InterPro : IPR002306

Name  Tryptophan-tRNA ligase Short Name  Trp-tRNA-ligase
Type  Family Description  This entry represents tryptophan-tRNA lgiase (also known as tryptophanyl-tRNA synthetase) (). The enzyme is widely distributed, being found in archaea, bacteria and eukaryotes. The crystal structure of tryptophan-tRNA ligase has been solved [].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[].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.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR020653 Tryptophan-tRNA ligase, archaea Tryptophan-tRNA-ligase_arc Family
IPR024109 Tryptophan-tRNA ligase, bacterial-type Trp-tRNA-ligase_bac-type Family

2 Contains

Id Name Short Name Type
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
Ilyin VA 2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site. 2000 Protein Sci 9 218-31



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)