InterPro : IPR006195

Name  Aminoacyl-tRNA synthetase, class II Short Name  aa-tRNA-synth_II
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 recognises all class-II enzymes except for heterodimeric glycyl-tRNA synthetases and alanyl-tRNA synthetases.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR004364 Aminoacyl-tRNA synthetase, class II (D/K/N) aa-tRNA-synt_II Domain

3 Contains

Id Name Short Name Type
IPR002314 Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain aa-tRNA-synt_IIb_cons-dom Domain
IPR007214 YbaK/aminoacyl-tRNA synthetase-associated domain YbaK/aa-tRNA-synth-assoc-dom Domain
IPR004115 GAD-like domain GAD-like Domain

21 Found In

Id Name Short Name Type
IPR018150 Aminoacyl-tRNA synthetase, class II (D/K/N)-like aa-tRNA-synt_II-like Family
IPR004522 Asparagine-tRNA ligase Asn-tRNA-ligase Family
IPR004516 Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit HisRS/HisZ Family
IPR004523 Aspartyl-tRNA synthetases Asp-tRNA_synthase Family
IPR002317 Serine-tRNA ligase, type1 Ser-tRNA-ligase_type_1 Family
IPR004500 Prolyl-tRNA synthetase, class IIa, bacterial-type Pro-tRNA-synth_IIa_bac-type Family
IPR004524 Aspartate-tRNA ligase, class IIb, bacterial/mitochondrial-type Asp-tRNA-ligase_IIb_bac/mt Family
IPR002319 Phenylalanyl-tRNA synthetase Phenylalanyl-tRNA_Synthase Domain
IPR002320 Threonine-tRNA ligase, class IIa Thr-tRNA-ligase_IIa Family
IPR002313 Lysine-tRNA ligase, class II Lys-tRNA-ligase_II Family
IPR002312 Aspartyl/Asparaginyl-tRNA synthetase, class IIb Asp/Asn-tRNA-synth_IIb Family
IPR015807 Histidine-tRNA ligase His-tRNA-ligase Family
IPR004499 Proline-tRNA ligase, class IIa, archaeal-type Pro-tRNA-ligase_IIa_arc-type Family
IPR004529 Phenylalanyl-tRNA synthetase, class IIc, alpha subunit Phe-tRNA-synth_IIc_asu Family
IPR002315 Glycyl-tRNA synthetase tRNA-synt_gly Family
IPR004530 Phenylalanyl-tRNA synthetase, class IIc, mitochondrial Phe-tRNA-synth_IIc_mito Family
IPR004618 Aspartate--ammonia ligase AsnA Family
IPR020780 Aspartyl-tRNA synthetase, archaea Asp-tRNA-synth_arc Family
IPR004517 ATP phosphoribosyltransferase regulatory subunit HisZ Family
IPR012739 Pyrrolysyl-tRNA ligase Pyrrolysyl-tRNA_ligase Family
IPR005246 O-phosphoseryl-tRNA(Cys) ligase O-Pseryl-tRNA(Cys)_ligase Family

0 Parent Features

6 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

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)