RNP1_HALMA
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 25-MAY-2022, entry version 89.
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=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}.
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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; -; 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..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