InterPro : IPR004532

Name  Phenylalanine-tRNA ligase, class IIc, beta subunit Short Name  Phe-tRNA-ligase_IIc_bsu
Type  Family Description  Phenylalanine-tRNA ligase () is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class IIc. In eubacteria, a small subunit (pheS gene) can be designated as beta (E. coli) or alpha subunit (see ). Reciprocally the large subunit(pheT gene) can be designated as alpha (E. coli) or beta. In all other kingdoms the two subunits have equivalent length in eukaryota, and can be identified by specific signatures. The enzyme from Thermus thermophilushas an alpha 2 beta 2 type quaternary structure and is one of the most complicated members of the synthetase family. Identification of phenylalanine-tRNA ligase as a member of class II aaRSs was based only on sequence alignment of the small alpha-subunit with other ligases [].This family describes the beta subunit. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps (see also ). This family represents the subfamily that includes the beta subunit from bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the N-terminal.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

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

6 Contains

Id Name Short Name Type
IPR009061 DNA binding domain, putative DNA-bd_dom_put Domain
IPR005147 tRNA synthetase, B5-domain tRNA_synthase_B5-dom Domain
IPR020825 Phenylalanyl-tRNA synthetase, B3/B4 Phe-tRNA_synthase_B3/B4 Domain
IPR005146 B3/B4 tRNA-binding domain B3/B4_tRNA-bd Domain
IPR002547 tRNA-binding domain tRNA-bd_dom Domain
IPR005121 Phenylalanine-tRNA ligase, beta subunit, ferrodoxin-fold anticodon-binding PheS_beta_Fdx_antiC-bd Domain

0 Found In

0 Parent Features

7 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
Mosyak L Phenylalanyl-tRNA synthetase from Thermus thermophilus has four antiparallel folds of which only two are catalytically functional. 1993 Biochimie 75 1091-8



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)