ID A0A1Q9JIS7_9FIRM Unreviewed; 132 AA.
AC A0A1Q9JIS7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=BHK98_08325 {ECO:0000313|EMBL:OLR56065.1};
OS Hornefia porci.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR56065.1, ECO:0000313|Proteomes:UP000187404};
RN [1] {ECO:0000313|EMBL:OLR56065.1, ECO:0000313|Proteomes:UP000187404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-3-10 {ECO:0000313|EMBL:OLR56065.1,
RC ECO:0000313|Proteomes:UP000187404};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLR56065.1}.
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DR EMBL; MJIE01000001; OLR56065.1; -; Genomic_DNA.
DR RefSeq; WP_075713319.1; NZ_MJIE01000001.1.
DR AlphaFoldDB; A0A1Q9JIS7; -.
DR STRING; 1261640.BHK98_08325; -.
DR OrthoDB; 9810867at2; -.
DR Proteomes; UP000187404; Unassembled WGS sequence.
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:UP000187404};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00227}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 132 AA; 15409 MW; 7AD3CF843361056F CRC64;
MSSRDEEPEA EKSSPHKKKR REDVLRYQKD FDRVYRKGKS VGDRYVVVFC LKNNLDHNRI
SFLASKKVGN SVRRNRARRL MKEAMRLSGM RLPCGYDFVI IARNTIDGAK CQQVQKSLES
AFRRTGVLKE VK
//
