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A0A327QNI3 · A0A327QNI3_9FLAO

  • Protein
    Valine--tRNA ligase
  • Gene
    valS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

1876100200300400500600700800
TypeIDPosition(s)Description
Binding site538ATP (UniProtKB | ChEBI)

GO annotations

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
      LV92_04065

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 23522
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Arenibacter

Accessions

  • Primary accession
    A0A327QNI3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain15-573Aminoacyl-tRNA synthetase class Ia
Motif43-53'HIGH' region
Motif535-539'KMSKS' region
Domain615-757Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding
Domain811-876Valyl-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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    876
  • Mass (Da)
    100,623
  • Last updated
    2018-10-10 v1
  • MD5 Checksum
    7C9435EE4145F83DD6EE7CB708803182
MEIPSKYEPQRVEGQWYDYWTKHNYFHSTPDNREPYTIVIPPPNVTGVLHMGHMLNNTIQDVLIRRARLMGKNACWVPGTDHASIATEAKVVAKLKEQGIDKKDITREEFLKHAWDWTHEYGGVILEQLKKLGCSCDWERTKFTMDDNMSASVIKVFVDLYNKGLIYRGYRMVNWDPEAKTTLSDEEVIYEERQGLLYYLAYKIEGSDETVTIATTRPETILGDTAICINPNDDRYAHLRGKQAIVPICNRVIPIIEDEYVDVEFGTGCLKVTPAHDINDKALGEKHNLETIDIFNEDASLNSFGLHYEGKDRFEVRKAISKELEEKGYLVKTEQHINKIGTSERTKAVIEPRLSDQWFLSMEDLAKPAIKAVLEDEDIKLFPKKFENTYRHWMENIRDWNISRQLWWGQQIPAFYFGDGQDDFVVAETKEVALDMAKKKSGKSHLTLEDLKQDADALDTWFSSWIWPISVFNGILEPNNKEIEYYYPTNDLVTGPDILFFWVARMIISGYEYRNERPFENVYLTGLVRDKQRRKMSKSLGNSPDALQLIEDYGADGVRVGLLLSSAAGNDLMFDEALCQQGKNFANKIWNGFRLVKGWEVADLPQPEASKLGVEWYTSKFNKTLEEIEDHFSKYRISDALMAIYKLVWDDYSSWLLEIIKPAYQQPIDKTTFDAVIQIFEENLKLLHPFMPFLTEEVWQHIAERTPEQALVIAKWPSAQPVNEELIEGFSFAADVIAGIRTIRKEKNIPIKDALQLAVLNDGDISKDWDVVIAKLTNVSAIDYVDSAVDGALTFRVKSNEYFVPMVGAIDIGAEIKKLEEELEYIKGFLISVRKKLSNERFVANAPAQVIDLERQKEADAIAKIDTLEKSLASLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QLLN01000010
EMBL· GenBank· DDBJ
RAJ06139.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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