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A0A556UEL2 · A0A556UEL2_9LACO

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

Function

function

Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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.

161450100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site174L-aspartate (UniProtKB | ChEBI)
Binding site220L-aspartate (UniProtKB | ChEBI)
Binding site220-222ATP (UniProtKB | ChEBI)
Binding site229ATP (UniProtKB | ChEBI)
Binding site448L-aspartate (UniProtKB | ChEBI)
Binding site482ATP (UniProtKB | ChEBI)
Binding site489L-aspartate (UniProtKB | ChEBI)
Binding site534-537ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaspartate-tRNA ligase activity
Molecular FunctionATP binding
Molecular Functionnucleic acid binding
Molecular Functiontransferase activity
Biological Processaspartyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate--tRNA ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )

Gene names

    • Name
      aspS
    • ORF names
      FOD82_04900

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LL6
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus

Accessions

  • Primary accession
    A0A556UEL2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain143-555Aminoacyl-transfer RNA synthetases class-II family profile
Region198-201Aspartate
Region590-614Disordered

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    70,021
  • Last updated
    2019-10-16 v1
  • MD5 Checksum
    A14A9748BD94FA5F88DE97FB1B72395A
MDKRTDYSGNITAKYLDQEVTLYGWVQRVRNLGNLVFIDLRDREGVVQVVVNKDSGKELMEIADSLGSEDVIEVKGKVVKRSSVNPDMKTGEVEVDANSIEVLNKSQVPPFEIKDDVEIGEQTRLKYRYLDLRRPTLQNAIILRSKILRAIHEYFDENGFINIETPILGKSSPEGARDYLVPSRIYPGSFYALPQSPQLFKQLLMAAGFDKYYQIARCFRDEDLRGDRQPEFTQIDMEASFVDEKGIQDYTEGLLKKVMKDVMGIDLKTPIRRITWDEAMNKYGSDKPDTRYEMFLHDLSPIFKDSDFKVFSGAIADGGFVKGIAVKGGAEKYSRKHIEQKQDYIKRYHAKGLAWVKFENGEFSGPVAKFLTDENKQALIKEFDLEGGELVIMVADKWKVVTDSLDHLRREFAKETGIIPKDVYDFVWVVDWPLFEYDEGWGRWIAAHHPFTMPDDKGIELLDTDPHKAHARSYDIVMNGDELGGGSIRIHKRSIQEKMFKALGFTKKRAYEQFGYLMDALDMGFPPEAGLAIGLDRFAMMLAQKDNIRDVLAFPKNASASEPMMHAPAPVADQQLADLGIEVEDQYADSVKETEARLEKEAKEDADKNSTWDE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VLLR01000001
EMBL· GenBank· DDBJ
TSO27071.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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