GGLGQSLIRW MGDRGARHMA ILSRRGIADA SGAKELVESL
     GRRGIQVESF VCDLSNKDQV VSVMQQISSK RPIKGIVHAA VSYLDLSFDK LSPSRWNQGL
     AAKVDGTKNL HEATLSMPLD FFVMITSALA VYAFATQGAY TAANNFQDVF ARYRRRMGLV
     ASTASFSLIR DITNVGTSDL TVDLFERNKT VTLGESQFLT SFEPAFLNNT TSANNLDSDG
     GDDSSEEQWF GQRDDPLSAA NLHTYLDPAA MLARRQQELA SGAAGSSSIP RWYGDGRVSR
     MMRGFLDAQR QSADLQASAA AAEEAGGKAT PASVRREFEA AVRSGGAGGR AATVALVQDA
     IVRAVAEMLF VDVEGIDPAK SVAELGVDSL IAAELRSWFL KALGASISML DLLDPSVSIA
     TRAASITDKA LEESA
//
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