| Function | Nucleotidyltransferase that catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs, which is necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Promotes tRNA repair and recycling downstream of the ribosome-associated quality control (RQC) pathway by mediating addition of the tRNA 3'-terminal CCA following cleavage by ANKZF1 and repair by ELAC1. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs and tRNA-like transcripts. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs beginning with GG are marked with CCACCA and rapidly degraded. The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA. This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle. Isoform 2: Adds 2 C residues (CC-) to the 3' terminus of tRNA molecules instead of a complete CCA end as isoform 1 does (in vitro). |
| Protein Name | Cca Trna Nucleotidyltransferase 1 - MitochondrialMitochondrial Trna Nucleotidyl Transferase - Cca-AddingMt Cca-Adding EnzymeMt Trna Cca-DiphosphorylaseMt Trna Cca-PyrophosphorylaseMt Trna Adenylyltransferase |
| Database Links | Reactome: R-HSA-6784531Reactome: R-HSA-6785470 |
| Cellular Localisation | MitochondrionCytoplasmNucleus |
| Alternative Antibody Names | Anti-Cca Trna Nucleotidyltransferase 1 - Mitochondrial antibodyAnti-Mitochondrial Trna Nucleotidyl Transferase - Cca-Adding antibodyAnti-Mt Cca-Adding Enzyme antibodyAnti-Mt Trna Cca-Diphosphorylase antibodyAnti-Mt Trna Cca-Pyrophosphorylase antibodyAnti-Mt Trna Adenylyltransferase antibodyAnti-TRNT1 antibodyAnti-CGI-47 antibody |
Information sourced from Uniprot.org
