ID   RNP1_HYPBU              Reviewed;         111 AA.
AC   A2BMC7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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}; OrderedLocusNames=Hbut_1308;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM81138.1; -; Genomic_DNA.
DR   RefSeq; WP_011822456.1; NC_008818.1.
DR   AlphaFoldDB; A2BMC7; -.
DR   SMR; A2BMC7; -.
DR   STRING; 415426.Hbut_1308; -.
DR   EnsemblBacteria; ABM81138; ABM81138; Hbut_1308.
DR   GeneID; 4782900; -.
DR   KEGG; hbu:Hbut_1308; -.
DR   eggNOG; arCOG00784; Archaea.
DR   HOGENOM; CLU_107020_3_0_2; -.
DR   OMA; WHELIGL; -.
DR   OrthoDB; 124913at2157; -.
DR   Proteomes; UP000002593; 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:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.210; -; 1.
DR   HAMAP; MF_00754; RNase_P_1; 1.
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   Pfam; PF01868; RNase_P-MRP_p29; 1.
DR   SMART; SM00538; POP4; 1.
DR   SUPFAM; SSF101744; SSF101744; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..111
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_1000046610"
SQ   SEQUENCE   111 AA;  12432 MW;  C35F35ADBBBF33F1 CRC64;
     MKRTAWNIVF HSLIGLRARV LATSDPGLRG LEGVVVEETR HSLVVETRDG RRVRVLKANS
     IFLFQLPGGS WVVVRGEEIA GSLAERVKRL GRLKGVGWLV RAGEKRRYTR G