A0A022VVP4 · A0A022VVP4_TRIRU

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.

1851100200300400500600700800
TypeIDPosition(s)Description
Binding site498Zn2+ (UniProtKB | ChEBI)
Binding site502Zn2+ (UniProtKB | ChEBI)
Binding site617Zn2+ (UniProtKB | ChEBI)
Binding site621Zn2+ (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
      H103_06541

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 288.86
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton

Accessions

  • Primary accession
    A0A022VVP4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-660Alanyl-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
    851
  • Mass (Da)
    94,584
  • Last updated
    2014-06-11 v1
  • Checksum
    22AE2AA9012060F7
MLGNWSFGDYFKKEAIQFSWELLTKVYGLDPDRLYVTYFEGNEAAGVGPDIEARDIWRSVGVKDDHILTGDMKDNFWEMGDQGPCGPCSEIHYDRIGGRNAAHLVNQDDPDVLEIWNNVFIQYNREPDRSLRPLPNQHVDTGLGYERLVSILQNKSSNYDTDVFTPLFTAIQNITGARPYTGKFGAEDADGIDTAYRVVADHLRTLTFAITDGAAPNNEGRGYVVRRVLRRGVRYARKYLQVEIGSFFSKLVPALVEQMGDMFPEIRRKQTDVMEILDEEEVSFAKTLDRGERQFENYAQQALDSGAGKLHGADVWRLYDTFGFPVDLTRLMAEERQLTIDDAEFEEARLKAKEASKGQAKTASDLLKLTVHTLSTLEKNGVPKTDDDAKFGKGNIVANIKAICHGKEVIDSTKDIPANEQIGIILDKTNFYAEQGGQEYDTGKIVIDGQAELDVQNVQMYGGYVLHTGFIKYGNFSVNDSVIAEYDELRRWPIRNNHTGTHILNFALREVLGDGVDQKGSLVAAEKLRFDFSHKSAISDSDLEKIEAKSTDYIRQNCAVYSQEVPLATAREITGVRAVFGETYPDPVRVVSVGVELDEILKNVKDPRWEGVSIEFCGGTHVQKTGDIKDLVILEESGIAKGIRRIIAVTGEDAHEVQRIAREFGERLNRFEKMPASPERDAEIKSLQVDLNQLTISAVEKTKYRNQFTQIHKKITDAQKAAQKAEVKTAIDAISAYFEENTESPSLVIKLPITANQKAISESLNHVKTKLSGKALYVFAADASKVAHGCYVTPDLTTKGASANEWASAVSSIVGGKAGGKAPVAIGNGTEVNKVDEALDEATKYLEKFKL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KK207893
EMBL· GenBank· DDBJ
EZF50009.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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