RNP2_METLZ
ID RNP2_METLZ Reviewed; 147 AA.
AC A2ST53;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=Mlab_1342;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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}.
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; CP000559; ABN07509.1; -; Genomic_DNA.
DR RefSeq; WP_011833712.1; NC_008942.1.
DR AlphaFoldDB; A2ST53; -.
DR SMR; A2ST53; -.
DR STRING; 410358.Mlab_1342; -.
DR EnsemblBacteria; ABN07509; ABN07509; Mlab_1342.
DR GeneID; 4795369; -.
DR KEGG; mla:Mlab_1342; -.
DR eggNOG; arCOG01365; Archaea.
DR HOGENOM; CLU_137733_1_0_2; -.
DR OMA; RYPRQKV; -.
DR OrthoDB; 89278at2157; -.
DR Proteomes; UP000000365; 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 Pfam; PF01900; RNase_P_Rpp14; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW tRNA processing.
FT CHAIN 1..147
FT /note="Ribonuclease P protein component 2"
FT /id="PRO_1000148366"
SQ SEQUENCE 147 AA; 16212 MW; 319F4C8535192CC7 CRC64;
MSVLPPTLRE NRRYVLFRII TLVNPTQKEV YRSMADSVSA LFGDAGAAKM HPAVVWSEGE
YAIARCTRGY EQSLIAALAV VTKVCGEPAS FRSLATSGTI LSLKKKVIPE SIDDTTYPGY
LCAGKKVNNL SKENGHRYLT RDDIIKE