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Database: UniProt
Entry: A0A2N6NUJ8_BEABA
LinkDB: A0A2N6NUJ8_BEABA
Original site: A0A2N6NUJ8_BEABA 
ID   A0A2N6NUJ8_BEABA        Unreviewed;      3945 AA.
AC   A0A2N6NUJ8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Nonribosomal peptide synthetase 14 {ECO:0000313|EMBL:PMB70939.1};
GN   Name=NRPS14_0 {ECO:0000313|EMBL:PMB70939.1};
GN   ORFNames=BM221_003399 {ECO:0000313|EMBL:PMB70939.1};
OS   Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS   shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB70939.1, ECO:0000313|Proteomes:UP000235728};
RN   [1] {ECO:0000313|EMBL:PMB70939.1, ECO:0000313|Proteomes:UP000235728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEF-007 {ECO:0000313|EMBL:PMB70939.1,
RC   ECO:0000313|Proteomes:UP000235728};
RX   PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA   Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT   "Characterization of T-DNA insertion mutants with decreased virulence in
RT   the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL   Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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:PMB70939.1}.
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DR   EMBL; MRVG01000003; PMB70939.1; -; Genomic_DNA.
DR   OMA; QFFNIPP; -.
DR   Proteomes; UP000235728; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; cd05930; A_NRPS; 1.
DR   CDD; cd19532; C_PKS-NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013120; Far_NAD-bd.
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; 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; 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:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-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; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235728};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..437
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2374..2449
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3513..3593
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2453..2510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2482..2510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3945 AA;  432449 MW;  E9CBCC8A9D11F94A CRC64;
     MSSHQNEPIA IIGNACRFPG DSTSPSKLWE LLKQPREVSR NIDRFQSAGF YNKDGHYHGA
     SNVQHSYLLN EDPRLFDAQF FNIPPGEAES IDPQQRMILE TVYDAVETSG LVLENLRGSN
     TAVYVGVMCD DYGNICYVDQ ESIPTYAATG TARSILSNRV SFIFDWRGPS MTIDTACSSS
     LVALHQGVQV LRSGTSPIAI AAGANLIFSP NMFIAESNLN MLSPTGHSQM WDANADGYAR
     GEGIAAVVMK RLSDAIRDGD NIECIIRETG VNQDGHTPGI TMPSQEAQTR LIHETYARAG
     LDLSKPEDRP QYFEAHGTGT KAGDGVESKA IYKAFFPESD DKHDTLWVGS IKTIIGHTEG
     TAGIAGVMKA SLAIQNKTIP PNMHFNTLNP EITPYYGKLQ IATAAQNWPK LASGSVPRAS
     INSFGFGGTN AHAIIEAYVP EAPNALTQAA PAVANPLALT FSATSEKSLT NLMANYLEYL
     TENSEVDIGK LAWTLHDRRS TFSYRSSVAA QTQDELVAKL QKSVEDQQSG NSSAVTRGTS
     AKKNLLGVFT GQGAQWATMG RDLISSSKFA ESIIDKLEKS LGELPEGDRP SWSLKEQMMV
     DPSKSRITEG ELSQPLCTAV QVMLVEMLKV AGIEFDSVVG HSSGEIGAAY ASGFISDTDA
     IRIAYYRGRY AYLARGPEGQ RGGMLAAGTT LEDARELCDL PAFEGRVSAA AYNSSSSVTL
     SGDLDAIEEV KEVLDDEKMF NRQLKVDTAY HSHHMIPCSQ KYYEALDACK INIMTPSGRT
     KWYSSVYDGK VMEPCDALKH QYWVDNMVNI VLFATALSAA LSSSEPKLTQ AIEVGPHAAL
     KGPASTVIEE TIKSTIPYTG TLSRGQNDVT AMATCLAYLW AQFGRSSADW KAYYGLFADS
     TPKTMLNLPS YPFNHERLFW YEARKSRVNR LREDPAHVLL GTRTDTINER EIRWRNYIHS
     GEIPWLQGHN IQGQTLFPAA GFLVMAVEAA RIAGRAEAIQ AIELKDSAIH RALAISEDKG
