Q68VQ7 (SYA_RICTY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
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: Alanine--tRNA ligase EC=6.1.1.7 Alternative name(s): Alanyl-tRNA synthetase Short name=AlaRS | ||||
| Gene names |
| ||||
| Organism | Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 257363 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › ![]() |
Protein attributes
| Sequence length | 877 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP-Rule MF_00036 |
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP-Rule MF_00036 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | alanyl-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 alanine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. Weinstock G.M.J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017197 Genomic DNA. Translation: AAU04299.1. |
| RefSeq | YP_067781.1. NC_006142.1. |
3D structure databases | |
| ProteinModelPortal | Q68VQ7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 257363.RT0845. |
Proteomic databases | |
| PRIDE | Q68VQ7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAU04299; AAU04299; RT0845. |
| GeneID | 2959272. |
| KEGG | rty:RT0845. |
| PATRIC | 17910942. VBIRicTyp34752_0862. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0013. |
| HOGENOM | HOG000156965. |
| KO | K01872. |
| OMA | EWFDFPK. |
| ProtClustDB | PRK00252. |
Enzyme and pathway databases | |
| BioCyc | RTYP257363:GJEQ-885-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00036_B. Ala_tRNA_synth_B. |
| InterPro | IPR002318. Ala-tRNA-lgiase_IIc. IPR018162. Ala-tRNA-ligase_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_ligase_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view] |
| PANTHER | PTHR11777:SF6. PTHR11777:SF6. 1 hit. |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| SMART | SM00863. tRNA_SAD. 1 hit. [Graphical view] |
| SUPFAM | SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit. |
| TIGRFAMs | TIGR00344. alaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYA_RICTY | ||||||||
| Accession | Primary (citable) accession number: Q68VQ7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| Rickettsia typhi Rickettsia typhi (strain Wilmington): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
