A0AAE6BL14 · A0AAE6BL14_RHIRD
- ProteinValine--tRNA ligase
- GenevalS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids947 (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
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Agrobacterium > Agrobacterium tumefaciens complex
Accessions
- Primary accessionA0AAE6BL14
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-631 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: IAKAWDEANAFRAGANAKPGAETFTIVIPPPNVTGSLHMGHALNNTLQDILVRFERMRGKDVLWQPGMDHAGIATQMVVERKLMEQQLPGRREMGREAFVEKVWEWKAESGGLIFNQLKRLGASCDWSRERFTMDEGLSEAVLEVFVTLYKQNLIYKDKRLVNWDPKLQTAISDMEVEQIEMKGNLWHFRYPLEKGVTYEYPVAFDADGTPTEFETRDYIVVATTRPETMLGDTGVAVNPEDERYKGIVGKHVILPIVGRKIPIVADDYADPTAGTGAVKITPAHDFNDFEVGKRCGLRAINVMNIDGTISIKENEDFLEGLNHPAALHGAWDRLEGQDRFTARKIIVEIFEEAGLLDKIEPHKHVVPHGDRGGVPIEPRLTDQWWVDNKTLAQPAIASVREGRTNFVPKNWENTYFQWMENIQPWCISRQLWWGHQIPAWYGPDGQVFVEKTEEEALQAAIQHYIAHEGPWKAWVEEKLEDFKPGEILTRDEDVLDTWFSSALWPFSTLGWPEETPELARYYPTNVLVTGFDIIPFWVVRMMQMGLHFMKDDAGNPVEPFSTVYIHALVRDKNGQKMSKSKGNVIDPLELIDEYGADALRFTLAIMAAQGRDVKLD | ||||||
Motif | 45-55 | 'HIGH' region | ||||
Sequence: PNVTGSLHMGH | ||||||
Motif | 591-595 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Domain | 673-821 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | ||||
Sequence: NRWILTELANTARDVTASLENFRFNDASGILYRFVWNQFCDWYLELLKPVFSGEDEKAKTESQACAAYVLDEIYKLLHPFMPFMTEELWAHTAGEGEERDDLLCLTDWPVPEFRDDASAAEINWLIDLVSGIRSTRAEMNVPPGATASL | ||||||
Coiled coil | 877-946 | |||||
Sequence: LVDLAAEKARLEKAIGKVDAEMERIDKKLSNEKFVANADPEVVATERERKAELEVQLTGLKTAMQRVNEA | ||||||
Domain | 879-942 | Valyl-tRNA synthetase tRNA-binding arm | ||||
Sequence: DLAAEKARLEKAIGKVDAEMERIDKKLSNEKFVANADPEVVATERERKAELEVQLTGLKTAMQR |
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
- Length947
- Mass (Da)106,939
- Last updated2024-05-29 v1
- Checksum18692A0611510520