ID J4UJF5_BEAB2 Unreviewed; 1843 AA.
AC J4UJF5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=AMP-binding enzyme {ECO:0000313|EMBL:EJP63992.1};
GN ORFNames=BBA_06997 {ECO:0000313|EMBL:EJP63992.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP63992.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP63992.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP63992.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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DR EMBL; JH725171; EJP63992.1; -; Genomic_DNA.
DR RefSeq; XP_008600316.1; XM_008602094.1.
DR STRING; 655819.J4UJF5; -.
DR GeneID; 19890009; -.
DR HOGENOM; CLU_000022_60_2_1; -.
DR InParanoid; J4UJF5; -.
DR OrthoDB; 3305653at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19542; CT_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
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; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT DOMAIN 641..716
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1289..1365
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1843 AA; 200508 MW; 2DE34BEED0F4951F CRC64;
MLSIDDHGGG GPLAVDIIPA GSGAQKTAPD AADPSLHGPG RANGDAVNAD ATAAEETGSR
DDESQQQQQQ QQQQQQQQQQ QRSLLSERDL DQLWQWNAVV PETIQRCIHD IISEQAAQRP
QDVAVQSWDG SLTYSELEHL STQLALHLRL LGVDIGVTVP LCFEKSKWTV VALLAVMKAG
AAFSLTDPSQ PEARLQTIVE QTGAKLLVTS ALQSSLGAKI APGATVVAVS QATFDTPLQQ
SSDPLPDVPS SSLMYVIFTS GSTGKPKGVS ISHENFTSGA IPRAEAVGYK STSRVFDFPS
YAFDVSIDCM LCTLACGGQV CVPSEQGRMN DLSGSIRDSK ANMVHMTPSV ARVLDSDIIP
SLDVLGLGGE VVSGSDAATW RQFTHLIIGY GPSECTVGCT VNNNTSLSTG IGKGVGCVMW
LVDPEDHNVL VPVGEVGELL IEGPVVGIGY LGEPAKTAEV FIEDPTWLTA GHGCYAGRHG
RLYKTGDLVR YEDNLSGSIE FVGRKDQQVK IRGQRVELTE VEHHIQTCLP TGVKVVAEVI
KPENASPTLV AFLAEKSSVG SQDGSLFVDP SPELSAALDK IDTTLGAKVP KYMIPAAFIT
LASMPTMVSM KTDRKKLREI GISIPRSKLG ATHADEGPQE EPETDAEKKL AHAWQLVLAS
SSPVYKASSF FGLGGDSLRA MKLVSAAREQ GLGLTVADIF NNPTLSAMAN KSTSISSATQ
EQVKPFSLLQ EGWDEQTARK DVAELCGIEP EQVEDVYPCT PLQEGLMALS SKVKEAYIAQ
RVVVLKDLET AKRLMAAYDE ASRGSPILRT RIVQVPRRGL MQVVVNRKLE YTTGNNVAAY
LASDRETPMD LGTALWRYAI ITDEAAGTVS FVLTMHHALY DGWSMPLVVE RINQAYQHPG
KPLSRPSEFK DFIKYLLSQD AAESEKYWRA QLEGAHRLQF PLLPHQGYQT AADELLEEYV
PLEQLPKNAT VATLIRAAWA IVASQYINST DVVFGETLTG RNAPVVGVDE IEGPMITTVP
LRVPVDAEAQ VGEFLQAIQE QTVGQIPHEH FGLQHIRRLS PDAREACELR AGLVLHPSAD
TAAPEVDATL PANNLIPHLA AREALKFNTF ALMLVCSMDP KGFQVMASFD SKMVDKSTMR
RALAQFKSVA QQLAQSTTTL LGNVRALSDD DAAALRDVVA TAQEDPVVKT YDGASAAYIV
RSDDASKMVP VGAIGELAIQ TSQPKDLSTL PVPSWLAALL PPSAPTDALY LTGKLARYDA
AGKIQVLGDK ASLTASTDAS AAARKPRVSA TSQRQRRLRA LWSHVLRTPE TEIGLDDSFF
LLGGDSISAM KLASEARPEG IRLTVAQMFS HKTLAEMAAV MECTDESSDS TAAAAAEAPI
APIAEPFELL DGLVDDKSAF LANVVKPQLQ DASWTVSNVL PTRFLQELTV RATISKPRFA
VRYELIFFDG PVDLRRLRQS CQRLVAHNEI LRTVYVESAD RIYAAVLDAL ETPFEEFAYT
NPAVDLSTFT KDICRADVDK PQPLGSSFVK WLYVADPQRP AARSCLVFRM SHAQYDEMCL
PIMLRQLSAL YAHDKTPEPS VPFSAYVSHV MRTAVPASLP YWRELLAGST ITSFRPDIPI
TDRRHAAIAQ TVDISARTRD VTLASLPTAT WALCLARRRA LRDVVFGEVV SGRNVGLPGA
ESIAGPCWQY VPLRVRFDPS WTGNDLLAFV QQQHVESAGH EAVSLREIAE NCGLGWEKQA
SMPGDDRPAQ WWFDTVCHQD VSHVKERENT DEEAQTKYET LYTDEEPLRE WKVQTYVRDG
GNSVVLEVVT FKSWEEHGKG LLADLVKAME QLVHRPGEKL FSD
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