A0A076JG35 · A0A076JG35_BIFAD

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).

Catalytic activity

Features

Showing features for site, binding site.

159950100150200250300350400450500550
TypeIDPosition(s)Description
Site35Important for tRNA non-discrimination
Site81Important for tRNA non-discrimination
Binding site180L-aspartate (UniProtKB | ChEBI)
Binding site226L-aspartate (UniProtKB | ChEBI)
Binding site226-228ATP (UniProtKB | ChEBI)
Binding site235ATP (UniProtKB | ChEBI)
Binding site457L-aspartate (UniProtKB | ChEBI)
Binding site491ATP (UniProtKB | ChEBI)
Binding site498L-aspartate (UniProtKB | ChEBI)
Binding site543-546ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
      AD0028_0611
      , AL0462_0567
      , AL0467_0632
      , B0070_0636
      , B0487_0639
      , B0703_03130
      , BBK15_07995
      , BIFAD42_03600
      , C8077_03130
      , ERS852382_01238
      , GA542_03215
      , GA629_01405
      , GA752_01895
      , NE692_00075
      , QEP23_03530

Organism names

  • Taxonomic identifier
  • Strains
    • 2789STDY5608824
    • 487B
    • 703B
    • 70B
    • AD2-8
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A076JG35

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain147-564Aminoacyl-transfer RNA synthetases class-II family profile
Region204-207Aspartate
Region566-599Disordered

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
    599
  • Mass (Da)
    66,945
  • Last updated
    2014-10-29 v1
  • Checksum
    3D858AE4CECF1F6E
MSQTAYRTHHATEVTEQLVGQKVTLAGWVDRRRDHGGVAFIDLRDNTGLVQVVIYDEEMARPLRSEFVIQVVGEVRLRPDGNENEHLATGKIEVVAESIEVLAKSDALPFQVSTALENESENKLPGEDVRLKYRYLDLRRPSMQRNLKLRAQMSKAARHALEEMGFEEIETPTMIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMAFVDQEDVMAMAEKVIAAIWKSAGYDIKLPIQRITWQDAMDKYGSDKPDLRFGNPLIELTDYFKNTPFRVFQAPYVGAVLFKGGAATPRRQFDAWQDWAKQRGAKGLAYVVFAENGELKGPVAKNLSEEERNGLKEAVGAEDGDAVFFAAGRRTSSQELLGAVRVELARRAGLLKPDDFAFTWVVDFPLFKPTDDPDDDDVAVGHSKWTSMHHPFTMPSKDWIDKFDKDPEHAMSDSYDIVCNGNEMGGGSVRIHRDDIQDRVLDVLGITPEEAADKFGFLLEAFKYGAPPHAGIALGWDRTAAILAGADSIRDVIAFPKAGGGRDPLTGAPAPISAEQRAETGVDYDPDEDED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP028341
EMBL· GenBank· DDBJ
AVT45009.1
EMBL· GenBank· DDBJ
Genomic DNA
CYYI01000004
EMBL· GenBank· DDBJ
CUN74947.1
EMBL· GenBank· DDBJ
Genomic DNA
BPPZ01000001
EMBL· GenBank· DDBJ
GJD13376.1
EMBL· GenBank· DDBJ
Genomic DNA
WDLT01000001
EMBL· GenBank· DDBJ
KAB5748255.1
EMBL· GenBank· DDBJ
Genomic DNA
WDIP01000001
EMBL· GenBank· DDBJ
KAB5887255.1
EMBL· GenBank· DDBJ
Genomic DNA
WDFR01000001
EMBL· GenBank· DDBJ
KAB6032192.1
EMBL· GenBank· DDBJ
Genomic DNA
JANFYM010000001
EMBL· GenBank· DDBJ
MCQ4791875.1
EMBL· GenBank· DDBJ
Genomic DNA
MAXD01000007
EMBL· GenBank· DDBJ
OFA34268.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKD01000001
EMBL· GenBank· DDBJ
OSG87721.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKC01000003
EMBL· GenBank· DDBJ
OSG88994.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKF01000002
EMBL· GenBank· DDBJ
OSG95370.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKH01000003
EMBL· GenBank· DDBJ
OSG98021.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKI01000001
EMBL· GenBank· DDBJ
OSH01573.1
EMBL· GenBank· DDBJ
Genomic DNA
CP123050
EMBL· GenBank· DDBJ
WGJ18151.1
EMBL· GenBank· DDBJ
Genomic DNA
CP133648
EMBL· GenBank· DDBJ
WNE85930.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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