AC MF_03035; DC Protein; auto TR HAMAP; MF_03035; -; 1; level=0 XX Names: Clp1 XX ID CLP1 case DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase Clp1; DE EC=2.7.1.78; DE AltName: Full=Polyadenylation factor Clp1; DE AltName: Full=Polynucleotide kinase Clp1; DE AltName: Full=Pre-mRNA cleavage complex II protein Clp1; else case DE RecName: Full=mRNA cleavage and polyadenylation factor ; else case DE RecName: Full=Protein clpf-1; else DE RecName: Full=Protein CLP1 homolog; end case case or GN Name=CLP1; else case GN Name=clpf-1; end case XX case CC -!- FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl CC groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), CC double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA CC is phosphorylated more efficiently than dsDNA, and the RNA component of CC a DNA:RNA hybrid is phosphorylated more efficiently than the DNA CC component. Appears to have roles in both tRNA splicing and mRNA 3'-end CC formation. Component of the tRNA splicing endonuclease complex. CC Phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA CC splicing; this phosphorylation event is a prerequisite for the CC subsequent ligation of the two exon halves and the production of a CC mature tRNA. Component of the pre-mRNA cleavage complex II (CF-II), CC which seems to be required for mRNA 3'-end formation. Also CC phosphorylates the 5'-terminus of exogenously introduced short CC interfering RNAs (siRNAs), which is a necessary prerequisite for their CC incorporation into the RNA-induced silencing complex (RISC). However, CC endogenous siRNAs and microRNAs (miRNAs) that are produced by the CC cleavage of dsRNA precursors by @gn(DICER1) already contain a 5'- CC phosphate group, so this protein may be dispensible for normal RNA- CC mediated gene silencing. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end CC 5'-phospho-2'-deoxyribonucleoside-DNA + ADP + H(+); CC Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412, CC ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'- CC phospho-ribonucleoside-RNA + ADP + H(+); Xref=Rhea:RHEA:54580, CC Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:15179, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:138282, ChEBI:CHEBI:138284, CC ChEBI:CHEBI:456216; EC=2.7.1.78; else case CC -!- FUNCTION: Component of the cleavage factor IA (CF IA) complex, which is CC involved in the endonucleolytic cleavage during polyadenylation- CC dependent pre-mRNA 3'-end formation. Associates with HRB1/CF IB to form CC the cleavage factor I (CF I) complex. CF I is required for correct CC positioning of a larger protein complex, the cleavage and CC polyadenylation factor (CPF) complex, which contains the catalytic CC subunits executing mRNA cleavage and polyadenylation. CLP1 mediates CC interactions between CF IA and CPF factors. CLP1 is also involved in CC maintaining the CF IA interaction with the C-terminal domain of RNA Pol CC II largest subunit via PCF11, which links pre-mRNA 3'-end processing to CC transcription termination. else CC -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation- CC dependent pre-mRNA 3'-end formation. end case case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; end case case CC -!- SUBUNIT: Component of the tRNA splicing endonuclease complex, composed CC of CLP1, TSEN2, TSEN15, TSEN34 and TSEN54. Component of pre-mRNA CC cleavage complex II (CF-II). Also associates with numerous components CC of the pre-mRNA cleavage complex I (CF-I/CFIm), including NUDT21, CC CPSF2, CPSF3, CPSF6 and CPSF7. Interacts with CSTF2 and SYMPK. else case CC -!- SUBUNIT: Component of the tRNA splicing endonuclease complex. Component CC of pre-mRNA cleavage complex II (CF-II). else case CC -!- SUBUNIT: Component of the cleavage factor IA (CF IA) complex, which is CC a heterohexameric complex with 2:2:1:1 stoichiometry of RNA14, RNA15, CC PCF11 and CLP1. It contains 2 copies of a RNA14-RNA15 dimer and 1 copy CC of CLP1-PCF11. The complex interacts with the cleavage factor HRB1/CF CC IB to form the cleavage factor I (CF I) complex, and binds to RNA. CC Interacts directly with PCF11. Interacts with the CPF components CFT1, CC PTA1, PFS2, YSH1 and SSU72. else case CC -!- SUBUNIT: Component of a pre-mRNA cleavage factor complex. Interacts CC directly with PCF11. end case CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily. case CC -!- CAUTION: May lack the polyribonucleotide 5'-hydroxyl-kinase and CC polynucleotide 5'-hydroxyl-kinase activities that are characteristic of CC the human ortholog. end case XX DR Pfam; PF06807; Clp1; 1; trigger=no XX KW mRNA processing KW Nucleus case KW ATP-binding KW Nucleotide-binding end case case KW Kinase KW Transferase KW tRNA processing end case case KW Magnesium KW Manganese KW Nickel end case XX GO GO:0005524; F:ATP binding GO GO:0031124; P:mRNA 3'-end processing GO GO:0005634; C:nucleus case GO GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity GO GO:0051736; F:ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity GO GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation GO GO:0070922; P:RISC complex assembly end case case GO GO:0000214; C:tRNA-intron endonuclease complex end case case or GO GO:0005849; C:mRNA cleavage factor complex end case XX FT From: CLP1_YEAST (Q08685) FT BINDING 133..138 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Tag: atp; Condition: x-x-G-[KR]-[ST]-[STA] FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [DE] FT BINDING 72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [KR] XX Size: 423-665; Related: None; Template: Q92989; Q08685; Q9SR06; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.18 2024/01/30 //