ID RPP21_MACMU Reviewed; 154 AA. AC Q5TM57; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Ribonuclease P protein subunit p21; DE Short=RNaseP protein p21; GN Name=RPP21; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15269276; DOI=10.1093/molbev/msh216; RA Kulski J.K., Anzai T., Shiina T., Inoko H.; RT "Rhesus macaque class I duplicon structures, organization, and evolution RT within the alpha block of the major histocompatibility complex."; RL Mol. Biol. Evol. 21:2079-2091(2004). CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that CC generates mature tRNA molecules by cleaving their 5'-ends. CC {ECO:0000250|UniProtKB:Q9H633}. CC -!- SUBUNIT: RNase P consists of a catalytic RNA moiety and about 10 CC protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, CC RPP38 and RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form CC the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' CC subcomplex. All subunits of the RNase P complex interact with the CC catalytic RNA. {ECO:0000250|UniProtKB:Q9H633}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus CC {ECO:0000250|UniProtKB:Q9H633}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 4 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB128049; BAD69769.1; -; Genomic_DNA. DR RefSeq; NP_001040603.1; NM_001047138.1. DR AlphaFoldDB; Q5TM57; -. DR SMR; Q5TM57; -. DR GeneID; 713056; -. DR KEGG; mcc:713056; -. DR CTD; 79897; -. DR InParanoid; Q5TM57; -. DR OrthoDB; 5482220at2759; -. DR Proteomes; UP000006718; Unassembled WGS sequence. DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC. DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central. DR Gene3D; 6.20.50.20; -; 1. 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. PE 3: Inferred from homology; KW Acetylation; Metal-binding; Nucleus; Reference proteome; tRNA processing; KW Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q9H633" FT CHAIN 2..154 FT /note="Ribonuclease P protein subunit p21" FT /id="PRO_0000236682" FT REGION 112..154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q9H633" SQ SEQUENCE 154 AA; 17565 MW; 49B3E9F2E88509EB CRC64; MAGPVKDREA FQRLNFLYQA AHCVLAQDPE NQALARFYCH TERTIAKRLV LRRDPSVKRT LCRGCSSLLV PGLTCTQRQR RCRGQRWTVQ TCLTCQRSQR FLNDPGHLLW GDRPEAQLGN QADSKPLQPL PNTAHSISDH LPEEKMQIQG SSDQ //