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   25-MAY-2022, entry version 105.
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}; 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}.
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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   EnsemblBacteria; AAB85192; AAB85192; MTH_687.
DR   GeneID; 24853829; -.
DR   KEGG; mth:MTH_687; -.
DR   PATRIC; fig|187420.15.peg.668; -.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OMA; NPWLIDY; -.
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; -; 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; SSF160350; 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