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Database: UniProt
Entry: Q12ZC1_METBU
LinkDB: Q12ZC1_METBU
Original site: Q12ZC1_METBU 
ID   Q12ZC1_METBU            Unreviewed;       122 AA.
AC   Q12ZC1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 84.
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=Mbur_0195 {ECO:0000313|EMBL:ABE51205.1};
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564 {ECO:0000313|EMBL:ABE51205.1, ECO:0000313|Proteomes:UP000001979};
RN   [1] {ECO:0000313|Proteomes:UP000001979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M
RC   {ECO:0000313|Proteomes:UP000001979};
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE51205.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12ZC1; -.
DR   STRING; 259564.Mbur_0195; -.
DR   KEGG; mbu:Mbur_0195; -.
DR   HOGENOM; CLU_137733_1_0_2; -.
DR   OMA; NPWLIDY; -.
DR   Proteomes; UP000001979; 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   InterPro; IPR016434; Rnp2_archaea.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   PIRSF; PIRSF004952; RNase_P_2; 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:ABE51205.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00755}.
SQ   SEQUENCE   122 AA;  13455 MW;  CA090DA0EC2FC521 CRC64;
     MKLKVLPPTL RHDRRYFAFE LIGGNIVDRS DLLREIFLCA SSLVGDNGLS ECGVRLLDFE
     DSKGIVRCLR DRMDMTRAVL ASVTSVNGKP VIIHVLGISG TVHGATTKYL EGCTVYSPEE
     KT
//
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