ID   RNP2_METM5              Reviewed;         130 AA.
AC   A4FXR3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=MmarC5_0686;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755}.
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; CP000609; ABO34997.1; -; Genomic_DNA.
DR   RefSeq; WP_011868451.1; NC_009135.1.
DR   AlphaFoldDB; A4FXR3; -.
DR   SMR; A4FXR3; -.
DR   STRING; 402880.MmarC5_0686; -.
DR   GeneID; 4928122; -.
DR   KEGG; mmq:MmarC5_0686; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OrthoDB; 19261at2157; -.
DR   Proteomes; UP000000253; 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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; tRNA processing.
FT   CHAIN           1..130
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_1000046622"
SQ   SEQUENCE   130 AA;  15270 MW;  72310EFF8A0E092C CRC64;
     MLKTLPPTLR EKKRYVALEI IFEEELFQKD VIAIVRNALM NYSGVLGCSR TNPWLIDYNH
     PYGILRISRE EVNNLRSSLS LTNEHRKKPI NIHIIGISNS VKHVREKFLH VPHEPYYKVI
     QKLKKKGPKK
//