A0QUY7 (SYE_MYCS2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 56.
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 |
| ||||
| Organism | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 246196 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. HAMAP-Rule MF_00022 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00022. |
| 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 | 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 – 486 | 486 | Glutamate--tRNA ligase HAMAP-Rule MF_00022 | PRO_0000330980 | |||||
Regions | |||||||||
| Motif | 12 – 22 | 11 | "HIGH" region HAMAP-Rule MF_00022 | ||||||
| Motif | 256 – 260 | 5 | "KMSKS" region HAMAP-Rule MF_00022 | ||||||
Sites | |||||||||
| Binding site | 259 | 1 | ATP By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [2] | "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [3] | "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: ATCC 700084 / mc(2)155. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000480 Genomic DNA. Translation: ABK74186.1. CP001663 Genomic DNA. Translation: AFP38793.1. |
| RefSeq | YP_006567088.1. NC_018289.1. YP_886725.1. NC_008596.1. |
3D structure databases | |
| ProteinModelPortal | A0QUY7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 246196.MSMEG_2383. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK74186; ABK74186; MSMEG_2383. |
| GeneID | 13428840. 4533604. |
| KEGG | msg:MSMEI_2323. msm:MSMEG_2383. |
| PATRIC | 18077190. VBIMycSme59918_2349. |
Phylogenomic databases | |
| eggNOG | COG0008. |
| HOGENOM | HOG000252722. |
| KO | K01885. |
| OMA | RYRDFKG. |
| ProtClustDB | PRK01406. |
Enzyme and pathway databases | |
| BioCyc | MSME246196:GJ4Y-2383-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. 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE_MYCS2 | ||||||||
| Accession | Primary (citable) accession number: A0QUY7 Secondary accession number(s): I7FJ34 | ||||||||
| Entry history |
| ||||||||
| 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
