The domain within your query sequence starts at position 425 and ends at position 627; the E-value for the Clp1 domain shown below is 5.8e-46.

GWVSDNGLRLLVDLIRVLSPNYVVQLYSDRCKFTPTLTSEYVELTDGLYTKSKIKRYRGF
EIPEFGDNLEFTYEEKESSPLPVFTGHVLLSVHSEFLSSKNEKNRAKYNRIFRDLAVLGY
LSQLMLPVPESLSPLHSLTPYQVPFSAVAIRVLHADVAPTHILYAVNASWVGLCRIVDDM
KGYTRGPILLAQNPICDCLGFGE

Clp1

Clp1
PFAM accession number:PF06807
Interpro abstract (IPR010655):

The yeast Clp1 is a subunit of cleavage factor IA (CF IA) and is involved in mRNA cleavage and polyadenylation [(PUBMED:22216186)]. Clp1 also mediates interactions between CF IA and another complex of the yeast mRNA cleavage and polyadenylation machinery, the Cleavage-Polyadenylation Factor (CPF) [(PUBMED:21993299)]. It seems that human Clp1 and yeast Clp1 are not functional orthologues [(PUBMED:18648070)]. Human Clp1, and its archeal homologue [(PUBMED:19299550)], but not yeast Clp1, are 5'-OH polynucleotide kinases. In humans Clp1 functions as a RNA kinase important in tRNA splicing [(PUBMED:18648070), (PUBMED:24766809)], and is also implicated in mRNA and siRNA maturation [(PUBMED:15109492), (PUBMED:17495927), (PUBMED:17786051)].

This entry represents the C-terminal domain of Clp1.

GO process:mRNA 3'-end processing (GO:0031124)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Clp1