InterPro domain: IPR038238

The yeast Clp1 is a subunit of cleavage factor IA (CF IA) and is involved in mRNA cleavage and polyadenylation [ 1 ]. Clp1 also mediates interactions between CF IA and another complex of the yeast mRNA cleavage and polyadenylation machinery, the Cleavage-Polyadenylation Factor (CPF) [ 2 ]. It seems that human Clp1 and yeast Clp1 are not functional orthologues [ 3 ]. Human Clp1, and its archeal homologue [ 4 ], but not yeast Clp1, are 5'-OH polynucleotide kinases. In humans Clp1 functions as a RNA kinase important in tRNA splicing [ 5 , 5 ], and is also implicated in mRNA and siRNA maturation [ 6 , 7 , 8 ].

Clp1 contains three domains, a small N-terminal beta sandwich domain, a C-terminal domain containing a novel alpha/beta-fold and a central domain that binds ATP [ 9 ]. This entry represents the Clp1 C-terminal domain superfamily.

1. The P-loop domain of yeast Clp1 mediates interactions between CF IA and CPF factors in pre-mRNA 3' end formation. PLoS ONE 6, e29139
2. The interaction of Pcf11 and Clp1 is needed for mRNA 3'-end formation and is modulated by amino acids in the ATP-binding site. Nucleic Acids Res. 40, 1214-25
3. Human RNA 5'-kinase (hClp1) can function as a tRNA splicing enzyme in vivo. RNA 14, 1737-45
4. Characterization of a thermostable archaeal polynucleotide kinase homologous to human Clp1. RNA 15, 923-31
5. Human CLP1 mutations alter tRNA biogenesis, affecting both peripheral and central nervous system function. Cell 157, 636-50
6. Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation. Cell 117, 311-21
7. The human RNA kinase hClp1 is active on 3' transfer RNA exons and short interfering RNAs. Nature 447, 222-6
8. hClp1: a novel kinase revitalizes RNA metabolism. Cell Cycle 6, 2133-7
9. Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. Nucleic Acids Res. 35, 87-99