Protein Domain : IPR002315

Type:  Family Name:  Glycyl-tRNA synthetase
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 [, ]. Short Name:  tRNA-synt_gly

2 Child Features

DB identifier Type Name
IPR022960 Family Glycine-tRNA ligase, archaeal
IPR022961 Family Glycine-tRNA ligase, bacterial

3 Contains

DB identifier Type Name
IPR004154 Domain Anticodon-binding
IPR006195 Domain Aminoacyl-tRNA synthetase, class II
IPR002314 Domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)

2 Cross Referencess

Identifier
TIGR00389
PR01043

0 Found In

5 GO Annotations

GO Term Gene Name Organism
GO:0000166 IPR002315
GO:0004820 IPR002315
GO:0005524 IPR002315
GO:0006426 IPR002315
GO:0005737 IPR002315

1 Parent Features

DB identifier Type Name
IPR027031 Family Glycyl-tRNA synthetase/DNA polymerase subunit gamma-2

247 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
230438 D8R0P1 PAC:15413946 Selaginella moellendorffii 604  
268427 D8SD08 PAC:15414222 Selaginella moellendorffii 676  
evm.TU.contig_43454.1 PAC:16431880 Carica papaya 220  
evm.model.supercontig_13.179 PAC:16407690 Carica papaya 439  
evm.model.supercontig_13.180 PAC:16407692 Carica papaya 216  
30128.m008560 B9RG03 PAC:16818150 Ricinus communis 686  
59511.m000017 B9TMP3 PAC:16829266 Ricinus communis 160  
Cucsa.178850.1 PAC:16967167 Cucumis sativus 729  
GSVIVT01008654001 D7SH83 PAC:17821225 Vitis vinifera 687  
GSVIVT01001092001 PAC:17817357 Vitis vinifera 599  
orange1.1g040142m PAC:18116065 Citrus sinensis 491  
orange1.1g041441m A0A067EGM5 PAC:18104453 Citrus sinensis 310  
orange1.1g042110m A0A067E876 PAC:18104449 Citrus sinensis 287  
AT3G44740.1 F4J376 PAC:19659992 Arabidopsis thaliana 244  
AT1G29880.1 O23627 PAC:19649548 Arabidopsis thaliana 729  
AT1G29870.1 Q9FXG2 PAC:19650679 Arabidopsis thaliana 463  
Thhalv10006931m V4KV36 PAC:20186954 Eutrema salsugineum 725  
Ciclev10005363m V4RJ07 PAC:20791723 Citrus clementina 339  
Ciclev10004625m V4SAQ7 PAC:20790596 Citrus clementina 578  
Ciclev10004524m V4S5C7 PAC:20790595 Citrus clementina 646  
Carubv10008480m R0IRA8 PAC:20890416 Capsella rubella 690  
Carubv10013104m R0HK00 PAC:20898533 Capsella rubella 691  
Carubv10004365m R0GYI3 PAC:20896377 Capsella rubella 631  
MDP0000146975 PAC:22663478 Malus domestica 649  
MDP0000199883 PAC:22675500 Malus domestica 649  
MDP0000226879 PAC:22645355 Malus domestica 1072  
Lus10029203 PAC:23151870 Linum usitatissimum 742  
Lus10042096 PAC:23153692 Linum usitatissimum 725  
Lus10008792 PAC:23177853 Linum usitatissimum 678  
Potri.003G162300.2 PAC:26997067 Populus trichocarpa 506  

11 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8364025
            8274143
            1852601
            2053131
            10673435
            2203971
            7665503
            6309809
            7962006
            7556056
            10064708