A1JJ29 (A1JJ29_YERE8) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Valine--tRNA ligase HAMAP-Rule MF_02004 EC=6.1.1.9 HAMAP-Rule MF_02004 Alternative name(s): Valyl-tRNA synthetase HAMAP-Rule MF_02004 | ||||
| Gene names |
| ||||
| Organism | Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP] EMBL CAL10618.1 | ||||
| Taxonomic identifier | 393305 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › ![]() |
Protein attributes
| Sequence length | 965 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 SAAS SAAS019499 |
| Catalytic activity | ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02004 SAAS SAAS019499 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_02004 SAAS SAAS019499 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_02004 SAAS SAAS019499. |
| Domain | The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP-Rule MF_02004 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 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. HAMAP-Rule MF_02004 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis HAMAP-Rule MF_02004 SAAS SAAS019499 |
| Cellular component | Cytoplasm HAMAP-Rule MF_02004 SAAS SAAS019499 |
| Domain | Coiled coil HAMAP-Rule MF_02004 SAAS SAAS019499 |
| Ligand | ATP-binding HAMAP-Rule MF_02004 SAAS SAAS019499 Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase HAMAP-Rule MF_02004 SAAS SAAS019499 EMBL CAL10618.1 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 | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Coiled coil | 896 – 965 | 70 | By similarity HAMAP-Rule MF_02004 | ||||||
| Motif | 56 – 66 | 11 | "HIGH" region By similarity HAMAP-Rule MF_02004 | ||||||
| Motif | 568 – 572 | 5 | "KMSKS" region By similarity HAMAP-Rule MF_02004 | ||||||
Sites | |||||||||
| Binding site | 571 | 1 | ATP By similarity HAMAP-Rule MF_02004 | ||||||
Sequences
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References
| [1] | "The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081." Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. Prentice M.B.PLoS Genet. 2:e206-e206(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 8081 EMBL CAL10618.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM286415 Genomic DNA. Translation: CAL10618.1. |
| RefSeq | YP_001004862.1. NC_008800.1. |
3D structure databases | |
| ProteinModelPortal | A1JJ29. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 393305.YE0498. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4715967. |
| KEGG | yen:YE0498. |
| PATRIC | 18560402. VBIYerEnt11519_0592. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0525. |
| HOGENOM | HOG000020094. |
| 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. 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 | A1JJ29_YERE8 | ||||||||
| Accession | Primary (citable) accession number: A1JJ29 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
