RPR2_YEAST
ID RPR2_YEAST Reviewed; 144 AA.
AC P40571; D6VVU5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ribonuclease P protein subunit RPR2;
DE EC=3.1.26.5;
DE AltName: Full=RNA-processing protein RPR2;
DE AltName: Full=RNase P 16.4 kDa subunit;
GN Name=RPR2; OrderedLocusNames=YIR015W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
RX PubMed=9620854; DOI=10.1101/gad.12.11.1678;
RA Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.;
RT "Purification and characterization of the nuclear RNase P holoenzyme
RT complex reveals extensive subunit overlap with RNase MRP.";
RL Genes Dev. 12:1678-1690(1998).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Component of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends.
CC {ECO:0000269|PubMed:9620854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Component of nuclear RNase P. RNase P consists of an RNA
CC moiety and at least 9 protein subunits including POP1, POP3, POP4,
CC POP5, POP6, POP7, POP8, RPP1 and RPR2, many of which are shared with
CC the RNase MPR complex. {ECO:0000269|PubMed:9620854}.
CC -!- INTERACTION:
CC P40571; P38336: POP4; NbExp=3; IntAct=EBI-25408, EBI-13646;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 4 family. {ECO:0000305}.
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DR EMBL; Z37996; CAA86085.1; -; Genomic_DNA.
DR EMBL; AY557849; AAS56175.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08561.1; -; Genomic_DNA.
DR PIR; S48359; S48359.
DR RefSeq; NP_012280.1; NM_001179537.1.
DR PDB; 6AGB; EM; 3.48 A; K=1-144.
DR PDB; 6AH3; EM; 3.48 A; K=1-144.
DR PDBsum; 6AGB; -.
DR PDBsum; 6AH3; -.
DR AlphaFoldDB; P40571; -.
DR SMR; P40571; -.
DR BioGRID; 35007; 18.
DR ComplexPortal; CPX-1873; Nucleolar ribonuclease P complex.
DR IntAct; P40571; 10.
DR MINT; P40571; -.
DR STRING; 4932.YIR015W; -.
DR MaxQB; P40571; -.
DR PaxDb; P40571; -.
DR PRIDE; P40571; -.
DR EnsemblFungi; YIR015W_mRNA; YIR015W; YIR015W.
DR GeneID; 854832; -.
DR KEGG; sce:YIR015W; -.
DR SGD; S000001454; RPR2.
DR VEuPathDB; FungiDB:YIR015W; -.
DR eggNOG; KOG4394; Eukaryota.
DR HOGENOM; CLU_079140_4_1_1; -.
DR InParanoid; P40571; -.
DR OMA; PRTIANQ; -.
DR BioCyc; YEAST:YIR015W-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40571; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40571; protein.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IDA:SGD.
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:0034965; P:intronic box C/D RNA processing; IDA:SGD.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:ComplexPortal.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..144
FT /note="Ribonuclease P protein subunit RPR2"
FT /id="PRO_0000153847"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 28..54
FT /evidence="ECO:0007829|PDB:6AGB"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:6AGB"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:6AGB"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6AGB"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6AGB"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6AGB"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6AGB"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6AGB"
SQ SEQUENCE 144 AA; 16344 MW; 91AEF14F80D76148 CRC64;
MGKKAHGGKM KPEIDENGTL LVPPPRTIAN QDHFHRLNYL YQISAYQTRA RQKARTDAHT
PLARNYIKSM DLISKKTKTS LLPTIKRTIC KKCHRLLWTP KKLEITSDGA LSVMCGCGTV
KRFNIGADPN YRTYSEREGN LLNS