     IETLFTLSNV TITETGEGTS VLTARFACDA CLQKQSDNFV SIASGDVIMT YGTPSSSALV
     EYPKEEGLGM LDVDADLFYA YLANIGYNYA DMFKGITSLR RTTDLAQGVI TTKVPEALAN
     EPIDQFLLHP STLDVAFQAI FAAISFPGDG ALWALHIPTT IRRVTINPVV CPMNGGVDEK
     VRFSATSNRA DDGTFSGCVD IFPVHSDFSM CQVEGLEVSP VSPPTARDDR PFFGQTNHWL
     SLPDADSFAA ALRITSTQEA EKSQLDRLAV SYLRNILQSS GHETDQLKSW AQTVLASLGK
     KASLPAIEQS DVAVQDNSAY KTNFSILKTI GAGIEKGELP QGFDASELLN TFYETSLGAA
     EAREALAILA QQIVRRYPHM NILDLSSGSG SVTKTVMDKI GALFSAYTCT GATDEHFAQL
     SKDHPAISTR TIDFSEDLEE QGFFAGAYDL VIAGNGFHSI KDNVEGMQKL RSLVRPGGYL
     LAQQITNSDS AHVGLTVASV ALQPEEISST TTLVADLGEY DDIFRTAGFS GIDTVTPDSA
     SPFTVFVSQA IDQQILNIRE PLHSSKVDLE NVLIIGGQRF QVSRMIETMK KSLSPFAKNI
     ETIRSLNDLD ASMLATRPYV VSLTELDDPF FENLTDTKWE ALKTLFFRSR YILWATQGAN
     GDAPYANVMK GVVRCMLVEI PHLHGQMFNI EGQLKPEQHS LTIVESVMRL HISDTWKDKV
     PTYDPLWTVE REYMLKDDKL WIMRYDSENT LNAGYNALRR RVIQEVSTKD QVVALTPEKQ
     LQQYRLSPKA TVEIEGIPNS TVTVHQSLSS AIKVEGLGYM HLSVGKEAET GATVVAFSDK
     NQSSLTLPKS RLLPVDVPEG KERSLLVAIA CNMLANDLLG KVTAGDRIVL HEPPTVLTKL
     LAERVANTGV QLLFTTTRRK AALQAQWKHI HAYSTDRDMR QITAANTAIF VDFSNNEKRR
     DVVEHLTEGL PFGTRKYELG DFLPSRSVLY SDSTEEQVST ALEKAYSTAT AERSSVPFDN
     VANTRVQQLA DDADLAETLT TVDWTDATPF PASVTLAMDE VNFRPDRTYF LIGMTGSLGL
     STCEYMMERG ARFFALSSRR PNVDKRWLEK VRKAYGAVVK AFPLDITSRA SLQKVHDDIN
     DTMPPIAGVA NGALIMRDGL FMDSSAATMN EALGPKVAGS VFLDDLFYNV NLDFFILYSS
     LVYVTGNIGQ TSYAAGNGFM VSLVHGRRAR GLNATVMNLG GISGIGYITR TDHGILGKLD
     ILGYGIMSEL DYKYFFAESV MAGAADSGRN PEVSAGLRYV NKTEKNPPKW VVDPKFSHYV
     IDRTSRDGGD KGGDSAMSTK AQLLEATTEK EAFNIILNAL MAMLGKKLDL PPTESVHSDV
     AIVEMGVDSL VAVDLRSWFS NEFEHDIPVI KILGGATLAD LVEDTVANMS PDICPNISGG
     SGDDAEAKPA PAAEAPIPVS AVDSSSGDSA SSSDERESAT SVETAPTTAS KVTKEVIAAP
     KPIVDVAPKC HFVREEKMTH GCSRFWFLRQ YLEDSTCFNV LVQTRLNGKI DSARLQEAVR
     KLGARHESLR TSFFVSEKGE PRMGVMSDSL LRLEVEKVQE ISQAEKAYKD MMGYNFDIER
     GEVIRMRLLS LSETDHVFIF AVHHIAMDGF SFNLMIRDLD MMYQGKPVPQ IPAQFTDFAI
     QQRRDVEAGR MRNDIAFWKK TFSNIPDPLP LFPFTGVGNR MPLVKYEHEE VEISLDAAMA
     QKIRNLCRQN RCTTFHFFLA TFQIFLGKWL EVDDLCIGIA DANRSDIKTL STIGFLLNLV
     PLRFSALNGK APFSSVLAAA KQTAYNSLAH SKLPFDLLLE ELNLPRSSST SPLFQAFLDY
     RQLAVKTPPM LESSAEGEQN FGATAYDVVL DVTDYAMADI KIKWQTQKAL YNTKHTEAMM
     ESYMNLLNHF ANSATSSVES APLYRPEDVK AAVEAGQGSQ FDGQWPETLS LKIDDISGKS
     PESIALADVS NSFTYSSMNR FIDQIIEELV QGGVKPGDKV GIFQQPSSLW ISSLLAVWRA
     GAVYVPLDPR NGVPRLASTV GVVQPQAIIH DNANAKDVSS LAAPASASII NINNVRKKDA
     TVAHRPNLST GNSSAIIVSS SGSTGVPKCI EVRHSSLINL FEGDSKTWNL GSAKVLQQSA
     YSFDISLDQI MTAFVNGGTL YVASEEERTN PELIAKVIVD NNINYTTATP SEYSNWIGFA
     AETLAKASSW RIANVGGEGW NSNLRDSFSN LKLPQLVIRN NYGPAEASVW ATRYPIEYPG
     KGTLIPAGPA LPNYSFYIID KKNNVVPTGV QGEILIGGAG VAVGYYKNAE LTKDKFITDK
     HATEAHTAKG WNRAYKTGDK GYLTEDGTLI VQGRISGDTQ IKLRGFRIEL EDIESTIVHA
     SQGVLTRAVA NVRGDGPASY LVAFAEFADG YPAEEQDAYL SKLISKLPLP QYMRPNIMVP
     IVDIPVNAHN KVNRLAIATL PIRTASSDDN LNTELTETAK TIRDIWVDIL PDSIVQNTTL
     YASSDFFVLG GNSLLTVRLQ SRLREIYGVF VPLIKIMESS TLSGLSNTLD DLLSNQEINW
     DVETALSDEM LSVTPVNPNT TRPKTTDLTV ILTGVSGFIG RHLLQRLIED KNVSAIHCVA
     VRNIEMDSPS RQKMKALIAS TNKVQLYPGD LSEPRLGLSE AEFDTLSRKA DMIVHSGANR
     SFWSAYDMVR APNVQSTKEL ALMAATALRD SNKVVPFHFM SGSEDAGIEP STDGSNGYVA
     SKWASEQFLQ RFADQLGLPV HVHRQLPVPE GRTAQGEELD SILQEFVDVA AKMPELPNPD
     TWRGYYDLIP ADRLSDDVVD LAMSGLVSTN NAFSKHSHYS SVRMDIGEVI KKIDSLDEYK
     NTDRPLIPAH VWVGKAKIAG FRYQFSTMKM SLQDAEGKNM GFLER
//
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