A0A011N5N4 · A0A011N5N4_9PROT
- ProteinValine--tRNA ligase
- GenevalS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids940 (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
- ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Candidatus Accumulibacter
Accessions
- Primary accessionA0A011N5N4
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-619 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: WYPEWEARGYFGAGLDTDKKPEDAFCILLPPPNVTGTLHMGHGFNQAIMDALTRYHRMRGDNTLWQPGTDHAGIATQIVVERQLDAQGVSRHDLGREKFLEKVWQWKEFSGNTITQQMRRLGTSPDWSRERFTMDAGLSTTVTETFVRLYKEGLIYRGKRLVNWDPVLQTAVSDLEVAQEEEQGHLWHIRYPLSDGSATLTVATTRPETMLGDTALMVHPEDERYRHLLGKTVKLPLCEREIPIIADAYVDLAFGTGCVKVTPAHDFNDYAVGQRHKLPMIPILTLDARINENAPACYQGMDRFTARQQIVADLEKQGFLDKVEAHTLKVPRGDRTGVVIEPMLTDQWFVAMSKAGADGSSIAGKALKCVASGEIKFFPENWVNTYNQWLNNIQDWCISRQLWWGHQIPAWYGDDGRIFVAHDEAEARAQAEEQGYSGPLARDPDVLDTWYSSALWPFSTLDWTPRWPAETNTALDLYLPSTVLVTGFDIIFFWVARMVMMTRHITGKIPFKHVYVHGLIRDAEGQKMSKSKGNVLDPIDLIDGIDLDALIGKRTSGLMNPKQAAQIEKRTRKEFPEGIQAFGTDALRFTFLSLASPGRDIKFD | ||||||
Motif | 47-57 | 'HIGH' region | ||||
Sequence: PNVTGTLHMGH | ||||||
Motif | 542-546 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Domain | 669-819 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | ||||
Sequence: DRWIVSKLQRTEAEVAQHFADYRFDLLARSVYEFVWDEFCDWYVELSKVQLQQGSEQEVRATRRTLARVLETVLRLAHPLLPFITEELWQALAPIAGRKTHDSLMLAAYPQAQPEKIDLASEANVQQLKDLAYACRNLRGEMNLSPAQKVP | ||||||
Domain | 874-938 | Valyl-tRNA synthetase tRNA-binding arm | ||||
Sequence: DVAVEGERLDKEIARLGGEIGKARAKLANENFVARAPAAVVEQEKKRLDDYLATLEKLTPQRERL |
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length940
- Mass (Da)106,332
- Last updated2014-06-11 v1
- Checksum5CA87BADE4AD8F5F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JEMX01000087 EMBL· GenBank· DDBJ | EXI77898.1 EMBL· GenBank· DDBJ | Genomic DNA |