InterPro : IPR010978

Name  tRNA-binding arm Short Name  tRNA-bd_arm
Type  Domain Description  This entry represents an alpha-helical tRNA-binding arm found in class I and II aminoacyl-tRNA synthetase enzymes, as well as in the methicillin resistance protein FemA.The tRNA-binding arm domain is conserved between class I and class II aminoacyl-tRNA synthetase enzymes (), consisting of two alpha helices in an antiparallel hairpin with a left-handed twist. The appended tRNA-binding domains recognise a small number of nucleotides that are conserved specifically in each cognate tRNA species for the discrimination between the cognate and noncognate tRNAs []. These nucleotides are called identity elements, and constitute the identity set. The tRNA-binding arm occurs as the C-terminal domain in some class I enzymes, such as valyl-tRNA synthetase, and as the N-terminal domain in some class II enzymes, such as phenylalanyl-tRNA synthetase.The methicillin resistance protein, FemA (factors essential for methicillin resistance), contains a probable tRNA-binding arm that is similar in structure to those found in tRNA synthetases. In FemA, the tRNA-binding arm is inserted into the C-terminal NAT-like domain, and is thought to bind tRNA-glycine. FemA, along with FemB and FemX, plays a vital role in peptidoglycan biosynthesis specific to Staphylococci [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

3 Child Features

Id Name Short Name Type
IPR015866 Serine-tRNA synthetase, type1, N-terminal Ser-tRNA-synth_1_N Domain
IPR019499 Valyl-tRNA synthetase, tRNA-binding arm Val-tRNA_synth_tRNA-bd Domain
IPR004188 Phenylalanine-tRNA ligase, class II, N-terminal Phe-tRNA_ligase_II_N Domain

0 Contains

2 Found In

Id Name Short Name Type
IPR002317 Serine-tRNA ligase, type1 Ser-tRNA-ligase_type_1 Family
IPR003447 FemABX peptidyl transferase FEMABX Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Fukai S Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase. 2003 RNA 9 100-11
Benson TE X-ray crystal structure of Staphylococcus aureus FemA. 2002 Structure 10 1107-15



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)