RPP21_MACMU
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 03-AUG-2022, entry version 68.
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}.
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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; 1560813at2759; -.
DR Proteomes; UP000006718; Unplaced.
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 InterPro; IPR007175; Rpr2/Snm1/Rpp21.
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