InterPro : IPR005146

Name  B3/B4 tRNA-binding domain Short Name  B3/B4_tRNA-bd
Type  Domain Description  This entry represents the B3/B4 domain found in tRNA synthetase beta subunits as well as in some non-tRNA synthetase proteins. This domain has a 3-layer structure, and contains a beta-sandwich fold of unusual topology, and contains a putative tRNA-binding structural motif []. In Thermus thermophilus, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit of tRNA synthetase indicates structural relationships among different families of RNA-binding proteins. Aminoacyl-tRNA synthetases can catalyse editing reactions to correct errors produced during amino acid activation and tRNA esterification, in order to prevent the attachment of incorrect amino acids to tRNA. The B3/B4 domain of the beta subunit contains an editing site, which lies close to the active site on the alpha subunit []. Disruption of this site abolished tRNA editing, a process that is essential for faithful translation of the genetic code.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR020825 Phenylalanyl-tRNA synthetase, B3/B4 Phe-tRNA_synthase_B3/B4 Domain

0 Contains

2 Found In

Id Name Short Name Type
IPR004531 Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic Phe-tRNA-synth_IIc_bsu_arc Family
IPR004532 Phenylalanine-tRNA ligase, class IIc, beta subunit Phe-tRNA-ligase_IIc_bsu Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Mosyak L Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. 1995 Nat Struct Biol 2 537-47
Roy H Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. 2004 EMBO J 23 4639-48



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)