Reviewed,
UniProtKB/Swiss-Prot A7ZV28 (SYK3_ECO24)
Last modified
February 9, 2010.
Version 17.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Putative lysyl-tRNA synthetase EC=6.1.1.6 Alternative name(s): Lysine--tRNA ligase Short name=LysRS GX | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331111 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 325 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Could be a lysyl-tRNA synthetase. HAMAP MF_00174 |
| Catalytic activity | ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP MF_00174 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lysyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP lysine-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 – 325 | 325 | Putative lysyl-tRNA synthetase HAMAP MF_00174 | PRO_1000058326 | |||
Sequences
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References
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000800 Genomic DNA. Translation: ABV17289.1. |
| RefSeq | YP_001465657.1. |
3D structure databases | |
| SMR | A7ZV28. Positions 14-325. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7ZV28. |
Genome annotation databases | |
| GeneID | 5586570. |
| GenomeReviews | Gene locus EcE24377A_4714 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_4714. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2269. |
| HOGENOM | HBG631383. |
| OMA | PGNEAHL. |
Family and domain databases | |
| HAMAP | MF_00174. Put_Lys_tRNA_synth. [Tree] |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-dom. IPR004525. Lys-tRNA-synth-rel. IPR018149. Lys-tRNA-synth_II_C. [Graphical view] |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. |
| Pfam | PF00152. tRNA-synt_2. 1 hit. [Graphical view] |
| PRINTS | PR00982. TRNASYNTHLYS. |
| TIGRFAMs | TIGR00462. genX. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYK3_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZV28 | ||||||||
| 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 |

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