ID   A4YCU8_METS5            Unreviewed;       141 AA.
AC   A4YCU8;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   28-JAN-2026, entry version 77.
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   OrderedLocusNames=Msed_0073 {ECO:0000313|EMBL:ABP94250.1};
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94250.1, ECO:0000313|Proteomes:UP000000242};
RN   [1] {ECO:0000313|EMBL:ABP94250.1, ECO:0000313|Proteomes:UP000000242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC   {ECO:0000313|Proteomes:UP000000242};
RX   PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94250.1; -; Genomic_DNA.
DR   RefSeq; WP_011921219.1; NC_009440.1.
DR   AlphaFoldDB; A4YCU8; -.
DR   STRING; 399549.Msed_0073; -.
DR   GeneID; 91756928; -.
DR   KEGG; mse:Msed_0073; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_1801579_0_0_2; -.
DR   Proteomes; UP000000242; 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   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|HAMAP-Rule:MF_00755};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00755, ECO:0000313|EMBL:ABP94250.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00755}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   141 AA;  15884 MW;  9BDAD4AE00184F8F CRC64;
     MYQTILDVIF VIWLLVITIL LLTRKNVIIV KSKRKVGRNK RRYIVFRVVG QGELSPRALE
     TSVREAVKEL VGRMWLEISD PHVIFYNPSN MSGIISTNRL GYRAVLASMP LVKSVSGTEV
     LLVPFKTTGS LKKAKSLIRS G
//