Q180A1 (Q180A1_CLOD6) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 60.
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 | Clostridium difficile (strain 630) [Complete proteome] [HAMAP] EMBL CAJ70153.1 | ||||
| Taxonomic identifier | 272563 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › ![]() |
Protein attributes
| Sequence length | 888 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 CAJ70153.1 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 | 814 – 888 | 75 | By similarity HAMAP-Rule MF_02004 | ||||||
| Motif | 47 – 57 | 11 | "HIGH" region By similarity HAMAP-Rule MF_02004 | ||||||
| Motif | 527 – 531 | 5 | "KMSKS" region By similarity HAMAP-Rule MF_02004 | ||||||
Sites | |||||||||
| Binding site | 530 | 1 | ATP By similarity HAMAP-Rule MF_02004 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. Barrell B.and.Parkhill.J.Nat. Genet. 38:779-786(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630 EMBL CAJ70153.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM180355 Genomic DNA. Translation: CAJ70153.1. |
| RefSeq | YP_001089772.1. NC_009089.1. |
3D structure databases | |
| ProteinModelPortal | Q180A1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272563.CD3256. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAJ70153; CAJ70153; CD630_32560. |
| GeneID | 4916580. |
| KEGG | cdf:CD630_32560. |
| PATRIC | 19445051. VBICloDif38397_3409. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0525. |
| HOGENOM | HOG000020093. |
| KO | K01873. |
| OMA | IMDALIR. |
| ProtClustDB | PRK05729. |
Enzyme and pathway databases | |
| BioCyc | CDIF272563:GJFE-3500-MONOMER. |
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 | Q180A1_CLOD6 | ||||||||
| Accession | Primary (citable) accession number: Q180A1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
