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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
 
 
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