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   27-MAR-2024, entry version 87.
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};
GN   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; Evidence={ECO:0000255|HAMAP-
CC         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   OrthoDB; 10058at2157; -.
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   Gene3D; 6.20.50.20; -; 1.
DR   Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR   HAMAP; MF_00757; RNase_P_4; 1.
DR   InterPro; IPR016432; RNP4.
DR   InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR   PANTHER; PTHR14742:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P21; 1.
DR   PANTHER; PTHR14742; RIBONUCLEASE P SUBUNIT P21; 1.
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
//