InterPro domain: IPR038239

Clp1 function involves some degree of adenine or guanine nucleotide binding and participates in the 3' end processing of mRNAs in eukaryotes [ 1 ]. Both human Clp1 (hsClp1) and Saccharomyces cerevisiae Clp1 (scClp1) were identified as components of the pre-mRNA 3end-processing machinery. Whereas hsClp1 was shown to also be part of the tRNA endonuclease complex, scClp1 exclusively contributes to mRNA maturation and appears to be enzymatically inactive.

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 [ 2 , 2 ]. This entry represents the N-terminal domain involved in DNA binding [ 3 ].

1. Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. Nucleic Acids Res. 35, 87-99
2. Structural basis for ATP loss by Clp1p in a G135R mutant protein. Biochimie 101, 203-7
3. RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase Clp1. Mol Cell 54, 975-86