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J9RKG7 · J9RKG7_9ACTN

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

Function

function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

1891100200300400500600700800
TypeIDPosition(s)Description
Binding site575Zn2+ (UniProtKB | ChEBI)
Binding site579Zn2+ (UniProtKB | ChEBI)
Binding site678Zn2+ (UniProtKB | ChEBI)
Binding site682Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alanine--tRNA ligase
  • EC number
  • Alternative names
    • Alanyl-tRNA synthetase
      (AlaRS
      )

Gene names

    • Name
      alaS
    • ORF names
      KTR9_2240

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KTR9
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Gordoniaceae > Gordonia

Accessions

  • Primary accession
    J9RKG7

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain1-721Alanyl-transfer RNA synthetases family profile
Coiled coil744-771

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    891
  • Mass (Da)
    95,476
  • Last updated
    2012-11-28 v1
  • MD5 Checksum
    5E57C2244415FFF415553E50D1B6F894
MQTHDIRKRFLDHFIKAGHTEVPSASLLLDDPNLLFVNAGMVPFKPFFLGEQTPPYSRATSVQKCVRTLDIDEVGITTRHNTFFQMAGNFSFGDYFKREAITFAWTLLTNSVEDGGYGIDPQKLWPTVYLDDDEAEAIWRDEIGVPAERIQRRGMKDNYWSMGVPGPCGPCSEIFYDRGPDYGVEGGPEADEDRYIEIWNLVFMQNVRGPGGGKDNYEILGPLPKQNIDTGMGVERVACLLQGVDNVYETDLCKPIIDLAAQLSGRAYGAGSHADDVRFRVVADHARTSAMLIGDGVLPGNDGRGYVLRRLLRRVVRSMRLLGTADNEPTMGAIIGKVIDLMSPSYPELETQRRHIVDVAVGEETSFSKTLAAGSKLFADAATATKSASRTTISGSDAFTLHDTYGFPIDLTLEMAAEAGLAVDQEGFTSLMAEQKQRAKADATARKTGHADLSVYRDFLDRGPTEFTGFDELVSEARVLGLVADGARLPAASAGQELTVVLDRTPLYAESGGQMADVGTITTGSGVRMSVTDVQKVGKSVWLHKVRIDEGEIEEGDEVLAAVDTAWRHGATQGHSGTHMVHAALREVLGPGATQAGSLNRPGYLRFDFNATGPVTEAQRREIEEISNAAVEANYQVNTFETGLSEAKAMGAMALFGENYGDVVRVVEIGGPFSMELCGGTHVASSSQIGPITLIGESSVGSGVRRVEAYVGMDSFRFLSKERALLAGLASSLKVPSEEVPGRVEQLVTKLRDAEKELERVRAEAARAAVSGLLDTATTVGATLVVEGRVPGLDANGLRSVVTDLRGRVADRQAVIALFSPSGDGPEAKVPFVIATTAAARDAGIKAGDLVKEVAPLLGGRGGGKPDLAQGAGTDPSGIDAALIRIREFVA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002907
EMBL· GenBank· DDBJ
AFR48877.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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