ID   RNP3_METM7              Reviewed;         232 AA.
AC   A6VJ64;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=MmarC7_1427;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR66490.1; -; Genomic_DNA.
DR   RefSeq; WP_012067956.1; NC_009637.1.
DR   AlphaFoldDB; A6VJ64; -.
DR   SMR; A6VJ64; -.
DR   STRING; 426368.MmarC7_1427; -.
DR   EnsemblBacteria; ABR66490; ABR66490; MmarC7_1427.
DR   GeneID; 5329611; -.
DR   KEGG; mmz:MmarC7_1427; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_074509_0_0_2; -.
DR   OMA; INRAACE; -.
DR   OrthoDB; 66325at2157; -.
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_1000046628"
SQ   SEQUENCE   232 AA;  26448 MW;  07F062EC96F83378 CRC64;
     MLEGIFDINH IFDEDGIKTL KRFGWDGSVA VQNHNEYSEE IINSAVEYGE KHDFKVFSGV
     KISTKNQNEM EKAVKKYRNK ADILLVEGGD IKINRRVLEM NDVDILSTPE LNRMDNGLDH
     ILARLGSTNR VAIELNFGNL LKSRNYDRSK ILWAFQRNLK LAKKYDTPVV ISSGASDIYG
     IKAPGDLRGF LNTVTDPLYS KKIMETTSKI IDYRLYLKKD TVLTLGIEIV EE