ID   RNP2_HALMA              Reviewed;         161 AA.
AC   Q5V2X7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=rrnAC1175;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46125.1; -; Genomic_DNA.
DR   RefSeq; WP_011223480.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V2X7; -.
DR   SMR; Q5V2X7; -.
DR   STRING; 272569.rrnAC1175; -.
DR   PaxDb; 272569-rrnAC1175; -.
DR   EnsemblBacteria; AAV46125; AAV46125; rrnAC1175.
DR   GeneID; 40152170; -.
DR   KEGG; hma:rrnAC1175; -.
DR   PATRIC; fig|272569.17.peg.1891; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_0_0_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..161
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_1000148365"
SQ   SEQUENCE   161 AA;  18212 MW;  3807E0C14AD338C9 CRC64;
     MKHLPKHLRP RWRYLAVGIE TWPNASFGRR AFQREVWYAA QNLLGDTGSA ETDMTVLQFH
     DYDGTAEAIV RTRRGQTNPA RAALTCLDSV DDDDVRVRVR GISGTVRACE EKYIRGPPEF
     TEQRHVVFEN ADRSATVRPP RYDVETASDG AFVGATALDF R
//