Description: Homo sapiens alanyl-tRNA synthetase (AARS1), mRNA. RefSeq Summary (NM_001605): 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]. Transcript (Including UTRs) Position: hg19 chr16:70,286,297-70,323,412 Size: 37,116 Total Exon Count: 21 Strand: - Coding Region Position: hg19 chr16:70,286,624-70,316,666 Size: 30,043 Coding Exon Count: 20
ID:SYAC_HUMAN DESCRIPTION: RecName: Full=Alanine--tRNA ligase, cytoplasmic; EC=6.1.1.7; AltName: Full=Alanyl-tRNA synthetase; Short=AlaRS; AltName: Full=Renal carcinoma antigen NY-REN-42; 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 (By similarity). CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). COFACTOR: Binds 1 zinc ion per subunit (Potential). SUBUNIT: Monomer. SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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 (By similarity). DOMAIN: The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli. PTM: ISGylated. DISEASE: Defects in AARS are the cause of Charcot-Marie-Tooth disease type 2N (CMT2N) [MIM:613287]. It is an axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies(designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
Pfam Domains: PF01411 - tRNA synthetases class II (A) PF02272 - DHHA1 domain PF07973 - Threonyl and Alanyl tRNA synthetase second additional domain
SCOP Domains: 101353 - Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS) 55681 - Class II aaRS and biotin synthetases 55186 - ThrRS/AlaRS common domain
ModBase Predicted Comparative 3D Structure on P49588
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
