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Database: UniProt
Entry: A0A1G1J7D8_9BACT
LinkDB: A0A1G1J7D8_9BACT
Original site: A0A1G1J7D8_9BACT 
ID   A0A1G1J7D8_9BACT        Unreviewed;       106 AA.
AC   A0A1G1J7D8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGW76592.1};
GN   ORFNames=A3J52_01020 {ECO:0000313|EMBL:OGW76592.1};
OS   Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_49_9.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801822 {ECO:0000313|EMBL:OGW76592.1, ECO:0000313|Proteomes:UP000179674};
RN   [1] {ECO:0000313|EMBL:OGW76592.1, ECO:0000313|Proteomes:UP000179674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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|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:OGW76592.1}.
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DR   EMBL; MHFH01000052; OGW76592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1J7D8; -.
DR   Proteomes; UP000179674; 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   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   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ   SEQUENCE   106 AA;  12266 MW;  327F448BE7D5438D CRC64;
     MLKGLLFRQN GVALHVLRKA PGTRSRLGIV VPKRVAKLAS ERNYFKRLVR EFFRIHEKDF
     EVPCDMVIRR IGAKKHIEHR EFGQVVGRLL AEAQIMAWTE KAEESG
//
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