ID A9DRI4_9FLAO Unreviewed; 131 AA.
AC A9DRI4;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 74.
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=KAOT1_16583 {ECO:0000313|EMBL:EDP96798.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP96798.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP96798.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP96798.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
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|ARBA:ARBA00002663, 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:EDP96798.1}.
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DR EMBL; ABIB01000003; EDP96798.1; -; Genomic_DNA.
DR RefSeq; WP_007095852.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DRI4; -.
DR STRING; 391587.KAOT1_16583; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_1_1_10; -.
DR OrthoDB; 1524972at2; -.
DR Proteomes; UP000002945; 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 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 {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:UP000002945};
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 131 AA; 15443 MW; A5AB243FE722C274 CRC64;
MNYRFPKEEK LKSKKCLDLL FSEGGAVSKF PLRLVYIATD LPKDVQIQAG VSVTKRRFKK
AVTRNRIKRL MREAYRLHKN DVFNTISTSY AFMFLYIGKK EPTFEEIEKS MIRLLQKFLE
KTNTIDAPEK E
//