RNPA_THEBO
ID RNPA_THEBO Reviewed; 162 AA.
AC Q7X5L6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 59.
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};
OS Thermus brockianus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=56956;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 11602 / BCRC 17272 / NBRC 110747 / NCIMB 12676 / YS38;
RX PubMed=12719542; DOI=10.1073/pnas.0931462100;
RA Feltens R., Gossringer M., Willkomm D.K., Urlaub H., Hartmann R.K.;
RT "An unusual mechanism of bacterial gene expression revealed for the RNase P
RT protein of Thermus strains.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5724-5729(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 -!- MISCELLANEOUS: The open reading frame (ORF) for this protein entirely
CC encompasses the ORF for the 50S ribosomal protein L34 (rpmH). The two
CC start codons are separated by four nucleotides.
CC -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00227}.
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DR EMBL; AY256337; AAO88967.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7X5L6; -.
DR SMR; Q7X5L6; -.
DR STRING; 56956.A0O31_01777; -.
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 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; RNA-binding; tRNA processing.
FT CHAIN 1..162
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198553"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 162 AA; 17867 MW; 4175E4CD315614C2 CRC64;
MDEKDLAAQP EEAGQDPRLP GPHEDPRRQE GAEAQAAEGP LAPHAQGERL KRPPPAPGGK
LVSLKGDRAF QRLRKGKAGR GRYVSVKWLP APELRVGIVV SKKVGKAVVR NKVKRRLREI
LRRLHLPKAH LLVVASPEAR EASYVELFQD VARALKKSGL IQ
