AARS2
Domain
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Function
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Involvement in disease
Combined oxidative phosphorylation deficiency 8
COXPD8
A mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected.
None
The disease is caused by variants affecting the gene represented in this entry.
Leukoencephalopathy, progressive, with ovarian failure
LKENP
An autosomal recessive neurodegenerative disorder characterized by childhood- to adulthood-onset of signs of neurologic deterioration consisting of ataxia, spasticity, and cognitive decline with features of frontal lobe dysfunction. Brain MRI shows leukoencephalopathy with striking involvement of deep white matter, and cerebellar atrophy. All female patients develop premature ovarian failure.
None
The disease is caused by variants affecting the gene represented in this entry.
Sequence Similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Cellular localization
- Mitochondrion
Alternative names
AARSL, KIAA1270, AARS2, Alanyl-tRNA synthetase, AlaRS