alanyl-tRNA synthetase Protein Overview: Sequence, Structure, Function and Protein Interaction

alanyl-tRNA synthetase Protein Overview

alanyl-tRNA synthetase reagents

The AARS gene encodes alanyl-tRNA synthetase. Each of the amino acid synthetases catalyzes the attachment of their respective amino acids to the appropriate tRNA. The class II Escherichia coli and human alanyl-tRNA synthetases cross-acylate their respective tRNAs and require, for aminoacylation, an acceptor helix G3:U70 basepair that is conserved in evolution (Shiba et al., 1995). Some of the amino acid synthetases are targets for autoantibodies in the autoimmune disease polymyositis/dermatomyositis (Nichols et al., 1995) including histidyl-RS (142810), threonyl-RS (187790), isoleucyl-RS (600709), glycyl-RS (600287) and alanyl-RS.

alanyl-tRNA synthetase protein family

Belongs to the class-II aminoacyl-tRNA synthetase family.

alanyl-tRNA synthetase protein name

Recommended name
Alanine--tRNA ligase, cytoplasmic
Aliases
alanine tRNA ligase 1, cytoplasmic, AlaRS, CMT2N
Alternative name
Alanyl-tRNA synthetaseUniRule annotation Renal carcinoma antigen NY-REN-42

alanyl-tRNA synthetase Gene family protein

Aminoacyl tRNA synthetases, Class II

alanyl-tRNA synthetase Protein Sequence

Species Human alanyl-tRNA synthetase protein
Length 968
Mass (Da) 106810
Sequence Human alanyl-tRNA synthetase protein sequence
Species Mouse alanyl-tRNA synthetase protein
Length 968
Mass (Da) 106909
Sequence Mouse alanyl-tRNA synthetase protein sequence
Species Rat alanyl-tRNA synthetase protein
Length 968
Mass (Da) 106790
Sequence Rat alanyl-tRNA synthetase protein sequence

alanyl-tRNA synthetase Protein Molecular Weight & PI

Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Renal carcinoma antigen NY-REN-42)Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 1-968 Alanine--tRNA ligase, cytoplasmic.

Molecular weight (Da)

106810.44

Theoretical pI

5.34

alanyl-tRNA synthetase Protein Structure

Crystal Structure of wild type human AlaRS catalytic domain
Deposited
2014-12-24   Released:  2016-02-17
Deposition Author(s)
Zhou, H., He, W., Yang, X.L.
Organism(s)
Homo sapiens
Expression System
Escherichia coli BL21(DE3)
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
1.2780 Å
R-Value Free
0.179
R-Value Work
0.161
4XEM From PDB

Human alanyl-tRNA synthetase protein Secondary structure

alanyl-tRNA synthetase Protein Interaction

Recombinant alanyl-tRNA synthetase Protein Feature

alanyl-tRNA synthetase Protein, Mouse, Recombinant (His Tag)

High Purity
> 88 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

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