A0A0L7KH58 · A0A0L7KH58_PLAFX
- ProteinAlanine--tRNA ligase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP + diphosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 995 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 999 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 1158 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 1162 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | alanine-tRNA ligase activity | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mitochondrial alanyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlanine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionA0A0L7KH58
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 87-114 | Disordered | |||
Compositional bias | 92-114 | Polar residues | |||
Domain | 374-1201 | Alanyl-transfer RNA synthetases family profile | |||
Region | 1015-1043 | Disordered | |||
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 statusComplete
- Length1,393
- Mass (Da)163,415
- Last updated2015-11-11 v1
- ChecksumA223CE7BB9B6C4C9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 92-114 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH672068 EMBL· GenBank· DDBJ | KOB62431.1 EMBL· GenBank· DDBJ | Genomic DNA |