RNPA_PROMM
ID RNPA_PROMM Reviewed; 128 AA.
AC Q7V612;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=PMT_1369;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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; BX548175; CAE21544.1; -; Genomic_DNA.
DR RefSeq; WP_011130737.1; NC_005071.1.
DR AlphaFoldDB; Q7V612; -.
DR SMR; Q7V612; -.
DR STRING; 74547.PMT_1369; -.
DR EnsemblBacteria; CAE21544; CAE21544; PMT_1369.
DR KEGG; pmt:PMT_1369; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_2_0_3; -.
DR OMA; MRLKGHR; -.
DR OrthoDB; 2014742at2; -.
DR Proteomes; UP000001423; Chromosome.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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 Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding;
KW tRNA processing.
FT CHAIN 1..128
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198508"
SQ SEQUENCE 128 AA; 14637 MW; D5FD2456869EE827 CRC64;
MVLPASMRLR GSRCFEHLQK WGYRFYGTSM VLRVIEANPQ LLKAPHRHHN STACRCAVVI
SSKVSKRAVI RNRLRRLLHD HLRSRLEVAP EHCNHWVLIS LKPVASAIEA SPLLEECDRL
LNQAGLLS