| Primary Identifier | IPR038238 | Type | Homologous_superfamily |
| Short Name | Clp1_C_sf |
| description | The yeast Clp1 is a subunit of cleavage factor IA (CF IA) and is involved in mRNA cleavage and polyadenylation []. Clp1 also mediates interactions between CF IA and another complex of the yeast mRNA cleavage and polyadenylation machinery, the Cleavage-Polyadenylation Factor (CPF) []. It seems that human Clp1 and yeast Clp1 are not functional orthologues []. Human Clp1, and its archeal homologue [], but not yeast Clp1, are 5'-OH polynucleotide kinases. In humans Clp1 functions as a RNA kinase important in tRNA splicing [, ], and is also implicated in mRNA and siRNA maturation [, , ].Clp1 contains three domains, a small N-terminal beta sandwich domain, a C-terminal domain containing a novel alpha/β-fold and a central domain that binds ATP []. This entry represents the Clp1 C-terminal domain superfamily. |
