Q7UK37 (Q7UK37_RHOBA) Unreviewed, UniProtKB/TrEMBL
Last modified
May 29, 2013.
Version 76.
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: Lysine--tRNA ligase HAMAP-Rule MF_00252 RuleBase RU000336 EC=6.1.1.6 HAMAP-Rule MF_00252 RuleBase RU000336 Alternative name(s): Lysyl-tRNA synthetase HAMAP-Rule MF_00252 | ||||
| Gene names |
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| Organism | Rhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 243090 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Planctomycetes › Planctomycetia › Planctomycetales › Planctomycetaceae › Rhodopirellula › ![]() |
Protein attributes
| Sequence length | 546 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-Rule MF_00252 SAAS SAAS002313 |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. HAMAP-Rule MF_00252 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00252 SAAS SAAS002313 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00252. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00252 RuleBase RU003746 |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Metal binding | 458 | 1 | Magnesium 1 By similarity HAMAP-Rule MF_00252 | ||||||
| Metal binding | 465 | 1 | Magnesium 1 By similarity HAMAP-Rule MF_00252 | ||||||
| Metal binding | 465 | 1 | Magnesium 2 By similarity HAMAP-Rule MF_00252 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the marine planctomycete Pirellula sp. strain 1." Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R. Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SH1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX294152 Genomic DNA. Translation: CAD77044.1. |
| RefSeq | NP_869666.1. NC_005027.1. |
3D structure databases | |
| ProteinModelPortal | Q7UK37. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243090.RB10883. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAD77044; CAD77044; RB10883. |
| GeneID | 1796815. |
| KEGG | rba:RB10883. |
| PATRIC | 23251995. VBIRhoBal59814_5254. |
Phylogenomic databases | |
| HOGENOM | HOG000236578. |
| KO | K04567. |
| OMA | EHKLEQP. |
| ProtClustDB | CLSK2759681. |
Family and domain databases | |
| Gene3D | 2.40.50.140. 1 hit. |
| HAMAP | MF_00252. Lys_tRNA_synth_class2. |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR002313. Lys-tRNA-ligase_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view] |
| PANTHER | PTHR22594. PTHR22594. 1 hit. PTHR22594:SF4. PTHR22594:SF4. 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 | Q7UK37_RHOBA | ||||||||
| Accession | Primary (citable) accession number: Q7UK37 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
