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A0A0S3SE77 · A0A0S3SE77_PHAAN

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.

1996100200300400500600700800900
TypeIDPosition(s)Description
Binding site640Zn2+ (UniProtKB | ChEBI)
Binding site644Zn2+ (UniProtKB | ChEBI)
Binding site759Zn2+ (UniProtKB | ChEBI)
Binding site763Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
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
      Vigan.06G239400
    • ORF names
      VIGAN_06239400

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Shumari
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Vigna

Accessions

  • Primary accession
    A0A0S3SE77

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain57-802Alanyl-transfer RNA synthetases family profile
Coiled coil842-869

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
    996
  • Mass (Da)
    109,532
  • Last updated
    2016-02-17 v1
  • MD5 Checksum
    19E7C27BB03B7BFFC4803CB7A2108058
MKRGFGVRALLISFRNCNPLPPPLLPLSLPFRAARSLHSPSSSVAAMPGADTQHVEWPAKRVRDTFMGFFEGKNHVNWKSSPVVPFNDPTLLFANAGMNQFKPIFLGTADPNTALSKLSRACNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKVEAISWAWELLTEVYKLPSDRLYATYFGGDDKAGLAPDFEARDIWLKFLPPGRVLPFGCKDNFWEMGDTGPCGPCTEIHFDRIGNRDAASLVNYDDPTCIEIWNLVFIQFNREADGSLKPLPAKHVDTGLGFERLTSVLQNKMSNYDTDIFMPIFDVIQKATGARPYSGKVGADDVDKIDMAYRVVADHIRTLSFAIADGSRPGNDGREYVLRRILRRAVRYGREVLKAKERFFSGFVSVVVNLMGDVFPELKQQETHIRNVIEEEEESFGRTLIKGIEKFETAVQHVQGKTLSGEEAFVLWDTYGFPLDLTQLMAEEKGLVVDVKGFDRAMEAARERSRSAQTKQAGGAIVMDADATSALHKRGISPTDDSFKYAWFKDHESVVQAIYTGSEFVDTVNTGDDVGLVLESTSFYAEQGGQIFDTGSLEGTIGSFEVHNTQVYGGFILHIGNGTGVSVGDRVVCKVDYGRRAIIAPNHTCTHMLNFALREVLGNHVDQKGSIVLPEKLRFDFSHGKPVDADNLRRIEAIVNEQIKAELDVSAKEATLADAKRINGLRAVFGEVYPDPVRVVSIGQKVEDLLADPDNEKWLSISSELCGGTHISNTREAKAFALLSEEGIAKGIRRITAVTTDRAYDAMKVADELEQQVDEAAKLDGSLLEEKVSSLKNNVETLSIPAAKKADIKTKIARLQDQVRKAQKQIAEENKRKAVNITAEKAELAASNGKTFCISRVNVGLDVAAVREAVTKVMDQKGLSVMVFSTDESTNKAVICAGVPEKGDKGKLDVAEWLSNALGPLKGRCGKGKGGLATGQGTDAAHVNEAMDLAEKFASMKLS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP015039
EMBL· GenBank· DDBJ
BAT91088.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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