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trl1 | tRNA ligase 1; Required for the splicing of precursor tRNA molecules containing introns. The ligation activity requires three enzymatic activities: phosphorylation of the 5' terminus of the 3' half-tRNA in the presence of ATP, opening of the 2'3'-cyclic phosphodiester bond of the 5' half-tRNA leaving a 2'-phosphomonoester and ligation of the two tRNA halves in an ATP-dependent reaction; Belongs to the TRL1 family. (787 aa) | ||||
hbs1 | Elongation factor 1 alpha-like protein; Involved in protein translation. Together with dom34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non- functional ribosomes and degrade damaged mRNAs (By similarity). (592 aa) | ||||
cbf5 | H/ACA ribonucleoprotein complex subunit cbf5; Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridy [...] (474 aa) | ||||
ubi4 | Polyubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys [...] (382 aa) | ||||
dom34 | Protein dom34; Involved in protein translation. Together with hbs1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non- functional ribosomes and degrade damaged mRNAs. The complex formed by dom34 and hbs1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of hbs1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions [...] (390 aa) |