P77984 (SYE_STAXY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
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: Glutamate--tRNA ligase EC=6.1.1.17 Alternative name(s): Glutamyl-tRNA synthetase Short name=GluRS | ||
| Gene names |
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| Organism | Staphylococcus xylosus | ||
| Taxonomic identifier | 1288 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus![]() |
Protein attributes
| Sequence length | 120 AA. |
| Sequence status | Fragment. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022_B |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022_B |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| 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 |
| Gene Ontology (GO) | |
| Biological_process | translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activityInferred from electronic annotation. Source: EC tRNA 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 – 120 | ›120 | Glutamate--tRNA ligase HAMAP-Rule MF_00022_B | PRO_0000119659 | ||||
Experimental info | ||||||||
| Non-terminal residue | 1 | 1 | ||||||
Sequences
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References
| [1] | "Identification of the serine acetyltransferase gene of Staphylococcus xylosus." Fiegler H., Brueckner R. FEMS Microbiol. Lett. 148:181-187(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 20267 / Isolate C2A. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y07614 Genomic DNA. Translation: CAA68886.1. |
3D structure databases | |
| ProteinModelPortal | P77984. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 1.10.10.350. 1 hit. |
| HAMAP | MF_00022_B. Glu_tRNA_synth_B. |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. [Graphical view] |
| SUPFAM | SSF48163. tRNA-synt_bind. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE_STAXY | ||||||||
| Accession | Primary (citable) accession number: P77984 | ||||||||
| 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 |

Clusters with
