Unreviewed,
UniProtKB/TrEMBL Q93RP5 (Q93RP5_THETH)
Last modified
June 16, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information
Names and origin
| Protein names | Submitted name: Arginyl-tRNA synthetase EMBL CAC39622.1 EC=6.1.1.19 | ||
| Gene names |
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| Organism | Thermus thermophilus EMBL CAC39622.1 | ||
| Taxonomic identifier | 274 [NCBI] | ||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 592 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. RuleBase RU003489V1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis RuleBase RU003489V1 |
| Ligand | ATP-binding RuleBase RU003489V1 Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase RuleBase RU003489V1 Ligase |
| Gene Ontology (GO) | |
| Biological process | arginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro arginine-tRNA ligase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Gene cloning, expression, crystallization and preliminary X-ray analysis of Thermus thermophilus arginyl-tRNA synthetase." Shimada A., Nureki O., Dohmae N., Takio K., Yokoyama S. Acta Crystallogr. 50:760-763(2001) Cited for: NUCLEOTIDE SEQUENCE. Strain: HB8 EMBL CAC39622.1. |
| [2] | "Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase." Shimada A., Nureki O., Goto M., Takahashi S., Yokoyama S. Proc. Natl. Acad. Sci. U.S.A. 98:13537-13542(2001) [PubMed: 11698642] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
Cross-references
Sequence databases | |
|---|---|
| AJ278815 Genomic DNA. Translation: CAC39622.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.19. 245. |
Family and domain databases | |
| InterPro | IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-synth_Ic. IPR015945. Arg-tRNA-synth_Ic_core. IPR005148. Arg-tRNA-synth_Ic_N. IPR008909. DALR_anticod_bd. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR11956. Arg_tRNA-synt_1c. 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. |
| TIGRFAMs | TIGR00456. argS. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q93RP5_THETH | ||||||||
| Accession | Primary (citable) accession number: Q93RP5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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