F2PH18 · F2PH18_TRIEC
- ProteinAlanine--tRNA ligase
- GeneALA1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids963 (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 | 610 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 614 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 729 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 733 | 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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton
Accessions
- Primary accessionF2PH18
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 18-772 | Alanyl-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 statusComplete
- Length963
- Mass (Da)106,929
- Last updated2011-05-31 v1
- Checksum97CBA5B014A09D58
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS995718 EMBL· GenBank· DDBJ | EGE01186.1 EMBL· GenBank· DDBJ | Genomic DNA |