RNP2_METMA
ID RNP2_METMA Reviewed; 116 AA.
AC Q8PTU2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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=MM_2619;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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}.
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; AE008384; AAM32315.1; -; Genomic_DNA.
DR RefSeq; WP_011034532.1; NC_003901.1.
DR AlphaFoldDB; Q8PTU2; -.
DR SMR; Q8PTU2; -.
DR STRING; 192952.MM_2619; -.
DR EnsemblBacteria; AAM32315; AAM32315; MM_2619.
DR GeneID; 44088069; -.
DR GeneID; 66134560; -.
DR KEGG; mma:MM_2619; -.
DR PATRIC; fig|192952.21.peg.3012; -.
DR eggNOG; arCOG01365; Archaea.
DR HOGENOM; CLU_137733_1_0_2; -.
DR OMA; NPWLIDY; -.
DR Proteomes; UP000000595; 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 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW tRNA processing.
FT CHAIN 1..116
FT /note="Ribonuclease P protein component 2"
FT /id="PRO_0000140022"
SQ SEQUENCE 116 AA; 12653 MW; F4FE4B094476C847 CRC64;
MKRLLPSLRA KKRYLAFELI SEEPASRSDI VKEVMSSASS LLGDVTTSDC DIRVLGFENG
KGIIQCSHTK VKQTRASLAA LTRINGKRAT LHVLGVSGTV KRATEKFLQD EGVFSS