Reviewed,
UniProtKB/Swiss-Prot Q60BG7 (SYE1_METCA)
Last modified
November 3, 2009.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamyl-tRNA synthetase 1 EC=6.1.1.17 Alternative name(s): Glutamate--tRNA ligase 1 Short name=GluRS 1 | ||||||
| Gene names |
| ||||||
| Organism | Methylococcus capsulatus [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 414 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamyl-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 glutamate-tRNA ligase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 466 | 466 | Glutamyl-tRNA synthetase 1 HAMAP MF_00022 | PRO_0000119597 | |||||
Regions | |||||||||
| Motif | 10 – 20 | 11 | "HIGH" region HAMAP MF_00022 | ||||||
| Motif | 247 – 251 | 5 | "KMSKS" region HAMAP MF_00022 | ||||||
Sites | |||||||||
| Metal binding | 103 | 1 | Zinc By similarity | ||||||
| Metal binding | 105 | 1 | Zinc By similarity | ||||||
| Metal binding | 130 | 1 | Zinc By similarity | ||||||
| Metal binding | 132 | 1 | Zinc By similarity | ||||||
| Binding site | 250 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. Eisen J.A.PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132. |
Cross-references
Sequence databases | |
|---|---|
| AE017282 Genomic DNA. Translation: AAU93301.1. | |
| RefSeq | YP_113029.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3103869. |
| GenomeReviews | Gene locus MCA0510 in contig AE017282_GR. |
| KEGG | mca:MCA0510. |
| NMPDR | fig|243233.4.peg.993. |
| TIGR | MCA0510. |
Phylogenomic databases | |
| HOGENOM | Q60BG7. |
| OMA | GSPAFFF. |
Enzyme and pathway databases | |
| BioCyc | MCAP243233:MCA_0510-MON. |
| BRENDA | 6.1.1.17. 2172. |
Family and domain databases | |
| HAMAP | MF_00022. [Tree] |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ic_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit. |
| PANTHER | PTHR10119. Glu_tRNA-synt_1c. 1 hit. |
| Pfam | PF00749. tRNA-synt_1c. 1 hit. [Graphical view] |
| PRINTS | PR00987. TRNASYNTHGLU. |
| TIGRFAMs | TIGR00464. gltX_bact. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE1_METCA | ||||||||
| Accession | Primary (citable) accession number: Q60BG7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

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