ID   RNP1_METST              Reviewed;          93 AA.
AC   Q2NFW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Ribonuclease P protein component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE            Short=RNase P component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00754};
DE   AltName: Full=Rpp29 {ECO:0000255|HAMAP-Rule:MF_00754};
GN   Name=rnp1 {ECO:0000255|HAMAP-Rule:MF_00754};
GN   OrderedLocusNames=Msp_0900;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(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_00754}.
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_00754};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00754}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 1 family. {ECO:0000255|HAMAP-Rule:MF_00754}.
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DR   EMBL; CP000102; ABC57288.1; -; Genomic_DNA.
DR   RefSeq; WP_011406487.1; NC_007681.1.
DR   AlphaFoldDB; Q2NFW5; -.
DR   SMR; Q2NFW5; -.
DR   STRING; 339860.Msp_0900; -.
DR   GeneID; 41325475; -.
DR   KEGG; mst:Msp_0900; -.
DR   eggNOG; arCOG00784; Archaea.
DR   HOGENOM; CLU_107020_2_1_2; -.
DR   OrthoDB; 39019at2157; -.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IEA:InterPro.
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:0033204; F:ribonuclease P RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.210; Ribonuclease P/MRP, subunit p29; 1.
DR   HAMAP; MF_00754; RNase_P_1; 1.
DR   InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR   InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR   InterPro; IPR023538; RNP1.
DR   InterPro; IPR023534; Rof/RNase_P-like.
DR   InterPro; IPR002730; Rpp29/RNP1.
DR   PANTHER; PTHR13348:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P29; 1.
DR   PANTHER; PTHR13348; RIBONUCLEASE P SUBUNIT P29; 1.
DR   Pfam; PF01868; RNase_P-MRP_p29; 1.
DR   SMART; SM00538; POP4; 1.
DR   SUPFAM; SSF101744; Rof/RNase P subunit-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..93
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_1000046616"
SQ   SEQUENCE   93 AA;  10689 MW;  9E45AB86D0F5A6C7 CRC64;
     MITPQNVFRH EFIGLNVEVI NSKHEKFIGI KGIIIDETRN TIRVDTGKNE KLIPKSDVVF
     LFTLPQGEKV SIDGKVITAR PEDRIKKKFT KIR
//