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Database: UniProt
Entry: I0JWU6_METFB
LinkDB: I0JWU6_METFB
Original site: I0JWU6_METFB 
ID   I0JWU6_METFB            Unreviewed;       128 AA.
AC   I0JWU6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=MFUM_200028 {ECO:0000313|EMBL:CCG91715.1};
OS   Methylacidiphilum fumariolicum (strain SolV).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=1156937 {ECO:0000313|EMBL:CCG91715.1, ECO:0000313|Proteomes:UP000004837};
RN   [1] {ECO:0000313|EMBL:CCG91715.1, ECO:0000313|Proteomes:UP000004837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolV {ECO:0000313|EMBL:CCG91715.1,
RC   ECO:0000313|Proteomes:UP000004837};
RX   PubMed=22740660; DOI=10.1128/JB.00501-12;
RA   Khadem A.F., Wieczorek A.S., Pol A., Vuilleumier S., Harhangi H.R.,
RA   Dunfield P.F., Kalyuzhnaya M.G., Murrell J.C., Francoijs K.-J.,
RA   Stunnenberg H.G., Stein L.Y., DiSpirito A.A., Semrau J.D., Lajus A.,
RA   Medigue C., Klotz M.G., Jetten M.S.M., Op den Camp H.J.M.;
RT   "Draft Genome Sequence of the Volcano-Inhabiting Thermoacidophilic
RT   Methanotroph Methylacidiphilum fumariolicum Strain SolV.";
RL   J. Bacteriol. 194:3729-3730(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, 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:CCG91715.1}.
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DR   EMBL; CAHT01000023; CCG91715.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0JWU6; -.
DR   STRING; 1156937.GCA_000953475_01561; -.
DR   eggNOG; COG0594; Bacteria.
DR   InParanoid; I0JWU6; -.
DR   OrthoDB; 196964at2; -.
DR   Proteomes; UP000004837; 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:UP000004837};
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   128 AA;  15174 MW;  E09F79BB8422A934 CRC64;
     MVYFGCSTNL NNKLPRRLIA KKKDEIALFF SHGKKFSSPF FILFVLPRET DSFPKVFFAV
     SKKIRGAAKR NLIKRRMREI FRQYAPFKLA PYSFGWIAKE RVLTANFKEM RKDMIELGEK
     AIHFFNRV
//
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