P59690 (SYE_CHLCV) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
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 | Chlamydophila caviae (strain GPIC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 227941 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydophila › ![]() |
Protein attributes
| Sequence length | 505 AA. |
| Sequence status | Complete. |
| 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 |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022 |
| 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 |
| 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 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 – 505 | 505 | Glutamate--tRNA ligase HAMAP-Rule MF_00022 | PRO_0000119537 | |||||
Regions | |||||||||
| Motif | 12 – 22 | 11 | "HIGH" region HAMAP-Rule MF_00022 | ||||||
| Motif | 253 – 257 | 5 | "KMSKS" region HAMAP-Rule MF_00022 | ||||||
Sites | |||||||||
| Binding site | 256 | 1 | ATP By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Homologs of Escherichia coli recJ, gltX and of a putative 'early' gene of avian Chlamydia psittaci are located upstream of the 'late' omp2 locus of Chlamydia psittaci strain guinea pig inclusion conjunctivitis." Hsia R.C., Bavoil P.M. Gene 176:163-169(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GPIC. |
| [2] | "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae." Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. Fraser C.M.Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GPIC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U41759 Genomic DNA. Translation: AAB41141.1. AE015925 Genomic DNA. Translation: AAP04933.1. |
| PIR | JC5208. |
| RefSeq | NP_829055.1. NC_003361.3. |
3D structure databases | |
| ProteinModelPortal | P59690. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 227941.CCA00182. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAP04933; AAP04933; CCA_00182. |
| GeneID | 1217867. |
| KEGG | cca:CCA00182. |
| PATRIC | 20269380. VBIChlCav107360_0190. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0008. |
| KO | K01885. |
| OMA | WENVRVR. |
| ProtClustDB | PRK01406. |
Enzyme and pathway databases | |
| BioCyc | CCAV227941:GH8L-189-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits. |
| HAMAP | MF_00022_B. Glu_tRNA_synth_B. |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| PANTHER | PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit. |
| Pfam | PF00749. tRNA-synt_1c. 1 hit. [Graphical view] |
| PRINTS | PR00987. TRNASYNTHGLU. |
| SUPFAM | SSF48163. tRNA-synt_bind. 1 hit. |
| TIGRFAMs | TIGR00464. gltX_bact. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE_CHLCV | ||||||||
| Accession | Primary (citable) accession number: P59690 Secondary accession number(s): P94662, Q06560 | ||||||||
| 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
