A0A0L0S1A9 · A0A0L0S1A9_ALLM3

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 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.

110261002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site676Zn2+ (UniProtKB | ChEBI)
Binding site680Zn2+ (UniProtKB | ChEBI)
Binding site795Zn2+ (UniProtKB | ChEBI)
Binding site799Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processmitochondrial alanyl-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
      ALA1
    • ORF names
      AMAG_02011

Organism names

Accessions

  • Primary accession
    A0A0L0S1A9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-48Disordered
Domain79-838Alanyl-transfer RNA synthetases family profile

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. Alax-L subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,026
  • Mass (Da)
    110,538
  • Last updated
    2015-11-11 v1
  • Checksum
    FCA1E67C8494D87E
MPPKSKKSPQKQAPAAAAPKAAAAPAPTKAAPAAAAPAPKAAAPAPAPVAKAAPAAAPKAAVVAAPKEATPAPAAAPAWSAPLVRETFIKFFQDKHQHAFVPSSKTIPHDDPTLLFANAGMNQFKPVFLGTVDPSAPMAKLTRAANSQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGNYFKKEAIEWAWDLLTNIFKLDKQRLYVTYFGGDAKQGLAADLEARDLWIKIGVPADRVIPYGAKENFWEMGDQGPCGPCSEIHYDLIGGRFVPALVNADDPTLIEIWNLVFMQFNREADGSLRPLPAKHVDTGMGFERLVCALQAKMSNYDTDVFTPIFSRIQEVAKVRPYEGKLGAADADGIDMAYRVVADHIRTLTVAISDGGMPSNEGRGYVLRRILRRGVRYARNAFKVPVGTFFSSLVDTVAEHMGAFFPELREHVETVKSVLDEEEAAFAKTLDRGLKLFDGILAKAGNAKTISGADAWRLYDTFGFPVDLTRLMAEEKGMTVDEAAFEAEQAKAKEQSKKRKDQAGDKAIKMDVHAIKEAETLGFPPTDDSYKYTAATLEANIAAIFHPHQEKKGASSHWVKSVSEGETVGILLNRTNFYAESGGQEYDTGSLVVDGEAEFVVENVQVYGGYVLHVGTLKYGTLTVDQEVVAAYDELRRWPLRNNHTATHVLNYALRKVLGDGIDQKGSLVSAGKLRFDFSYRSAVTADQLRAIEKECSAVIAKALTVFAKDIPLAQAKSIHSLRAVFGEVYPDPVRVVSIGVAVEELLKNPNNAAWMDLSIELCGGTHAPTTKELAAFVVMEESAIAKGVRRIVAVTGHEAAEAAKEGKAVLAEIAQLKSLSGHALGEAVKNATKDLEARTMSALDKAAARDLLASLKKQFDDWDKAQKAAKAAAATDEVKAYFADENAKPFLVRSLDVGGNGKALTSAINAVKSLPGKAALLLAVDGDKVMYHVYVDKTLHGKITALQWADIVAQKVGGKKGGRDESAQGAGTNVNAVDEAVKLATEFAAMKLK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG745330
EMBL· GenBank· DDBJ
KNE56176.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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