RNP4_METMJ
ID RNP4_METMJ Reviewed; 105 AA.
AC A3CX01;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ribonuclease P protein component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE Short=RNase P component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00757};
DE AltName: Full=Rpp21 {ECO:0000255|HAMAP-Rule:MF_00757};
GN Name=rnp4 {ECO:0000255|HAMAP-Rule:MF_00757}; OrderedLocusNames=Memar_1975;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC Rule:MF_00757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00757};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00757};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00757};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00757}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 4 family. {ECO:0000255|HAMAP-Rule:MF_00757}.
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DR EMBL; CP000562; ABN57901.1; -; Genomic_DNA.
DR RefSeq; WP_011844810.1; NC_009051.1.
DR AlphaFoldDB; A3CX01; -.
DR SMR; A3CX01; -.
DR STRING; 368407.Memar_1975; -.
DR EnsemblBacteria; ABN57901; ABN57901; Memar_1975.
DR GeneID; 4847390; -.
DR KEGG; mem:Memar_1975; -.
DR eggNOG; arCOG04345; Archaea.
DR HOGENOM; CLU_079140_3_1_2; -.
DR OMA; HVVITCL; -.
DR OrthoDB; 128960at2157; -.
DR Proteomes; UP000002146; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00757; RNase_P_4; 1.
DR InterPro; IPR016432; RNP4.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
DR PIRSF; PIRSF004878; RNase_P_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW tRNA processing; Zinc.
FT CHAIN 1..105
FT /note="Ribonuclease P protein component 4"
FT /id="PRO_1000083505"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ SEQUENCE 105 AA; 12322 MW; 2728FF3AADAEA985 CRC64;
MADTTRKSGS RRLARERIAV LFARAAEFYP ESPDRSNRCV ELARKIGMRH RIRIERPLKR
RFCRRCYTYL VPGSNARVRV HRGRVVVTCL ACGHRSRFPV GRPRQ