RNPA_SYNY3
ID RNPA_SYNY3 Reviewed; 124 AA.
AC Q55005;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
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=slr1469;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8898883; DOI=10.1111/j.1432-1033.1996.0017t.x;
RA Pascual A., Vioque A.;
RT "Cloning, purification and characterization of the protein subunit of
RT ribonuclease P from the cyanobacterium Synechocystis sp. PCC 6803.";
RL Eur. J. Biochem. 241:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 -!- 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.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; X81989; CAA57516.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18242.1; -; Genomic_DNA.
DR PIR; S75681; S75681.
DR AlphaFoldDB; Q55005; -.
DR SMR; Q55005; -.
DR STRING; 1148.1653327; -.
DR PaxDb; Q55005; -.
DR EnsemblBacteria; BAA18242; BAA18242; BAA18242.
DR KEGG; syn:slr1469; -.
DR eggNOG; COG0594; Bacteria.
DR InParanoid; Q55005; -.
DR OMA; ECKYEHF; -.
DR PhylomeDB; Q55005; -.
DR Proteomes; UP000001425; 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 InterPro; IPR020539; RNase_P_CS.
DR PANTHER; PTHR33992; PTHR33992; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00188; rnpA; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW tRNA processing.
FT CHAIN 1..124
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198551"
SQ SEQUENCE 124 AA; 14498 MW; 9469A37102F5A583 CRC64;
MGLPKTLRLK HWQDFQTVYQ QGKRHRHSNL LMRVLGDRQA DHSRFGITVS QKVSKKATVR
NRLKRQIRAV INHFQPQIKP GFDVVIIVLP QGIGCNYERF LRELEQLFSQ AGIIDHGHSR
NHLL