P56000 (SYV_HELPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 82.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Valine--tRNA ligase EC=6.1.1.9 Alternative name(s): Valyl-tRNA synthetase Short name=ValRS | ||||
| Gene names |
| ||||
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 85962 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 874 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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 By similarity. HAMAP-Rule MF_02004 |
| Catalytic activity | ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02004 |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | 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 By similarity. HAMAP-Rule MF_02004 The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP-Rule MF_02004 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Domain | Coiled coil |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | regulation of translational fidelity Inferred from electronic annotation. Source: GOC valyl-tRNA aminoacylationInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activityInferred from electronic annotation. Source: InterPro valine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 874 | 874 | Valine--tRNA ligase HAMAP-Rule MF_02004 | PRO_0000106227 | |||||
Regions | |||||||||
| Coiled coil | 813 – 873 | 61 | Potential | ||||||
| Motif | 51 – 61 | 11 | "HIGH" region HAMAP-Rule MF_02004 | ||||||
| Motif | 533 – 537 | 5 | "KMSKS" region HAMAP-Rule MF_02004 | ||||||
Sites | |||||||||
| Binding site | 536 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000511 Genomic DNA. Translation: AAD08195.1. |
| PIR | A64664. |
| RefSeq | NP_207944.1. NC_000915.1. |
3D structure databases | |
| ProteinModelPortal | P56000. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 85962.HP1153. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD08195; AAD08195; HP_1153. |
| GeneID | 899913. |
| KEGG | hpy:HP1153. |
| PATRIC | 20593657. VBIHelPyl33062_1207. |
Phylogenomic databases | |
| eggNOG | COG0525. |
| KO | K01873. |
| OMA | DPLEMIE. |
| ProtClustDB | PRK05729. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 2 hits. 3.90.740.10. 1 hit. |
| HAMAP | MF_02004. Val_tRNA_synth_type1. |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR014729. Rossmann-like_a/b/a_fold. IPR010978. tRNA-bd_arm. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR019499. Val-tRNA_synth_tRNA-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. IPR002303. Valyl-tRNA_ligase. [Graphical view] |
| PANTHER | PTHR11946:SF5. PTHR11946:SF5. 1 hit. |
| Pfam | PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF10458. Val_tRNA-synt_C. 1 hit. [Graphical view] |
| PRINTS | PR00986. TRNASYNTHVAL. |
| SUPFAM | SSF46589. tRNA_binding_arm. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit. |
| TIGRFAMs | TIGR00422. valS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYV_HELPY | ||||||||
| Accession | Primary (citable) accession number: P56000 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
