ID   RNP4_SULIK              Reviewed;         104 AA.
AC   C4KJF8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=M164_0042;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; 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; CP001402; ACR40678.1; -; Genomic_DNA.
DR   RefSeq; WP_012710221.1; NC_012726.1.
DR   AlphaFoldDB; C4KJF8; -.
DR   SMR; C4KJF8; -.
DR   GeneID; 84060538; -.
DR   KEGG; sid:M164_0042; -.
DR   HOGENOM; CLU_079140_3_1_2; -.
DR   Proteomes; UP000001479; 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   tRNA processing; Zinc.
FT   CHAIN           1..104
FT                   /note="Ribonuclease P protein component 4"
FT                   /id="PRO_1000212863"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ   SEQUENCE   104 AA;  12608 MW;  8ABE13847A57EE08 CRC64;
     MRIKNKIKKR IIELIELAYI TARKGDLELA REYIKLAEMY SRKGRVKIPL KYKRMFCRKC
     YTPLITGVTE RRRIRSKILI RTCLICNWQR RYVLSRNKGS NKEN
//