ID   RNP4_METPE              Reviewed;         106 AA.
AC   B8GET9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=Mpal_0533;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP001338; ACL15906.1; -; Genomic_DNA.
DR   RefSeq; WP_012617225.1; NC_011832.1.
DR   AlphaFoldDB; B8GET9; -.
DR   SMR; B8GET9; -.
DR   STRING; 521011.Mpal_0533; -.
DR   GeneID; 7271949; -.
DR   KEGG; mpl:Mpal_0533; -.
DR   eggNOG; arCOG04345; Archaea.
DR   HOGENOM; CLU_079140_3_1_2; -.
DR   OrthoDB; 10058at2157; -.
DR   Proteomes; UP000002457; 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   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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..106
FT                   /note="Ribonuclease P protein component 4"
FT                   /id="PRO_1000148373"
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   106 AA;  12603 MW;  32EC60A25A511EB1 CRC64;
     MTVKSQNRQT KKLAGERIAI LFTQAKVFAG INPAWSDRCV ERARAIAMRQ RMRMEREQRR
     QYCHHCYAYF LHGVNVRVRV HRGHVIVTCL NCGRQTRYQV VRTDNR
//