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Database: UniProt
Entry: L0JX58_9EURY
LinkDB: L0JX58_9EURY
Original site: L0JX58_9EURY 
ID   L0JX58_9EURY            Unreviewed;       161 AA.
AC   L0JX58;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=Natoc_1529 {ECO:0000313|EMBL:AGB37336.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB37336.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB37336.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB37336.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) 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|ARBA:ARBA00010800, ECO:0000256|HAMAP-
CC       Rule:MF_00755}.
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DR   EMBL; CP003929; AGB37336.1; -; Genomic_DNA.
DR   RefSeq; WP_015320786.1; NC_019974.1.
DR   AlphaFoldDB; L0JX58; -.
DR   STRING; 694430.Natoc_1529; -.
DR   GeneID; 14404613; -.
DR   KEGG; nou:Natoc_1529; -.
DR   eggNOG; arCOG01365; Archaea.
DR   HOGENOM; CLU_137733_0_0_2; -.
DR   OrthoDB; 19261at2157; -.
DR   Proteomes; UP000010878; 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   PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR   PANTHER; PTHR15441:SF2; RIBONUCLEASE P/MRP PROTEIN SUBUNIT POP5; 1.
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:AGB37336.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010878};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00755}.
SQ   SEQUENCE   161 AA;  17886 MW;  6759259A7A4EA315 CRC64;
     MKHLPKHLQP RWRYLVLELE GWPDAEIDRR AFQRECWYAG QNLLGDPGSA AADLTVVRFE
     FDDGTGSAIV RVRRGETESA RAAIACIDEI DGATVGIRVC GISGTIRAGE ENYLGRRRQD
     SKERNVVFGN EERVAVVRDG SADVRLDDAF VGTTDLDCDF A
//
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