ID A0A1H3W0J0_9EURY Unreviewed; 113 AA.
AC A0A1H3W0J0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 02-APR-2025, entry version 19.
DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE Short=RNase P component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00755};
DE AltName: Full=Pop5 {ECO:0000256|HAMAP-Rule:MF_00755};
GN Name=rnp2 {ECO:0000256|HAMAP-Rule:MF_00755};
GN ORFNames=SAMN04488065_0457 {ECO:0000313|EMBL:SDZ80569.1};
OS Haloplanus vescus.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Haloplanus.
OX NCBI_TaxID=555874 {ECO:0000313|EMBL:SDZ80569.1, ECO:0000313|Proteomes:UP000236755};
RN [1] {ECO:0000313|EMBL:SDZ80569.1, ECO:0000313|Proteomes:UP000236755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8712 {ECO:0000313|EMBL:SDZ80569.1,
RC ECO:0000313|Proteomes:UP000236755};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00755};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000256|HAMAP-Rule:MF_00755}.
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DR EMBL; FNQT01000001; SDZ80569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3W0J0; -.
DR STRING; 555874.SAMN04488065_0457; -.
DR OrthoDB; 19261at2157; -.
DR Proteomes; UP000236755; Unassembled WGS sequence.
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 Pfam; PF01900; RNase_P_Rpp14; 1.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00755}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00755};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00755};
KW Reference proteome {ECO:0000313|Proteomes:UP000236755};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00755}.
SQ SEQUENCE 113 AA; 12362 MW; 18B7EC7B0A6F4EBE CRC64;
MKHLPKHLRP HWRYLAVGLE AEADLSRSAF QRAVWYAASN LLGDPGSADA DLRVLRFDFE
DGTGEAVVRA RRGEVGPARA ALACVHDIDG DSVGVWVRGV SGTIRACEET YLD
//
