P41258 (SYK_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 91.
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 | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| 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 Reference 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 501 | 501 | Lysine--tRNA ligase HAMAP MF_00252 | PRO_0000152608 | |||||
Sites | |||||||||
| Metal binding | 404 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 411 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 411 | 1 | Magnesium 2 By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 19 | 1 | N → K in AAA23029. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lysyl-tRNA synthetase gene of Campylobacter jejuni." Chan V.L., Bingham H.L. J. Bacteriol. 174:695-701(1992) [PubMed: 1732205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43431 / TGH 9011 / Serotype O:3. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| [3] | "Characterisation of a Campylobacter jejuni fur mutant." van Vliet A.H.M., Wooldridge K.G., Ketley J.M. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-355. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M63448 Genomic DNA. Translation: AAA23029.1. AL111168 Genomic DNA. Translation: CAL34551.1. AF052056 Genomic DNA. Translation: AAC64260.1. |
| PIR | A42609. G81383. |
| RefSeq | YP_002343838.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | P41258. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P41258. 56 interactions. |
Proteomic databases | |
| PRIDE | P41258. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 904725. |
| GenomeReviews | Gene locus Cj0401 in contig AL111168_GR. |
| KEGG | cje:Cj0401. |
| PATRIC | 20057717. VBICamJej33762_0392. |
Phylogenomic databases | |
| HOGENOM | HBG631383. |
| OMA | VTFHNAL. |
| ProtClustDB | PRK00484. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0401-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 | SYK_CAMJE | ||||||||
| Accession | Primary (citable) accession number: P41258 Secondary accession number(s): O68607, Q0PBA9 | ||||||||
| 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 |

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