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MGP000005

UniProt Annotations

Entry Information
Gene Namealanyl-tRNA synthetase
Protein EntrySYAC_HUMAN
UniProt IDP49588
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P49588-1; Sequence=Displayed; Name=2; IsoId=P49588-2; Sequence=VSP_057201, VSP_057202; Note=No experimental confirmation available.;
Catalytic ActivityATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP- Rule:MF_03133}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03133}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- Rule:MF_03133};
DiseaseCharcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: 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 degeneration 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. {ECO:0000269|PubMed:20045102, ECO:0000269|PubMed:22009580, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainConsists 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. {ECO:0000255|HAMAP-Rule:MF_03133}.
DomainThe 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. {ECO:0000269|PubMed:19661429}.
FunctionCatalyzes 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. {ECO:0000255|HAMAP-Rule:MF_03133}.
PtmISGylated. {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:16139798}.
SimilarityBelongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_03133}.
Subcellular LocationCytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
SubunitMonomer.
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