ID   RPP29_BOVIN             Reviewed;         220 AA.
AC   Q2KIB9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Ribonuclease P protein subunit p29;
GN   Name=POP4; Synonyms=RPP29;
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=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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.
CC       {ECO:0000250|UniProtKB:O95707}.
CC   -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins.
CC       RNase P consists of a catalytic RNA moiety and 10 different protein
CC       chains; 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:O95707}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:O95707}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 1 family. {ECO:0000305}.
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DR   EMBL; BC112695; AAI12696.1; -; mRNA.
DR   RefSeq; NP_001106753.1; NM_001113282.2.
DR   AlphaFoldDB; Q2KIB9; -.
DR   SMR; Q2KIB9; -.
DR   STRING; 9913.ENSBTAP00000002876; -.
DR   PaxDb; Q2KIB9; -.
DR   PRIDE; Q2KIB9; -.
DR   Ensembl; ENSBTAT00000002876; ENSBTAP00000002876; ENSBTAG00000002223.
DR   GeneID; 614870; -.
DR   KEGG; bta:614870; -.
DR   CTD; 10775; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002223; -.
DR   VGNC; VGNC:33164; POP4.
DR   eggNOG; KOG4046; Eukaryota.
DR   GeneTree; ENSGT00390000010067; -.
DR   HOGENOM; CLU_078577_2_1_1; -.
DR   InParanoid; Q2KIB9; -.
DR   OMA; IPKSECV; -.
DR   OrthoDB; 1362700at2759; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000002223; Expressed in oocyte and 102 other tissues.
DR   GO; GO:0030681; C:multimeric ribonuclease P complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR   GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; ISS:UniProtKB.
DR   Gene3D; 2.30.30.210; -; 1.
DR   InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR   InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR   InterPro; IPR023534; Rof/RNase_P-like.
DR   InterPro; IPR002730; Rpp29/RNP1.
DR   PANTHER; PTHR13348; PTHR13348; 1.
DR   Pfam; PF01868; RNase_P-MRP_p29; 1.
DR   PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR   SMART; SM00538; POP4; 1.
DR   SUPFAM; SSF101744; SSF101744; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT   CHAIN           1..220
FT                   /note="Ribonuclease P protein subunit p29"
FT                   /id="PRO_0000236680"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95707"
SQ   SEQUENCE   220 AA;  25524 MW;  0F9F42C93BD1D627 CRC64;
     MTSVVYHAFS QKEAKELDVQ HSGAQRAEAF VRAFLKRSMP RMSQQALEDH LQRKAVVLEY
     FTHRKQKEKR KKSKGLSAKQ RRELRLFDIK PEQQRYSLFL PLHELWKQYI RDLCNGLKPD
     TQPQMIQAKL LKADLHGAIV SVTKSKCPSY VGVTGILLQE TKHVFKIITK EDRLKVIPKL
     NCVFTVEIDG FISYIYGSKF QLRSSERSAK KFKAKGTIDL