LOCUS       BAM57766.1               921 aa    PRT              BCT 07-OCT-2016
DEFINITION  Bacillus subtilis BEST7003 isoleucyl-tRNA synthetase protein.
ACCESSION   AP012496-1565
PROTEIN_ID  BAM57766.1
SOURCE      Bacillus subtilis BEST7003
  ORGANISM  Bacillus subtilis BEST7003
            Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
REFERENCE   1  (bases 1 to 4043042)
  AUTHORS   Watanabe,S., Shiwa,Y., Itaya,M. and Yoshikawa,H.
  TITLE     Direct Submission
  JOURNAL   Submitted (02-AUG-2012) to the DDBJ/EMBL/GenBank databases.
            Contact:Hirofumi Yoshikawa
            Tokyo University of Agriculture, Department of Bioscience; 1-1-1
            Sakuragaoka, Setagaya-ku, Tokyo 156-8502, Japan
            URL    :http://nodai.cc-town.net/laboratory/single.php?id=23
REFERENCE   2
  AUTHORS   Watanabe,S., Shiwa,Y., Itaya,M. and Yoshikawa,H.
  TITLE     Complete Sequence of the First Chimera Genome Constructed by
            Cloning the Whole Genome of Synechocystis Strain PCC6803 into the
            Bacillus subtilis 168 Genome
  JOURNAL   J. Bacteriol. 194, 7007 (2012)
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Velevt v. 1.1.02
            Genome Coverage       :: 60x
            Sequencing Technology :: llumina Solexa
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /db_xref="taxon:1204342"
                     /mol_type="genomic DNA"
                     /organism="Bacillus subtilis BEST7003"
                     /strain="BEST7003"
     protein         /gene="ileS"
                     /locus_tag="BEST7003_1565"
                     /note="IleRS; catalyzes the formation
                     ofisoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile);
                     sinceisoleucine and other amino acids such as valine
                     aresimilar, there are additional editing function in
                     thisenzyme; one is involved in hydrolysis of
                     activatedvaline-AMP and the other is involved in
                     deacylation ofmischarged Val-tRNA(Ile); there are two
                     active sites, onefor aminoacylation and one for editing;
                     class-Iaminoacyl-tRNA synthetase; some organisms carry
                     twodifferent copies of this enzyme"
                     /transl_table=11
BEGIN
        1 MDFKDTLLMP KTDFPMRGNL PNREPDIQKK WEEEDIYRLV QERTKDRPKF VLHDGPPYAN
       61 GDIHMGHALN KILKDFIVRY KSMSGYNAPY VPGWDTHGLP IETALTKNKK VNRKEMSVAE
      121 FRKLCEEYAW KQIEGQREQF KRLGVRGDWE NPYVTLKPEY EAQQIRVFGE MAKRGYIYKG
      181 LKPVNWSPSS ESALAEAEIE YQDKRSASIY VAFGVKDGKG VLENGERIII WTTTPWTIPA
      241 NLGISVHPDL EYSVIAVGED RFVVASALVE NVASACGFDQ YEVTRTVKGK DLENIIAEHP
      301 LYGRDSLVML GEHVTTDAGT GCVHTAPGHG EDDFIIGQKY GLDVLCPVDE KGVMTSEAPG
      361 FEGMFYDDAN KAITQQLDEK GALVKLEFIT HSYPHDWRTK KPTIFRATAQ WFASIKDFRS
      421 DLLDAIKETK WVPEWGEQRL HNMVRDRGDW CISRQRAWGV PIPVFYAENG EPVITDETIE
      481 HVSELFRQHG SNIWFEKEAK DLLPEGFTHP GSPNGTFTKE QDIMDVWFDS GSSHQAVLEE
      541 RDDLVRPADL YLEGSDQYRG WFNSSLSTAV AVTGKAPYKG VLSHGFALDG EGRKMSKSIG
      601 NVVVPAKVMK QLGADILRLW VSSVDYQADV RVSDAILKQV AEVYRKIRNT FRFLHGNLFD
      661 FDPKTNAVAV EDLREVDQYM LIKLNKLIDK VKKAYDEYEF AVVYHSIHNF CTIELSSFYL
      721 DFAKDIVYIE HADHPDRRSM QTVFYETLLA LVKLSAPILP HTADELWSHL TFVEEQSVQL
      781 TDMPETITVP NSEATEEKFD RFMALRDDVL KALETARNEK IIGKSLEANL KLYPNKENKE
      841 LLASIKENLS QLFIVSELTI SEENEAPNDA QSFATGKIAV EKAEGEMCER SRVISKDVGA
      901 NPKYPTLSLR NAEIVEKYYQ K
//