A0A5K7SCC0 · A0A5K7SCC0_9BACT
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids872 (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 Ser-tRNA(Ala) and Gly-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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Marinilabiliales > Prolixibacteraceae > Aquipluma
Accessions
- Primary accessionA0A5K7SCC0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-708 | Alanyl-transfer RNA synthetases family profile | ||||
Sequence: MNSKEIRKAFVDFFAGKGHQIVASAPMVVKNDPTLMFTNAGMNQFKDIFLGNQPAKYVRVADTQKCLRVSGKHNDLEEVGHDTYHHTMFEMLGNWSFGDYFKEDAINWAWELLHDVLKIPADRMYASVFEGSADDKLERDDEAFELWRKFLPAHQIINGSKKDNFWEMGDTGPCGPCSEIHVDLRDDAERAKIPGQNLVNKDNPLVIEIWNLVFIQFNRKADGKLEELPDKHVDTGMGFERLCMVLQGKKSNYDTDVFQNTIAKIAELSNKKYGDDQKADVAMRVIADHLRAISFSIADGQLPSNNKAGYVIRRILRRAVRYGYTFLDFREPFICKLVEVLKENMGDAFPELVSQQGLIENVIREEEESFLRTLETGIRLLDDLVAKAKAAGKTEISGDNAFTLYDTFGFPFDLTSLILREKGLTVDEAGFNAEMEKQKERSRNAAAQETDDWVELMKIEQVEFVGYDHLEAEVHISRYRKVTQKNKEFYHLVFDKTPFYGESGGQVGDSGYIIADGHRTRILDTQKENNLTIHIANKLPENPSATFMAVVDAGTRTLTMNNHSATHLLDQALREVLGTHVEQKGSLVNSEYLRFDFAHFQKVTKEELEKIQTRVNELVRKNLALEENRAVAFDEAKKLGAIALFGEKYGDFVRVIKFGESVELCGGTHVPSTGQIGSFIITSESAISAGVRRIEAITADRAEEFVKK | ||||||
Coiled coil | 601-628 | |||||
Sequence: QKVTKEELEKIQTRVNELVRKNLALEEN | ||||||
Coiled coil | 706-757 | |||||
Sequence: VKKHMDELAEVKAVLNNTQNLKKSVEDLVAQNSRLQKQIEEFERKAASGIKD |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length872
- Mass (Da)97,422
- Last updated2020-02-26 v1
- ChecksumDE3A914D29E19701
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP018694 EMBL· GenBank· DDBJ | BBE19220.1 EMBL· GenBank· DDBJ | Genomic DNA |