RNPA_THEFI
ID RNPA_THEFI Reviewed; 240 AA.
AC Q7X5L2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 60.
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 filiformis.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tok4A2;
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; AY256339; AAO88971.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7X5L2; -.
DR SMR; Q7X5L2; -.
DR STRING; 276.THFILI_01295; -.
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..240
FT /note="Ribonuclease P protein component"
FT /id="PRO_0000198554"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..123
FT /note="Insert"
SQ SEQUENCE 240 AA; 25329 MW; A6D12A561AEEEF38 CRC64;
MDEKDLATQQ AQAGQDPRLP GPDEDQERAE GAEAQAAEGA PPPHRVIPPH PGLRQDGGPG
KPPRPSLRWD GGPGKAFPKP ADGATYAKEA AEKGMTPPQL GAGQAGGPGK PPHPGPDRDG
GSKASRASSP KKAGGKGLVS LKGDRAFQRL KKGRSGRGRL VLVRWLPRQE GVAVGIVVSK
KVGKAVVRNK VRRRIREILR RLHLPPADLL VIAQPEAKDA GFAELARDLF LALKKSGLVQ
