ID   RNP3_METM6              Reviewed;         232 AA.
AC   A9A6K3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Ribonuclease P protein component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE            Short=RNase P component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00756};
DE   AltName: Full=Rpp30 {ECO:0000255|HAMAP-Rule:MF_00756};
GN   Name=rnp3 {ECO:0000255|HAMAP-Rule:MF_00756}; OrderedLocusNames=MmarC6_0481;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) 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:0000255|HAMAP-
CC       Rule:MF_00756}.
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_00756};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00756}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 3 family. {ECO:0000255|HAMAP-Rule:MF_00756}.
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DR   EMBL; CP000867; ABX01299.1; -; Genomic_DNA.
DR   RefSeq; WP_012193267.1; NC_009975.1.
DR   AlphaFoldDB; A9A6K3; -.
DR   SMR; A9A6K3; -.
DR   STRING; 444158.MmarC6_0481; -.
DR   EnsemblBacteria; ABX01299; ABX01299; MmarC6_0481.
DR   GeneID; 5738475; -.
DR   KEGG; mmx:MmarC6_0481; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_074509_0_0_2; -.
DR   OMA; INRAACE; -.
DR   OrthoDB; 66325at2157; -.
DR   PhylomeDB; A9A6K3; -.
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   HAMAP; MF_00756; RNase_P_3; 1.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR023539; RNase_P_comp-3_arc.
DR   InterPro; IPR002738; RNase_P_p30.
DR   Pfam; PF01876; RNase_P_p30; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; tRNA processing.
FT   CHAIN           1..232
FT                   /note="Ribonuclease P protein component 3"
FT                   /id="PRO_1000194591"
SQ   SEQUENCE   232 AA;  26514 MW;  7FA6AE065705D13E CRC64;
     MLEGIIDINH IFDEEGIKTL KRFGWDGSVA VQNHNEYSEE IINSTVEYGE KHDFKVFSGV
     KISTKNQNEM EKAIKKYRNK VDILLVEGGD IKINRRVLEM NDVDILSTPE LNRMDNGLDH
     ILARLGSTNR VAIELNFGNL LKSRNYDRSK ILWAFQRNLK LAKKYDTPVV ISSGASDIYG
     IKAPGDLRGF LNTITDPLYS KKIMETTSKI IDYRLYLKKD TVLTLGIEIV EE