ID A0A271IXX9_9BACT Unreviewed; 155 AA.
AC A0A271IXX9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=BSZ37_06150 {ECO:0000313|EMBL:PAP76052.1};
OS Rubrivirga marina.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubrivirga.
OX NCBI_TaxID=1196024 {ECO:0000313|EMBL:PAP76052.1, ECO:0000313|Proteomes:UP000216339};
RN [1] {ECO:0000313|EMBL:PAP76052.1, ECO:0000313|Proteomes:UP000216339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-28 {ECO:0000313|EMBL:PAP76052.1,
RC ECO:0000313|Proteomes:UP000216339};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
RL Submitted (NOV-2016) 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}.
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:PAP76052.1}.
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DR EMBL; MQWD01000001; PAP76052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A271IXX9; -.
DR OrthoDB; 1524972at2; -.
DR Proteomes; UP000216339; 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; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR Pfam; PF00825; Ribonuclease_P; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00227};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00227};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00227};
KW Reference proteome {ECO:0000313|Proteomes:UP000216339};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00227};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00227}.
SQ SEQUENCE 155 AA; 17467 MW; 8D0D6C5EA8FB4729 CRC64;
MPARAASPVR PAAFPRSRRL KRRRLIRPLF DRGRADVGRV RAGTVVLLYR TVPREATGHD
VGAQVGFAPG RRATNTIRTR VRRHLREAFR LHQGPLLDRF GGRPDCLTMM TLYRGRDDGA
GEAIRRDLPR ALARLAEREI PLAEAIPAPS ERPRP
//