ID RNP1_HALMA Reviewed; 94 AA. AC P22527; P20573; Q48239; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 22-FEB-2023, entry version 91. 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=rrnAC1603.1; OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM OS B-1809) (Halobacterium marismortui). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Haloarcula. OX NCBI_TaxID=272569; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2143141; DOI=10.1016/0014-5793(90)80923-7; RA Arndt E.; RT "Nucleotide sequence of four genes encoding ribosomal proteins from the RT 'S10 and spectinomycin' operon equivalent region in the archaebacterium RT Halobacterium marismortui."; RL FEBS Lett. 267:193-198(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809; RX PubMed=15520287; DOI=10.1101/gr.2700304; RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., RA Hood L., Ng W.V.; RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the RT Dead Sea."; RL Genome Res. 14:2221-2234(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67. RX PubMed=2406244; DOI=10.1016/s0021-9258(19)39729-7; RA Arndt E., Kroemer W., Hatakeyama T.; RT "Organization and nucleotide sequence of a gene cluster coding for eight RT ribosomal proteins in the archaebacterium Halobacterium marismortui."; RL J. Biol. Chem. 265:3034-3039(1990). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X55311; CAA39016.1; -; Genomic_DNA. DR EMBL; AY596297; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; J05222; AAA86867.1; -; Genomic_DNA. DR PIR; S10732; S10732. DR RefSeq; WP_007187647.1; NZ_CP039138.1. DR AlphaFoldDB; P22527; -. DR SMR; P22527; -. DR GeneID; 40152569; -. DR Proteomes; UP000001169; Chromosome I. 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..94 FT /note="Ribonuclease P protein component 1" FT /id="PRO_0000128426" SQ SEQUENCE 94 AA; 10277 MW; C88798425DEA2FA3 CRC64; MPLTPETLPR HELVGLDCEV VAASNPDVIG ISGTVVMETT QMLTLEGADR VWHVPKDSAT FAFDLSTETV LVDGDRLVAR PARRTENTGD SLWR //