| Accession | TIGR00211 |
| Name | glyS |
| Function | glycine--tRNA ligase, beta subunit |
| Gene Symbol | glyS |
| Trusted Cutoff | 321.95 |
| Domain Trusted Cutoff | 321.95 |
| Noise Cutoff | 296.90 |
| Domain Noise Cutoff | 296.90 |
| Isology Type | equivalog_domain |
| EC Number | 6.1.1.14 |
| HMM Length | 691 |
| Mainrole Category | Protein synthesis |
| Subrole Category | tRNA aminoacylation |
| Gene Ontology Term | GO:0004820: glycine-tRNA ligase activity molecular_function |
| | GO:0006426: glycyl-tRNA aminoacylation biological_process |
| | GO:0009345: glycine-tRNA ligase complex cellular_component |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:07PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | The glycyl-tRNA synthetases differ even among the eubacteria in oligomeric structure. In Escherichia coli and most others, it is a heterodimer of two alpha chains and two beta chains, encoded by tandem genes. The genes are similar, but fused, in Chlamydia trachomatis. By contrast, the glycyl-tRNA synthetases of Thermus thermophilus and of archaea and eukaryotes differ considerably; they are homodimeric, mutually similar, and not detected by this model. |
| References | RM 98149692
RT Glycyl-tRNA synthetase from Thermus thermophilus--wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems.
RA Mazauric MH, Keith G, Logan D, Kreutzer R, Giege R, Kern D.
RL Eur J Biochem. 1998 Feb 1;251(3):744-57.
SE TIGR
DR HAMAP; MF_00255; 151 of 157 |
| Genome Property | GenProp0258: tRNA aminoacylation (HMM) |
