A0A847BPJ0 · A0A847BPJ0_9FIRM

  • Protein
    Multifunctional fusion protein
  • Gene
    aspS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
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.

TypeIDPosition(s)Description
Binding site176L-aspartate (UniProtKB | ChEBI)
Binding site222L-aspartate (UniProtKB | ChEBI)
Binding site222-224ATP (UniProtKB | ChEBI)
Binding site231ATP (UniProtKB | ChEBI)
Binding site450L-aspartate (UniProtKB | ChEBI)
Binding site484ATP (UniProtKB | ChEBI)
Binding site491L-aspartate (UniProtKB | ChEBI)
Binding site536-539ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionaspartate-tRNA ligase activity
Molecular FunctionATP binding
Molecular Functionglutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Molecular Functionnucleic acid binding
Molecular Functiontransferase activity
Biological Processaspartyl-tRNA aminoacylation
Biological Processregulation of translational fidelity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Aspartate--tRNA ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )
  • Recommended name
    Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
  • EC number
  • Short names
    Asp/Glu-ADT subunit C

Gene names

    • Name
      aspS
    • Synonyms
      gatC
    • ORF names
      GX777_06790

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AS09scLD_276
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Fastidiosipila

Accessions

  • Primary accession
    A0A847BPJ0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterotrimer of A, B and C subunits.
Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain153-557Aminoacyl-transfer RNA synthetases class-II family profile
Region200-203Aspartate

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    700
  • Mass (Da)
    79,347
  • Last updated
    2021-09-29 v1
  • Checksum
    0BF83737C0C167AF
MKRTKYCGHFSEKDVGKEACACGWVHSKRDMGGVIFIDLIDREGVLQIVFNPENTDSETFALAERVRSQSVLEVYGNLHLRDAETVNPKIATGTVELRVKKAKLLSAAETLPFVPEEAGNVRDELRLRYRYLDLRRHDLKNNLLLRHRASALIHSFMDKNGFIEVETPVLGKSTPEGARDYLVPSRVHPGSFYALPQSPQIYKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDLEMSFVEVDDVLEILEALMKYLVRELKDVEIESAFPRISWQEAMDRYGSDKPDLRFDLPIIDISDIAEKSDFSIFRQALKRGGVVRAICVPGKADFSRSVIDDLTEFAITEGAKGMAWIAWREDGEIYSILDKYFTEELMHELLERVQAKPGDFILFSADQLKTVRHVSGALRLRLADLLELRSSDQLHFSFVVDFPMFEFSEEEDRYVAQHHPFTMPKAEDLRFLENEPERMESQAYDLVLNGTELGSGSIRIHDRAIQDQIFRKLGLAEDDIQQRFGFLLDAFRYGAPPHGGFALGLDRLVMLLADAPSLREVIAFPKLSNASDPLTDAPSPVDQAQLDELQISLTEQAAAASGLFSEQKDDSAAKTFDLQHLEQLSSLRLTNSERTGMQKEIENLITFADQMAEQDTDSVEPTRSMIKDQGIFQRKEREPSLSQEAALANAAVTEDGAFVVPAAVEQEL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAZEE010000227
EMBL· GenBank· DDBJ
NLC26310.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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