Reviewed,
UniProtKB/Swiss-Prot Q4JWU8 (SYV_CORJK)
Last modified
June 16, 2009.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Valyl-tRNA synthetase EC=6.1.1.9 Alternative name(s): Valine--tRNA ligase Short name=ValRS | ||||
| Gene names |
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| Organism | Corynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 306537 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 932 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP 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. The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. |
| 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 | valyl-tRNA aminoacylation Inferred 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 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 – 932 | 932 | Valyl-tRNA synthetase HAMAP MF_02004 | PRO_0000224468 | |||||
Regions | |||||||||
| Coiled coil | 863 – 929 | 67 | Potential | ||||||
| Motif | 75 – 85 | 11 | "HIGH" region HAMAP MF_02004 | ||||||
| Motif | 568 – 572 | 5 | "KMSKS" region HAMAP MF_02004 | ||||||
Sites | |||||||||
| Binding site | 571 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora." Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A. J. Bacteriol. 187:4671-4682(2005) [PubMed: 15968079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CR931997 Genomic DNA. Translation: CAI36709.1. | |
| RefSeq | YP_250327.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3433539. |
| GenomeReviews | Gene locus jk0550 in contig CR931997_GR. |
| KEGG | cjk:jk0550. |
| NMPDR | fig|306537.3.peg.546. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q4JWU8. |
| OMA | Q4JWU8. TDQWYVS. |
Enzyme and pathway databases | |
| BioCyc | CJEI306537:JK0550-MON. |
Family and domain databases | |
| HAMAP | MF_02004. [Tree] |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR002303. Val-tRNA_synth_Ia. IPR019754. Val-tRNA_synth_Ia_N. IPR019499. Val-tRNA_synth_Ia_tRNA-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR11946:SF5. tRNA-synt_val. 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. |
| TIGRFAMs | TIGR00422. valS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYV_CORJK | ||||||||
| Accession | Primary (citable) accession number: Q4JWU8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


