The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure.
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Protein Aliases: ATP-dependent RNA helicase A; D-E-A-D (aspartate-glutamate-alanine-aspartate) box polypeptide 9; DEAD (aspartate-glutamate-alanine-aspartate) box polypeptide 9; DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 9; DEAH (Asp-Glu-Ala-His) box helicase 9; DEAH (Asp-Glu-Ala-His) box polypeptide 9; DEAH box protein 9; DExH-box helicase 9; FLJ17406; Leukophysin; LKP; mHEL-5; NDH II; Nuclear DNA helicase II; OTTHUMP00000033287; RHA; RNA helicase; RNA helicase A
Gene Aliases: AI326842; DDX9; DHX9; HEL-5; LKP; mHEL-5; NDH2; NDHII; RHA
Molecular Function: RNA helicase