RNP1_NITMS
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 25-MAY-2022, entry version 68.
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=Nmar_0802;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC 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 OMA; GRIENET; -.
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; -; 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..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