A0A2G3JZ82 · A0A2G3JZ82_9NEIS
- ProteinValine--tRNA ligase
- GenevalS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids938 (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.
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 > Betaproteobacteria > Neisseriales > Chitinibacteraceae > Chitinimonas
Accessions
- Primary accessionA0A2G3JZ82
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-625 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: WYAHWETSGYFKPSMDAAVPSFSIQLPPPNVTGTLHMGHAFNQTIMDGLTRYYRMKGHNTLWVPGTDHAGIATQIVVERQLADQKINRHDLGRDAFISKVWEWKAKSGGIITEQMRRVGCSVDWQREYFTMDAVRSETVADVFVRLYKQGLIYRGKRLVNWDPKLGTAVSDLEVVSEEEDGHMWHIRYPVVGSDEAIVVATTRPETLLGDVAVAVSATDERYTHLHGKQLQLPLTGRQIPLIVDEYVDAAFGTGCVKITPAHDFNDYQVGKRHNTLLINVMSLQANMLANAEVFSFDGKSVDSIALPAAYAGLDTKAARKAVVADLEAQGFLVEVKPHKLQVPRGDRTGSVIEPLLTDQWFMAMSKVGEGDETGKSIAQKSIDAVESGQVRFIPENWVNTYNQWMKNLQDWCISRQLWWGHQIPAWYDAEGNIYVANTEAEAQAQAPGKALRRDEDVLDTWFSSALVPFSTMGWPADTAELKAFLPSTVLVTGYEIIFFWVARMIMMTTHFTGKVPFKDVYIHGMVRDSDGKKMSKSEGNVIDPVDLIDGIAIDPLLVKRTTGLRRPETAPKVEKKTRADFPEGIPAYGTDALRFTMASYATLGRNVNFD | ||||||
Motif | 44-54 | 'HIGH' region | ||||
Sequence: PNVTGTLHMGH | ||||||
Motif | 548-552 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Domain | 669-820 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | ||||
Sequence: DQWIIGRLQQTELDVTEALDTYRFDLAAQAIYEFVWNEYCDWYVELAKVQIQNGSEAQQRATRRTLVRVLEVALRLAHPIIPFITEELWQTVAPLANAKKTEALMLAQWPVAQPEKINAAANARMETFRALTMAVRTLRAEMNLSPSQRVPL | ||||||
Domain | 875-938 | Valyl-tRNA synthetase tRNA-binding arm | ||||
Sequence: AAETVRLSKEVARLEGEIVKATAKLANPAFADKAPAAVVEQERKRLGDFSETVGKLKTQLAKLA |
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
- Length938
- Mass (Da)105,255
- Last updated2018-01-31 v1
- ChecksumF439B5B7232609E8
Keywords
- Technical term