Q8Z3X8 (SYK1_SALTI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lysine--tRNA ligase EC=6.1.1.6 Alternative name(s): Lysyl-tRNA synthetase Short name=LysRS | ||||
| Gene names |
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| Organism | Salmonella typhi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90370 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 505 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP MF_00252 |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. HAMAP MF_00252 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00252 |
| Subcellular location | |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-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: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lysine-tRNA ligase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW nucleic acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 505 | 504 | Lysine--tRNA ligase HAMAP MF_00252 | PRO_0000152625 | |||||
Sites | |||||||||
| Metal binding | 415 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 422 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 422 | 1 | Magnesium 2 By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. Barrell B.G.Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18. |
| [2] | "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL627277 Genomic DNA. Translation: CAD02870.1. AE014613 Genomic DNA. Translation: AAO70510.1. |
| RefSeq | NP_457438.1. NC_003198.1. NP_806650.1. NC_004631.1. |
3D structure databases | |
| ProteinModelPortal | Q8Z3X8. |
| SMR | Q8Z3X8. Positions 12-503. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1068608. 1249480. |
| GenomeReviews | Gene locus t2958 in contig AE014613_GR. Gene locus STY3196 in contig AL513382_GR. |
| KEGG | stt:t2958. sty:STY3196. |
| PATRIC | 18544456. VBISalEnt120419_3254. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG631383. |
| OMA | VEHKLEQ. |
| ProtClustDB | PRK00484. |
Enzyme and pathway databases | |
| BioCyc | SENT209261:T2958-MONOMER. SENT220341:STY3196-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00252. Lys_tRNA_synth_class2. [Tree] |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR002313. Lys-tRNA-synth_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| KO | K04567. |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF4. tRNA-synt_lys_2. 1 hit. |
| Pfam | PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] |
| PRINTS | PR00982. TRNASYNTHLYS. |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. |
| TIGRFAMs | TIGR00499. LysS_bact. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYK1_SALTI | ||||||||
| Accession | Primary (citable) accession number: Q8Z3X8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with