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Database: UniProt
Entry: M0GPC3_HALL2
LinkDB: M0GPC3_HALL2
Original site: M0GPC3_HALL2 
ID   M0GPC3_HALL2            Unreviewed;       159 AA.
AC   M0GPC3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=C456_11479 {ECO:0000313|EMBL:ELZ73387.1};
OS   Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS   (Haloferax alicantei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1230452 {ECO:0000313|EMBL:ELZ73387.1, ECO:0000313|Proteomes:UP000011535};
RN   [1] {ECO:0000313|EMBL:ELZ73387.1, ECO:0000313|Proteomes:UP000011535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa
RC   2.2 {ECO:0000313|Proteomes:UP000011535};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELZ73387.1}.
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DR   EMBL; AOLH01000018; ELZ73387.1; -; Genomic_DNA.
DR   RefSeq; WP_004063947.1; NZ_AOLH01000018.1.
DR   AlphaFoldDB; M0GPC3; -.
DR   GeneID; 80786648; -.
DR   PATRIC; fig|1230452.3.peg.2226; -.
DR   Proteomes; UP000011535; 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|HAMAP-Rule:MF_00755};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00755};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00755}.
SQ   SEQUENCE   159 AA;  17436 MW;  DD901C42C4BEF759 CRC64;
     MKHLPKHLRP RRRYLAVEVE TWPDADLARG PFQRELWYAA QNLYGDAGSA DADLTVLGFD
     YADGVAETVV RARRGHVEDA RAALACIDAV GGDPVGVRVR GVSGTVRACS ERYLHGRAGI
     SEERTVVFEN DSRTAVVRDS LFDVRGSDGF TGATQLDFE
//
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