ID   RNP2_NATPD              Reviewed;         161 AA.
AC   Q3IPJ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=NP_3736A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49959.1; -; Genomic_DNA.
DR   RefSeq; WP_011323576.1; NC_007426.1.
DR   AlphaFoldDB; Q3IPJ2; -.
DR   SMR; Q3IPJ2; -.
DR   STRING; 348780.NP_3736A; -.
DR   EnsemblBacteria; CAI49959; CAI49959; NP_3736A.
DR   GeneID; 3703113; -.
DR   KEGG; nph:NP_3736A; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_0_0_2; -.
DR   OMA; QRELWYA; -.
DR   OrthoDB; 89278at2157; -.
DR   Proteomes; UP000002698; 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..161
FT                   /note="Ribonuclease P protein component 2"
FT                   /id="PRO_1000148370"
SQ   SEQUENCE   161 AA;  17554 MW;  370AE862D8DD1AD3 CRC64;
     MKHLPKHLRP RWRYLAVGLE SWPDADIDRR AFQRELWFAA QNLIGDAGSA ALDGSVLHFR
     FEDGDGEAVI RARRGEVDAL RAVLATLSTV DGHPLGVVVR GVSGTVRACE EKYIRGPQEG
     TEERTVAFAG ADRPAVVRND RVTVELSGGP VGATALDIRD N