ID I4VUB6_9GAMM Unreviewed; 100 AA.
AC I4VUB6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Ribonuclease P protein component {ECO:0000313|EMBL:EIL90807.1};
GN ORFNames=UU7_15245 {ECO:0000313|EMBL:EIL90807.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL90807.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL90807.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL90807.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL90807.1}.
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DR EMBL; AJXT01000048; EIL90807.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VUB6; -.
DR STRING; 1163407.UU7_15245; -.
DR PATRIC; fig|1163407.3.peg.3064; -.
DR eggNOG; COG0594; Bacteria.
DR Proteomes; UP000003226; Unassembled WGS sequence.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:InterPro.
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ SEQUENCE 100 AA; 11403 MW; 9CBBF6EF9C778953 CRC64;
MRFRENELGH ARLGLAISKR VSKRAVERNR IKRLLRESFR RVRHQLPAVD MMVMAREQAA
GVPGPQLLTE LDGLWKKLLA SQTASSEPLK RAGDTTTIER
//
