ID   RPP30_BOVIN             Reviewed;         268 AA.
AC   Q3SZ21;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Ribonuclease P protein subunit p30;
DE            Short=RNaseP protein p30;
DE   AltName: Full=RNase P subunit 2;
GN   Name=RPP30; Synonyms=RNASEP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC       generates mature tRNA molecules by cleaving their 5'-ends. Also a
CC       component of the MRP ribonuclease complex, which cleaves pre-rRNA
CC       sequences. {ECO:0000250|UniProtKB:P78346}.
CC   -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins.
CC       RNase P consists of a catalytic RNA moiety and about 10 protein
CC       subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and
CC       RPP40. Within the RNase P complex, POP1, POP7 and RPP25 form the
CC       'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the
CC       '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. Several subunits of RNase P are also part of the RNase
CC       MRP complex. RNase MRP consists of a catalytic RNA moiety and about 8
CC       protein subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly
CC       also POP4 and POP5. {ECO:0000250|UniProtKB:P78346}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 3 family. {ECO:0000305}.
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DR   EMBL; BC103240; AAI03241.1; -; mRNA.
DR   RefSeq; NP_001030538.1; NM_001035461.1.
DR   AlphaFoldDB; Q3SZ21; -.
DR   SMR; Q3SZ21; -.
DR   STRING; 9913.ENSBTAP00000003871; -.
DR   PaxDb; Q3SZ21; -.
DR   Ensembl; ENSBTAT00000003871; ENSBTAP00000003871; ENSBTAG00000002973.
DR   GeneID; 615098; -.
DR   KEGG; bta:615098; -.
DR   CTD; 10556; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002973; -.
DR   VGNC; VGNC:34123; RPP30.
DR   eggNOG; KOG2363; Eukaryota.
DR   GeneTree; ENSGT00390000000883; -.
DR   InParanoid; Q3SZ21; -.
DR   OMA; PWDVINL; -.
DR   OrthoDB; 1197518at2759; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000002973; Expressed in oocyte and 108 other tissues.
DR   ExpressionAtlas; Q3SZ21; baseline and differential.
DR   GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IEA:Ensembl.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:Ensembl.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR002738; RNase_P_p30.
DR   PANTHER; PTHR13031; PTHR13031; 1.
DR   Pfam; PF01876; RNase_P_p30; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Nucleus; Phosphoprotein; Reference proteome; rRNA processing;
KW   tRNA processing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P78346"
FT   CHAIN           2..268
FT                   /note="Ribonuclease P protein subunit p30"
FT                   /id="PRO_0000236681"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P78346"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P78346"
SQ   SEQUENCE   268 AA;  29395 MW;  D61883E7AFAFED73 CRC64;
     MAVFADLDLR AGSDLKALRG LVENAAHLGY SVVAINHVVE FKEKKQEIEK PVAVSELFTT
     LPIVQGKSKP IKILTRLTII VSDPSHCNVL RATSSRVRLY DIVAVFPKTE KLFHVACTHL
     DVDLVCITVT EKLPFYFKRP PINVAIDRGV GFELLYSPAI KDSTMRRYTI SNALNLMQVC
     KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAVLL HGETRKTAFG
     IISTVKKPRT SEADDDSLPA CKKAKCES