Q87F36 (SYV_XYLFT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
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 | Xylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 183190 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella › ![]() |
Protein attributes
| Sequence length | 994 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 |
| 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 – 994 | 994 | Valine--tRNA ligase HAMAP-Rule MF_02004 | PRO_0000106245 | |||||
Regions | |||||||||
| Coiled coil | 928 – 994 | 67 | Potential | ||||||
| Motif | 43 – 53 | 11 | "HIGH" region HAMAP-Rule MF_02004 | ||||||
| Motif | 585 – 589 | 5 | "KMSKS" region HAMAP-Rule MF_02004 | ||||||
Sites | |||||||||
| Binding site | 588 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa." Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M. Kitajima J.P.J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Temecula1 / ATCC 700964. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE009442 Genomic DNA. Translation: AAO28001.1. |
| RefSeq | NP_778352.1. NC_004556.1. |
3D structure databases | |
| ProteinModelPortal | Q87F36. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 183190.PD0102. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAO28001; AAO28001; PD_0102. |
| GeneID | 1144314. |
| KEGG | xft:PD0102. |
| PATRIC | 24147614. VBIXylFas71109_0142. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0525. |
| KO | K01873. |
| OMA | IMDALIR. |
| ProtClustDB | PRK05729. |
Family and domain databases | |
| Gene3D | 1.10.287.380. 1 hit. 3.40.50.620. 3 hits. 3.90.740.10. 2 hits. |
| 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_XYLFT | ||||||||
| Accession | Primary (citable) accession number: Q87F36 | ||||||||
| 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
