RNPA_RHOBA
ID RNPA_RHOBA Reviewed; 146 AA.
AC Q7UNR1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227};
DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227};
GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; OrderedLocusNames=RB7431;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC RNA substrates such as 4.5S RNA. The protein component plays an
CC auxiliary but essential role in vivo by binding to the 5'-leader
CC sequence and broadening the substrate specificity of the ribozyme.
CC {ECO:0000255|HAMAP-Rule:MF_00227}.
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_00227};
CC -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC protein subunit. {ECO:0000255|HAMAP-Rule:MF_00227}.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; BX294146; CAD75357.1; -; Genomic_DNA.
DR RefSeq; NP_867810.1; NC_005027.1.
DR RefSeq; WP_011121387.1; NC_005027.1.
DR AlphaFoldDB; Q7UNR1; -.
DR SMR; Q7UNR1; -.
DR STRING; 243090.RB7431; -.
DR EnsemblBacteria; CAD75357; CAD75357; RB7431.
DR KEGG; rba:RB7431; -.
DR PATRIC; fig|243090.15.peg.3585; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_9_2_0; -.
DR InParanoid; Q7UNR1; -.
DR OMA; HGVENGR; -.
DR OrthoDB; 2014742at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004526; F:ribonuclease P activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00227; RNase_P; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW tRNA processing.
FT CHAIN 1..146
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198516"
SQ SEQUENCE 146 AA; 16299 MW; 452AC34BA15A9B76 CRC64;
MSRTGGKRPL EFPKSSRVVR SSEFTKALRR GGVAANDCLV VFALPHDVPD ADGEPSPDES
KTVKCRLGVT IPKKTGNAVV RNRWKRLIRE AFRLNQTQLP SGFDYVVRPK KDVTADWKMI
EKGFVKLVGR AVRRSQSSAD RSSTRS
