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AARS

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. [provided by RefSeq, Jul 2008]
Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets

Predicted location

Intracellular

Single cell type specificity

Group enriched (Cytotrophoblasts, Syncytiotrophoblasts, Extravillous trophoblasts, Hofbauer cells, Cardiomyocytes)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Monomer (PubMed:27911835). Interacts with ANKRD16; the interaction is direct (By similarity).

Molecular function

Aminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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