Polyribonucleotide 5-hydroxyl-kinase Clp1 is a component of the cleavage factor IA (CF IA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation []. It is involved in both the endonucleolyitc cleavage and polyadenylation steps of mRNA 3'-end maturation []. Human Clp1 can also function as a tRNA splicing enzyme [, ]. In human, mutations in Clp1 affect tRNA biogenesis and lead to impairment of both peripheral and central nervous system function, causing severe motor-sensory defects, cortical dysgenesis and microcephaly [].
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 [, , ].This entry represents the C-terminal domain of Clp1.
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.
This entry includes Clp1 and Grc3/NOL9.Polyribonucleotide 5-hydroxyl-kinase Clp1 is a component of the cleavage factor IA (CF IA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation []. It is involved in both the endonucleolyitc cleavage and polyadenylation steps of mRNA 3'-end maturation []. Human Clp1 can also function as a tRNA splicing enzyme [, ]. In human, mutations in Clp1 affect tRNA biogenesis and lead to impairment of both peripheral and central nervous system function, causing severe motor-sensory defects, cortical dysgenesis and microcephaly [].Grc3 and its homologue, NOL9, are polynucleotide 5'-kinases involved in rRNA processing [, ].
Clp1 function involves some degree of adenine or guanine nucleotide binding and participates in the 3' end processing of mRNAs in eukaryotes []. 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/β-fold and a central domain that binds ATP [, ]. This entry represents the N-terminal domain involved in DNA binding [].
Clp1 function involves some degree of adenine or guanine nucleotide binding and participates in the 3' end processing of mRNAs in eukaryotes []. Both human Clp1 (hsClp1) and Saccharomyces cerevisiae Clp1 (scClp1) were identified as components of the pre-mRNA 3end-processing machinery. WhereashsClp1 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 involved in DNA binding [], a C-terminal domain containing a novel alpha/β-fold and a central domain that binds ATP [, ]. This entry represents the short N-terminal domain of the pre-mRNA cleavage complex II protein Clp1.
This entry represents the P-loop containing domain of Clp1, a mRNA cleavage and polyadenylation factor. Clp1 is essential for 3'-end processing of mRNAs. This domain carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide [].
This entry includes Pcf11 and related proteins from animals, fungi and plants.PCF11 is a subunit and essential component of cleavage and polyadenylation factor IA (CF IA), involved in pre-mRNA 3' end processing and in transcription termination [, , ]. It has been reported that PCF11-mediated termination is essential for vertebrate development and its own levels are maintained by an auto-regulatory mechanism involving premature termination of its transcript []. PCF11 binds to Clp1, another subunit of CFIA whose interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery [, ].
This entry represents the Clp1-interacting domain of Pcf11, found towards the C-terminal end of these proteins.PCF11 is a subunit and essential component of cleavage and polyadenylation factor IA (CF IA), involved in pre-mRNA 3' end processing and in transcription termination [, , ]. It has been reported that PCF11-mediated termination is essential for vertebrate development and its own levels are maintained by an auto-regulatory mechanism involving premature termination of its transcript []. PCF11 binds to Clp1, another subunit of CFIA whose interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery [, ].
This entry represents a group of fungal nucleolar proteins, including Dnt1 from fission yeasts and Tof2/Net1 from budding yeasts. Net1 regulates the homologous MEN (mitotic exit network) pathway by sequestering Cdc14 phosphatase in the nucleolus before mitotic exit []. Dnt1 is a homologue of Net1. Both Dnt1 and Net1 negatively regulate the homologous SIN (septation initiation network) and MEN pathways. They are both required for rDNA silencing and minichromosome maintenance. However, Net1 regulates the MEN through the Cdc14 phosphatase, while Dnt1 inhibit SIN signaling independently of Clp1 (a Cdc14-family phosphatase) [].Tof2 is a paralogue of Net1. It is required for rDNA silencing and mitotic rDNA condensation [, ]. It coordinates the biphasic release of Cdc14 during anaphase by restraining a population of Cdc14 in the nucleolus [].
