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A0A8A3P398 · A0A8A3P398_9HELO

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.

1960100200300400500600700800900
TypeIDPosition(s)Description
Binding site602Zn2+ (UniProtKB | ChEBI)
Binding site606Zn2+ (UniProtKB | ChEBI)
Binding site721Zn2+ (UniProtKB | ChEBI)
Binding site725Zn2+ (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
      DSL72_003814

Organism names

  • Taxonomic identifier
  • Strain
    • RL-1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Monilinia

Accessions

  • Primary accession
    A0A8A3P398

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain10-764Alanyl-transfer RNA synthetases family profile
Coiled coil805-832

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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    960
  • Mass (Da)
    106,880
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    332059E427FB6EFC0594EE10A95B2BBB
MASSPDTSKWTAPVVRKEFLSFFEKNAHSVVPSSSVVPHNDPTLLFTNAGMNQFKPIFLGTVSKADDMAQLKRAVDTQKCIRAGGKHNDLDDVGKDSYHHTFFEMLGNWSFGDYFKKDAIGMAWELLTKVYGLDPDRLYVTYFEGDSKNGVAADTEAKELWLKAGVKEDHILTGNMKDNFWEMGETGPCGPCSEIHYDRIGGRNAARLVNQDDPNVLEIWNIVFIQFDRQKDRSLKTLPAKHIDTGMGFERLVSVLQDKSSNYDTDVFSPLFAKIQEVTNARPYTDKYGKDDTDGIDTAYRVIADHIRLLTFAISDGGVPNNEGRGYVVRRVLRRGSRYARKYFNVEIGSFFSKILPALVEQMGEQFPEIVKKQQDVKEILDEEEEAFARTLDRGEKMFEKYAAQAIKTNTKKLSGADVWRLYDTFGFPEDLTKIMAEERGLETDEGEIEIAKEKARDASKSVKEAAHTFAKLDVHQIAELDKMGVPQTNDDAKFSKGDTVGKIQLIYDGKNFHKSTSDLPSDKPFAILLDKTNFYAEQGGQIFDTGKIIIDGVAEFKVLDTQTCGGYIVHNGYMDYGTLKAGDEVICEYDELRRQPIRNNHTGTHILNHALREHLGEDINQKGSLVDQDKLRFDFSHKAPVSLPELKKIEDSSNSYIKQNCKIYSKDVDLDIAKGIEGVRAVFGETYPNPVRVVSVGVEVDILLAEPKNPEWRKVSVEFCGGTHVDQTGIIKDLVIVEESGIAKGIRRIVAYTGDTAHEVQRVALEFGKRIDALDALPHGVEKEQETKTTQNDLNQLTISVLAKADLKKKFDKVQKDVLDEQKRKQKAESKTALETVTAHFADPKNKDSTAYIAQLPISANSKAIADVMNHFKSKVKDKTVYLFGGSVSEGAVVHGVYVGTDAASKGVSAEQWAAAVSEVVGGRSGGKEPTRLGQGTNPDKIGDAVAVAEKWFAEKLKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP063405
EMBL· GenBank· DDBJ
QSZ29301.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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