InterPro : IPR018163

Name  Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain Short Name  Thr/Ala-tRNA-synth_IIc_edit
Type  Domain 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.This entry represents a structural domain containing a two-layer core alpha/beta structure: alpha-beta(2)-alpha-beta(2). This domain is thought to be a putative editing domain found in the N-terminal part of threonyl-tRNA synthetase (ThrRS), the C-terminal of alanyl-tRNA synthetase (AlaRS), and as the stand-alone hypothetical protein from the archaea Pyrococcus horikoshii[]; probable circular permutation of LuxS [, , ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR012947 Threonyl/alanyl tRNA synthetase, SAD tRNA_SAD Domain

4 Found In

Id Name Short Name Type
IPR002320 Threonine-tRNA ligase, class IIa Thr-tRNA-ligase_IIa Family
IPR002318 Alanine-tRNA ligase, class IIc Ala-tRNA-lgiase_IIc Family
IPR018165 Alanyl-tRNA synthetase, class IIc, core domain Ala-tRNA-synth_IIc_core Domain
IPR022429 Alanine-tRNA ligase, archaea Ala-tRNA_lgiase_arc Family

0 Parent Features

10 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
Dock-Bregeon AC Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. 2004 Mol Cell 16 375-86
Ishijima J Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A resolution. 2006 Proteins 62 1133-7
Beebe K A domain for editing by an archaebacterial tRNA synthetase. 2004 Proc Natl Acad Sci U S A 101 5958-63
Beebe K Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. 2003 EMBO J 22 668-75

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)