RNP1_HALS3
ID RNP1_HALS3 Reviewed; 123 AA.
AC B0R664;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=OE_3398F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP14233.1; -; Genomic_DNA.
DR RefSeq; WP_010903242.1; NC_010364.1.
DR AlphaFoldDB; B0R664; -.
DR SMR; B0R664; -.
DR EnsemblBacteria; CAP14233; CAP14233; OE_3398F.
DR GeneID; 5954228; -.
DR GeneID; 62887094; -.
DR KEGG; hsl:OE_3398F; -.
DR HOGENOM; CLU_107020_0_0_2; -.
DR OMA; RVVMVPK; -.
DR PhylomeDB; B0R664; -.
DR Proteomes; UP000001321; 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; tRNA processing.
FT CHAIN 1..123
FT /note="Ribonuclease P protein component 1"
FT /id="PRO_1000194585"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 123 AA; 13135 MW; E6941EE7E22237EB CRC64;
MTTITPESLP RHELLGLHAR VAADTDQSRV GIAGRVVDET MQTVVLRTAS GVAQVPKKGA
TFEFRLTDEA AAPDNGVGTA FKPAGGETRQ TTGESVAYVT VDGGRLLSRP ERRSENGVDS
KWR