GenomeNet

Database: UniProt
Entry: A0A194UPC3_9PEZI
LinkDB: A0A194UPC3_9PEZI
Original site: A0A194UPC3_9PEZI 
ID   A0A194UPC3_9PEZI        Unreviewed;      2596 AA.
AC   A0A194UPC3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Lovastatin diketide synthase LovF {ECO:0000313|EMBL:KUI53493.1};
GN   ORFNames=VP1G_01033 {ECO:0000313|EMBL:KUI53493.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI53493.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN714669; KUI53493.1; -; Genomic_DNA.
DR   STRING; 694573.A0A194UPC3; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000078576; 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: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; 3.40.47.10; -; 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; 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; 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; PF13602; ADH_zinc_N_2; 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; 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   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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          12..452
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2596 AA;  282141 MW;  5A0786BF06BCDBC4 CRC64;
     MGSQSNGVDW ANEPIAIIGM SCKFGSDATS PEKLWEMVSK GGSAWSEIPS SRFNWKGSYH
     PDSERRGTTH VTGGHFMEED IGLFDAAFFN YSAETASSLD PSFRLQLESA YEALENAGLP
     LHQVAGSKTS VYAGVFFHDY KDAMIRDEDN IPRLYATGTG SAMASNRISH FFDLRGPSMT
     IDTGCSTTLT ALHQAVQGLR LGEADMSIVG GANVLLNPDW FKAFSSLGMV SADGRSYAFD
     SRASGYGRGE GVATVVIKRL RDAIASGDVI RAVIRETMLN QDGKTETITT PSSTAQESLI
     RECYNKAGLD PADTQYFEAH GTGTPAGDPI EMGAVVGAFI NDPNNARLKG NSKRKTRTEP
     LRIGSVKTNL GHTETTSGLA SVIKVALALE HGVIPPTVNF EKLNPKIGHL DEKQLKVATE
     LESWPVTPDA IRRASINNFG YGGSNAHIIM ENAETWLQQE GGITPGASLK ISTHDDHNDI
     PQTVLENGTS NTSLSKVLVL SARDEQGCQR TVENVKLYLQ NRLDHSTATE DEELLLQRLV
     YTMGERRTLF PWVAAHAIPC NQGINGVIEV LGSAAFKPLR TSRRPRIGLV FTGQGAQWYA
     MGRELLGAYP AYKASINEAS GYLTELGATW SLEEELTRGA ETSRVNDVAL ATAICVAVQI
     SLVHLLQTWG VRPVAVTSHS SGEIAAAYTV GALTYRSAMA VAYYRGVLVA DKSLHGPVDG
     GMIALGLGIE DVQMYLDRIA ARQGEGGQVR AVAACINSPS SVTVSGDLDA INDIETMAKA
     DKVFARRLRV QTAYHSHHMA PIAYPYLSAL RNTISDQEDP TSVQGGLHVA FSSPVTGGRV
     VELKDISCPE YWVESLLQPV QFVDAFTDMV LGDFDPSGSS VDILIEIGPH TALGGPIQQA
     LALPEFSDVK VSYYGSLVRN KNAVETMQDL SANLLKEGYP LDMGAVNFPL SKSPHISILS
     DLPSYPWNHQ TRHWAEPRLN RALRERQHRP HELLGSLVLG TNPEVPSWRN ILRLSQSPWL
     RDHVVQSNIL YPGAGYICLA IEGISRLVTS DRQVEPESDG GKCKTIAGYK LRNVDLHQAL
     VVAESSEGTE ILTTLYTVSE KDIGSRGWKR FNVSSVTQDN KWTEHATGLI MVEYQGLDHI
     SPRISAQQRE VTGYVRHVDP ADMYEGMRAA GIAHGPKFRN MKKITQSGKE MRSVSNFIVA
     EKSSSDEPDG SSGLVLHPTT LDSVIQAAYT ALPGAGSVNA PPMVPKSIAE LWISGGISSQ
     ASHKFTACSR LDRQDQQSFQ GDVSIVDQIC GDDIADSAAV LEMKGLICQS LGISVSPGSM
     SKTWEKEICS KLEWAADLSL ASADTWDNLR KQLSYGSCEP QEAAVILELR RVCMYFVQDA
     VNALTAADVA QLEKHHTAFY QWMQQQIELT AAGKMGPGSA DWLREGPLKR QLHIEKAALD
     SVNGEMTCRV GPRLIDVLCH NISPLELMME EKLLYRYYQE CIKLDRSFVQ LVELFRLAVH
     KSPRARILEI GAGTGGATRH MLKVLGESGA SLGEMYHFTD ISSGFFEDAR GEFAPWIDIM
     AFDKLDIGQD PVEQGFILGS YDIVISCQCL HATATMSETM SNVRKLMKPG GSLLLIETTN
     DQLDVQFAFG LLPGWWLGAQ DGRTSSPSLS EPLWDEVLRK TGFTGLDLGL RDCEDDGLYS
     STTILSRSLP HAEASDQVTT NEVVIITDNK DSPPSDLLSL LRNSMMKATG GQGQPNVYSL
     ADCSSAVMFQ GRYCVFVGEL DKPLLHNLDH DGLAALKALA TGCNGLLWVT RGGAVACEDP
     NLSMAPGFLR TLRNEYVGRR YVSLDLDPSR PAWCSESIQT IVRVVKASLD LVDDTAYSAA
     GAAPTEFEYA ERAGVVMIPR YYKDQSRNNY VSQETSEASV RNTSVTELLH QETRSLKLEV
     GVPGQLDSLV FSDDIPTYDE DELADDCLEI EPRAYGVNFR DVMLAMGQLH GHTDILGIEC
     AGIVRRVGRD AGAHGFKVGD RVFCMRQGFC KSRLRVEWLL AAHIPPNFTF EDAAALPVVF
     GTAYIGLYDV AGLQAGQSVL IHAASGGVGQ AAIMLAQRVG ADVFVTAGTA EKRQYLMDKY
     GIPANRVYHS RDASFGTGIL RATSGRGVDV VLNSLAGPLL QESFRVLAPY GHFIEIGKRD
     ILSNNHLEMG SFIHNTTFAA VDLHAMLCDR HQYVHRIMTG IERLAELGSI SAPKPVTVFP
     MADASTALRH LQTGKHMGKA VVSAGPREMV PVVPQARIVK FPANESYLLV GGVGGIGRSV
     AHWMVAHGAK NLILLSRSAA SSEKTGAFIS ELQEAGCRVI AVSCDVADEA GLAEALCASE
     RELPPIRGII HGGMVLQDSI LEQMTLDDYT TAFRPKVKGS WNLHNEFTRR GRHLDFFIML
     SSLAGIIGHA SQSNYSASGA YQDALARYRV GQNLPGVSID VGIVKSVGYV AERADVAERM
     ARLGYMPISE DQVLRVLESA ILEPCSPQVL VGLQTGPGRV WEPNGESQLG RDSRFAALRH
     CQTMKIQQKT SSGARSDREV LTLSDKLAEA TSRDDAETLV SQAIAEKLST IFMIPIGEID
     PTTKLSHYGV DSLVAQ
//
DBGET integrated database retrieval system