ID A0A095VTL9_9GAMM Unreviewed; 95 AA.
AC A0A095VTL9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Ribonuclease P protein component {ECO:0000313|EMBL:KGE04433.1};
DE EC=3.1.26.5 {ECO:0000313|EMBL:KGE04433.1};
GN ORFNames=HRUBRA_00958 {ECO:0000313|EMBL:KGE04433.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE04433.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE04433.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE04433.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
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}.
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:KGE04433.1}.
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DR EMBL; AUVB01000026; KGE04433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095VTL9; -.
DR STRING; 1265313.HRUBRA_00958; -.
DR eggNOG; COG0594; Bacteria.
DR HOGENOM; CLU_117179_11_3_6; -.
DR Proteomes; UP000029640; Unassembled WGS sequence.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 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 4: Predicted;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KGE04433.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ SEQUENCE 95 AA; 10799 MW; 148F5F5E063027BB CRC64;
MSVKAGQREF LLLARPSEQS HHRLGLAVAK KHVARAVRRN RIKRIARECF RHLPTPTVPL
DIVFLTRPGA GDLDKVALAR GIDRQFRRLL ERATA
//
