Q03R43 · SYA_LEVBA

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 Ser-tRNA(Ala) and Gly-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.

1879100200300400500600700800
TypeIDPosition(s)Description
Binding site567Zn2+ (UniProtKB | ChEBI)
Binding site571Zn2+ (UniProtKB | ChEBI)
Binding site669Zn2+ (UniProtKB | ChEBI)
Binding site673Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular Functiontransferase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-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
      alaS
    • Ordered locus names
      LVIS_1223

Organism names

Accessions

  • Primary accession
    Q03R43

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003476431-879Alanine--tRNA ligase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    879
  • Mass (Da)
    95,924
  • Last updated
    2006-11-14 v1
  • Checksum
    0028486F50F79ED2
MKELTSSQIRQMYLDFFKSKGHTIEPSASLVPKDDPSLLWINSGVATMKKYFSGQVVPENPRLTSSQKSIRTNDIENVGKTARHHTLFEMLGNFSVGDYFKKEAIAWAWELLTSPDWFGWDPDKLYMTVYPKDTDAKDAWEAVGVAPDHIIAVEDNFWDIGEGPSGPDSEIFYDRGEAFNNLAADDPENYPGGENERYLEVWNIVFSQFNHEPDGTYKPLPRKNIDTGMGLERVVSIFQNAKTNFETDLFMPLIEKTAALSAGKHYGANAEDDISFKVIADHARAITFAIGDGALPGNEGRGYVIRRLIRRAIVNGQKLGIEGAFLDQLVPVVGQIMQAYYPEVLEQSDYIAKVVRSEEDRFGETLTDGLNLLNSLIADLKQQGGNQIAGADAFKLYDTYGFPVELTEEYADDQGITVDEAGFKAEMQKQKDRARNARGKQKAMGLQHDLLINVKTPSEYVGYTQLATTSKLTVLVAGDELVDHVTSGTAEAMFDVTPFYAEMGGQVADKGDILDEAGHVVAHVADVQHAPNGQNLHTLTVVAPMETGATYQLKVDTIFHSKVEKNHTATHLLDKALREVFGEHTQQAGSLVEGDYLRFDFTHFGQVDPADLAKAEALVNQKIFEELPVTTVETDIESAKKMGAIALFSEKYGKVVRVVSAGDFVTEFCGGNHVKNTNEIGLFKITSESGVGAGVRRIEAVTSAAAYAYLHDHDEILNAVGADLKVTQVDEIEQKVQALQAQVKALEQQQATLEGKLASQEAGAVFDHVTTAGNYQLISGTVQVSKMDQLRALADTWRDQALSDVLVLGAEVNGKANLIVAVSADKQKQVKAGDLIKAISPKINGGGGGRPNLAQAGGKNPAGLPDAMTAAADWLAEQK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000416
EMBL· GenBank· DDBJ
ABJ64329.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp