LOCUS       BAQ46552.1               519 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum methionine--tRNA ligase protein.
ACCESSION   AP014704-3172
PROTEIN_ID  BAQ46552.1
SOURCE      Methylobacterium aquaticum
  ORGANISM  Methylobacterium aquaticum
            Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
            Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (bases 1 to 5348274)
  AUTHORS   Tani,A. and Ogura,Y.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-JAN-2015) to the DDBJ/EMBL/GenBank databases.
            Contact:Akio Tani
            Okayama University, Institute of Plant Science and Resources; Chuo
            2-20-1, Kurashiki, Okayama 710-0046, Japan
REFERENCE   2
  AUTHORS   Tani,A., Ogura,Y., Hayashi,T. and Kimbara,K.
  TITLE     Complete Genome Sequence of Methylobacterium aquaticum Strain 22A,
            Isolated from Racomitrium japonicum Moss
  JOURNAL   Genome Announc 3, e00266-15 (2015)
  REMARK    Publication Status: Online-Only
            DOI:10.1128/genomeA.00266-15
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.7
            Genome Coverage       :: 47x
            Sequencing Technology :: 454 GS FLX; ABI 3730; Illumina PE
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /culture_collection="NBRC:FERM BP-11078"
                     /db_xref="taxon:270351"
                     /mol_type="genomic DNA"
                     /organism="Methylobacterium aquaticum"
                     /strain="MA-22A"
     protein         /EC_number="6.1.1.10"
                     /gene="metG"
                     /inference="similar to AA sequence:RefSeq:WP_018263310.1"
                     /locus_tag="Maq22A_c17165"
                     /note="324c0009"
                     /note="methionine--tRNA ligase; MetRS; adds methionine to
                     tRNA(Met) with cleavage of ATP to AMP and diphosphate;
                     some MetRS enzymes form dimers depending on a C-terminal
                     domain that is also found in other proteins such as
                     Trbp111 in Aquifex aeolicus and the cold-shock protein
                     CsaA from Bacillus subtilis while others do not; four
                     subfamilies exist based on sequence motifs and zinc
                     content; Derived by automated computational analysis using
                     gene prediction method: Protein Homology."
                     /transl_table=11
BEGIN
        1 MAGEPFFITT AISYPNGVPH IGHAYEVIAA DAIARFKRLD GYDVFFTTGT DEHGLKIQQT
       61 AAKAGIGPRA FVDDMAPRFR TMAEQLDCSF DRFIRTTDAD HVAAAQALWR RMEENGDIYL
      121 AKYAGWYSVR DEAYYDEAEL VTAPDGSRRA EKTGTPVEWV EEESYFFRLS AYGERLLALY
      181 EANPDFIGPD SRRNEVTSFV RSGLQDLSVS RTTFDWGVPV PGNPAHVMYV WVDALTNYIT
      241 SCGFPDEGAP RWRQWPAALH VIGKDIIRFH AVYWPAFLMS AGLPVPQRVF GHGFLLNKGE
      301 KMSKSLGNVV APTALAEAYG VDPLRYFMLR EVPFGQDGSY SHEAIVNRLN ADLANDLGNL
      361 AQRSLTMIAR NCGGQIPAPF PQAGEPSAAD RALLALADAL PEKARGLMRD LALHAVLAEI
      421 WAVVAEANRY FAGQEPWALR KTDPARMEAV LYTTAEVLRA VGILVQPFIP SAAARLLDLL
      481 AVAPDARNLA AIGPDHRLAP GTALPAPSPI FPRYVEPEA
//