ID RNP4_METJA Reviewed; 128 AA. AC Q58372; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 110. 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}; OrderedLocusNames=MJ0962; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18558617; DOI=10.1093/nar/gkn360; RA Pulukkunat D.K., Gopalan V.; RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into the RT roles of RNA and protein cofactors in RNase P catalysis."; RL Nucleic Acids Res. 36:4172-4180(2008). RN [3] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012; RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.; RT "Cooperative RNP assembly: complementary rescue of structural defects by RT protein and RNA subunits of archaeal RNase P."; RL J. Mol. Biol. 411:368-383(2011). RN [4] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RX PubMed=22298511; DOI=10.1093/nar/gks013; RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., RA Gopalan V.; RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional RT dependence of archaeal and eukaryal RNase P on multiple protein RT cofactors."; RL Nucleic Acids Res. 40:4666-4680(2012). 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, ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. 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 protein CC subunits. Forms a subcomplex with Rnp1 which stimulates the catalytic CC RNA. {ECO:0000269|PubMed:18558617, ECO:0000269|PubMed:21683084, CC ECO:0000269|PubMed:22298511}. 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; L77117; AAB98964.1; -; Genomic_DNA. DR PIR; B64420; B64420. DR RefSeq; WP_010870476.1; NC_000909.1. DR PDB; 6K0A; EM; 4.60 A; G/H=1-128. DR PDB; 6K0B; EM; 4.30 A; G/H=1-128. DR PDBsum; 6K0A; -. DR PDBsum; 6K0B; -. DR AlphaFoldDB; Q58372; -. DR EMDB; EMD-9900; -. DR SMR; Q58372; -. DR STRING; 243232.MJ_0962; -. DR PaxDb; 243232-MJ_0962; -. DR EnsemblBacteria; AAB98964; AAB98964; MJ_0962. DR GeneID; 1451860; -. DR KEGG; mja:MJ_0962; -. DR eggNOG; arCOG04345; Archaea. DR HOGENOM; CLU_079140_3_1_2; -. DR InParanoid; Q58372; -. DR OrthoDB; 10058at2157; -. DR PhylomeDB; Q58372; -. DR Proteomes; UP000000805; 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 Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; tRNA processing; Zinc. FT CHAIN 1..128 FT /note="Ribonuclease P protein component 4" FT /id="PRO_0000153852" FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757" SQ SEQUENCE 128 AA; 15567 MW; 462D677CE5B159D3 CRC64; MKKFLEKKLK KIAYERIDIL MSLAEEEAKK GNWDRAKRYV YLARRIAMKM RIRFPKKWKR RICKKCGTFL LYGRNARVRI KSKRYPHVVI TCLECGAIYR IPMIREKKEK RRKKLEERLK AKSNSQTS //