UniProt ID: F1QBG7 |
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. {ECO:0000256|HAMAP-Rule:MF_03133}. CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; SUBUNIT: Monomer. Interacts with ANKRD16; the interaction is direct. {ECO:0000256|HAMAP-Rule:MF_03133}. 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. {ECO:0000256|HAMAP-Rule:MF_03133}. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000256|HAMAP-Rule:MF_03133}. CAUTION: Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03133}. |
UniProt ID: Q1LVL2 |
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. {ECO:0000256|HAMAP-Rule:MF_03133}. CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03133}; SUBUNIT: Monomer. Interacts with ANKRD16; the interaction is direct. {ECO:0000256|HAMAP-Rule:MF_03133}. 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. {ECO:0000256|HAMAP-Rule:MF_03133}. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}. |
UniProt ID: Q1LVL3 |
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. {ECO:0000256|HAMAP-Rule:MF_03133}. CATALYTIC ACTIVITY: Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03133}; SUBUNIT: Monomer. Interacts with ANKRD16; the interaction is direct. {ECO:0000256|HAMAP-Rule:MF_03133}. 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. {ECO:0000256|HAMAP-Rule:MF_03133}. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}. |
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