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valine--tRNA ligase [Listeria monocytogenes].


LOCUS       WP_010989740             883 aa            linear   BCT 28-NOV-2019
ACCESSION   WP_010989740
VERSION     WP_010989740.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 883)
  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 883)
  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 883)
  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 883)
  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 883)
  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 883)
  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 883)
  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..883
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..883
                     /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=101962
     Region          9..881
                     /region_name="ValS"
                     /note="Valyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0525"
                     /db_xref="CDD:440291"
ORIGIN      
        1 mttehneinm ptkyepsnve agkykwwlek effkaegntd kepysivipp pnvtgklhlg
       61 hawdttlqdi itrmkrmqgf dtlylpgmdh agiatqakve aklkesnisr ydlgrenfvd
      121 ktwewkeeya efireqwekl glgldysrer ftlddglsda vkkvfvtlyn kgliyrgqyi
      181 inwdpeakta lsdievihkd iegsfyhlky pltdgsgyle vattrpetip gdtavavhpk
      241 deryqhligk timlpilnre ipivadeyve refgsgavki tpahdpndfe vgnrhnlpri
      301 ivmhedgtmn enagkydgld rfvarkeiiq dfkdlglfik qephlhsvgh sertgavvep
      361 ylslqwfvkm eplaaealel qktenkvnfv parfektyet wmdnihdwci srqlwwghri
      421 pawyhketge iyvgekepen lseweqdedv ldtwfssalw pfstmgwpdt espdfqhffp
      481 tntlvtgydi iffwvsrmif qsveftgerp fkdtlihglv rdsegrkmsk slgngvdpie
      541 vidkygadsl rytlatgssp gqdlkfsyek vestwnfink iwnasrfvlm nldgmkynei
      601 dlsnvtevsd kwiltrlnet iqavtslgek yefgevgrtl ynfiwddfcd wyieiakipl
      661 ygedevakqt trsvlaytln atmrllhpfm pfvteeiwqn lphegesiti aewpkvneqq
      721 idtksstama tlveviravr nirsevntpl skpivleikp kdttykeile qnisyierfc
      781 npeqvtisfd veasktamta vvsgaeifip lealidlnve iarlekelek wnkevarvqg
      841 klnnerfisk apesvvaeer lkekdyldkk asvlerietl kev