A0A0L7KH58 · A0A0L7KH58_PLAFX

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.

113931002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Binding site995Zn2+ (UniProtKB | ChEBI)
Binding site999Zn2+ (UniProtKB | ChEBI)
Binding site1158Zn2+ (UniProtKB | ChEBI)
Binding site1162Zn2+ (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
      PFHG_04153

Organism names

  • Taxonomic identifier
  • Strain
    • HB3
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)

Accessions

  • Primary accession
    A0A0L7KH58

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region87-114Disordered
Compositional bias92-114Polar residues
Domain374-1201Alanyl-transfer RNA synthetases family profile
Region1015-1043Disordered

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
    1,393
  • Mass (Da)
    163,415
  • Last updated
    2015-11-11 v1
  • Checksum
    A223CE7BB9B6C4C9
MIVYSFSFLIFLYFCLYLNIKESIILGNCKIILSRPFKEEKKKKDIYFFFNSGKNLLKRKKSTFDLLPLHSNKRRRINLFINNDKKKKIKSNSNNNNSNNNSNNNNSNNNNNNSSSIKRECGEPFFSFYSYENILTVHNNKILKDQNNNYVLLHLCKKIKKKYKKEKNKKREYCNHYKFMYLNSIKRKDIFIKLNKINNKSHFYKDIHKSNKCIKTFIYSSSHNFHNSNYSSLNAFSFKSLFTKNTYNRSFLNFLKYTTKNNLKEKKNIKDFFSFSIKLGKDKNINLDNLKKGYYKDINTNNRSNHNKHNNNKYNYNNNNCSSNHFCSNHFCINMDMNDKLNNRNNWSNTNNPKDDNIKNTNCSTNDEGQKKYMSAEEVRNNFINYFHKKNHTIIESSSVVPYNDNTLLFTNAGMNQFKKIFLGNADKNSDLGKLKRAVDTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGNWSFGDYFKEESISFAWDLLTNVYKINPDRLYVTYFGGDENLSTCPADHETKKIWMKYISEDRILPFGLKENFWEMAETGPCGPCSEIHYDRIGNRDASSLVNKDDPSVLEIWNIVFMQYNKDENKNMNKLPFPCIDTGMGLERITSILQNVDSNYDTDLFQPIFKQIKELFPYLPNYEGKINEQDVDKIDTAYRVISDHIRCVTVAISDGCLPSNEGRNYVIRRIIRRAIRFGKQVFNIKSNVLWFYKLVDSVCFILGNTFKDLQNPDKINFIKNTIKQEEMVFNKTLEKGVEQFHKIIKKNTKNNIFSGKDAFDLYTSFGFPIDLIQIMCEEKSFNLDLQEFNDLFKKHQLVSDTNNFKINKFFDIPVEKSHELKNVHNINPTVDHFKYEWNNNCANDGDNKDIKFETYVQVIYDGNNFLDNFTLPSNNDEQVLEKEKSIEENKKKYALILKETNFYYENGGQIYDTGIIQNDNMKFQVLNVQKINEYVLHIGVFLKGYVSKNDKVQTIVDFDRRKLVACNHTATHMLNFMLRKVLTEKYTNSGKSSKTHEGNNEKHEMSENDINSNNNYDNNKEEKGFSIFTCEQKGSLVDDEKLRFDFSFIENINIDAITKIENEINKLIKEELNVTVKTMDLDESKKIKGIRAIFEEDYADKVNVVFINKDVNNILNNMNIDYTYLHSIELCGGTHIGNTKLIRKFLVTSEESIGKGIYRITAVTNKKADEIEKTFNDLYDKYKHVLQEPNENKLADVQNYKRTLKENKFLPYIKKYHILQELEQIEKTIVEKTKNMQKELFNKATNIGKDYAVQDKNNILLDIKFFDEIKGNQKVLEKIVQSYSKNNKNLSYFFIICDENNTYCVLEVKEALKNKNVQADLFMKEIMKSVLGHSGGSKNKAFGSVEKDKGMVIKEHAEEMLKNINK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias92-114Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH672068
EMBL· GenBank· DDBJ
KOB62431.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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