C16orf42 (Vector Vector will be determined during the manufacturing process, either pENTR223.1 or pU

Length: 531 Sequence: atgcgaggga gccacttgcg cctgttgccc tacctggtgg ccgccaaccc cgtgaactat ggccggccct acagactttc ctgcgtggaa gcgtttgctg ccaccttctg catcgtaggc tttccagacc ttgctgtcat tttgctgcgg aagtttaaat ggggcaaggg cttcttggac ctgaaccgcc agctcctgga caagtacgcg gcctgcggca gcccggagga ggtgctgcag gcggagcagg agttcttggc caatgccaag gagagccccc aggaggagga gatcgatccc ttcgatgtgg attcagggag agagtttgga aaccccaaca ggcctgtggc cagcacccgg ctgccctcgg acactgatga cagtgatgcg tctgaggacc cagggcctgg cgccgagcgc ggaggagcca gcagcagctg ctgtgaagag gagcagacgc agggacgggg ggctgaggcc agggccccgg ctgaggtttg gaaaggaatc aagaaacggc agagagactg Protein function: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template (PubMed:3516995). Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate (PubMed:3516995). tRNA 3'-terminal CCA addition is required both for tRNA processing and repair (PubMed:22076379). Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs (PubMed:22076379). While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded (PubMed:22076379). 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. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi (PubMed:15210699). Displays a metal-independent phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP (PubMed:15210699). Without metal or in the presence of Mg(2+), this protein hydrolyzes 2',3'-cyclic substrates with the formation of 2'- nucleotides, whereas in the presence of Ni(2+), it also produces some 3'-nucleotides (PubMed:15210699). These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases (PubMed:15210699). [The UniProt Consortium]