LOCUS       WP_268779184             882 aa            linear   BCT 13-DEC-2022
DEFINITION  valine--tRNA ligase [Natronobacillus azotifigens].
ACCESSION   WP_268779184
VERSION     WP_268779184.1
KEYWORDS    RefSeq.
SOURCE      Natronobacillus azotifigens
  ORGANISM  Natronobacillus azotifigens
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Natronobacillus.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Fukunaga,R. and Yokoyama,S.
  TITLE     Structural basis for non-cognate amino acid discrimination by the
            valyl-tRNA synthetase editing domain
  JOURNAL   J Biol Chem 280 (33), 29937-29945 (2005)
   PUBMED   15970591
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Tardif,K.D. and Horowitz,J.
  TITLE     Functional group recognition at the aminoacylation and editing
            sites of E. coli valyl-tRNA synthetase
  JOURNAL   RNA 10 (3), 493-503 (2004)
   PUBMED   14970394
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Fukai,S., Nureki,O., Sekine,S., Shimada,A., Vassylyev,D.G. and
            Yokoyama,S.
  TITLE     Mechanism of molecular interactions for tRNA(Val) recognition by
            valyl-tRNA synthetase
  JOURNAL   RNA 9 (1), 100-111 (2003)
   PUBMED   12554880
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Hountondji,C., Lazennec,C., Beauvallet,C., Dessen,P.,
            Pernollet,J.C., Plateau,P. and Blanquet,S.
  TITLE     Crucial role of conserved lysine 277 in the fidelity of tRNA
            aminoacylation by Escherichia coli valyl-tRNA synthetase
  JOURNAL   Biochemistry 41 (50), 14856-14865 (2002)
   PUBMED   12475234
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Fukai,S., Nureki,O., Sekine,S., Shimada,A., Tao,J., Vassylyev,D.G.
            and Yokoyama,S.
  TITLE     Structural basis for double-sieve discrimination of L-valine from
            L-isoleucine and L-threonine by the complex of tRNA(Val) and
            valyl-tRNA synthetase
  JOURNAL   Cell 103 (5), 793-803 (2000)
   PUBMED   11114335
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Heck,J.D. and Hatfield,G.W.
  TITLE     Valyl-tRNA synthetase gene of Escherichia coli K12. Primary
            structure and homology within a family of aminoacyl-TRNA
            synthetases
  JOURNAL   J Biol Chem 263 (2), 868-877 (1988)
   PUBMED   3275660
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Hartlein,M., Frank,R. and Madern,D.
  TITLE     Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene
            valS
  JOURNAL   Nucleic Acids Res 15 (21), 9081-9082 (1987)
   PUBMED   3317277
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF004349.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05729
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Natronobacillus azotifigens"
                     /db_xref="taxon:472978"
     Protein         1..882
                     /product="valine--tRNA ligase"
                     /EC_number="6.1.1.9"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0004812 - aminoacyl-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0004832 - valine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006438 - valyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=102080
     Region          7..881
                     /region_name="ValS"
                     /note="Valyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0525"
                     /db_xref="CDD:440291"
ORIGIN      
        1 mtengqnlpp kydstaveag ryqywvegkf featreetkq pytvvipppn vtgklhigha
       61 wdttlqdiia rmkrmqgydv lylpgmdhag iatqakveak lreegvsryd lgrekfleka
      121 wdwkesyasf ireqwakmgl gldysrerft ldeglseavk evfvklyeeg liyrgeyiin
      181 wdpatktals dieviheevt ghfyhmrypl kdeegyieia ttrpetmlgd tavavhpkde
      241 ryqhligkkv vlpivgreie ivaddyvdme fgsgavkitp ahdpndfeig nrhnlervlv
      301 mnedgtmnek agkykgldrf acrkqlvkdl qeegilfkie ehihsvghse rsgavvepyl
      361 stqwfvhmqp ladaavelqq knssekvnfv perfegtylr wmenirdwci srqlwwghri
      421 pawyhketge iyvgkeapad senweqdtdv ldtwfssalw pfstmnwpdt edpdfqsyfp
      481 tstlvtgydi iffwvarmif qskkftderp fkdvlihglv rdadgrkmsk slgngvdpmd
      541 viekygadsl ryflatgstp gqdlrfqwek vestwnfink iwnasrfvlm nvegmkynei
      601 dltteknvad kwiltrlnet itqvnkqter ydfgeagryl ynfiwddfcd wyiemaklpl
      661 ygedeqakqt trsvlvhvld qimrmlhpfm pfvteeiwqy lphegesitq aawpevndal
      721 ndpqsaaemq rlvgiirsvr niraevdtpm skqivlaika ndptieqqlk dnrhyldrfc
      781 ntseltiaid vkapekamsa vvtgaelylp laglidaeke iarlqaelek lnkevervqk
      841 klanegftkk apekvveeer qkeadylekr akvaarieel qq
//