ID RNP2_METTH Reviewed; 124 AA. AC O26783; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000255|HAMAP-Rule:MF_00755}; DE Short=RNase P component 2 {ECO:0000255|HAMAP-Rule:MF_00755}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00755}; DE AltName: Full=Pop5 {ECO:0000255|HAMAP-Rule:MF_00755}; GN Name=rnp2 {ECO:0000255|HAMAP-Rule:MF_00755}; GN OrderedLocusNames=MTH_687; OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H; RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997; RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., RA Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: RT functional analysis and comparative genomics."; RL J. Bacteriol. 179:7135-7155(1997). RN [2] RP FUNCTION, SUBUNIT, AND INDUCTION. RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H; RX PubMed=12003490; DOI=10.1017/s1355838202028492; RA Hall T.A., Brown J.W.; RT "Archaeal RNase P has multiple protein subunits homologous to eukaryotic RT nuclear RNase P proteins."; RL RNA 8:296-306(2002). 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_00755, ECO:0000269|PubMed:12003490}. 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_00755}; CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein CC subunits. {ECO:0000255|HAMAP-Rule:MF_00755, CC ECO:0000269|PubMed:12003490}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755}. CC -!- INDUCTION: Constitutively expressed (at protein level). CC {ECO:0000269|PubMed:12003490}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 2 family. {ECO:0000255|HAMAP-Rule:MF_00755}. 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; AE000666; AAB85192.1; -; Genomic_DNA. DR PIR; E69191; E69191. DR RefSeq; WP_010876326.1; NC_000916.1. DR AlphaFoldDB; O26783; -. DR SMR; O26783; -. DR IntAct; O26783; 1. DR STRING; 187420.MTH_687; -. DR PaxDb; 187420-MTH_687; -. DR EnsemblBacteria; AAB85192; AAB85192; MTH_687. DR GeneID; 1470648; -. DR KEGG; mth:MTH_687; -. DR PATRIC; fig|187420.15.peg.668; -. DR HOGENOM; CLU_137733_1_0_2; -. DR InParanoid; O26783; -. DR Proteomes; UP000005223; 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:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1. DR HAMAP; MF_00755; RNase_P_2; 1. DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like. DR InterPro; IPR038085; Rnp2-like_sf. DR InterPro; IPR016434; Rnp2_archaea. DR Pfam; PF01900; RNase_P_Rpp14; 1. DR PIRSF; PIRSF004952; RNase_P_2; 1. DR SUPFAM; SSF160350; Rnp2-like; 1. PE 1: Evidence at protein level; KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome; KW tRNA processing. FT CHAIN 1..124 FT /note="Ribonuclease P protein component 2" FT /id="PRO_0000140024" SQ SEQUENCE 124 AA; 14568 MW; 5034454559C101A6 CRC64; MKILPPTLRV PRRYIAFEVI SERELSREEL VSLIWDSCLK LHGECETSNF RLWLMKLWRF DFPDAVRVRG ILQCQRGYER RVMMALTCAH HHSGVRVAIH ILGLSGTIRS ATQKFIKPSK KDKY //