A0AAD9GFV1 · A0AAD9GFV1_BABDI

  • Protein
    Alanine--tRNA ligase
  • 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 tRNA(Ala) via its editing domain.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site626Zn2+ (UniProtKB | ChEBI)
Binding site630Zn2+ (UniProtKB | ChEBI)
Binding site738Zn2+ (UniProtKB | ChEBI)
Binding site742Zn2+ (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

    • ORF names
      X943_003921

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 1802A
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0AAD9GFV1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-775Alanyl-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    983
  • Mass (Da)
    108,589
  • Last updated
    2024-05-29 v1
  • Checksum
    E3306A0FF1DA3C46
MASSRSDLNATGKAMNDLGFEVNSSAWVRSEFIRYFESKGHVFWRSSPVLPHNDATLLFANAGMNQFKDIIVGKADSTTEYGRLKRVCNSQKCIRAGGKHNDLDDVGKDSYHHTFFEMLGNWSFGDYFKKEAIDFAWELLTEVYKLDKSRLYVTYYGGDPKLPACKPDDEAHELWLRYLPPERVLPFGMKDNFWEMADTGPCGPCSEIHYDHIGGRDAAALVNADDPMVVELWNLVFMQYNRKASGDVELLPKPCVDTGMGLERVAAVLKNSNSNYECDLFTDIFAYINKLMPQLPPYGGSDSIVDIAYRVVADHTRCLTVAIADGVEPSNDGRGYVLRRILRRAVRYGKEHLGSTGPFLSKLVDCVVASLGAAFPEIQNQNDKIAATIHNEELLFLETLDKGCDRFRKMVAKLQSTSQGGNPPVVSGSDAFLLYSSFGFPLDLTQLMAREMGLDVDIEGFNEHFKRHQLLSEKKQVKSDDPVEQGLHDVVESLSADVLATISAAIGNKSTDDSLKYHGIDVAYACDTEFDVEVLAVWSSDGLNKSPKDGEVVAVVLDKTPFYAEQGGQIWDEGLLGPLKVLKILKMGGMVFHFCVYESGRNCIKPGSTVKAKVDYERRVKVACNHTGTHLLNFVLREIYDEQSYQRGSQLDAEKLKFDIAANKPLTDDVLQKIESRIQTIIDEDWKLEVKEVPFKDAIKIPGIRANFTDVYPEFVRVVCITKNGQAVDGHANSIEVCGGTHVPSTGVLKSVIMVGEEGISKGIRRLTLATNEQSENSKAILASYENSLSELEGKLFKFTDDMDTALMAQQANENMRLLTALRFQMQNEKLLPLLGKRNLKARFDALINAQIDAGKVHQKKLGAIAKNLSTDYVNKFKSGDFCGLKTSREGVDLIHMEANALEGDAKSLNVLTQTIAKAFPKLALLLTSSNKDGSAVSCRCVVPAGSALDALSLANEAAANLGHQSDVARGSRTNASWSVDSQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHBMH010000033
EMBL· GenBank· DDBJ
KAK1937692.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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