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Database: UniProt
Entry: A0A0D8IB07_9CLOT
LinkDB: A0A0D8IB07_9CLOT
Original site: A0A0D8IB07_9CLOT 
ID   A0A0D8IB07_9CLOT        Unreviewed;       112 AA.
AC   A0A0D8IB07;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Ribonuclease P protein component {ECO:0000256|HAMAP-Rule:MF_00227};
DE            Short=RNase P protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE            Short=RNaseP protein {ECO:0000256|HAMAP-Rule:MF_00227};
DE            EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00227};
DE   AltName: Full=Protein C5 {ECO:0000256|HAMAP-Rule:MF_00227};
GN   Name=rnpA {ECO:0000256|HAMAP-Rule:MF_00227,
GN   ECO:0000313|EMBL:AKL97373.1};
GN   ORFNames=CACET_c39470 {ECO:0000313|EMBL:AKL97373.1}, TZ02_14580
GN   {ECO:0000313|EMBL:KJF26381.1};
OS   Clostridium aceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL97373.1, ECO:0000313|Proteomes:UP000035704};
RN   [1] {ECO:0000313|EMBL:AKL97373.1, ECO:0000313|Proteomes:UP000035704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL97373.1,
RC   ECO:0000313|Proteomes:UP000035704};
RA   Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium aceticum DSM 1496.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KJF26381.1, ECO:0000313|Proteomes:UP000032372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF26381.1,
RC   ECO:0000313|Proteomes:UP000032372};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT   butanol broducer through syngas fermentation.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00227};
CC   -!- SUBUNIT: Consists of a catalytic RNA component (M1 or rnpB) and a
CC       protein subunit. {ECO:0000256|HAMAP-Rule:MF_00227}.
CC   -!- SIMILARITY: Belongs to the RnpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00227}.
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DR   EMBL; CP009687; AKL97373.1; -; Genomic_DNA.
DR   EMBL; JYHU01000016; KJF26381.1; -; Genomic_DNA.
DR   RefSeq; WP_044825686.1; NZ_JYHU01000016.1.
DR   AlphaFoldDB; A0A0D8IB07; -.
DR   STRING; 84022.CACET_c39470; -.
DR   KEGG; cace:CACET_c39470; -.
DR   PATRIC; fig|84022.5.peg.1201; -.
DR   OrthoDB; 9810867at2; -.
DR   Proteomes; UP000032372; Unassembled WGS sequence.
DR   Proteomes; UP000035704; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR000100; RNase_P.
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.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00227};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00227};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00227};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035704};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00227}.
SQ   SEQUENCE   112 AA;  13041 MW;  DBF7725A2BA51149 CRC64;
     MEAANRLRKN EDFRKVYKEG NSIANKLLIL YIKKNAFDYN RAGFTVSKKV GKSVIRSKVK
     RRMRESYRLN DSKLLQGYDL VFVARQGCNE ATFQEIESAL LHLIGKKKLL KK
//
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