ID RNP4_HYPBU Reviewed; 115 AA. AC A2BN51; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Ribonuclease P protein component 4 {ECO:0000255|HAMAP-Rule:MF_00757}; DE Short=RNase P component 4 {ECO:0000255|HAMAP-Rule:MF_00757}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00757}; DE AltName: Full=Rpp21 {ECO:0000255|HAMAP-Rule:MF_00757}; GN Name=rnp4 {ECO:0000255|HAMAP-Rule:MF_00757}; GN OrderedLocusNames=Hbut_1593; OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae; OC Hyperthermus. OX NCBI_TaxID=415426; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5; RX PubMed=17350933; DOI=10.1155/2007/745987; RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., RA She Q., Garrett R.A., Klenk H.-P.; RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."; RL Archaea 2:127-135(2007). CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP- CC Rule:MF_00757}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00757}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00757}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00757}; CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein CC subunits. {ECO:0000255|HAMAP-Rule:MF_00757}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 4 family. {ECO:0000255|HAMAP-Rule:MF_00757}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000493; ABM81412.1; -; Genomic_DNA. DR RefSeq; WP_011822730.1; NC_008818.1. DR AlphaFoldDB; A2BN51; -. DR SMR; A2BN51; -. DR STRING; 415426.Hbut_1593; -. DR EnsemblBacteria; ABM81412; ABM81412; Hbut_1593. DR GeneID; 4781977; -. DR KEGG; hbu:Hbut_1593; -. DR eggNOG; arCOG04345; Archaea. DR HOGENOM; CLU_079140_3_1_2; -. DR OrthoDB; 10058at2157; -. DR Proteomes; UP000002593; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule. DR Gene3D; 6.20.50.20; -; 1. DR HAMAP; MF_00757; RNase_P_4; 1. DR InterPro; IPR016432; RNP4. DR InterPro; IPR007175; Rpr2/Snm1/Rpp21. DR PANTHER; PTHR14742:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P21; 1. DR PANTHER; PTHR14742; RIBONUCLEASE P SUBUNIT P21; 1. DR Pfam; PF04032; Rpr2; 1. DR PIRSF; PIRSF004878; RNase_P_4; 1. PE 3: Inferred from homology; KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; tRNA processing; Zinc. FT CHAIN 1..115 FT /note="Ribonuclease P protein component 4" FT /id="PRO_1000194593" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" SQ SEQUENCE 115 AA; 13132 MW; 7C447AC1AAC7137C CRC64; MSGSKAKSRE LARDVALQAI RTLYLAAVDA VRRGDYELAR RLVAEADETR RVMRLRKPRF LRRGVCRNCS LPLVPGVTAR YRLVRDGSVT RLVVTCLACG YIHRHVLVQR RRGSR //