A0A011N5N4 · A0A011N5N4_9PROT

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site.

1940100200300400500600700800900
TypeIDPosition(s)Description
Binding site545ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      AW10_03385

Organism names

Accessions

  • Primary accession
    A0A011N5N4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain16-619Aminoacyl-tRNA synthetase class Ia
Motif47-57'HIGH' region
Motif542-546'KMSKS' region
Domain669-819Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding
Domain874-938Valyl-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
    940
  • Mass (Da)
    106,332
  • Last updated
    2014-06-11 v1
  • Checksum
    5CA87BADE4AD8F5F
MELAKSFEPADIERRWYPEWEARGYFGAGLDTDKKPEDAFCILLPPPNVTGTLHMGHGFNQAIMDALTRYHRMRGDNTLWQPGTDHAGIATQIVVERQLDAQGVSRHDLGREKFLEKVWQWKEFSGNTITQQMRRLGTSPDWSRERFTMDAGLSTTVTETFVRLYKEGLIYRGKRLVNWDPVLQTAVSDLEVAQEEEQGHLWHIRYPLSDGSATLTVATTRPETMLGDTALMVHPEDERYRHLLGKTVKLPLCEREIPIIADAYVDLAFGTGCVKVTPAHDFNDYAVGQRHKLPMIPILTLDARINENAPACYQGMDRFTARQQIVADLEKQGFLDKVEAHTLKVPRGDRTGVVIEPMLTDQWFVAMSKAGADGSSIAGKALKCVASGEIKFFPENWVNTYNQWLNNIQDWCISRQLWWGHQIPAWYGDDGRIFVAHDEAEARAQAEEQGYSGPLARDPDVLDTWYSSALWPFSTLDWTPRWPAETNTALDLYLPSTVLVTGFDIIFFWVARMVMMTRHITGKIPFKHVYVHGLIRDAEGQKMSKSKGNVLDPIDLIDGIDLDALIGKRTSGLMNPKQAAQIEKRTRKEFPEGIQAFGTDALRFTFLSLASPGRDIKFDLSRCEGYRNFCNKLWNATRYVLMHTAEHDLGLPSCTPESCSTALSFSFADRWIVSKLQRTEAEVAQHFADYRFDLLARSVYEFVWDEFCDWYVELSKVQLQQGSEQEVRATRRTLARVLETVLRLAHPLLPFITEELWQALAPIAGRKTHDSLMLAAYPQAQPEKIDLASEANVQQLKDLAYACRNLRGEMNLSPAQKVPLLATGDSTALAAFAPYLKPLCKLSEMQIVDDLPADASAPTAIVGQTRLMLEVEIDVAVEGERLDKEIARLGGEIGKARAKLANENFVARAPAAVVEQEKKRLDDYLATLEKLTPQRERLRR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JEMX01000087
EMBL· GenBank· DDBJ
EXI77898.1
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