InterPro : IPR002315

Name  Glycyl-tRNA synthetase Short Name  tRNA-synt_gly
Type  Family Description  The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [, , ]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c.In eubacteria, glycine-tRNA ligase() is an alpha2/beta2 tetramer composed of 2 different subunits [, , ]. In some eubacteria,in archaea and eukaryota, glycine-tRNA ligase is an alpha2 dimer, this family. It belongs to class IIc and is one of the most complex ligases. What is most interestingis the lack of similarity between the two types: divergence at the sequencelevel is so great that it is impossible to infer descent from common genes. The alpha (see ) and beta subunits (see ) also lack significant sequence similarity.However, they are translated from a single mRNA [], and a single chain glycine-tRNA ligase from Chlamydia trachomatishas been found to have significant similarity with both domains, suggesting divergence from a single polypeptide chain [].The sequence and crystal structure of the homodimeric glyccine-tRNA ligase from Thermus thermophilus, shows that each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel beta-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA ligase due to the conserved nature of the class II active site [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR022960 Glycine-tRNA ligase, archaeal Gly_tRNA_ligase_arc Family
IPR022961 Glycine-tRNA ligase, bacterial Gly_tRNA_ligase_bac Family

3 Contains

Id Name Short Name Type
IPR004154 Anticodon-binding Anticodon-bd Domain
IPR002314 Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain aa-tRNA-synt_IIb_cons-dom Domain
IPR006195 Aminoacyl-tRNA synthetase, class II aa-tRNA-synth_II Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR027031 Glycyl-tRNA synthetase/DNA polymerase subunit gamma-2 Gly-tRNA_synthase/POLG2 Family

11 Publications

First Author Title Year Journal Volume Pages
Perona JJ Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. 1993 Biochemistry 32 8758-71
Delarue M The aminoacyl-tRNA synthetase family: modules at work. 1993 Bioessays 15 675-87
Cusack S Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. 1991 Nucleic Acids Res 19 3489-98
Schimmel P Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. 1991 Trends Biochem Sci 16 1-3
Sugiura I The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. 2000 Structure 8 197-208
Eriani G Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. 1990 Nature 347 203-6
Wagar EA The glycyl-tRNA synthetase of Chlamydia trachomatis. 1995 J Bacteriol 177 5179-85
Webster TA Primary structures of both subunits of Escherichia coli glycyl-tRNA synthetase. 1983 J Biol Chem 258 10637-41
Shiba K Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. 1994 J Biol Chem 269 30049-55
Logan DT Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. 1995 EMBO J 14 4156-67
Arnez JG Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. 1999 J Mol Biol 286 1449-59

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)