ID   RNP1_NITMS              Reviewed;          88 AA.
AC   A9A5I7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=Nmar_0802;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX12698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A5I7; -.
DR   SMR; A9A5I7; -.
DR   STRING; 436308.Nmar_0802; -.
DR   EnsemblBacteria; ABX12698; ABX12698; Nmar_0802.
DR   KEGG; nmr:Nmar_0802; -.
DR   eggNOG; arCOG00784; Archaea.
DR   HOGENOM; CLU_107020_2_0_2; -.
DR   InParanoid; A9A5I7; -.
DR   OrthoDB; 39019at2157; -.
DR   PhylomeDB; A9A5I7; -.
DR   Proteomes; UP000000792; 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; Ribonuclease P/MRP, subunit p29; 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; Rof/RNase P subunit-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..88
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_1000148363"
SQ   SEQUENCE   88 AA;  9687 MW;  7E301F07E4633906 CRC64;
     MITADNITSH EFIGLNTEIV QSTNPQVIGL NGRIENETKS MFTINTENGM KSIAKSTSNW
     KFSIDSNDVI VEGSRIAKRP FDRIGGKA
//