A0A6V8SGE2 · A0A6V8SGE2_9CLOT
- ProteinThreonine--tRNA ligase
- GenethrS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids587 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H+ + L-threonyl-tRNA(Thr)
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | threonine-tRNA ligase activity | |
Molecular Function | transferase activity | |
Molecular Function | tRNA binding | |
Biological Process | threonyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThreonine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A6V8SGE2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 219-484 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: PNGVVLKNKLIEYWRELHRKYGYEEIETPLILNRDLWQTSGHWYHYKENMYTVNIDEEEYAIKPMNCPGGMLVYKSESHSYKELPIRAAELGRVHRHELSGALHGLMRVRAFTQDDAHIFMLPEQIKDEIKSVIKLINEVYSRFGFKYNVELSTRPENSMGSDSEWEIAEESLKNALEEINMSFKINPGDGAFYGPKIDFHLEDSIGRTWQCGTIQLDFQLPQRFDLEYVGSDGEKHKPIVIHRVIFGSIERFIGILIEHFEGKFP |
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)67,918
- Last updated2020-12-02 v1
- ChecksumF5F7BF96ED5ECBBE
Keywords
- Technical term