RNP4_METMP
ID RNP4_METMP Reviewed; 110 AA.
AC P62378;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=MMP0921;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=S2 / LL;
RX PubMed=20675586; DOI=10.1073/pnas.1005556107;
RA Cho I.M., Lai L.B., Susanti D., Mukhopadhyay B., Gopalan V.;
RT "Ribosomal protein L7Ae is a subunit of archaeal RNase P.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14573-14578(2010).
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, ECO:0000269|PubMed:20675586}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for pre-tRNA-Tyr in the absence of L7Ae
CC {ECO:0000269|PubMed:20675586};
CC KM=0.044 uM for pre-tRNA-Tyr in the presence of L7Ae
CC {ECO:0000269|PubMed:20675586};
CC Note=kcat 10 min(-1) in absence of L7Ae, 63 min(-1) in presence of
CC L7Ae. Kinetic parameters determined at 37 degrees Celsius.;
CC Temperature dependence:
CC Optimum temperature is 36-38 degrees Celsius in the absence of L7Ae,
CC 48-50 degrees Celsius in presence of L7Ae.
CC {ECO:0000269|PubMed:20675586};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 5 protein
CC subunits. {ECO:0000269|PubMed:20675586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757,
CC ECO:0000269|PubMed:20675586}.
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; BX950229; CAF30477.1; -; Genomic_DNA.
DR RefSeq; WP_011170865.1; NC_005791.1.
DR AlphaFoldDB; P62378; -.
DR SMR; P62378; -.
DR STRING; 267377.MMP0921; -.
DR EnsemblBacteria; CAF30477; CAF30477; MMP0921.
DR GeneID; 2761316; -.
DR KEGG; mmp:MMP0921; -.
DR PATRIC; fig|267377.15.peg.949; -.
DR eggNOG; arCOG04345; Archaea.
DR HOGENOM; CLU_079140_3_1_2; -.
DR OMA; HVVITCL; -.
DR OrthoDB; 128960at2157; -.
DR BioCyc; MMAR267377:MMP_RS04780-MON; -.
DR BRENDA; 3.1.26.5; 3262.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030677; C:ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..110
FT /note="Ribonuclease P protein component 4"
FT /id="PRO_0000153855"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ SEQUENCE 110 AA; 12891 MW; 46B9447B948D0F48 CRC64;
MKLKKKFLEK SKKVAEERIN ILMNLAEKES NSGKTERSKN YVLLGKKIAM RMRMPYPKEW
KRRICKNCGS FLIYGKNARV RTKAKNYPHV VITCLECNSI TRIPIKTAKK
