P67569 (SYR_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 61.
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: Arginine--tRNA ligase EC=6.1.1.19 Alternative name(s): Arginyl-tRNA synthetase Short name=ArgRS | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 550 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_00123 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00123. |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | arginyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP growthInferred from mutant phenotype PubMed 12657046. Source: MTBBASE |
| Cellular_component | cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE plasma membraneInferred from direct assay PubMed 15525680. Source: MTBBASE |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP arginine-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 – 550 | 550 | Arginine--tRNA ligase HAMAP-Rule MF_00123 | PRO_0000151580 | |||||
Regions | |||||||||
| Motif | 130 – 140 | 11 | "HIGH" region HAMAP-Rule MF_00123 | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842576 Genomic DNA. Translation: CAA97757.1. AE000516 Genomic DNA. Translation: AAK45593.1. AL123456 Genomic DNA. Translation: CCP44049.1. |
| PIR | H70772. |
| RefSeq | NP_215808.1. NC_000962.3. NP_335779.1. NC_002755.2. YP_006514668.1. NC_018143.1. |
3D structure databases | |
| ProteinModelPortal | P67569. |
| SMR | P67569. Positions 5-550. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 83332.Rv1292. |
Proteomic databases | |
| PRIDE | P67569. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAK45593; AAK45593; MT1331. |
| GeneID | 13319873. 886964. 924742. |
| KEGG | mtc:MT1331. mtu:Rv1292. |
| PATRIC | 18124692. VBIMycTub22151_1464. |
Organism-specific databases | |
| TubercuList | Rv1292. |
Phylogenomic databases | |
| eggNOG | COG0018. |
| HOGENOM | HOG000247214. |
| KO | K01887. |
| OMA | HTSANPN. |
| ProtClustDB | PRK01611. |
Family and domain databases | |
| Gene3D | 3.30.1360.70. 1 hit. 3.40.50.620. 1 hit. |
| HAMAP | MF_00123. Arg_tRNA_synth. |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-ligase_Ia. IPR015945. Arg-tRNA-synth_Ia_core. IPR005148. Arg-tRNA-synth_N. IPR008909. DALR_anticod-bd. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view] |
| PANTHER | PTHR11956. PTHR11956. 1 hit. |
| Pfam | PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit. [Graphical view] |
| PRINTS | PR01038. TRNASYNTHARG. |
| SMART | SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit. [Graphical view] |
| SUPFAM | SSF55190. Arg-tRNA-synth_Ic_N. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit. |
| TIGRFAMs | TIGR00456. argS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYR_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P67569 Secondary accession number(s): L0T8Y6, Q10609 | ||||||||
| 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 |
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
