The domain within your query sequence starts at position 425 and ends at position 665; the E-value for the Clp1 domain shown below is 1.9e-67.
GWVSDNGLRLLVDLIRVLSPNYVVQLYSDRCKFTPTLTSEYVELTDGLYTKSKIKRYRGF EIPEFGDNLEFTYEEKESSPLPVFTGHVLLSVHSEFLSSKNEKNRAKYNRIFRDLAVLGY LSQLMLPVPESLSPLHSLTPYQVPFSAVAIRVLHADVAPTHILYAVNASWVGLCRIVDDM KGYTRGPILLAQNPICDCLGFGICRGIDMDKRTYHILTPLPPEELKTVNCLLVGSISIPH C
Clp1 |
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PFAM accession number: | PF06807 |
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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