UniProt ID: A0A0R4I9C1 |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L- tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; Evidence={ECO:0000256|ARBA:ARBA00034238}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10221; Evidence={ECO:0000256|ARBA:ARBA00034238}; SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU361234}. |
UniProt ID: Q6TGS6 |
FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250|UniProtKB:P54577}. CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L- tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; Evidence={ECO:0000250|UniProtKB:P54577}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10221; Evidence={ECO:0000250|UniProtKB:P54577}; SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P54577}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54577}. Nucleus {ECO:0000250|UniProtKB:P54577}. DOMAIN: The nuclear localization signal, which mediates localization to the nucleus, is also important for interacting with tRNA(Tyr), suggesting that it is sterically blocked when tRNA(Tyr) is bound. {ECO:0000250|UniProtKB:P54577}. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. {ECO:0000305}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |