A0A4P6UZI7 · A0A4P6UZI7_9HYPH
- ProteinValine--tRNA ligase
- GenevalS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids953 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic activity
- tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP + diphosphate
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 605 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | valine-tRNA ligase activity | |
Biological Process | valyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameValine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Ahrensiaceae > Roseitalea
Accessions
- Primary accessionA0A4P6UZI7
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif, coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 15-642 | Aminoacyl-tRNA synthetase class Ia | |||
Motif | 45-55 | 'HIGH' region | |||
Motif | 602-606 | 'KMSKS' region | |||
Domain | 684-825 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | |||
Coiled coil | 884-918 | ||||
Domain | 886-946 | Valyl-tRNA synthetase tRNA-binding arm | |||
Domain
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length953
- Mass (Da)106,727
- Last updated2019-07-31 v1
- MD5 Checksum76EC7F41A2DE292415ADE57DE7C386B2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP036532 EMBL· GenBank· DDBJ | QBK30547.1 EMBL· GenBank· DDBJ | Genomic DNA |