|Function||glycine--tRNA ligase, beta subunit|
|Domain Trusted Cutoff||321.95|
|Domain Noise Cutoff||296.90|
|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|
|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.|
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.
DR HAMAP; MF_00255; 151 of 157|
|Genome Property||GenProp0258: tRNA aminoacylation (HMM)|
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