A0A258TPD9 · A0A258TPD9_9PROT

Function

function

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).

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 site, binding site.

158850100150200250300350400450500550
TypeIDPosition(s)Description
Site30Important for tRNA non-discrimination
Site81Important for tRNA non-discrimination
Binding site172L-aspartate (UniProtKB | ChEBI)
Binding site218L-aspartate (UniProtKB | ChEBI)
Binding site218-220ATP (UniProtKB | ChEBI)
Binding site227ATP (UniProtKB | ChEBI)
Binding site451L-aspartate (UniProtKB | ChEBI)
Binding site485ATP (UniProtKB | ChEBI)
Binding site492L-aspartate (UniProtKB | ChEBI)
Binding site537-540ATP (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate--tRNA(Asp/Asn) ligase
  • EC number
  • Alternative names
    • Aspartyl-tRNA synthetase
      (AspRS
      )
    • Non-discriminating aspartyl-tRNA synthetase
      (ND-AspRS
      )

Gene names

    • Name
      aspS
    • ORF names
      B7Y41_11085

Organism names

Accessions

  • Primary accession
    A0A258TPD9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain139-558Aminoacyl-transfer RNA synthetases class-II family profile
Region196-199Aspartate

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    588
  • Mass (Da)
    66,441
  • Last updated
    2017-12-20 v1
  • Checksum
    5A822528C2929179
MRTHYCGAVNADHNGQIVNLCGWAHRRRDHGGVIFIDLRDREGTVQVVIDPDTPEAFKVAEETRSEFVLRVVGKVRARPAGTENPNLPTGMIEVLTQSLEVLNPSLTPPFQIDDDNINENIRLQYRYLDLRREPMQKNMRLRYRVSKLMRDYLDQQGFLEIETPMLTRSTPEGARDYLVPSRVHDGMFYALPQSPQLFKQLLMVAGYDRYFQLTKCFRDEDLRADRQPEFTQVDLETSFMGEEEIMTLVEGMIRDMFKKAQDIDLPNPFPRMTYAEAMGRYGSDKPDMRVTLEITELTEAMKDVDFKVFSGPANDPTGRVAVLRVPKGAEISRGEIDGYTEFAKIYGAKGLAWIKVNEMAKGRDGLQSPIVKNIHDAALSAILERTGAQDGDILFFGADKAKVVNDALGALRLKIGHEKGHVDGRAWAPLWVLDFPMFERNEDEGRWDALHHPFTAPKDGHEDYLSSNPGAALSKAYDMVLNGWEVGGGSVRIHRQEVQEKVFAALNIGEEERREKFGFLLDALQYGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRASCLMTSAPNVVDEKQLRELHIRLRS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NCGJ01000010
EMBL· GenBank· DDBJ
OYY93320.1
EMBL· GenBank· DDBJ
Genomic DNA

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