InterPro : IPR002307

Name  Tyrosine-tRNA ligase Short Name  Tyr-tRNA-ligase
Type  Family Description  Tyrosine-tRNA ligases (also known as Tyrosyl-tRNA synthetases) () are widely distributed, being found in archaea, bacteria and eukaryotes. Studies on tyrosine-tRNA ligase have shown that the 'KMSKS' motif plays a role in the initial binding of tRNA(Tyr) to tyrosine-tRNA ligase [].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.The class Ia aminoacyl-tRNA synthetases consist of the isoleucyl, methionyl, valyl, leucyl, cysteinyl, and arginyl-tRNA synthetases; the class Ib include the glutamyl and glutaminyl-tRNA synthetases, and the class Ic are the tyrosyl and tryptophanyl-tRNA synthetases[].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR024088 Tyrosine-tRNA ligase, bacterial-type Tyr-tRNA-ligase_bac-type Family
IPR023617 Tyrosine-tRNA ligase, archaeal/eukaryotic-type Tyr-tRNA-ligase_arc/euk-type Family

3 Contains

Id Name Short Name Type
IPR002942 RNA-binding S4 domain S4_RNA-bd Domain
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain
IPR001412 Aminoacyl-tRNA synthetase, class I, conserved site aa-tRNA-synth_I_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002305 Aminoacyl-tRNA synthetase, class Ic aa-tRNA-synth_Ic Family

8 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
Ribas de Pouplana L Aminoacyl-tRNA synthetases: potential markers of genetic code development. 2001 Trends Biochem Sci 26 591-6
Xin Y The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr). 2000 Biochemistry 39 340-7



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)