A0A2Z6ESF2 · A0A2Z6ESF2_9BURK

Function

function

Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.

Catalytic activity

Features

Showing features for binding site.

1952100200300400500600700800900
TypeIDPosition(s)Description
Binding site554ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functionvaline-tRNA ligase activity
Biological Processvalyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Valine--tRNA ligase
  • EC number
  • Alternative names
    • Valyl-tRNA synthetase
      (ValRS
      )

Gene names

    • Name
      valS
    • ORF names
      MCB1EB_0163

Organism names

  • Taxonomic identifier
  • Strain
    • B1-EB
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Mycoavidus

Accessions

  • Primary accession
    A0A2Z6ESF2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain30-627Aminoacyl-tRNA synthetase class Ia
Motif55-65'HIGH' region
Motif551-555'KMSKS' region
Domain671-826Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding
Domain886-951Valyl-tRNA synthetase tRNA-binding arm

Domain

The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    952
  • Mass (Da)
    107,294
  • Last updated
    2018-10-10 v1
  • Checksum
    B7CA3F20C1AC6DAB
MLENIVMNKIDTTLSKSFEPHAIEAHWRPQWEQKGYAKPTFSPGCEDFSILLPPPNVTGTLHMGHAFNQTIMDSLTRYHRMQGANTLWVPGTDHAGIATQLVVERQLKQHNLSRHELGRQAFVERVWAWKETSGSIITQQIKRLGASTDWSREYFTMSPHMSQAVVEVFVRLYEQGLIYRGKRLVNWDPKLGTAVSDLEVISTEEDGSLWHIRYPLVDDSSTYLTVATTRPETMLGDAALMVHPQDERYQAFIGKMVRLPLSEREIPVIADDYVDPTFGSGVVKVTPAHDFNDYQVGQRHQLPLINIFTLDAKINENAPARWRGLEQHEARRLIVAELEVQGLLAAVKPHKLMVPRGDRTQAVIEPMLTDQWFVAVNKPAPAGSLHPGQSMAATAIEAVRQGKIKFTPENWSNTYYQWLENIQDWCISRQLWWGHQIPAWYGAEGQIYVARNEDEAREEARAQGYTGPLTRDADVLDTWFSSALVPFSAHGWPNQTKELAHFLPSSVLVTGFDIIFFWVARMVMLTQHFTGQVPFHTVYIHGLVRDANGQKMSKSKGNILDPIDLIDGIDLDALIAKRLASSQDPQQAAELEQKTRAEFPHGIPSFGTDALRFTFASLATPGRNINFALARCEGYRNFCNKLWNATRFVLMNCEDQDSSINLAHNESSLADRWILSLLQQVTDEIDKGFTELRFDLIANALYKFVWDEYCDWYLEFAKVQLQTGTPAQQQNTRYTLLYVLETVLRLAHPIIPFITEALWQKVAPLAGRYPTPAASEEASIMVQPYPRALKEKVDLAAEQWATQLKAVIDACRNLRSEMNLGPAQRVPLFASGDTQLLTTFAPYVRALARLSEVTLSADEATLDAATAGAPVALVGALKLALKVEIDIGAEHARLTKEVQRIELEISKCNAKLQNNHFVAKAPAEVVELERKRLSEYALILSKLNTQLTRLAG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018150
EMBL· GenBank· DDBJ
BBE08324.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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