A6Q3R4 (SYV_NITSB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 42.
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 |
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| Organism | Nitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 387092 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Nitratiruptor![]() |
Protein attributes
| Sequence length | 871 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. HAMAP-Rule MF_02004 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_02004. |
| 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 |
| 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 – 871 | 871 | Valine--tRNA ligase HAMAP-Rule MF_02004 | PRO_1000022170 | |||||
Regions | |||||||||
| Coiled coil | 805 – 871 | 67 | Potential | ||||||
| Motif | 47 – 57 | 11 | "HIGH" region HAMAP-Rule MF_02004 | ||||||
| Motif | 534 – 538 | 5 | "KMSKS" region HAMAP-Rule MF_02004 | ||||||
Sites | |||||||||
| Binding site | 537 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens." Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K. Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SB155-2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP009178 Genomic DNA. Translation: BAF70123.1. |
| RefSeq | YP_001356480.1. NC_009662.1. |
3D structure databases | |
| ProteinModelPortal | A6Q3R4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 387092.NIS_1013. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAF70123; BAF70123; NIS_1013. |
| GeneID | 5360927. |
| KEGG | nis:NIS_1013. |
| PATRIC | 22684104. VBINitSp82229_1056. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0525. |
| HOGENOM | HOG000020093. |
| KO | K01873. |
| OMA | IMDALIR. |
| ProtClustDB | PRK05729. |
Enzyme and pathway databases | |
| BioCyc | NSP387092:GHA5-1052-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.287.380. 1 hit. 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_NITSB | ||||||||
| Accession | Primary (citable) accession number: A6Q3R4 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with
