6.1.1.9	?	-	529	
6.1.1.9	?	x * 140000, SDS-PAGE, valyl-tRNA synthetase component purified from the heterotypic complex	528	
6.1.1.9	monomer	1 * 100000, SDS-PAGE	-, 546	
6.1.1.9	monomer	1 * 108000, SDS-PAGE	-, 67	
6.1.1.9	monomer	1 * 125000, SDS-PAGE	-, 529	
6.1.1.9	monomer	1 * 126000, urea-SDS-PAGE	434, 537	
6.1.1.9	monomer	1 * 140000, SDS-PAGE	-, 11, 529, 530	
6.1.1.9	monomer	the high molecular weight valyl-tRNA synthetase is a homotypic tetramer which converts to the monomeric valyl-tRNA synthetase after cleavage of a small peptide	530	
6.1.1.9	additional information	glp-4 VARS-2 has two tRNA recognition domains (1 and 2), a split class 1 Rossmann-fold, which functions in catalyzing the synthesis of aminoacyl-adenylate and aminoacyl-tRNAval, an editing domain, and the connective polypeptide (CP1) domain, which also functions in post-transfer editing. Structural analysis of glp-4 VARS-2, homology modeling, overview	745020	
6.1.1.9	additional information	the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview	673963