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   08-NOV-2023, entry version 65.
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; Deinococcota; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
DR   InterPro; IPR020539; RNase_P_CS.
DR   NCBIfam; TIGR00188; rnpA; 1.
DR   PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR   Pfam; PF00825; Ribonuclease_P; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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
//