Q72E47 · SYV_NITV2

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.

1884100200300400500600700800
TypeIDPosition(s)Description
Binding site528ATP (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
    • Ordered locus names
      DVU_0732

Organism names

Accessions

  • Primary accession
    Q72E47

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002244741-884Valine--tRNA ligase

Proteomic databases

Interaction

Subunit

Monomer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q72E47DVU_0412 Q72F062EBI-10070747, EBI-10071594

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif, coiled coil.

TypeIDPosition(s)Description
Motif47-57'HIGH' region
Motif525-529'KMSKS' region
Coiled coil812-884

Domain

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.
The C-terminal coiled-coil domain is crucial for aminoacylation activity.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    884
  • Mass (Da)
    99,823
  • Last updated
    2004-07-05 v1
  • Checksum
    EE3713482FFF4304
MAENALPKGYEPRDVEERWRRHWEDNRTFTPDMDAPGEPYSIVIPPPNVTGALHIGHALNHVLIDVLCRNARQQGKKVLWLPGTDHAGIATQNVVERALAKEGLSRHDLGREAFIERVWQWKEEYGNRILNQIRMLGDSVDWTRERFTMDEGLSKAVRKVFVDLYNGGYIYRGNYIINWCNRCHTALADDEVDHMPEQGHLYHVRYDFEDGSGSVVIATTRPETIMADTGVCVHPEDERYAGLIGKKILVPVIGRAVPLFADTYVDREFGTGALKVTPCHDPNDWTLGERHGLAFIQCIDEDGNMTAEAGPYAGLTKEECRKRIVADLEASGQLVRVEELNHSVGHCYRCKTVVEPHMSEQWFVASTKLAPRARAAVPQMTQIFPESWMKTYFNWLDNIRDWCISRQIWWGHRIPAWTCGKCGKLIVSEQDPTACPDCGCTDLTQDPDVLDTWFSSALWPFSTMGWPDKTKDLATFYPTSVLVTGFDILFFWVARMMMLGMHFMDEVPFKHVYLHALVRDGEGRKMSKSTGNVIDPLAMIDKYGTDSLRFTLAAFAAMGRDIKLSEDRIEGYRHFVNKVWNAARFSLMNLPEEAPAALDLDNVKGMHHKWILHRLEELKASQAAGIDGYRFNEVAQGLYRFWWNEFCDWYLELIKPDMQAGGERQATAQYVLWTVLREALLLLHPFMPFVTAEVWQALPGHAGDDIATKLYPAARPGCRDVKDAEHMELVQATISAVRTIRAELNIAPSYRLTTLVRPASAEDAATLEEGREMLMTLARLDGLTVAVDVEAPKASASSVVAGNEVIVPLTGAVDFEAELARLDKELGKIEKDFVQVNKKLANESFVSKAPADVVAKERARAEELSDAKAKLEALQQRFRDAIGK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017285
EMBL· GenBank· DDBJ
AAS95212.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp