Reviewed,
UniProtKB/Swiss-Prot Q55522 (SYV_SYNY3)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 |
| ||||
| Organism | Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1148 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechocystis |
Protein attributes
| Sequence length | 910 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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 protein bindingInferred from physical interaction. Source: IntAct 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 – 910 | 910 | Valyl-tRNA synthetase HAMAP MF_02004 | PRO_0000106237 | |||||
Regions | |||||||||
| Coiled coil | 845 – 909 | 65 | Potential | ||||||
| Motif | 46 – 56 | 11 | "HIGH" region HAMAP MF_02004 | ||||||
| Motif | 539 – 543 | 5 | "KMSKS" region HAMAP MF_02004 | ||||||
Sites | |||||||||
| Binding site | 542 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BA000022 Genomic DNA. Translation: BAA10881.1. | |
| PIR | S76034. |
| RefSeq | NP_442810.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IVS based on UniProtKB P96142. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q55522. 2 interactions. |
Genome annotation databases | |
| GeneID | 952772. |
| GenomeReviews | Gene locus slr0557 in contig BA000022_GR. |
| KEGG | syn:slr0557. |
| NMPDR | fig|1148.1.peg.2911. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q55522. |
| OMA | Q55522. TDQWYVS. |
Enzyme and pathway databases | |
| BioCyc | SSP1148:SLR0557-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. IPR011321. Val-tRNA_synth_Ia_C. 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. G3DSA:1.10.287.380. Val-tRNA_synth_Ia_C. 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_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55522 | ||||||||
| 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 |
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |

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