ID   RNP3_METBF              Reviewed;         239 AA.
AC   Q469M8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Mbar_A2501;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71414.1; -; Genomic_DNA.
DR   RefSeq; WP_011307459.1; NC_007355.1.
DR   AlphaFoldDB; Q469M8; -.
DR   SMR; Q469M8; -.
DR   STRING; 269797.Mbar_A2501; -.
DR   EnsemblBacteria; AAZ71414; AAZ71414; Mbar_A2501.
DR   GeneID; 3625694; -.
DR   KEGG; mba:Mbar_A2501; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_074509_1_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   PANTHER; PTHR13031; PTHR13031; 1.
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..239
FT                   /note="Ribonuclease P protein component 3"
FT                   /id="PRO_1000046625"
SQ   SEQUENCE   239 AA;  26090 MW;  C77F34E1D35ECE48 CRC64;
     MGKPKFYDFC VHAVPDGENT VDQLSALARH LGYSGIALTN HSDKLPQSQP VLPSTNEFEV
     FKGIELVEEN PSKLHGLIGK FRKSVDVLIV HGGSENVNRA ALENPRVDIL NHPAFAKSSG
     LNQVLAKSAA ENDVAISLII RPLLHSRGPR RVRLLSNLRA NLDLARKYDV SLVLSSGAMS
     CFDLRSPMET LALAEVCGLE EDEALEAITV VPERIISRNR PGPGHVREGI EVLEEGDYS